|
Name |
Accession |
Description |
Interval |
E-value |
| put_anti_recept |
TIGR01665 |
phage minor structural protein, N-terminal region; This model represents the conserved ... |
30-353 |
4.69e-77 |
|
phage minor structural protein, N-terminal region; This model represents the conserved N-terminal region, typically from about residue 25 to about residue 350, of a family of uncharacterized phage proteins 500 to 1700 residues in length. [Mobile and extrachromosomal element functions, Prophage functions]
Pssm-ID: 273743 [Multi-domain] Cd Length: 317 Bit Score: 258.11 E-value: 4.69e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262435273 30 DNRHWEIKNNIDMLEFKTFDGTPHAVTLQQQNLVLKEVRDGRIVPYVINNEVEKDSDDRSLTVHASGAWVQIAKDGIIKP 109
Cdd:TIGR01665 2 DIKISEEKNNLDTLTFSLPFDDPLWEKIKEENYIKKHDDDLKNEQLFRINNVSEDASDDSISVEAIHVAVDLLDHVIIPI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262435273 110 QRIESETVNTFIDIAlADSKWQRGITDYSSFHTMTIDEFIDPLTFLKKIAALFESEIqYRVEVSGSQITGWYVDMIKKRG 189
Cdd:TIGR01665 82 KREKNTTSAALERLA-KTTWEVWKLGECSDIKTISITFYQTSRNALQAIAKLYKLSI-FYQWGGDNTITGKIVNLYKKIG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262435273 190 RETGKEVTLGKDIVGIRRIEHSRDICTALVGFVRGE-GDKLITIESINNGHLYITDSDAFQRWNAHGKHKFGFYTPETED 268
Cdd:TIGR01665 160 SETGKEFEYGKNLVGLNRKEDTKNIVTRLIPFGKGEgGEKGLTIESSNVGDEYIVDKDRQYKPNVDTTWVDGRYTDETTL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262435273 269 QNMTPQRLMTLMKmelkkrVNSSVSYEVEAQSIGRIFG-LAHELINEGDTIRIKDTGFTPKLYleARVIAGDESFTDPTQ 347
Cdd:TIGR01665 240 RAYAKQKLMTLKK------DMPKVSYEVTVADLENLSEyKSLEPIGIGDTVRLKHTDFNIKVY--ARVIKVEYSPVTPKQ 311
|
....*.
gi 1262435273 348 DKYVFG 353
Cdd:TIGR01665 312 NSIEFG 317
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
97-628 |
2.17e-55 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 204.04 E-value: 2.17e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262435273 97 AWVQIAKDGIIKPQRIESETVNTFIDIALADSKWQRGITDYSSFHTMTIDEFIDPLTFLKKIAALFESEIQYRVEVSGSQ 176
Cdd:COG5185 1 AVQRSKFLQVKNPLAKEGNANKELIEILLESSKSEGKTLVFITILFFPLGISRDSLRVTLRSVINVLDGLNYQNDVKKSE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262435273 177 ITGWYVDMIKKRGRETGKEVTLGKDIVGIRRIEHSRDICTALVGFVRGEGDKLITIESINNGHLYITDSDAFQRWNAHGK 256
Cdd:COG5185 81 SSVKARKFLKEKKLDTKILQEYVNSLIKLPNYEWSADILISLLYLYKSEIVALKDELIKVEKLDEIADIEASYGEVETGI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262435273 257 HKFGFYTPETEDQNMTPQRLMTLMKMELKKRVNSSVSYEVEAQSIGRIFGLAHELINEGDTIRIKDTGFTPKLYLearvi 336
Cdd:COG5185 161 IKDIFGKLTQELNQNLKKLEIFGLTLGLLKGISELKKAEPSGTVNSIKESETGNLGSESTLLEKAKEIINIEEAL----- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262435273 337 agdESFTDPTQDKYVFG----DYREITDPNEELRkiynriLGSLGNKQElidqldkLVKDANETASNAKKESEAAKtlaE 412
Cdd:COG5185 236 ---KGFQDPESELEDLAqtsdKLEKLVEQNTDLR------LEKLGENAE-------SSKRLNENANNLIKQFENTK---E 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262435273 413 KVQENLKNNT------------------VNIIESKQPPTENLQIGntiWRDISNGKPGILKVWNGKDWELLIPDPETI-- 472
Cdd:COG5185 297 KIAEYTKSIDikkatesleeqlaaaeaeQELEESKRETETGIQNL---TAEIEQGQESLTENLEAIKEEIENIVGEVEls 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262435273 473 -KKETMEQVNKDIQLTKEELNKKVEEAQsetaGQFKEVTENLQE-VSLTIKNVQNSQGEIDKTVSEMKQTNEGFTKSIDS 550
Cdd:COG5185 374 kSSEELDSFKDTIESTKESLDEIPQNQR----GYAQEILATLEDtLKAADRQIEELQRQIEQATSSNEEVSKLLNELISE 449
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1262435273 551 LMKKNGEITEKLNTVVEtsEGTIKKISEVQQTTNDLKKTTTEIEEKAGEISEKLTSVEKKVDNTEIGIRNLLLETANK 628
Cdd:COG5185 450 LNKVMREADEESQSRLE--EAYDEINRSVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLERQLEGVRSKLDQVAES 525
|
|
| PblB |
COG4926 |
Phage-related protein [Mobilome: prophages, transposons]; |
26-450 |
3.62e-23 |
|
Phage-related protein [Mobilome: prophages, transposons];
Pssm-ID: 443954 [Multi-domain] Cd Length: 438 Bit Score: 104.36 E-value: 3.62e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262435273 26 DYWADNRHWEIkNNIDMLEFKTFDGTPHAVTLQQQNLVLKEVRDGRiVPYVINnEVEKDSDdRSLTVHASGAWVQIAKDg 105
Cdd:COG4926 23 NAYDAVVTEEL-NGEYTLEFEYPYDGEKAEHLENENIIKVDTPRGN-QLFRIY-RVTKTMD-GTITVYAEHIFYDLLDN- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262435273 106 IIKPQRIESETVNTFIDIALADSKWQRGITDYSSF---HTMTIdEFIDPLTFLK----KIAALFESEIQYRVevsgsqit 178
Cdd:COG4926 98 FIEDTRVTNVTAQTALNDILDGTQYPHPFTGSSDItttRSAYV-VKKNALEALLgdenSFASRWGGELRFDN-------- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262435273 179 gWYVDMIKKRGRETGKEVTLGKDIVGIRRIEHSRDICTALVGFvrgeGDKLITIESINNGHlYITDSdafqrwnAHGKHK 258
Cdd:COG4926 169 -YTVDLLKRRGRDRGVVIRYRKNLTGLERTVDTTEVVTRIYPY----GKDGITLPEYIDSP-YIEDY-------PYPKIK 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262435273 259 FGFYTPETEDQNMT-PQRLMTLMKMELKKRVN-SSVSYEVEAQSIGRIFGLAH----ELINEGDTIRIKDTGFtpKLYLE 332
Cdd:COG4926 236 VIDYVSKFDDEDFTtPEQLREAAKEELKNGVDkPRVSYKVDFADLSQTEEYKHfkqlEAVRLGDTVTVYDEKL--GIDLK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262435273 333 ARVIAGDesfTDPTQDKYVfgdyrEITdpneelrkiynrilgsLGNKQELIdqldklvKDANETASNAKKESEAAKTLAE 412
Cdd:COG4926 314 ARVVAYQ---YDVLAPEYT-----EIE----------------LGSFVPSL-------TDSLTSIDKLLDQVEESSKNIN 362
|
410 420 430
....*....|....*....|....*....|....*...
