|
Name |
Accession |
Description |
Interval |
E-value |
| CCDC73 |
pfam15818 |
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil ... |
35-1095 |
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: 1014.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 35 RLLDFKTSLLETIEELRIRRETEINYEEQLSKIVVEKQELEWQKETLQHQTDTLQQQNKEAMAAFKKQLQARMFAMEEEK 114
Cdd:pfam15818 1 QLLDFKTSLLEALEELRMRREAETQYEEQIGKIIVETQELKWQKETLQNQKETLAKQHKEAMAVFKKQLQMKMCALEEEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 115 GKYQLAVEIKEKEIDGLKETLKELQISKHTLQKKLNEMDQKLQMHLTGREEHNKKLNEVERCYATIACQFGIVKGVHEKL 194
Cdd:pfam15818 81 GKYQLATEIKEKEIEGLKETLKALQVSKYSLQKKVSEMEQKLQLHLLAKEDHHKQLNEIEKYYATITGQFGLVKENHGKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 195 EHSVQEAIQLNKKLTSVNKRQETEISNLKEELKKVTTDLIRSKVTSQHRVGEENINLAAKEKQFQELQQKIRMETAISKR 274
Cdd:pfam15818 161 EQNVQEAIQLNKRLSALNKKQESEICSLKKELKKVTSDLIKSKVTCQYKMGEENINLTIKEQKFQELQERLNMELELNKK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 275 VQEENANIKEEKLEILSSLQCVQKQLQQITQTNVRMESELNALREEYQTLERDNELQREKAKENEEKFLNLQNEHEKALR 354
Cdd:pfam15818 241 INEEITHIQEEKQDIIISFQHMQQLLQQQTQANTEMEAELKALKENNQTLERDNELQREKVKENEEKFLNLQNEHEKALG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 355 IWKKDEENLRREMDTIKNELNSLKKTQGHLDDCHPPQGNQ----HSEQVENLQIHSTVHpvirnsGQEQSKGSEIQAIQK 430
Cdd:pfam15818 321 TWKKHVEELNGEINEIKNELSSLKETHIKLQEHYNKLCNQkkfeEDKKFQNVPEVNNEN------SEMSTEKSENLIIQK 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 431 KNDcmpsilrkdnnsghEDEIEVKNTVSFSLSTEELQIEQK------------LQVLENGFKDEINVASPLEGKEREVSP 498
Cdd:pfam15818 395 YNS--------------EQEIREENTKSFCSDTEYRETEKKkgppveeiiiedLQVLEKSFKNEIDTSVPQDKNQSEISL 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 499 RNTLCTDTDLITQGQNseMHVTECKEAENLETTCRVLLEGNSANLQQKLQDSTGPAAPHHTETSKVLLDAADRVIVSDKN 578
Cdd:pfam15818 461 SKTLCTDKDLISQGQT--LNVTDFRKSVTTEIKDKLCLEKDNGCSEFKSPNNLFLVADQSIETEKIHLESTEGLGLHHAD 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 579 AIQEMNSSNQELCSTTHESICTKvdknssiiELNSSVLTTKASKKESEAAVCTEKSAVCERNTDNHQVSEFHFGILSYPK 658
Cdd:pfam15818 539 IHLETESNRSSFNGTLNEMAHNT--------NHNKDVSENEPFKQQFRLLLCTQENATEKRITNSDQTKAGLDSSLDVKK 610
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 659 ENCQtgYQKCSLLNSDN-NVDNRLCRIERslLNLSDLPRDKFPFKQTHIDAEDKNYNDNAA--NINRSGALRHIGFPpmd 735
Cdd:pfam15818 611 NPVQ--CQKYSLQDSSNvSLDDKQCKIEQ--LLNKKSECSTLPLKQTSSFQQLCNDTSEKPglTIPCDTVVSHPISP--- 683
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 736 aqnvlAIYCDNASTD-KAAKEQSSNMPFTGTYNLCPEKINKGINVDDVHSKQPE-HDSTEQSGGDESMCTLNAEAMSPVK 813
Cdd:pfam15818 684 -----AAFSDNLKADlKNSDNNVNIMPMLVKPNSSPGKRTTRKNLDDMQSSQFKnCLGGLENGVTISHLQVNNENSHASQ 758
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 814 AHDLDTTVQKVPADGIDVDKL----NEEIQIQSIKNEHSLDINDDSINNSMLK--QEKDSVHSTVPGRKFAEGHLKESCS 887
Cdd:pfam15818 759 AKDLKTAVHPKTSTEIQFSSKesqiDENQITEATKNDLFLLVNVNERQHTLLNntEKTESLNDIVSGKIYSEGQLEESHS 838
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 888 LPMRTSGNLVNASGRSSFDLSNSDKKAEKTSVCFKFLGLSSCSRVNQMRSQATWTSSSQEPSVLKEKLPCLVENKKVPSR 967
Cdd:pfam15818 839 FHIKPSGDLVNRSGRSAFDLSTSDKKTEKTPVYLNFLDPSPWSKVNQTEGQTVSTSTSSIPLLLKEKPIGPSENTKIISV 918
