|
Name |
Accession |
Description |
Interval |
E-value |
| CCDC73 |
pfam15818 |
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil ... |
48-1010 |
0e+00 |
|
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil containing proteins. The function is not known. The alternative name is sarcoma antigen NY-SAR-79.
Pssm-ID: 464893 [Multi-domain] Cd Length: 1048 Bit Score: 845.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503306 48 EELRIRRISKHTLQKKLNEMDQKLQMHLTGREEHNKKLNEVERCYATIACQFGIVKGVHEKLEHSVQEAIQLNKKLTSVN 127
Cdd:pfam15818 99 ETLKALQVSKYSLQKKVSEMEQKLQLHLLAKEDHHKQLNEIEKYYATITGQFGLVKENHGKLEQNVQEAIQLNKRLSALN 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503306 128 KRQETEISNLKEELKKVTTDLIRSKVTSQHRVGEENINLAAKEKQFQELQQKIRMETAISKRVQEENANIKEEKLEILSS 207
Cdd:pfam15818 179 KKQESEICSLKKELKKVTSDLIKSKVTCQYKMGEENINLTIKEQKFQELQERLNMELELNKKINEEITHIQEEKQDIIIS 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503306 208 LQCVQKQLQQITQTNVRMESELNALREEYQTLERDNELQREKAKENEEKFLNLQNEHEKALRIWKKDEENLRREMDTIKN 287
Cdd:pfam15818 259 FQHMQQLLQQQTQANTEMEAELKALKENNQTLERDNELQREKVKENEEKFLNLQNEHEKALGTWKKHVEELNGEINEIKN 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503306 288 ELNSLKKTQGHLDDCHPPQGNQ----HSEQVENLQIHSTVHpvirnsGQEQSKGSEIQAIQKKNDcmpsilrkdnnsghE 363
Cdd:pfam15818 339 ELSSLKETHIKLQEHYNKLCNQkkfeEDKKFQNVPEVNNEN------SEMSTEKSENLIIQKYNS--------------E 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503306 364 DEIEVKNTVSFSLSTEELQIEQK------------LQVLENGFKDEINVASPLEGKEREVSPRNTLCTDTDLITQGQNse 431
Cdd:pfam15818 399 QEIREENTKSFCSDTEYRETEKKkgppveeiiiedLQVLEKSFKNEIDTSVPQDKNQSEISLSKTLCTDKDLISQGQT-- 476
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503306 432 MHVTECKEAENLETTCRVLLEGNSANLQQKLQDSTGPAAPHHTETSKVLLDAADRVIVSDKNAIQEMNSSNQELCSTTHE 511
Cdd:pfam15818 477 LNVTDFRKSVTTEIKDKLCLEKDNGCSEFKSPNNLFLVADQSIETEKIHLESTEGLGLHHADIHLETESNRSSFNGTLNE 556
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503306 512 SICTKvdknssiiELNSSVLTTKASKKESEAAVCTEKSAVCERNTDNHQVSEFHFGILSYPKENCQtgYQKCSLLNSDN- 590
Cdd:pfam15818 557 MAHNT--------NHNKDVSENEPFKQQFRLLLCTQENATEKRITNSDQTKAGLDSSLDVKKNPVQ--CQKYSLQDSSNv 626
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503306 591 NVDNRLCRIERslLNLSDLPRDKFPFKQTHIDAEDKNYNDNAA--NINRSGALRHIGFPpmdaqnvlAIYCDNASTD-KA 667
Cdd:pfam15818 627 SLDDKQCKIEQ--LLNKKSECSTLPLKQTSSFQQLCNDTSEKPglTIPCDTVVSHPISP--------AAFSDNLKADlKN 696
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503306 668 AKEQSSNMPFTGTYNLCPEKINKGINVDDVHSKQPE-HDSTEQSGGDESMCTLNAEAMSPVKAHDLDTTVQKVPADGIDV 746
Cdd:pfam15818 697 SDNNVNIMPMLVKPNSSPGKRTTRKNLDDMQSSQFKnCLGGLENGVTISHLQVNNENSHASQAKDLKTAVHPKTSTEIQF 776
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503306 747 DKL----NEEIQIQSIKNEHSLDINDDSINNSMLK--QEKDSVHSTVPGRKFAEGHLKESCSLPMRTSGNLVNASGRSSF 820
Cdd:pfam15818 777 SSKesqiDENQITEATKNDLFLLVNVNERQHTLLNntEKTESLNDIVSGKIYSEGQLEESHSFHIKPSGDLVNRSGRSAF 856
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503306 821 DLSNSDKKAEKTSVCFKFLGLSSCSRVNQMRSQATWTSSSQEPSVLKEKLPCLVENKKVPSRELFQNVSENVGRKETGPG 900
Cdd:pfam15818 857 DLSTSDKKTEKTPVYLNFLDPSPWSKVNQTEGQTVSTSTSSIPLLLKEKPIGPSENTKIISVTLCKNVGVDDVRKDIGPD 936
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503306 901 STSSNRAADTLNTSRIHRDPQGDPTEEWNAIAKTFYDSSFPTEHVKEGFTALNEQKSSPMTVTSAQSERTLGDEDRFPTH 980
Cdd:pfam15818 937 TTSISRVADTLNNSSIHPDPKGEPSEERNATAKTFYDSSFPTEHVKTEPLKSTVLQSHFQTVKIKDSPDLLKSSPGEDDW 1016
|
970 980 990
....*....|....*....|....*....|
gi 2024503306 981 NSTVQSQIEEIEKYLNLETLCSSRKRKYED 1010
Cdd:pfam15818 1017 QSLITNQITEIEKLLSLENDNQPKKRKAEE 1046
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
23-292 |
2.59e-09 |
|
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: 61.61 E-value: 2.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503306 23 ALQSPSETLLSIRLLDFKTSLLETIEELRIRRISKHTLQKKLNEMDQKLQMHltgREEHNKKLNEVERCYATIACQFGIV 102
Cdd:TIGR02168 687 EELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARL---EAEVEQLEERIAQLSKELTELEAEI 763
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503306 103 KGVHEKLEHSVQEAIQLNKKLTSVNKRQET---EISNLKEELKKVTTDLIRSKV---TSQHRVGEENINLAAKEKQFQEL 176
Cdd:TIGR02168 764 EELEERLEEAEEELAEAEAEIEELEAQIEQlkeELKALREALDELRAELTLLNEeaaNLRERLESLERRIAATERRLEDL 843
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503306 177 QQKIRMETAISKRVQEENANIKEEKLEILSSLQCVQKQLQQitqtnvrMESELNALREEYQTLERDNELQREKAKENEEK 256
Cdd:TIGR02168 844 EEQIEELSEDIESLAAEIEELEELIEELESELEALLNERAS-------LEEALALLRSELEELSEELRELESKRSELRRE 916
|
250 260 270
....*....|....*....|....*....|....*.