gi 1262435273 413 KVQENLkNNTVNIIESKQPPTENLQIgntIWRDISNGK 450
Cdd:COG4926 363 QASDNA-TGLINSGNGKLVPEYPAEI---LIMDTENGE 396
|
|
| Prophage_tail |
pfam06605 |
Prophage endopeptidase tail; This family is of prophage tail proteins that are probably acting ... |
98-337 |
8.94e-14 |
|
Prophage endopeptidase tail; This family is of prophage tail proteins that are probably acting as endopeptidases.
Pssm-ID: 429028 Cd Length: 253 Bit Score: 72.74 E-value: 8.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262435273 98 WVQIAKDGIIKPQRIESETVNTFIDIALADS----KWQRGITDysSFHTMTIDEF--IDPLTFLKKIAALFESEIQYRve 171
Cdd:pfam06605 1 LYDLLDSEIQDDAKTGALSLEQALNFALDNNttgtTWEIGTVD--SFPSRTVENFgnNNALELLQQILEDFGGELRFD-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262435273 172 vsgsqiTGWYVDMIKKRGRETGKEVTLGKDIVGIRRIEHSRDICTAlvgfVRGEGDKLITIESINNGHLYITDSDAFQRW 251
Cdd:pfam06605 77 ------SNRHVDIYKLVGKDTGATFRYGYNLKDIEIETDTTSLATR----IYGYGKDDLTIETINDGKEYLEDSPAVDKY 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262435273 252 NAHGKHKFgfytpeTEDQNMT-PQRLMTLMKMELKKRVNSSVSYEVEAQSIGRIfGLAHELINEGDTIRIKDTGFtpKLY 330
Cdd:pfam06605 147 GISRKADP------ITDDRFTdPDSLKEYAKEQLQEYSKPDVSLTVTAADLSKL-TGEIEDFELGDYVRVIDEEL--GLD 217
|
....*..
gi 1262435273 331 LEARVIA 337
Cdd:pfam06605 218 VKVRIVG 224
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
370-638 |
5.94e-09 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 60.80 E-value: 5.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262435273 370 NRILGSLGNKQELIDQLDKLVKDANETASNAKKE-----SEAAKTLAEKVQENLKNNTVNIIESKQPPTENLQIGNTIWR 444
Cdd:TIGR04523 263 NKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEisdlnNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNE 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262435273 445 DISNGKpgilKVWNGKDWELLIPDPETIKKET-MEQVNKDIQLTKEELnKKVEEAQSETAGQFKEVTENLQEVSLTIKNV 523
Cdd:TIGR04523 343 QISQLK----KELTNSESENSEKQRELEEKQNeIEKLKKENQSYKQEI-KNLESQINDLESKIQNQEKLNQQKDEQIKKL 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262435273 524 QNSQGEIDKTVSEMKQTNEGFTKSIDSLMKKNGE----------ITEKLNTVVETSEGTIKKI-SEVQQTTNDLKKTTTE 592
Cdd:TIGR04523 418 QQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVkeliiknldnTRESLETQLKVLSRSINKIkQNLEQKQKELKSKEKE 497
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1262435273 593 IE---EKAGEISEKLTSVEKKVDNTEIGIRNLLLETANKSHSVKTGENK 638
Cdd:TIGR04523 498 LKklnEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDE 546
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
363-638 |
1.35e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 49.72 E-value: 1.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262435273 363 EELRKIYNRILGSLGNKQELIDQLD---KLVKDANETASNAKKESEAAKTLAEKVQENLKNNTVNIIE---SKQPPTEN- 435
Cdd:pfam05483 296 KELEDIKMSLQRSMSTQKALEEDLQiatKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEEllrTEQQRLEKn 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262435273 436 ---LQIGNTIWRDISNGKPGILKVWNGKDWELLIPDPETIKKETMEQVNKDIQLTKEELNKKVEEAQSETAGQFKEVTEn 512
Cdd:pfam05483 376 edqLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHD- 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262435273 513 lQEVSLTIknVQNSQGEIDKTVSEMKQ-------TNEGFTKSIDSLMKKNGEIT--------------EKLNTVVETSEG 571
Cdd:pfam05483 455 -LEIQLTA--IKTSEEHYLKEVEDLKTelekeklKNIELTAHCDKLLLENKELTqeasdmtlelkkhqEDIINCKKQEER 531
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1262435273 572 TIKKISEVQQTTNDLKKtttEIEEKAGEISEKLTSVEKKVDNTEIGIRNLLLETANKSHSVKTGENK 638
Cdd:pfam05483 532 MLKQIENLEEKEMNLRD---ELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENK 595
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
356-613 |
6.64e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.75 E-value: 6.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262435273 356 REITDPNEELRKIYNRILGSLGNKQE---LIDQLDKLVKD-ANETASNAKKESEAAKTLAEKVQENLKNNTVNIIESKQp 431
Cdd:PRK03918 341 EELKKKLKELEKRLEELEERHELYEEakaKKEELERLKKRlTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKK- 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262435273 432 ptenlqigntiwrDISNGKPGI--LKVWNGKDWELLIPDPETIKKETMEQVNKDIQLTKEELnKKVEEAQSETAGQFKEV 509
Cdd:PRK03918 420 -------------EIKELKKAIeeLKKAKGKCPVCGRELTEEHRKELLEEYTAELKRIEKEL-KEIEEKERKLRKELREL 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262435273 510 TENLQEVSLTIKNvqnsqgeiDKTVSEMKQTNEGFTKSIDSLMKKNGEITEKLNTVVETSEGTIKKISEVQQTTNDLKKT 589
Cdd:PRK03918 486 EKVLKKESELIKL--------KELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKK 557
|
250 260
....*....|....*....|....
gi 1262435273 590 TTEIEEKAGEISEKLTSVEKKVDN 613
Cdd:PRK03918 558 LAELEKKLDELEEELAELLKELEE 581
|
|
| COG6 |
smart01087 |
Conserved oligomeric complex COG6; COG6 is a component of the conserved oligomeric golgi ... |
490-567 |
2.03e-03 |
|
Conserved oligomeric complex COG6; COG6 is a component of the conserved oligomeric golgi complex, which is composed of eight different subunits and is required for normal golgi morphology and localisation.