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 968 ELFQNVSENVGRKETGPGSTSSNRAADTLNTSRIHRDPQGDPTEEWNAIAKTFYDSSFPTEHVKEGFTALNEQKSSPMTV 1047
Cdd:pfam15818 919 TLCKNVGVDDVRKDIGPDTTSISRVADTLNNSSIHPDPKGEPSEERNATAKTFYDSSFPTEHVKTEPLKSTVLQSHFQTV 998
|
1050 1060 1070 1080
....*....|....*....|....*....|....*....|....*...
gi 2024503276 1048 TSAQSERTLGDEDRFPTHNSTVQSQIEEIEKYLNLETLCSSRKRKYED 1095
Cdd:pfam15818 999 KIKDSPDLLKSSPGEDDWQSLITNQITEIEKLLSLENDNQPKKRKAEE 1046
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
54-377 |
1.24e-11 |
|
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: 69.32 E-value: 1.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 54 RETEI-NYEEQLSKIVVEKQELEWQKETLQHQTDTLQQQNKEAMAAfKKQLQARMFAMEEEKGKYQLAVEIKEKEIDGLK 132
Cdd:TIGR02168 675 RRREIeELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKE-LEELSRQISALRKDLARLEAEVEQLEERIAQLS 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 133 ETLKELQISKHTLQKKLNEMDQKLQMHLTGREEHNKKLNEVERCYATIACQFGIVKGVHEKLEHSVQEAIQLNKKLTSVN 212
Cdd:TIGR02168 754 KELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRI 833
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 213 KRQETEISNLKEELKKVTTDLIRSkvtsQHRVGEENINLAAKEKQFQELQQKirmetaisKRVQEENANIKEEKLEILSs 292
Cdd:TIGR02168 834 AATERRLEDLEEQIEELSEDIESL----AAEIEELEELIEELESELEALLNE--------RASLEEALALLRSELEELS- 900
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 293 lqcvqKQLQQITQTNVRMESELNALREEYQTLERD-----NELQREKAKENEEKFLNLQNEHEKALRIwKKDEENLRREM 367
Cdd:TIGR02168 901 -----EELRELESKRSELRRELEELREKLAQLELRlegleVRIDNLQERLSEEYSLTLEEAEALENKI-EDDEEEARRRL 974
|
330
....*....|
gi 2024503276 368 DTIKNELNSL 377
Cdd:TIGR02168 975 KRLENKIKEL 984
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
15-341 |
7.54e-11 |
|
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: 66.63 E-value: 7.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 15 LKMQALDSALQSPSETLLSIRLLDFKTSLLETIEELRiRRETEIN--------YEEQLSKIVVEKQELEWQKETLQHQTD 86
Cdd:TIGR02169 662 PRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELR-RIENRLDelsqelsdASRKIGEIEKEIEQLEQEEEKLKERLE 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 87 TLQ------QQNKEAMAAFKKQLQARMFAMEEEKGKYQLAVE------------IKEKEIDGLKETLKELQISKHTLQKK 148
Cdd:TIGR02169 741 ELEedlsslEQEIENVKSELKELEARIEELEEDLHKLEEALNdlearlshsripEIQAELSKLEEEVSRIEARLREIEQK 820
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 149 LNEMDQKLQMhltGREEHNKKLNEVERCYATIAcqfgivkgvheklehSVQEAIQLNK----KLTSVNKRQETEISNLKE 224
Cdd:TIGR02169 821 LNRLTLEKEY---LEKEIQELQEQRIDLKEQIK---------------SIEKEIENLNgkkeELEEELEELEAALRDLES 882
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 225 ELKKVTTDliRSKVTSQHRVGEENINLAAKEKQFQELQQKIRMETAisKRVQEENANIKEEKLEILS------SLQCVQK 298
Cdd:TIGR02169 883 RLGDLKKE--RDELEAQLRELERKIEELEAQIEKKRKRLSELKAKL--EALEEELSEIEDPKGEDEEipeeelSLEDVQA 958
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 2024503276 299 QLQQITQTNVRMESELNALREEYQ-TLERDNELQREKAKENEEK 341
Cdd:TIGR02169 959 ELQRVEEEIRALEPVNMLAIQEYEeVLKRLDELKEKRAKLEEER 1002
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
72-378 |
8.70e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 66.50 E-value: 8.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 72 QELEWQKETLQHQ----------TDTLQQQNKEAMAAFKKQLQARMFAMEEEKGKYQLAVEIKEKEIDGLKETLKELQIS 141