gi 2024503306 257 FLNLQNEHEKAlriwKKDEENLRREMDTIKNELNSL 292
Cdd:TIGR02168 917 LEELREKLAQL----ELRLEGLEVRIDNLQERLSEE 948
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
12-294 |
2.21e-08 |
|
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: 58.54 E-value: 2.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503306 12 DEDLKMQALDSALQSPSETLLSIRLLDFKTSLLETIEELRIRRISKHTLQKKLNEMDQKLQMHLTGREEHNKKLNEV-ER 90
Cdd:TIGR02169 208 EKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgEE 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503306 91 CYATIACQFGIVKGVHEKLEHSVQEAIQLNKKLTSVNKRQETEISNLKEELKKVTTDLIRSKVtSQHRVGEENINLAAK- 169
Cdd:TIGR02169 288 EQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERK-RRDKLTEEYAELKEEl 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503306 170 EKQFQELQQ---KIRMETAISKRVQEENANIKEEKLEILSSLQCVQKQLQQITQTNVRMESELNALREEYQTLERDNELQ 246
Cdd:TIGR02169 367 EDLRAELEEvdkEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDK 446
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 2024503306 247 REKAKENEEKFLNLQNEHEKAlriwKKDEENLRREMDTIKNELNSLKK 294
Cdd:TIGR02169 447 ALEIKKQEWKLEQLAADLSKY----EQELYDLKEEYDRVEKELSKLQR 490
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
36-301 |
2.30e-08 |
|
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: 58.54 E-value: 2.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503306 36 LLDFKTSLLETIEELRIRRISKHTLQKKLNEMDQKLqmHLTGREEHNKKLNEVERCYATIACQfgiVKGVHEKLEHSVQE 115
Cdd:TIGR02169 192 IIDEKRQQLERLRREREKAERYQALLKEKREYEGYE--LLKEKEALERQKEAIERQLASLEEE---LEKLTEEISELEKR 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503306 116 AIQLNKKLTSVNKR----QETEISNLKEELKKVTTDLIRSKVtsqhrvgeeniNLAAKEKQFQELQQKIRmetaiskRVQ 191
Cdd:TIGR02169 267 LEEIEQLLEELNKKikdlGEEEQLRVKEKIGELEAEIASLER-----------SIAEKERELEDAEERLA-------KLE 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503306 192 EENANIKEEKLEILSSLQCVQKQLQQITQTNVRMESELNALREEYQTLERDNELQREKAKENEEKFLNLQNEHEKALRIW 271
Cdd:TIGR02169 329 AEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKREL 408
|
250 260 270
....*....|....*....|....*....|...
gi 2024503306 272 KKDEENLRR---EMDTIKNELNSLKKTQGHLDD 301
Cdd:TIGR02169 409 DRLQEELQRlseELADLNAAIAGIEAKINELEE 441
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
48-296 |
1.98e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 55.33 E-value: 1.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503306 48 EELRIRRISKhtLQKKLNEMDQKLQMHLTGREEHNKKLNEVERCYATIAcqfgivkgvhEKLEHSVQEAIQLNKKLtsvN 127
Cdd:COG1196 220 EELKELEAEL--LLLKLRELEAELEELEAELEELEAELEELEAELAELE----------AELEELRLELEELELEL---E 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503306 128 KRQEtEISNLKEELKKVTTDLIRSKVTSQhrvgEENINLAAKEKQFQELQQKIRMETAISKRVQEENANIKEEKLEILSS 207
Cdd:COG1196 285 EAQA-EEYELLAELARLEQDIARLEERRR----ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAE 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503306 208 LQCVQKQLQQITQTNVRMESELNALREEYQTLERDNELQREKAKENEEKFLNLQNEHEKALRIWKKDEENLRREMDTIKN 287
Cdd:COG1196 360 LAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEE 439
|
....*....
gi 2024503306 288 ELNSLKKTQ 296
Cdd:COG1196 440 EEEALEEAA 448
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
128-301 |
2.17e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 55.33 E-value: 2.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503306 128 KRQETEISNLKEELKKVTTDLIRSKVTSQH---RVGEENINLAAKEKQFQELQQKIRMETAISKRVQEENANIKEEKLEI 204
Cdd:COG1196 235 RELEAELEELEAELEELEAELEELEAELAEleaELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRREL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503306 205 LSSLQCVQKQLQQITQTNVRMESELNALREEYQTLERDNELQREKAKENEEKFLNLQNEHEKALRIWKKDEENLRREMDT 284
Cdd:COG1196 315 EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRA 394
|
170
....*....|....*..