Pssm-ID: 215018 Cd Length: 598 Bit Score: 42.69 E-value: 2.03e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1262435273 490 ELNKKVEEAQSETAGQFKEVTENLQEVSLTIKNVQNSQGEIDKTVSEMKQTNEGFTKSIDSLMKKNGEITEKLNTVVE 567
Cdd:smart01087 11 DLEKRLLKINGEFLSEFKPVAEQLQRLSEDVQKLNNSCDSMKDQLNTAKNQTQDLISEASELQEELALLELKKKLLDA 88
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| put_anti_recept |
TIGR01665 |
phage minor structural protein, N-terminal region; This model represents the conserved ... |
30-353 |
4.69e-77 |
|
phage minor structural protein, N-terminal region; This model represents the conserved N-terminal region, typically from about residue 25 to about residue 350, of a family of uncharacterized phage proteins 500 to 1700 residues in length. [Mobile and extrachromosomal element functions, Prophage functions]
Pssm-ID: 273743 [Multi-domain] Cd Length: 317 Bit Score: 258.11 E-value: 4.69e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262435273 30 DNRHWEIKNNIDMLEFKTFDGTPHAVTLQQQNLVLKEVRDGRIVPYVINNEVEKDSDDRSLTVHASGAWVQIAKDGIIKP 109
Cdd:TIGR01665 2 DIKISEEKNNLDTLTFSLPFDDPLWEKIKEENYIKKHDDDLKNEQLFRINNVSEDASDDSISVEAIHVAVDLLDHVIIPI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262435273 110 QRIESETVNTFIDIAlADSKWQRGITDYSSFHTMTIDEFIDPLTFLKKIAALFESEIqYRVEVSGSQITGWYVDMIKKRG 189
Cdd:TIGR01665 82 KREKNTTSAALERLA-KTTWEVWKLGECSDIKTISITFYQTSRNALQAIAKLYKLSI-FYQWGGDNTITGKIVNLYKKIG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262435273 190 RETGKEVTLGKDIVGIRRIEHSRDICTALVGFVRGE-GDKLITIESINNGHLYITDSDAFQRWNAHGKHKFGFYTPETED 268
Cdd:TIGR01665 160 SETGKEFEYGKNLVGLNRKEDTKNIVTRLIPFGKGEgGEKGLTIESSNVGDEYIVDKDRQYKPNVDTTWVDGRYTDETTL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262435273 269 QNMTPQRLMTLMKmelkkrVNSSVSYEVEAQSIGRIFG-LAHELINEGDTIRIKDTGFTPKLYleARVIAGDESFTDPTQ 347
Cdd:TIGR01665 240 RAYAKQKLMTLKK------DMPKVSYEVTVADLENLSEyKSLEPIGIGDTVRLKHTDFNIKVY--ARVIKVEYSPVTPKQ 311
|
....*.
gi 1262435273 348 DKYVFG 353
Cdd:TIGR01665 312 NSIEFG 317
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
97-628 |
2.17e-55 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 204.04 E-value: 2.17e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262435273 97 AWVQIAKDGIIKPQRIESETVNTFIDIALADSKWQRGITDYSSFHTMTIDEFIDPLTFLKKIAALFESEIQYRVEVSGSQ 176
Cdd:COG5185 1 AVQRSKFLQVKNPLAKEGNANKELIEILLESSKSEGKTLVFITILFFPLGISRDSLRVTLRSVINVLDGLNYQNDVKKSE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262435273 177 ITGWYVDMIKKRGRETGKEVTLGKDIVGIRRIEHSRDICTALVGFVRGEGDKLITIESINNGHLYITDSDAFQRWNAHGK 256
Cdd:COG5185 81 SSVKARKFLKEKKLDTKILQEYVNSLIKLPNYEWSADILISLLYLYKSEIVALKDELIKVEKLDEIADIEASYGEVETGI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262435273 257 HKFGFYTPETEDQNMTPQRLMTLMKMELKKRVNSSVSYEVEAQSIGRIFGLAHELINEGDTIRIKDTGFTPKLYLearvi 336
Cdd:COG5185 161 IKDIFGKLTQELNQNLKKLEIFGLTLGLLKGISELKKAEPSGTVNSIKESETGNLGSESTLLEKAKEIINIEEAL----- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262435273 337 agdESFTDPTQDKYVFG----DYREITDPNEELRkiynriLGSLGNKQElidqldkLVKDANETASNAKKESEAAKtlaE 412
Cdd:COG5185 236 ---KGFQDPESELEDLAqtsdKLEKLVEQNTDLR------LEKLGENAE-------SSKRLNENANNLIKQFENTK---E 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262435273 413 KVQENLKNNT------------------VNIIESKQPPTENLQIGntiWRDISNGKPGILKVWNGKDWELLIPDPETI-- 472
Cdd:COG5185 297 KIAEYTKSIDikkatesleeqlaaaeaeQELEESKRETETGIQNL---TAEIEQGQESLTENLEAIKEEIENIVGEVEls 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262435273 473 -KKETMEQVNKDIQLTKEELNKKVEEAQsetaGQFKEVTENLQE-VSLTIKNVQNSQGEIDKTVSEMKQTNEGFTKSIDS 550
Cdd:COG5185 374 kSSEELDSFKDTIESTKESLDEIPQNQR----GYAQEILATLEDtLKAADRQIEELQRQIEQATSSNEEVSKLLNELISE 449
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1262435273 551 LMKKNGEITEKLNTVVEtsEGTIKKISEVQQTTNDLKKTTTEIEEKAGEISEKLTSVEKKVDNTEIGIRNLLLETANK 628
Cdd:COG5185 450 LNKVMREADEESQSRLE--EAYDEINRSVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLERQLEGVRSKLDQVAES 525
|
|
| PblB |
COG4926 |
Phage-related protein [Mobilome: prophages, transposons]; |
26-450 |
3.62e-23 |
|
Phage-related protein [Mobilome: prophages, transposons];
Pssm-ID: 443954 [Multi-domain] Cd Length: 438 Bit Score: 104.36 E-value: 3.62e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262435273 26 DYWADNRHWEIkNNIDMLEFKTFDGTPHAVTLQQQNLVLKEVRDGRiVPYVINnEVEKDSDdRSLTVHASGAWVQIAKDg 105
Cdd:COG4926 23 NAYDAVVTEEL-NGEYTLEFEYPYDGEKAEHLENENIIKVDTPRGN-QLFRIY-RVTKTMD-GTITVYAEHIFYDLLDN- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262435273 106 IIKPQRIESETVNTFIDIALADSKWQRGITDYSSF---HTMTIdEFIDPLTFLK----KIAALFESEIQYRVevsgsqit 178
Cdd:COG4926 98 FIEDTRVTNVTAQTALNDILDGTQYPHPFTGSSDItttRSAYV-VKKNALEALLgdenSFASRWGGELRFDN-------- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262435273 179 gWYVDMIKKRGRETGKEVTLGKDIVGIRRIEHSRDICTALVGFvrgeGDKLITIESINNGHlYITDSdafqrwnAHGKHK 258
Cdd:COG4926 169 -YTVDLLKRRGRDRGVVIRYRKNLTGLERTVDTTEVVTRIYPY----GKDGITLPEYIDSP-YIEDY-------PYPKIK 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262435273 259 FGFYTPETEDQNMT-PQRLMTLMKMELKKRVN-SSVSYEVEAQSIGRIFGLAH----ELINEGDTIRIKDTGFtpKLYLE 332
Cdd:COG4926 236 VIDYVSKFDDEDFTtPEQLREAAKEELKNGVDkPRVSYKVDFADLSQTEEYKHfkqlEAVRLGDTVTVYDEKL--GIDLK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262435273 333 ARVIAGDesfTDPTQDKYVfgdyrEITdpneelrkiynrilgsLGNKQELIdqldklvKDANETASNAKKESEAAKTLAE 412
Cdd:COG4926 314 ARVVAYQ---YDVLAPEYT-----EIE----------------LGSFVPSL-------TDSLTSIDKLLDQVEESSKNIN 362
|
410 420 430
....*....|....*....|....*....|....*...