Cdd:COG1196 196 GELERQLEPLERQaekaeryrelKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLE 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 142 KHTLQKKLNEMDQKLQMHLTGREEHNKKLNEVErcyatiacqfgivkgvhEKLEHSVQEAIQLNKKLtsvnKRQETEISN 221
Cdd:COG1196 276 LEELELELEEAQAEEYELLAELARLEQDIARLE-----------------ERRRELEERLEELEEEL----AELEEELEE 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 222 LKEELKKVTTDLIRskvtSQHRVGEENINLAAKEKQFQELQQKIRMETAISKRVQEENANIKEEKLEILSSLQCVQKQLQ 301
Cdd:COG1196 335 LEEELEELEEELEE----AEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEE 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 302 QITQTNVRMESELNALREEYQTLERDNELQREKAKENEEKFLNLQNEHEKALRI---WKKDEENLRREMDTIKNELNSLK 378
Cdd:COG1196 411 ALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELlaeLLEEAALLEAALAELLEELAEAA 490
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
43-379 |
2.83e-10 |
|
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: 64.70 E-value: 2.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 43 LLETIEELRIRRETEINYEEQLSkivvEKQELEWqketlqhqtdTLQQQNKEAMAAFKKQLQARMFAMEEEKGKYQLAVE 122
Cdd:TIGR02169 196 KRQQLERLRREREKAERYQALLK----EKREYEG----------YELLKEKEALERQKEAIERQLASLEEELEKLTEEIS 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 123 IKEKEIDGLKETLKEL--QISKHT------LQKKLNEMDQKLQMHLTGREEHNKKLNEVERCYATIACQFGIVKGVHEKL 194
Cdd:TIGR02169 262 ELEKRLEEIEQLLEELnkKIKDLGeeeqlrVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEEL 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 195 EHSVQEaiqLNKKLTSVnkrqETEISNLKEELkkvttDLIRSKvtsqhrvgeeninLAAKEKQFQELQQKirmetaiSKR 274
Cdd:TIGR02169 342 EREIEE---ERKRRDKL----TEEYAELKEEL-----EDLRAE-------------LEEVDKEFAETRDE-------LKD 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 275 VQEENANIKEEKLEILSSLQCVQKQLQQITQTNVRMESELNALREEYQTLERDNELQREKAKENEEKFLNLQNEHEKAlr 354
Cdd:TIGR02169 390 YREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKY-- 467
|
330 340
....*....|....*....|....*
gi 2024503276 355 iwKKDEENLRREMDTIKNELNSLKK 379
Cdd:TIGR02169 468 --EQELYDLKEEYDRVEKELSKLQR 490
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
112-386 |
1.14e-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: 59.70 E-value: 1.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 112 EEKGKYQLAVEIKEKEIDGLKETLKELQISKHT------LQKKLNEMDQKLqmHLTGREEHNKKLNEVERCYATIACQfg 185
Cdd:TIGR02169 177 EELEEVEENIERLDLIIDEKRQQLERLRREREKaeryqaLLKEKREYEGYE--LLKEKEALERQKEAIERQLASLEEE-- 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 186 iVKGVHEKLEHSVQEAIQLNKKLTSVNKR----QETEISNLKEELKKVTTDLIRSKVtsqhrvgeeniNLAAKEKQFQEL 261
Cdd:TIGR02169 253 -LEKLTEEISELEKRLEEIEQLLEELNKKikdlGEEEQLRVKEKIGELEAEIASLER-----------SIAEKERELEDA 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 262 QQKIRmetaiskRVQEENANIKEEKLEILSSLQCVQKQLQQITQTNVRMESELNALREEYQTLERDNELQREKAKENEEK 341
Cdd:TIGR02169 321 EERLA-------KLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREK 393
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 2024503276 342 FLNLQNEHEKALRIWKKDEENLRR---EMDTIKNELNSLKKTQGHLDD 386
Cdd:TIGR02169 394 LEKLKREINELKRELDRLQEELQRlseELADLNAAIAGIEAKINELEE 441
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
31-358 |