gi 2024503306 285 IKNELNSLKKTQGHLDD 301
Cdd:COG1196 395 AAELAAQLEELEEAEEA 411
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
39-299 |
3.06e-07 |
|
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: 54.69 E-value: 3.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503306 39 FKTSLLETIEELRIR----RISKHTLQKKLNEMDQKLQMHLTGREEHNKKLNEVERCYATIAcqfgivkgvhEKLEHSVQ 114
Cdd:TIGR02169 668 FSRSEPAELQRLRERleglKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLE----------QEEEKLKE 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503306 115 EAIQLNKKLTSVnkrqETEISNLKEELKKVttdlirskvtsQHRVGEENINLAAKEKQFQELQQKIRMEtaISKRVQEEN 194
Cdd:TIGR02169 738 RLEELEEDLSSL----EQEIENVKSELKEL-----------EARIEELEEDLHKLEEALNDLEARLSHS--RIPEIQAEL 800
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503306 195 ANIKEEKLEILSSLQCVQKQLQQITQtnvrmesELNALREEYQTLERDNELQREKAKENEEKFLNLQ----------NEH 264
Cdd:TIGR02169 801 SKLEEEVSRIEARLREIEQKLNRLTL-------EKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNgkkeeleeelEEL 873
|
250 260 270
....*....|....*....|....*....|....*
gi 2024503306 265 EKALRIWKKDEENLRREMDTIKNELNSLKKTQGHL 299
Cdd:TIGR02169 874 EAALRDLESRLGDLKKERDELEAQLRELERKIEEL 908
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
57-344 |
3.76e-07 |
|
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: 54.29 E-value: 3.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503306 57 KHTLQKKLNEMDQKLQMHLTGREEHNKKLNEVERcYATIACQFgivKGVHEKLEH-----SVQEAIQLNKKLTSVN---K 128
Cdd:TIGR02168 174 RKETERKLERTRENLDRLEDILNELERQLKSLER-QAEKAERY---KELKAELRElelalLVLRLEELREELEELQeelK 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503306 129 RQETEISNLKEELKKVTTDL--IRSKVTS--------QHRVGEENINLAAKEKQFQELQQKIRMETAISKRVQEENANIK 198
Cdd:TIGR02168 250 EAEEELEELTAELQELEEKLeeLRLEVSEleeeieelQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELE 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503306 199 EEKLEILSSLQCVQKQLQQITQTNVRMESELNALREEYQTLERDNELQREKAKENEEKFLNLQNEHEKAlriwKKDEENL 278
Cdd:TIGR02168 330 SKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASL----NNEIERL 405
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024503306 279 RREMDTIKNELNSLKKTQ-GHLDDCHPPQGNQHSEQVENL--QIHSTVHPVIRNSGQEQSKGSEIQAIQ 344
Cdd:TIGR02168 406 EARLERLEDRRERLQQEIeELLKKLEEAELKELQAELEELeeELEELQEELERLEEALEELREELEEAE 474
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
32-256 |
1.01e-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: 49.68 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503306 32 LSIRLLDFKTSLLETIEELRIRRISKHTLQKKLNEMDQKLQMHL--TGREEHNKKLNEVERCYATIACQFGIVKGVH--- 106
Cdd:TIGR02169 749 LEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRipEIQAELSKLEEEVSRIEARLREIEQKLNRLTlek 828
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503306 107 EKLEHSVQEAIQLNKKLTSVNKRQETEISNLK----------EELKKVTTDLI---------RSKVTSQHRVGEENINLA 167
Cdd:TIGR02169 829 EYLEKEIQELQEQRIDLKEQIKSIEKEIENLNgkkeeleeelEELEAALRDLEsrlgdlkkeRDELEAQLRELERKIEEL 908
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503306 168 AKEKQFQELQQKIRMETAisKRVQEENANIKEEKLEILS------SLQCVQKQLQQITQTNVRMESELNALREEYQ-TLE 240
Cdd:TIGR02169 909 EAQIEKKRKRLSELKAKL--EALEEELSEIEDPKGEDEEipeeelSLEDVQAELQRVEEEIRALEPVNMLAIQEYEeVLK 986
|
250
....*....|....*.
gi 2024503306 241 RDNELQREKAKENEEK 256
Cdd:TIGR02169 987 RLDELKEKRAKLEEER 1002
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
78-294 |
8.39e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 46.65 E-value: 8.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503306 78 REEHNKKLNEVERCYATIACQFGIVKGVHEKLEHSVQEAIQLNKKLTSVNKRQETEisnlKEELKKVTTDLIRSKVT--- 154
Cdd:pfam15921 418 RRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLEST----KEMLRKVVEELTAKKMTles 493
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503306 155 SQHRVGEENINLAAKEK------------------QFQELQQkIRMETAISKRVQEENANIKEEKLEILSSLQCVQKQLQ 216
Cdd:pfam15921 494 SERTVSDLTASLQEKERaieatnaeitklrsrvdlKLQELQH-LKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIE 572
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503306 217 QITQ--------------TNVRMESELNALREEYQTLERDNELQREKAKENEE----------KFLNLQNEHEKALRIWK 272
Cdd:pfam15921 573 NMTQlvgqhgrtagamqvEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEArvsdlelekvKLVNAGSERLRAVKDIK 652
|
250 260
....*....|....*....|..