gi 1262435273 413 KVQENLkNNTVNIIESKQPPTENLQIgntIWRDISNGK 450
Cdd:COG4926 363 QASDNA-TGLINSGNGKLVPEYPAEI---LIMDTENGE 396
|
|
| Prophage_tail |
pfam06605 |
Prophage endopeptidase tail; This family is of prophage tail proteins that are probably acting ... |
98-337 |
8.94e-14 |
|
Prophage endopeptidase tail; This family is of prophage tail proteins that are probably acting as endopeptidases.
Pssm-ID: 429028 Cd Length: 253 Bit Score: 72.74 E-value: 8.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262435273 98 WVQIAKDGIIKPQRIESETVNTFIDIALADS----KWQRGITDysSFHTMTIDEF--IDPLTFLKKIAALFESEIQYRve 171
Cdd:pfam06605 1 LYDLLDSEIQDDAKTGALSLEQALNFALDNNttgtTWEIGTVD--SFPSRTVENFgnNNALELLQQILEDFGGELRFD-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262435273 172 vsgsqiTGWYVDMIKKRGRETGKEVTLGKDIVGIRRIEHSRDICTAlvgfVRGEGDKLITIESINNGHLYITDSDAFQRW 251
Cdd:pfam06605 77 ------SNRHVDIYKLVGKDTGATFRYGYNLKDIEIETDTTSLATR----IYGYGKDDLTIETINDGKEYLEDSPAVDKY 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262435273 252 NAHGKHKFgfytpeTEDQNMT-PQRLMTLMKMELKKRVNSSVSYEVEAQSIGRIfGLAHELINEGDTIRIKDTGFtpKLY 330
Cdd:pfam06605 147 GISRKADP------ITDDRFTdPDSLKEYAKEQLQEYSKPDVSLTVTAADLSKL-TGEIEDFELGDYVRVIDEEL--GLD 217
|
....*..
gi 1262435273 331 LEARVIA 337
Cdd:pfam06605 218 VKVRIVG 224
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
370-638 |
5.94e-09 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 60.80 E-value: 5.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262435273 370 NRILGSLGNKQELIDQLDKLVKDANETASNAKKE-----SEAAKTLAEKVQENLKNNTVNIIESKQPPTENLQIGNTIWR 444
Cdd:TIGR04523 263 NKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEisdlnNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNE 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262435273 445 DISNGKpgilKVWNGKDWELLIPDPETIKKET-MEQVNKDIQLTKEELnKKVEEAQSETAGQFKEVTENLQEVSLTIKNV 523
Cdd:TIGR04523 343 QISQLK----KELTNSESENSEKQRELEEKQNeIEKLKKENQSYKQEI-KNLESQINDLESKIQNQEKLNQQKDEQIKKL 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262435273 524 QNSQGEIDKTVSEMKQTNEGFTKSIDSLMKKNGE----------ITEKLNTVVETSEGTIKKI-SEVQQTTNDLKKTTTE 592
Cdd:TIGR04523 418 QQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVkeliiknldnTRESLETQLKVLSRSINKIkQNLEQKQKELKSKEKE 497
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1262435273 593 IE---EKAGEISEKLTSVEKKVDNTEIGIRNLLLETANKSHSVKTGENK 638
Cdd:TIGR04523 498 LKklnEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDE 546
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
357-876 |
9.29e-06 |
|
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: 50.82 E-value: 9.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262435273 357 EITDPNEELRKIYNRILGSLGNKQelIDQLDKLVKDA----NETASNAKKESEAAKTLaEKVQENLKnntvnIIESKQPP 432
Cdd:TIGR01612 861 KIDSEHEQFAELTNKIKAEISDDK--LNDYEKKFNDSksliNEINKSIEEEYQNINTL-KKVDEYIK-----ICENTKES 932
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262435273 433 TENLQIGNTIWRDISNGKPGILKVWNG--KDWELLIPDPETIKKETMEQVNKDIQLT----------------KEELNKK 494
Cdd:TIGR01612 933 IEKFHNKQNILKEILNKNIDTIKESNLieKSYKDKFDNTLIDKINELDKAFKDASLNdyeaknnelikyfndlKANLGKN 1012
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262435273 495 VEEAQSETAGQFKEVTENLQEVSLTI-KNVQNSQGEIDKTVSEMKQTNEGFT-KSIDSLmkkNGEITEKLNTVVET---- 568
Cdd:TIGR01612 1013 KENMLYHQFDEKEKATNDIEQKIEDAnKNIPNIEIAIHTSIYNIIDEIEKEIgKNIELL---NKEILEEAEINITNfnei 1089
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262435273 569 -------------SEGTIKKISEVQQTTNDLK----------KTTTEIEEKA----GEISEKLTSVEKKVDNT------- 614
Cdd:TIGR01612 1090 keklkhynfddfgKEENIKYADEINKIKDDIKnldqkidhhiKALEEIKKKSenyiDEIKAQINDLEDVADKAisnddpe 1169
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262435273 615 --EIGIRNLLLETANKSHSVKTGENKPHTYFGVVKDAITLMQGKNIAMSF------LFTGKVTEWGTTDKWV--GFEVKI 684
Cdd:TIGR01612 1170 eiEKKIENIVTKIDKKKNIYDEIKKLLNEIAEIEKDKTSLEEVKGINLSYgknlgkLFLEKIDEEKKKSEHMikAMEAYI 1249
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262435273 685 TFIDNtFAYPSCRIENRLTLGKQYKQE------------RFTASAVVMDKPIKEILVYALG--RDFTGDVLIEKPKLEVG 750
Cdd:TIGR01612 1250 EDLDE-IKEKSPEIENEMGIEMDIKAEmetfnishdddkDHHIISKKHDENISDIREKSLKiiEDFSEESDINDIKKELQ 1328
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262435273 751 TVptawtpALEDQVTNEEFTK------------KTTEIEKSVNGIKESIKTVEKTQVDFSQRVTTVEKTADGIKENVtSL 818
Cdd:TIGR01612 1329 KN------LLDAQKHNSDINLylneianiynilKLNKIKKIIDEVKEYTKEIEENNKNIKDELDKSEKLIKKIKDDI-NL 1401
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1262435273 819 QEIQTKqgtqlqeakagwettakaLEGKVEIKDVEdyvGGIGNQTVLRNVLW----NNDTKY 876
Cdd:TIGR01612 1402 EECKSK------------------IESTLDDKDID---ECIKKIKELKNHILseesNIDTYF 1442
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
354-809 |
1.10e-05 |
|
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: 50.44 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262435273 354 DYREITDPNEELRKIYNRILGSLGNkqelIDQLDKLVKDANETASNAKKESEAAKTLAEKVQENLKNNTV-----NIIES 428
Cdd:TIGR01612 1413 DDKDIDECIKKIKELKNHILSEESN----IDTYFKNADENNENVLLLFKNIEMADNKSQHILKIKKDNATndhdfNINEL 1488
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262435273 429 KqpptENLQIGNTIWRDISNGKPGIlkvwnGKDWELLipdpETIKKETMEQVNKDIQLtkeELNKKVEEAQSETAGQFKE 508