2.95e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.02 E-value: 2.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 31 LLSIRLLDFKTSLLETIEELRIRRETEINYEEQLSKIVVEKQELewqKETLQHQTDTLQqqnkeamaafkkQLQARMFAM 110
Cdd:COG1196 229 LLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEEL---RLELEELELELE------------EAQAEEYEL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 111 EEEkgkyqlaVEIKEKEIDGLKETLKELQISKHTLQKKLNEMDQKLQMHLTGREEHNKKLNEVErcyatiacqfgivkgv 190
Cdd:COG1196 294 LAE-------LARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAE---------------- 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 191 hEKLEHSVQEAIQLNKKLTSVNKRQETEISNLKEELkkvttdliRSKVTSQHRVGEENINLAAKEKQFQELQQKIRMETA 270
Cdd:COG1196 351 -EELEEAEAELAEAEEALLEAEAELAEAEEELEELA--------EELLEALRAAAELAAQLEELEEAEEALLERLERLEE 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 271 ISKRVQEENANIKEEKLEILSSLQCVQKQLQQITQTNVRMESELNALREEYQTLER---DNELQREKAKENEEKFLNLQN 347
Cdd:COG1196 422 ELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAalaELLEELAEAAARLLLLLEAEA 501
|
330
....*....|.
gi 2024503276 348 EHEKALRIWKK 358
Cdd:COG1196 502 DYEGFLEGVKA 512
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
23-336 |
1.26e-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: 56.22 E-value: 1.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 23 ALQSPSETLLSIRLLDFKTSLLETIEELRIRRETEINYEEQLSKIVVEKQELEWQKETLQHQTDTLQQQNKEAMA----- 97
Cdd:TIGR02168 687 EELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAeieel 766
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 98 -AFKKQLQARMFAMEEEKGKYQLAVEIKEKEIDGLKETLKELQISKHTLQKKLNEMDQKLQMHLTGREEHNKKLNEVERC 176
Cdd:TIGR02168 767 eERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQ 846
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 177 YATIACQFGIVKGVHEKLEHSVQEAIQLNKKLTSVNKRQETEISNLKEELKKVTTDL--IRSKVT--------SQHRVGE 246
Cdd:TIGR02168 847 IEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELreLESKRSelrreleeLREKLAQ 926
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 247 ENINLAAKEKQFQELQQKIRMETAISKRVQEENANIKEEKLEIL-SSLQCVQKQLQQITQTNVRMESELNALREEYQTLE 325
Cdd:TIGR02168 927 LELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEArRRLKRLENKIKELGPVNLAAIEEYEELKERYDFLT 1006
|
330
....*....|..
gi 2024503276 326 R-DNELQREKAK 336
Cdd:TIGR02168 1007 AqKEDLTEAKET 1018
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
116-381 |
1.26e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.10 E-value: 1.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 116 KYQ-LAVEIKEKEIDGLKETLKELQISKHTLQKKLNEMDQKLQMHLTGREEHNKKLNEVERcyatiacqfgivkgVHEKL 194
Cdd:COG1196 214 RYReLKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRL--------------ELEEL 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 195 EHSVQEAIQLNKKLTSVNKRQETEISNLKEELKkvttdlirskvtsqhrvgEENINLAAKEKQFQELQQKIRMETAISKR 274
Cdd:COG1196 280 ELELEEAQAEEYELLAELARLEQDIARLEERRR------------------ELEERLEELEEELAELEEELEELEEELEE 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 275 VQEENANIKEEKLEILSSLQCVQKQLQQITQTNVRMESELNALREEYQTLERDNELQREKAKENEEKFLNLQNEHEKALR 354
Cdd:COG1196 342 LEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEE 421
|
250 260
....*....|....*....|....*..