gi 2024503306 273 KDEENLRREMDTIKNELNSLKK 294
Cdd:pfam15921 653 QERDQLLNEVKTSRNELNSLSE 674
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
166-299 |
2.18e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 44.75 E-value: 2.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503306 166 LAAKEKQFQELQQKIRMETAISKRVQEENANIKEEKLEILSSLQCVQKQLQQITQTNVRMESELNALREEYQTLERDNEL 245
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEA 101
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024503306 246 QREKAKE-----------NEEKFLNLQ---NEHEKALRIWKKDEENLRREMDTIKNELNSLKKTQGHL 299
Cdd:COG4942 102 QKEELAEllralyrlgrqPPLALLLSPedfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAEL 169
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
60-294 |
2.66e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 44.37 E-value: 2.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503306 60 LQKKLNEMDQKLQmhltgreEHNKKLNEVERCYATIACQfgiVKGVHEKLEHSVQEAIQLNKKLTSVNKRQ---ETEISN 136
Cdd:COG4942 25 AEAELEQLQQEIA-------ELEKELAALKKEEKALLKQ---LAALERRIAALARRIRALEQELAALEAELaelEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503306 137 LKEELKKVTTDLIRSKVTSQHRVGEENINLAAKEKQFQELQQKIRMETAISKRVQEENANIKEEkleilsslqcvQKQLQ 216
Cdd:COG4942 95 LRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRAD-----------LAELA 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024503306 217 QITQtnvrmesELNALREEYQTLERDNELQREKAKENEEKFLNLQNEHEKALRIWKKDEENLRREMDTIKNELNSLKK 294
Cdd:COG4942 164 ALRA-------ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEA 234
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
40-265 |
4.28e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.37 E-value: 4.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503306 40 KTSLLETIEELRIRRiskhtLQKKLNEM----DQKLQMHLTGREEHNKKLNEVERcyatiacqfgivkgVHEKLEHSVQE 115
Cdd:COG4717 36 KSTLLAFIRAMLLER-----LEKEADELfkpqGRKPELNLKELKELEEELKEAEE--------------KEEEYAELQEE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503306 116 AIQLNKKLtsvnKRQETEISNLKEELKKVttDLIRSKVTSQHRVGEENINLAAKEKQFQELQQKIR----METAISKRVQ 191
Cdd:COG4717 97 LEELEEEL----EELEAELEELREELEKL--EKLLQLLPLYQELEALEAELAELPERLEELEERLEelreLEEELEELEA 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024503306 192 E-ENANIKEEKLEILSSLQcVQKQLQQITQTNVRMESELNALREEYQTLERDNELQREKAKENEEKFLNLQNEHE 265
Cdd:COG4717 171 ElAELQEELEELLEQLSLA-TEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEER 244
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
106-300 |
4.84e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.14 E-value: 4.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503306 106 HEKLEHSVQEAIQLNKKLTSVNKRQ-----ETEISNLKEELKKVTTDLirskvtsqhrvgeeninlAAKEKQFQELQQKI 180
Cdd:COG4913 264 YAAARERLAELEYLRAALRLWFAQRrlellEAELEELRAELARLEAEL------------------ERLEARLDALREEL 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503306 181 R-METAISKRVQEENANIKEEkleilssLQCVQKQLQQITQTNVRMESELNALREEYQTLERDNELQREKAKENEEKFLN 259
Cdd:COG4913 326 DeLEAQIRGNGGDRLEQLERE-------IERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEE 398
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2024503306 260 LQNEHEKALRIWKKDEENLRREMDTIKNELNSLKKTQGHLD 300
Cdd:COG4913 399 ELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIP 439
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
114-301 |
6.23e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.60 E-value: 6.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503306 114 QEAIQLNKKLTSVNKRQETEISNLKEELK--KVTTDLIRSKVTSQHRVGEEninLAAKEKQFQELQQKIR-METAISKR- 189
Cdd:COG4717 53 KEADELFKPQGRKPELNLKELKELEEELKeaEEKEEEYAELQEELEELEEE---LEELEAELEELREELEkLEKLLQLLp 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503306 190 VQEENANIKEEKLEILSSLQCVQKQLQQITQtnvrMESELNALREEYQTLERD-NELQREKAKENEEKFLNLQNEHE--- 265
Cdd:COG4717 130 LYQELEALEAELAELPERLEELEERLEELRE----LEEELEELEAELAELQEElEELLEQLSLATEEELQDLAEELEelq 205
|
170 180 190
....*....|....*....|....*....|....*.