Cdd:TIGR01612 1489 K----EHIDKSKGCKDEADKNAKAI-----EKNKELF----EQYKKDVTELLNKYSAL---AIKNKFAKTKKDSEIIIKE 1552
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262435273 509 VTENLQEVSL-------TIKNVQNSQGEIDKTVSEMKQTNE---GFTKSIDSLMKKNGEITE---KLNTVVETSEGTIKK 575
Cdd:TIGR01612 1553 IKDAHKKFILeaekseqKIKEIKKEKFRIEDDAAKNDKSNKaaiDIQLSLENFENKFLKISDikkKINDCLKETESIEKK 1632
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262435273 576 ISEVQQTTND-------------------LKKTTTEIEEKAGEISE---KLTSVEKKVD----NTEIGIRNLLLETAnks 629
Cdd:TIGR01612 1633 ISSFSIDSQDtelkengdnlnslqeflesLKDQKKNIEDKKKELDEldsEIEKIEIDVDqhkkNYEIGIIEKIKEIA--- 1709
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262435273 630 hsvKTGENKPHTYFGVVKDAItlmqgKNIAMSFlFTGKVTEWGTTDKWVGFEVKITFIDNTFAYPSCRIENRL-TLGK-- 706
Cdd:TIGR01612 1710 ---IANKEEIESIKELIEPTI-----ENLISSF-NTNDLEGIDPNEKLEEYNTEIGDIYEEFIELYNIIAGCLeTVSKep 1780
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262435273 707 ----QYKQERFTASavvmDKPIKEILVYALGRDFTGDVLIEkpklEVGTVPTAWTPALEDqvTNEEFTKKTTEIEKSVNG 782
Cdd:TIGR01612 1781 itydEIKNTRINAQ----NEFLKIIEIEKKSKSYLDDIEAK----EFDRIINHFKKKLDH--VNDKFTKEYSKINEGFDD 1850
|
490 500
....*....|....*....|....*..
gi 1262435273 783 IKESIKTVeKTQVDFSQRVTTVEKTAD 809
Cdd:TIGR01612 1851 ISKSIENV-KNSTDENLLFDILNKTKD 1876
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
358-609 |
1.33e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 48.75 E-value: 1.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262435273 358 ITDPNEELRKIYNRILGSLGNKQELIDQLDKLVKDANETASNAKKESEAAKTLAEKVQENLK-----NNTVNiiESKQPP 432
Cdd:COG1340 3 TDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREkrdelNEKVK--ELKEER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262435273 433 TENLQIGNTIWRDISNGKPGILKVWNGKdwelliPDPETIKKEtMEQVNKDIQ---LTKEE----------LNKKVEEAQ 499
Cdd:COG1340 81 DELNEKLNELREELDELRKELAELNKAG------GSIDKLRKE-IERLEWRQQtevLSPEEekelvekikeLEKELEKAK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262435273 500 S---------ETAGQFKEVTENLQEVSLTIKNVQNSQGEIDKTVSEMKQTNEGFTKSIDSLMKKNGEITEKLNTVVETSE 570
Cdd:COG1340 154 KalekneklkELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEII 233
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1262435273 571 GTIKKISEVQQTTNDLKKTTT---------EIEEKAGEISEKLTSVEK 609
Cdd:COG1340 234 ELQKELRELRKELKKLRKKQRalkrekekeELEEKAEEIFEKLKKGEK 281
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
363-638 |
1.35e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 49.72 E-value: 1.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262435273 363 EELRKIYNRILGSLGNKQELIDQLD---KLVKDANETASNAKKESEAAKTLAEKVQENLKNNTVNIIE---SKQPPTEN- 435
Cdd:pfam05483 296 KELEDIKMSLQRSMSTQKALEEDLQiatKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEEllrTEQQRLEKn 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262435273 436 ---LQIGNTIWRDISNGKPGILKVWNGKDWELLIPDPETIKKETMEQVNKDIQLTKEELNKKVEEAQSETAGQFKEVTEn 512
Cdd:pfam05483 376 edqLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHD- 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262435273 513 lQEVSLTIknVQNSQGEIDKTVSEMKQ-------TNEGFTKSIDSLMKKNGEIT--------------EKLNTVVETSEG 571
Cdd:pfam05483 455 -LEIQLTA--IKTSEEHYLKEVEDLKTelekeklKNIELTAHCDKLLLENKELTqeasdmtlelkkhqEDIINCKKQEER 531
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1262435273 572 TIKKISEVQQTTNDLKKtttEIEEKAGEISEKLTSVEKKVDNTEIGIRNLLLETANKSHSVKTGENK 638
Cdd:pfam05483 532 MLKQIENLEEKEMNLRD---ELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENK 595
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
339-638 |
3.03e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 48.48 E-value: 3.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262435273 339 DESFTDPTQDKYVFGDYREITDPNEELRKIYNRILGSLGNKQELIDQLDKLVKDANETASNAKKESEAAKTLAEKVQE-- 416
Cdd:TIGR04523 145 TEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISElk 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262435273 417 NLKNNTVNIIESKQPPTENLQ--IGNTIWR--DISNGKPGILKVWNGKDWELlipdpETIKKeTMEQVNKDIQLTKEELN 492
Cdd:TIGR04523 225 KQNNQLKDNIEKKQQEINEKTteISNTQTQlnQLKDEQNKIKKQLSEKQKEL-----EQNNK-KIKELEKQLNQLKSEIS 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262435273 493 KKVEEAQSETAgqfKEVTENLQEVSLTIKNVQNSQGEIDKTVSEMKQTNEGFTKSIDSL----MKKNGEITEKLN---TV 565
Cdd:TIGR04523 299 DLNNQKEQDWN---KELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSesenSEKQRELEEKQNeieKL 375
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1262435273 566 VETSEGTIKKISEVQQTTNDLKKTTTEIEEKAGEISEKLTSVEKKVDNTEIGIRNLLLETANKSHSVKTGENK 638
Cdd:TIGR04523 376 KKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQ 448
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
475-629 |
3.99e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.59 E-value: 3.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262435273 475 ETMEQVNKDIQLTKEELNKKVEEAQ------SETAGQFKEVTENLQEVSLTIKNVQNSQGEIDKTVSEMKQTNEGFTKSI 548
Cdd:COG4372 38 FELDKLQEELEQLREELEQAREELEqleeelEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEEL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262435273 549 DSLMKKNGEITEKLNTVVETSEGTIKKISEVQQTTNDLKKTTTEIEEKAGEISEKLTSVEKKVDNTEIgirNLLLETANK 628
Cdd:COG4372 118 EELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQAL---DELLKEANR 194
|
.