gi 2024503306 266 KALRIWKKDEENLRREMDTIKNELNSLKKTQGHLDD 301
Cdd:COG4717 206 QRLAELEEELEEAQEELEELEEELEQLENELEAAAL 241
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
7-298 |
7.04e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 43.57 E-value: 7.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503306 7 QVLKMDEDLKMQALDSALQSPSETL-----LSIRLLDFKTSLLETIEELRIRRISKHTLQKKLNEMDQKLQMHLTGREEH 81
Cdd:pfam15921 436 KAMKSECQGQMERQMAAIQGKNESLekvssLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEAT 515
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503306 82 NKKLNEVERCYATIACQFGIVKGVHEKLEHSVQEAIQLnkKLTSVNKRQETEIsnLKEELKKVTtdlirsKVTSQH--RV 159
Cdd:pfam15921 516 NAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEAL--KLQMAEKDKVIEI--LRQQIENMT------QLVGQHgrTA 585
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503306 160 GEENINLAAKEKQFQ----ELQQKIRMETAISKRVQEENANIKEEKLEI----------LSSLQCVQKQLQQITQTNVRM 225
Cdd:pfam15921 586 GAMQVEKAQLEKEINdrrlELQEFKILKDKKDAKIRELEARVSDLELEKvklvnagserLRAVKDIKQERDQLLNEVKTS 665
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024503306 226 ESELNALREEYQTLERDnelqrekakeneekFLNLQNEHEKALRIWKKDEENLRREMDTIKNELNSLKKTQGH 298
Cdd:pfam15921 666 RNELNSLSEDYEVLKRN--------------FRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGH 724
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
156-299 |
7.09e-04 |
|
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: 42.22 E-value: 7.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503306 156 QHRVGEENINLAAKEKQFQELQQKIrmeTAISKRVQEENANIKEEKLEILSslqcVQKQLQQIT--QTNVRMESELNALR 233
Cdd:COG1579 23 EHRLKELPAELAELEDELAALEARL---EAAKTELEDLEKEIKRLELEIEE----VEARIKKYEeqLGNVRNNKEYEALQ 95
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024503306 234 EEYQTLERDNELQREKAKENEEKFLNLQNEHEKALRIWKKDEENLRREMDTIKNELNSLKKTQGHL 299
Cdd:COG1579 96 KEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEEL 161
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
199-301 |
7.36e-04 |
|
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: 42.22 E-value: 7.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503306 199 EEKLEILSSLQCVQKQLQQITQTNVRMESELNALREEYQTLERDNELQREKAKENEEKFLNLQNEHEKALRIWKKDEENL 278
Cdd:COG1579 3 PEDLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQL 82
|
90 100
....*....|....*....|....*...
gi 2024503306 279 R-----REMDTIKNELNSLKKTQGHLDD 301
Cdd:COG1579 83 GnvrnnKEYEALQKEIESLKRRISDLED 110
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
59-269 |
8.93e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.89 E-value: 8.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503306 59 TLQKKLNEMDQKLqmhltgrEEHNKKLNEVErcyatiacqfgivkgvhEKLEHSVQEAIQLNKKLTsvnkRQETEISNLK 138
Cdd:COG3883 34 AAQAELDALQAEL-------EELNEEYNELQ-----------------AELEALQAEIDKLQAEIA----EAEAEIEERR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503306 139 EELKKvttdLIRSKVTSQHRVGEENINLAAKEkqFQELQQKIRMETAISKRVQEENANIKEEKLEILSSLQCVQKQLQQI 218
Cdd:COG3883 86 EELGE----RARALYRSGGSVSYLDVLLGSES--FSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAEL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2024503306 219 TQTNVRMES---ELNALREEYQTLERDNELQREKAKENEEKFLNLQNEHEKALR 269
Cdd:COG3883 160 EALKAELEAakaELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAA 213
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
114-301 |
9.22e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.83 E-value: 9.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503306 114 QEAIQLNKKLTSVNKrqetEISNLKEELKKVTTDliRSKVTSQHRVGEENINLAAK-----EKQFQELQQKIRmetAISK 188
Cdd:COG4942 20 DAAAEAEAELEQLQQ----EIAELEKELAALKKE--EKALLKQLAALERRIAALARriralEQELAALEAELA---ELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503306 189 RVQEENANIKEEKLEILSSLQCVQKQ------------------------LQQITQTNVRMESELNALREEYQTLERDNE 244
Cdd:COG4942 91 EIAELRAELEAQKEELAELLRALYRLgrqpplalllspedfldavrrlqyLKYLAPARREQAEELRADLAELAALRAELE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2024503306 245 LQREKAKENEEKFLNLQNEHEKALRIWKKDEENLRREMDTIKNELNSLKKTQGHLDD 301
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEA 227
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
128-301 |
1.07e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.58 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503306 128 KRQETEISNLKEELKKVTTDLIRSKVTSQhrvgEENINLAAKEKQFQELQQKIRMETAISKRVQEENANIKEEKLEILSS 207
Cdd:COG4372 41 DKLQEELEQLREELEQAREELEQLEEELE----QARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503306 208 LQCVQKQLQQITQTNVRMESELNALREEYQTLERDNELQREKAKENEEKFLNLQNEHEKAlriwkkDEENLRREMDTIKN 287
Cdd:COG4372 117 LEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQAL------SEAEAEQALDELLK 190
|
170
....*....|....
gi 2024503306 288 ELNSLKKTQGHLDD 301
Cdd:COG4372 191 EANRNAEKEEELAE 204
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
161-275 |
1.23e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 42.54 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503306 161 EENINLAAKEKQFQELQQKIrmetaisKRVQEENANIK---EEKLEILSSLQCVQKQLQQITQTNVRMESELNALREEYQ 237
Cdd:COG2433 403 HEERELTEEEEEIRRLEEQV-------ERLEAEVEELEaelEEKDERIERLERELSEARSEERREIRKDREISRLDREIE 475
|
90 100 110
....*....|....*....|....*....|....*...
gi 2024503306 238 TLERdnELQREKaKENEEkflnLQNEHEKALRIWKKDE 275
Cdd:COG2433 476 RLER--ELEEER-ERIEE----LKRKLERLKELWKLEH 506
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
35-294 |
1.94e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.36 E-value: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503306 35 RLLDFKTSLLETIEELRIRRISKHTLQKKLNEMDQKLqmhltgrEEHNKKLNEVERCYATIACQFGIVKGVHEKLEHSVQ 114
Cdd:PRK03918 166 NLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKEL-------EEVLREINEISSELPELREELEKLEKEVKELEELKE 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503306 115 EAIQLNKKLTSVNKRQ---ETEISNLK---EELKKVTTDL--IRSKVTSQHRVGEENINLAAKEKQFQELQQKIRMETAi 186
Cdd:PRK03918 239 EIEELEKELESLEGSKrklEEKIRELEeriEELKKEIEELeeKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLS- 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503306 187 skRVQEENANIkEEKLEILSSLQcvqKQLQQITQTNVRMESELNALREEYQTLER----DNELQREKAK---ENEEKFLN 259
Cdd:PRK03918 318 --RLEEEINGI-EERIKELEEKE---ERLEELKKKLKELEKRLEELEERHELYEEakakKEELERLKKRltgLTPEKLEK 391
|
250 260 270
....*....|....*....|....*....|....*
gi 2024503306 260 LQNEHEKALRIWKKDEENLRREMDTIKNELNSLKK 294
Cdd:PRK03918 392 ELEELEKAKEEIEEEISKITARIGELKKEIKELKK 426
|
|
| ANIS5_cation-bd |
pfam02520 |
SXP/RAL-2 family protein Ani s 5-like, metal-binding domain; This domain is found in proteins ... |
162-236 |
2.11e-03 |
|
SXP/RAL-2 family protein Ani s 5-like, metal-binding domain; This domain is found in proteins from nematodes, including SXP/RAL-2 family protein Ani s 5 (ANIS5) from Anisakis simplex, and comprises two conserved motifs: SXP1 and SXP2. Although the function of this domain is not clear, structural information from ANIS5 revealed an alpha helical arrangement with a Calmodulin-like fold. Functional studies indicates that ANIS5 can bind magnesium and calcium, suggesting that this domain plays a role in cation binding. These proteins are interesting targets to develop control strategies against the diseases caused by parasites.
Pssm-ID: 396877 [Multi-domain] Cd Length: 107 Bit Score: 38.72 E-value: 2.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503306 162 ENINLAAKEKQFQELQQKIRMETAIS---KRVQEENANIKEEKLEILSSLQCVQKQLQQI----TQTNVRMESELNALRE 234
Cdd:pfam02520 12 ETLTIAEKEEQLAAWAEKYGVTDQYKefqANVTALKEEVKKNVTAVISNLSSVLNQLSAIldnkNQTRAQQHEAIDALKQ 91
|
..
gi 2024503306 235 EY 236
Cdd:pfam02520 92 QY 93
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
40-322 |
2.28e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 41.88 E-value: 2.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503306 40 KTSLLETIEELRIRRiskhtlQKKLNEMDQKLQMHlTGREEHNKKLNEVERCYATIACQFGIVKGVHEKLEHSVQEAIQ- 118
Cdd:TIGR00618 165 KKELLMNLFPLDQYT------QLALMEFAKKKSLH-GKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQq 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503306 119 -------LNKKLTSVNKRQ--ETEISNLKEELKKVTTDLIRskvtsqHRVGEENINLAAKEKQFQELQQKIrmeTAISKR 189
Cdd:TIGR00618 238 tqqshayLTQKREAQEEQLkkQQLLKQLRARIEELRAQEAV------LEETQERINRARKAAPLAAHIKAV---TQIEQQ 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503306 190 VQEENANIKEEKLEILSSLQCVQKQLQQiTQTNVRMESELNALREEYQTLERDNELQR------EKAKENEEKFLNLQNE 263
Cdd:TIGR00618 309 AQRIHTELQSKMRSRAKLLMKRAAHVKQ-QSSIEEQRRLLQTLHSQEIHIRDAHEVATsireisCQQHTLTQHIHTLQQQ 387
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024503306 264 HEKA---LRIWKKDEENLRREMDTIKNELNSLKKTQGHLDDCHPPQGNQHsEQVENLQIHST 322
Cdd:TIGR00618 388 KTTLtqkLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQ-RYAELCAAAIT 448
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
38-450 |
2.57e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 42.03 E-value: 2.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503306 38 DFKTSLLETIEELRIRRISKHTLQKKLN-EMDQKLQMHLTgreeHNKKLNEVErcyaTIACQFGIVKG--VHEKLEHSVQ 114
Cdd:pfam15921 142 DLRNQLQNTVHELEAAKCLKEDMLEDSNtQIEQLRKMMLS----HEGVLQEIR----SILVDFEEASGkkIYEHDSMSTM 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503306 115 EAIQLNKKLTSVNKRQETEISNLKEELKKVTTDLIRSKVTSQHRVgeeninlaakEKQFQELQQkiRMETAISKR----- 189
Cdd:pfam15921 214 HFRSLGSAISKILRELDTEISYLKGRIFPVEDQLEALKSESQNKI----------ELLLQQHQD--RIEQLISEHeveit 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503306 190 -VQEENANIKEEKLEILSSLQCVQKQLQQITQTNVR----MESELNALREEYqtlerdnelqREKAKENEEKFlnlqNEH 264
Cdd:pfam15921 282 gLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMRqlsdLESTVSQLRSEL----------REAKRMYEDKI----EEL 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503306 265 EKALRIWKKDEENLRREMDTIKNELNSL-KKTQGHLDDCHPPQGNQHSEQVENLQIHS-------TVHPVIRNSGQEQSK 336
Cdd:pfam15921 348 EKQLVLANSELTEARTERDQFSQESGNLdDQLQKLLADLHKREKELSLEKEQNKRLWDrdtgnsiTIDHLRRELDDRNME 427
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503306 337 GSEIQAIQK--KNDCMPSILRKDNN-SGHEDEIEVKNTVSFSL-STEEL------QIEQKLQVLENGFKDEINVASPLEG 406
Cdd:pfam15921 428 VQRLEALLKamKSECQGQMERQMAAiQGKNESLEKVSSLTAQLeSTKEMlrkvveELTAKKMTLESSERTVSDLTASLQE 507