gi 1262435273 629 S 629
Cdd:COG4372 195 N 195
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
363-634 |
5.91e-05 |
|
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: 47.76 E-value: 5.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262435273 363 EELRKIYNRILGSLGNKQELIDQLDKLVKDANETASNAKKESEAAKTLAEKVQENLKNNTVNIIESKQPPTENlqignti 442
Cdd:TIGR02169 684 EGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENV------- 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262435273 443 wrdisngkpgilkvwngkdwellipdpetikKETMEQVNKDI---QLTKEELNKKVEEAQSETAGQ-FKEVTENLQEVSL 518
Cdd:TIGR02169 757 -------------------------------KSELKELEARIeelEEDLHKLEEALNDLEARLSHSrIPEIQAELSKLEE 805
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262435273 519 TIKNVQNSQGEIDKTVSEMKQTNEGFTKSIDSLMKKNGEITEKLNTVVETSEGTIKKISEVQQTTNDLKKTTTEIEEKAG 598
Cdd:TIGR02169 806 EVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLG 885
|
250 260 270
....*....|....*....|....*....|....*.
gi 1262435273 599 EISEKLTSVEKKVDNTEIGIRNLLLETANKSHSVKT 634
Cdd:TIGR02169 886 DLKKERDELEAQLRELERKIEELEAQIEKKRKRLSE 921
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
356-613 |
6.64e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.75 E-value: 6.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262435273 356 REITDPNEELRKIYNRILGSLGNKQE---LIDQLDKLVKD-ANETASNAKKESEAAKTLAEKVQENLKNNTVNIIESKQp 431
Cdd:PRK03918 341 EELKKKLKELEKRLEELEERHELYEEakaKKEELERLKKRlTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKK- 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262435273 432 ptenlqigntiwrDISNGKPGI--LKVWNGKDWELLIPDPETIKKETMEQVNKDIQLTKEELnKKVEEAQSETAGQFKEV 509
Cdd:PRK03918 420 -------------EIKELKKAIeeLKKAKGKCPVCGRELTEEHRKELLEEYTAELKRIEKEL-KEIEEKERKLRKELREL 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262435273 510 TENLQEVSLTIKNvqnsqgeiDKTVSEMKQTNEGFTKSIDSLMKKNGEITEKLNTVVETSEGTIKKISEVQQTTNDLKKT 589
Cdd:PRK03918 486 EKVLKKESELIKL--------KELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKK 557
|
250 260
....*....|....*....|....
gi 1262435273 590 TTEIEEKAGEISEKLTSVEKKVDN 613
Cdd:PRK03918 558 LAELEKKLDELEEELAELLKELEE 581
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
370-638 |
2.80e-04 |
|
chromosome segregation protein SMC, common bacterial 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. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 45.82 E-value: 2.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262435273 370 NRILGSLGNKQElIDQLDKLVKDANETASNAKKESEAAKTLAEKVQENLKnntvniieskqpptENLQIGNTIWRDISNG 449
Cdd:TIGR02168 667 KTNSSILERRRE-IEELEEKIEELEEKIAELEKALAELRKELEELEEELE--------------QLRKELEELSRQISAL 731
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262435273 450 KPGILKvwngkdwellipdpETIKKETMEQVNKDIQLTKEELNKKVEEAQS---ETAGQFKEVTENLQEVSLTIKNVQNS 526
Cdd:TIGR02168 732 RKDLAR--------------LEAEVEQLEERIAQLSKELTELEAEIEELEErleEAEEELAEAEAEIEELEAQIEQLKEE 797
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262435273 527 QGEIDKTVS----EMKQTNEGFTksidslmkkngEITEKLNTVVETSEGTIKKISEVQQTtndLKKTTTEIEEKAGEI-- 600
Cdd:TIGR02168 798 LKALREALDelraELTLLNEEAA-----------NLRERLESLERRIAATERRLEDLEEQ---IEELSEDIESLAAEIee 863
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1262435273 601 --------SEKLTSVEKKVDNTEIGIRNLLLETANKSHSVKTGENK 638
Cdd:TIGR02168 864 leelieelESELEALLNERASLEEALALLRSELEELSEELRELESK 909
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
364-638 |
3.10e-04 |
|
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: 45.81 E-value: 3.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262435273 364 ELRKIYNrilgslGNKQELIDQLDKLVKDANETASNAKKESEAAKTLAEKVQENLKNNTVNIIESKQPPTENLQigNTIW 443
Cdd:TIGR01612 664 ELSKIYE------DDIDALYNELSSIVKENAIDNTEDKAKLDDLKSKIDKEYDKIQNMETATVELHLSNIENKK--NELL 735
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262435273 444 RDISNGKPGILKVWNgKDWELLIPDPETIKKETMEQVNkDIQLTKEELNK---KVEEAQSETAGQF-------KEVTENL 513
Cdd:TIGR01612 736 DIIVEIKKHIHGEIN-KDLNKILEDFKNKEKELSNKIN-DYAKEKDELNKyksKISEIKNHYNDQInidnikdEDAKQNY 813
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262435273 514 QEVSLTIKNVQNSQGEIDKTVSEMKQTNEGFTKSIDSLMKKNGEITEKLNTVVET---------SEGTIKKISEVQQTTN 584
Cdd:TIGR01612 814 DKSKEYIKTISIKEDEIFKIINEMKFMKDDFLNKVDKFINFENNCKEKIDSEHEQfaeltnkikAEISDDKLNDYEKKFN 893
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262435273 585 DLK----KTTTEIEEKAGEIS--EKLTSVEKKVDNTEIGIRNLlletANKSHSVKTGENK 638
Cdd:TIGR01612 894 DSKslinEINKSIEEEYQNINtlKKVDEYIKICENTKESIEKF----HNKQNILKEILNK 949
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
474-609 |
3.57e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 44.83 E-value: 3.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262435273 474 KETMEQVNKDI-----QLTKE-ELNKKVEEAQSETAGQFKEVTENLQEVSLTIKNVQNS----QGEIDKTvsemkqtnEG 543
Cdd:PRK04778 281 EEKNEEIQERIdqlydILEREvKARKYVEKNSDTLPDFLEHAKEQNKELKEEIDRVKQSytlnESELESV--------RQ 352
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1262435273 544 FTKSIDSLMKKNGEITEKLNTvvetsegtiKKI--SEVQQTTNDLKKTTTEIEEKAGEISEKLTSVEK 609
Cdd:PRK04778 353 LEKQLESLEKQYDEITERIAE---------QEIaySELQEELEEILKQLEEIEKEQEKLSEMLQGLRK 411
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
473-612 |
8.61e-04 |
|
chromosome segregation protein SMC, common bacterial 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. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 43.89 E-value: 8.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262435273 473 KKETMEQVNK-DIQLTK-----EELNKKVE--EAQSETAGQFKEVTENLQEVSLTI---------KNVQNSQGEIDKTVS 535
Cdd:TIGR02168 174 RKETERKLERtRENLDRledilNELERQLKslERQAEKAERYKELKAELRELELALlvlrleelrEELEELQEELKEAEE 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262435273 536 EMKQTNEGFTK---SIDSLMKKNGEITEKLNTV----------VETSEGTIKKISE-VQQTTNDLKKTTTEIEE---KAG 598
Cdd:TIGR02168 254 ELEELTAELQEleeKLEELRLEVSELEEEIEELqkelyalaneISRLEQQKQILRErLANLERQLEELEAQLEElesKLD 333
|
170
....*....|....
gi 1262435273 599 EISEKLTSVEKKVD 612
Cdd:TIGR02168 334 ELAEELAELEEKLE 347
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
476-621 |
1.12e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.97 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262435273 476 TMEQVNKDIQLTKEELNKKVEEAQSETagqfKEVTENLQEVSltiKNVQNSQGEIDKTVSEMKQTNEGFTKSIDSLMKKN 555
Cdd:COG4372 28 ALSEQLRKALFELDKLQEELEQLREEL----EQAREELEQLE---EELEQARSELEQLEEELEELNEQLQAAQAELAQAQ 100
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1262435273 556 GEIT---EKLNTVVETSEGTIKKISEVQQTTNDLKKTTTEIEEKAGEISEKLTSVEKKVDNTEIGIRNL 621
Cdd:COG4372 101 EELEslqEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAAL 169
|
|
| COG6 |
smart01087 |
Conserved oligomeric complex COG6; COG6 is a component of the conserved oligomeric golgi ... |
490-567 |
2.03e-03 |
|
Conserved oligomeric complex COG6; COG6 is a component of the conserved oligomeric golgi complex, which is composed of eight different subunits and is required for normal golgi morphology and localisation.
Pssm-ID: 215018 Cd Length: 598 Bit Score: 42.69 E-value: 2.03e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1262435273 490 ELNKKVEEAQSETAGQFKEVTENLQEVSLTIKNVQNSQGEIDKTVSEMKQTNEGFTKSIDSLMKKNGEITEKLNTVVE 567
Cdd:smart01087 11 DLEKRLLKINGEFLSEFKPVAEQLQRLSEDVQKLNNSCDSMKDQLNTAKNQTQDLISEASELQEELALLELKKKLLDA 88
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
470-605 |
2.16e-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: 40.71 E-value: 2.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262435273 470 ETIKKETMEQVNKDIQLTKEELNKKVEEAQsetagqfKEVTENLQEVsltiknvqnsQGEIDKTVSEMKQTNEGFTKSI- 548
Cdd:pfam01442 21 GPVAQELVDRLEKETEALRERLQKDLEEVR-------AKLEPYLEEL----------QAKLGQNVEELRQRLEPYTEELr 83
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1262435273 549 DSLMKKNGEITEKLNTVV-ETSEGTIKKISEVQQTTNDL-KKTTTEIEEKAGEISEKLT 605
Cdd:pfam01442 84 KRLNADAEELQEKLAPYGeELRERLEQNVDALRARLAPYaEELRQKLAERLEELKESLA 142
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
475-609 |
2.52e-03 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 42.15 E-value: 2.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262435273 475 ETMEQVNKDIQ---------LTKEELNKK-VEEAQSETAGQFKEVTENLQEVSLTIKNVQNS----QGEIDKTvsemkqt 540
Cdd:pfam06160 259 DEAEEALEEIEeridqlydlLEKEVDAKKyVEKNLPEIEDYLEHAEEQNKELKEELERVQQSytlnENELERV------- 331
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1262435273 541 nEGFTKSIDSLMKKNGEITEKLNTvvetsegtiKKI--SEVQQTTNDLKKTTTEIEEKAGEISEKLTSVEK 609
Cdd:pfam06160 332 -RGLEKQLEELEKRYDEIVERLEE---------KEVaySELQEELEEILEQLEEIEEEQEEFKESLQSLRK 392
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
470-610 |
2.63e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.06 E-value: 2.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262435273 470 ETIKKETMEQVnKDIQLTKEELNKKVEEAQSETAG---QFKEVTENLQEVSLTIKNVQNSQGEIdKTVSEMkqtnEGFTK 546
Cdd:COG1579 23 EHRLKELPAEL-AELEDELAALEARLEAAKTELEDlekEIKRLELEIEEVEARIKKYEEQLGNV-RNNKEY----EALQK 96
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1262435273 547 SIDSLMKKNGEITEKLNTVVETSEGTIKKISEVQ----QTTNDLKKTTTEIEEKAGEISEKLTSVEKK 610
Cdd:COG1579 97 EIESLKRRISDLEDEILELMERIEELEEELAELEaelaELEAELEEKKAELDEELAELEAELEELEAE 164
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
482-612 |
3.33e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.74 E-value: 3.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262435273 482 KDIQLTKEELNKKVEEAQSETAGQFKEVTENLQEVSLTIKNVQNSQGEIDKTVSEMKQTNEGFTKSIDSL------MKKN 555
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELgeraraLYRS 98
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1262435273 556 GEITEKLNTVVETSE--------GTIKKISEVQQTT-NDLKKTTTEIEEKAGEISEKLTSVEKKVD 612
Cdd:COG3883 99 GGSVSYLDVLLGSESfsdfldrlSALSKIADADADLlEELKADKAELEAKKAELEAKLAELEALKA 164
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
511-621 |
4.15e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.59 E-value: 4.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262435273 511 ENLQEVSLTIKNVQN-------SQGEIDKTVSEMKQTNEGFTKSIDSLMKKNGEITEKLNTV---VETSEGTIKKISEVQ 580
Cdd:PRK03918 165 KNLGEVIKEIKRRIErlekfikRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLekeVKELEELKEEIEELE 244
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1262435273 581 QTTNDLKKTTTEIEEKAGEISEKLTSVEKKVDNTEIGIRNL 621
Cdd:PRK03918 245 KELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKEL 285
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
474-604 |
4.25e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 41.96 E-value: 4.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262435273 474 KETMEQVNKDIQLTKEELNKkvEEAQSETAGQFKEVTENLQEVSLTIKNVQNSQGEIDKTVSEMKQTNEG--FTKSIDSL 551
Cdd:TIGR00606 750 RNKLQKVNRDIQRLKNDIEE--QETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGsdLDRTVQQV 827
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1262435273 552 MKKNGEITEKLNTVVETSEGTIKKISEVQQTTNDLKKTTTEIEEKAGEISEKL 604
Cdd:TIGR00606 828 NQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNL 880
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
357-604 |
5.25e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 41.16 E-value: 5.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262435273 357 EITDPNEELRKIYNRIlgslGNKQELIDQLDKLVKDANETASNAKKESEAAKTLAEKVQENLKNNTVNIIESKQpptENL 436
Cdd:TIGR04523 434 TIIKNNSEIKDLTNQD----SVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNE---EKK 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262435273 437 QIGNTIWRDISNGKPGILKVwngKDWELLIPDPET-IKKETMEQVNKDIQLTKEELNKKVEEAQSETAgQFKEVTENL-- 513
Cdd:TIGR04523 507 ELEEKVKDLTKKISSLKEKI---EKLESEKKEKESkISDLEDELNKDDFELKKENLEKEIDEKNKEIE-ELKQTQKSLkk 582
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262435273 514 --QEVSLTIKNVQNSQGEIDKTVSEMKQTNEGFTKSIDSLMKKNGEITEKLNTVVETSEGTIKKISEVQQTTNDLKKTTT 591
Cdd:TIGR04523 583 kqEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWP 662
|
250
....*....|...