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 2024503306 407 KEREVSPRNTLCTD--TDLITQGQNSEMHVTECKEAENLETTCRVL 450
Cdd:pfam15921 508 KERAIEATNAEITKlrSRVDLKLQELQHLKNEGDHLRNVQTECEAL 553
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
150-270 |
3.76e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.44 E-value: 3.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503306 150 RSKVTSQHRVGEENIN-LAAKEKQFQELQQKIRMETAISKRVQEENANIkEEKLEILSSLQCV----------------- 211
Cdd:COG4913 595 RRRIRSRYVLGFDNRAkLAALEAELAELEEELAEAEERLEALEAELDAL-QERREALQRLAEYswdeidvasaereiael 673
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024503306 212 QKQLQQITQTNV---RMESELNALREEYQTLERDNELQREKAKENEEKFLNLQNEHEKALRI 270
Cdd:COG4913 674 EAELERLDASSDdlaALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDR 735
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
60-255 |
4.13e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.52 E-value: 4.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503306 60 LQKKLNEMDQKLQMHLTGREEHNKKLNEVERCYATIAcqfgivkgvhEKLEHSVQEAIQLNKKLTSVNKRQ---ETEISN 136
Cdd:COG4942 32 LQQEIAELEKELAALKKEEKALLKQLAALERRIAALA----------RRIRALEQELAALEAELAELEKEIaelRAELEA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503306 137 LKEELKKVT---------------------TDLIRSKVTSQHRVGEENINLAAKEKQFQELQQKIRMETAISKRVQEENA 195
Cdd:COG4942 102 QKEELAELLralyrlgrqpplalllspedfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLA 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024503306 196 NIKEEKLEILSSLQCVQKQLQQITQTNVRMESELNALREEYQTLERD-NELQREKAKENEE 255
Cdd:COG4942 182 ELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALiARLEAEAAAAAER 242
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
9-248 |
4.79e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.77 E-value: 4.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503306 9 LKMDEDLKMQALDSALQspsetLLSIRLLDFKTSLLETIEELRIRRIskhtlQKKLNEMDQKLQMHLTGREEHNKKLNEV 88
Cdd:COG3206 162 LEQNLELRREEARKALE-----FLEEQLPELRKELEEAEAALEEFRQ-----KNGLVDLSEEAKLLLQQLSELESQLAEA 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503306 89 ERCYATIacqfgivkgvhEKLEHSVQEAIQLNKKlTSVNKRQETEISNLKEELKKVTTDL--IRSKVTSQHRvgeeninl 166
Cdd:COG3206 232 RAELAEA-----------EARLAALRAQLGSGPD-ALPELLQSPVIQQLRAQLAELEAELaeLSARYTPNHP-------- 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503306 167 aakekQFQELQQKIR-METAISKRVQEENANIKEEKLEILSSLQCVQKQLQQITQTNvrmeSELNALREEYQTLERDNEL 245
Cdd:COG3206 292 -----DVIALRAQIAaLRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARL----AELPELEAELRRLEREVEV 362
|
...
gi 2024503306 246 QRE 248
Cdd:COG3206 363 ARE 365
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
114-300 |
5.03e-03 |
|
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: 40.86 E-value: 5.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503306 114 QEAIQLNKK-----LTSVNKRQETEIsNLKEELKKVTTDLI--RSKVTSQHRVGEENINLAAKEKQFQELQQKIRMETAI 186
Cdd:pfam05483 519 QEDIINCKKqeermLKQIENLEEKEM-NLRDELESVREEFIqkGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCN 597
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503306 187 SKRVQEENANIKEEKLeilsslqcvQKQLQQITQTNVRMESELNALREEYQTLErdneLQREKAKEneeKFLNLQNEHEK 266
Cdd:pfam05483 598 NLKKQIENKNKNIEEL---------HQENKALKKKGSAENKQLNAYEIKVNKLE----LELASAKQ---KFEEIIDNYQK 661
|
170 180 190
....*....|....*....|....*....|....
gi 2024503306 267 ALRIWKKDEENLRREMDTIKNELNSLKKTQGHLD 300
Cdd:pfam05483 662 EIEDKKISEEKLLEEVEKAKAIADEAVKLQKEID 695
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
118-289 |
5.03e-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: 39.91 E-value: 5.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503306 118 QLNKKLTSVNKRQET---EISNLKEELKKVTTDLIRSKVtsqhRVGEENINLAAKEKQFQELQQKIrmetaisKRVQEEN 194
Cdd:COG1579 14 ELDSELDRLEHRLKElpaELAELEDELAALEARLEAAKT----ELEDLEKEIKRLELEIEEVEARI-------KKYEEQL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503306 195 ANIKEEKleilsSLQCVQKQLQQITQTNVRMESELNALREEYQTLERDNELQREKAKENEEKFLNLQNEHEKALRIWKKD 274
Cdd:COG1579 83 GNVRNNK-----EYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAE 157
|
170
....*....|....*
gi 2024503306 275 EENLRREMDTIKNEL 289
Cdd:COG1579 158 LEELEAEREELAAKI 172
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
185-348 |
5.25e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 40.58 E-value: 5.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503306 185 AISKR-------VQEENANIKEEKLEI---LSSLQCVQKQLQQITQtnvrmesELNALREEYQTLERDNELQREKAKENE 254
Cdd:PRK00409 492 EIAKRlglpeniIEEAKKLIGEDKEKLnelIASLEELERELEQKAE-------EAEALLKEAEKLKEELEEKKEKLQEEE 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503306 255 EKFL-NLQNEHEKALRIWKKDEENLRREMDTIKNELNS------LKKTQGHLDDCHPP---QGNQHSEQVENLQIHSTVH 324
Cdd:PRK00409 565 DKLLeEAEKEAQQAIKEAKKEADEIIKELRQLQKGGYAsvkaheLIEARKRLNKANEKkekKKKKQKEKQEELKVGDEVK 644
|
170 180
....*....|....*....|....