gi 1262435273 592 EIEEKAGEISEKL 604
Cdd:TIGR04523 663 EIIKKIKESKTKI 675
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
471-629 |
5.57e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 41.16 E-value: 5.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262435273 471 TIKKETMEQVNKDIQLTKEELNKKVEEAQSETA---GQFKEVTENLQEV--SLTIKNVQNSQGEIDKTVSEMKQTNegft 545
Cdd:TIGR04523 502 NEEKKELEEKVKDLTKKISSLKEKIEKLESEKKekeSKISDLEDELNKDdfELKKENLEKEIDEKNKEIEELKQTQ---- 577
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262435273 546 ksiDSLMKKNGEITEKLNTVVETSEGTIKKISEVQQTTNDLKKTTTEIEEKAGEISEKLTSVEKKVDNTE---IGIRNLL 622
Cdd:TIGR04523 578 ---KSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKqevKQIKETI 654
|
....*..
gi 1262435273 623 LETANKS 629
Cdd:TIGR04523 655 KEIRNKW 661
|
|
| PRK09343 |
PRK09343 |
prefoldin subunit beta; Provisional |
504-604 |
7.26e-03 |
|
prefoldin subunit beta; Provisional
Pssm-ID: 181787 [Multi-domain] Cd Length: 121 Bit Score: 38.13 E-value: 7.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262435273 504 GQFKEVTENLQEVSLTIKNVQNSQGEIDKTVSEMKQTNEGFT--KSIDSLMKKngeiTEKLNTVVETSEGtiKKISEVQQ 581
Cdd:PRK09343 14 AQLQQLQQQLERLLQQKSQIDLELREINKALEELEKLPDDTPiyKIVGNLLVK----VDKTKVEKELKER--KELLELRS 87
|
90 100
....*....|....*....|...
gi 1262435273 582 TTndLKKTTTEIEEKAGEISEKL 604
Cdd:PRK09343 88 RT--LEKQEKKLREKLKELQAKI 108
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
363-610 |
7.48e-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: 40.82 E-value: 7.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262435273 363 EELRKIYNRILGS-LGNKQELIDQLDKLVKDaNETASNAKKESEAAKTLAEKVQENLKNNTVNIIESKQpptenLQIgNT 441
Cdd:TIGR02169 779 EALNDLEARLSHSrIPEIQAELSKLEEEVSR-IEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLK-----EQI-KS 851
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262435273 442 IWRDISNGkpgilkvwNGKDWELlipdpETIKKETMEQVN------KDIQLTKEELNKKVEEAQS-----ETAGQFKEVT 510
Cdd:TIGR02169 852 IEKEIENL--------NGKKEEL-----EEELEELEAALRdlesrlGDLKKERDELEAQLRELERkieelEAQIEKKRKR 918
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262435273 511 ENLQEVSLTIKNVQNSqgEIDKTVSEMKQTNEGfTKSIDSLMKKNGEITEKLNTVVETSEGTIKKISEVQQTTNDLKKTT 590
Cdd:TIGR02169 919 LSELKAKLEALEEELS--EIEDPKGEDEEIPEE-ELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKR 995
|
250 260
....*....|....*....|
gi 1262435273 591 TEIEEKAGEISEKLTSVEKK 610
Cdd:TIGR02169 996 AKLEEERKAILERIEEYEKK 1015
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
381-631 |
8.14e-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: 40.82 E-value: 8.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262435273 381 ELIDQLDKLVKDANET----ASNAKKESEAAKTLAEKVQENLKnntvniieSKQpptenlqignTIWRDISNGKPGILKV 456
Cdd:TIGR02169 195 EKRQQLERLRREREKAeryqALLKEKREYEGYELLKEKEALER--------QKE----------AIERQLASLEEELEKL 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262435273 457 wngkdwELLIPDpetiKKETMEQVNKDIqltkEELNKKVEEaqsETAGQFKEVTENLQEVSLTIKNVQNSqgeIDKTVSE 536
Cdd:TIGR02169 257 ------TEEISE----LEKRLEEIEQLL----EELNKKIKD---LGEEEQLRVKEKIGELEAEIASLERS---IAEKERE 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262435273 537 MKQTNEGFTKSIDSLMKKNGEItEKLNTVVET----SEGTIKKISEVQQTTNDLKKTTTEIEEKAGEISEKLTSVEKKVD 612
Cdd:TIGR02169 317 LEDAEERLAKLEAEIDKLLAEI-EELEREIEEerkrRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLE 395
|
250 260
....*....|....*....|....*
gi 1262435273 613 ------NTEIGIRNLLLETANKSHS 631
Cdd:TIGR02169 396 klkreiNELKRELDRLQEELQRLSE 420
|
|
| ApoLp-III |
pfam07464 |
Apolipophorin-III precursor (apoLp-III); This family consists of several insect ... |
500-637 |
8.45e-03 |
|
Apolipophorin-III precursor (apoLp-III); This family consists of several insect apolipoprotein-III sequences. Exchangeable apolipoproteins constitute a functionally important family of proteins that play critical roles in lipid transport and lipoprotein metabolism. Apolipophorin III (apoLp-III) is a prototypical exchangeable apolipoprotein found in many insect species that functions in transport of diacylglycerol (DAG) from the fat body lipid storage depot to flight muscles in the adult life stage.
Pssm-ID: 462172 [Multi-domain] Cd Length: 143 Bit Score: 38.50 E-value: 8.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1262435273 500 SETAGQFKEV--TENLQEVSLTIKNvqNSqgeiDKTVSEMKQtnegFTKSIDSLMKKNGEITEklntvvETSEGTIKKIS 577
Cdd:pfam07464 3 EELQQSVQKQlgLPSQQEVVETIKE--NT----ENLVDQLKQ----VQKSLQEELKKASGEAE------EALKELNTKIV 66
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1262435273 578 EvqqTTNDLKKTTTEIEEKAGEISEKLTSvekkvdnteiGIRNLLLETAN-----KSHSVKTGEN 637
Cdd:pfam07464 67 E---TADKLSEANPEVVQKANELQEKFQS----------GVQSLVTESQKlaksiSENSQGATEK 118
|
|
| |