gi 2024503306 325 pvIRNSGQeqsKGsEIQAIQKKND 348
Cdd:PRK00409 645 --YLSLGQ---KG-EVLSIPDDKE 662
|
|
| BLOC1_2 |
pfam10046 |
Biogenesis of lysosome-related organelles complex-1 subunit 2; Members of this family of ... |
225-300 |
5.57e-03 |
|
Biogenesis of lysosome-related organelles complex-1 subunit 2; Members of this family of proteins play a role in cellular proliferation, as well as in the biogenesis of specialized organelles of the endosomal-lysosomal system.
Pssm-ID: 462951 [Multi-domain] Cd Length: 96 Bit Score: 37.18 E-value: 5.57e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024503306 225 MESELNALREEYQTLERDNELQREKAKENEEKFLNLQNEHEKalrIWKKDEE--NLRREMDTIKNELNSLKKTQGHLD 300
Cdd:pfam10046 11 LEAELEATVEDYKLLEKMNEATSLKYKDMKDVAASLEKELEE---LNQKYEElqPYLQQIDQIEEQVTKLEETVYELD 85
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
4-300 |
7.00e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 40.34 E-value: 7.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503306 4 KDRQVLKMDEDLKMQALDSALQSPSETLLSIrLLDFKTSLLETIEELRIRRISKHTLQKKLNEMDQKLQMHLTGR---EE 80
Cdd:TIGR00618 562 KEQMQEIQQSFSILTQCDNRSKEDIPNLQNI-TVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQqcsQE 640
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503306 81 HNKKLNEVERCYATIAcqfgivkgvHEKLEHSVQEAIQLNKKLTSVNKRQETEISNLKEELK--KVTTDLIRSKVTSQHR 158
Cdd:TIGR00618 641 LALKLTALHALQLTLT---------QERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTywKEMLAQCQTLLRELET 711
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503306 159 VGEENinlaakEKQFQELQQKirMETAISKRVQEENA-NIKEEKLEILSSLQCvqKQLQQITQTNVRMESELNALREEYQ 237
Cdd:TIGR00618 712 HIEEY------DREFNEIENA--SSSLGSDLAAREDAlNQSLKELMHQARTVL--KARTEAHFNNNEEVTAALQTGAELS 781
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024503306 238 TLERDNELQREKAKENEEKFLNLQNEHEKALR----IWKKDEENLRREMDTIKNELNSLKKTQGHLD 300
Cdd:TIGR00618 782 HLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPsdedILNLQCETLVQEEEQFLSRLEEKSATLGEIT 848
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
58-301 |
7.48e-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: 40.42 E-value: 7.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503306 58 HTLQKKLNEMDQKL-QMHLTGREEHNkklNEVERCYATIACQFGIVKG--------VHEKLEHSV-QEAIQLNKKLTSVN 127
Cdd:TIGR01612 970 NTLIDKINELDKAFkDASLNDYEAKN---NELIKYFNDLKANLGKNKEnmlyhqfdEKEKATNDIeQKIEDANKNIPNIE 1046
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503306 128 KRQETEISNLKEELKKVTTDLIRSKVTSQHRVGEENINlaakekQFQELQQKIRMETaISKRVQEENANIKEE----KLE 203
Cdd:TIGR01612 1047 IAIHTSIYNIIDEIEKEIGKNIELLNKEILEEAEINIT------NFNEIKEKLKHYN-FDDFGKEENIKYADEinkiKDD 1119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503306 204 ILSSLQCVQKQLQQITQTNVRMESELNALREEYQTLER--DNELQREKAKENEEKFLNLQNEHEKalriwkkdEENLRRE 281
Cdd:TIGR01612 1120 IKNLDQKIDHHIKALEEIKKKSENYIDEIKAQINDLEDvaDKAISNDDPEEIEKKIENIVTKIDK--------KKNIYDE 1191
|
250 260
....*....|....*....|
gi 2024503306 282 MDTIKNELNSLKKTQGHLDD 301
Cdd:TIGR01612 1192 IKKLLNEIAEIEKDKTSLEE 1211
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
107-288 |
8.99e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 39.50 E-value: 8.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503306 107 EKLEHSVQEAIQLNKKLtsvnKRQETEISNLKEELKKVTTDL--IRSKVTS-QHRVGEENINLAAKEKQFQELQQKIRME 183
Cdd:COG4372 38 FELDKLQEELEQLREEL----EQAREELEQLEEELEQARSELeqLEEELEElNEQLQAAQAELAQAQEELESLQEEAEEL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503306 184 TAISKRVQEENANIKEEKLEILSSLQCVQKQLQQITQTNVRMESELNALREEYQTLERdnELQREKAKENEEKFLNLQNE 263
Cdd:COG4372 114 QEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQ--ELQALSEAEAEQALDELLKE 191
|
170 180
....*....|....*....|....*
gi 2024503306 264 HEKALRIWKKDEENLRREMDTIKNE 288
Cdd:COG4372 192 ANRNAEKEEELAEAEKLIESLPREL 216
|
|
| |