gi 2024503276 355 IWKKDEENLRREMDTIKNELNSLKKTQ 381
Cdd:COG1196 422 ELEELEEALAELEEEEEEEEEALEEAA 448
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
16-288 |
1.44e-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: 55.83 E-value: 1.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 16 KMQALDSALQSPSETLLSIRLLDFKTSL---LETIEELRIRRE---TEIN-YEEQLSKIVVEKQELEWQKETLQHQTDTL 88
Cdd:TIGR02168 214 RYKELKAELRELELALLVLRLEELREELeelQEELKEAEEELEeltAELQeLEEKLEELRLEVSELEEEIEELQKELYAL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 89 QQ------QNKEAMAAFKKQLQARMFAMEEEKGKYQLAVEIKEKEIDGLKETLKELQISKHTLQKKLNEMDQKLQMHLTG 162
Cdd:TIGR02168 294 ANeisrleQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESR 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 163 REEHNKKLNEVERCYA-------TIACQFGIVKGVHEKLEHSV----QEAIQLNKKLTSVN-KRQETEISNLKEELKKVT 230
Cdd:TIGR02168 374 LEELEEQLETLRSKVAqlelqiaSLNNEIERLEARLERLEDRRerlqQEIEELLKKLEEAElKELQAELEELEEELEELQ 453
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024503276 231 T---DLIRSKVTSQHRVGEENINLAAKEKQFQELQQKIRMETAISKRVQEENANIKEEKLE 288
Cdd:TIGR02168 454 EeleRLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKN 514
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
40-384 |
2.76e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.07 E-value: 2.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 40 KTSLLETIEELRIRRETEINYEEQLSKIVVEKQELEWQKE---TLQHQTDTLqQQNKEAMAAFKKQLQARMFAME----- 111
Cdd:PRK03918 199 EKELEEVLREINEISSELPELREELEKLEKEVKELEELKEeieELEKELESL-EGSKRKLEEKIRELEERIEELKkeiee 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 112 -EEKGKYQLAVEIKEKEIDGLKETLKELQISKHTLQKKLNEMDQK---LQMHLTGREEHNKKLNEVERCYATIACQFGIV 187
Cdd:PRK03918 278 lEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEingIEERIKELEEKEERLEELKKKLKELEKRLEEL 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 188 KGVHEKLEHSVQ---EAIQLNKKLTSVN----KRQETEISNLKEELKKVTTDLIRSKVTSQHRVGEENINLAAKEKQ--- 257
Cdd:PRK03918 358 EERHELYEEAKAkkeELERLKKRLTGLTpeklEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAkgk 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 258 ----FQELQQKIRMEtaISKRVQEENANIKEEKLEILSSLQCVQKQLQQItQTNVRMESELNALREEYQTL----ERDNE 329
Cdd:PRK03918 438 cpvcGRELTEEHRKE--LLEEYTAELKRIEKELKEIEEKERKLRKELREL-EKVLKKESELIKLKELAEQLkeleEKLKK 514
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024503276 330 LQREKAKENEEKFLNLQ---NEHEKALRIWKKD---EENLRREMDTIKNELNSLKKTQGHL 384
Cdd:PRK03918 515 YNLEELEKKAEEYEKLKeklIKLKGEIKSLKKElekLEELKKKLAELEKKLDELEEELAEL 575
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
213-386 |
5.38e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.17 E-value: 5.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 213 KRQETEISNLKEELKKVTTDLIRSKVTSQH---RVGEENINLAAKEKQFQELQQKIRMETAISKRVQEENANIKEEKLEI 289
Cdd:COG1196 235 RELEAELEELEAELEELEAELEELEAELAEleaELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRREL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 290 LSSLQCVQKQLQQITQTNVRMESELNALREEYQTLERDNELQREKAKENEEKFLNLQNEHEKALRIWKKDEENLRREMDT 369
Cdd:COG1196 315 EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRA 394
|
170
....*....|....*..
gi 2024503276 370 IKNELNSLKKTQGHLDD 386
Cdd:COG1196 395 AAELAAQLEELEEAEEA 411
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
16-379 |
1.33e-06 |
|
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: 52.81 E-value: 1.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 16 KMQALDSALQSPSETLLSirlldfktSLLETIEELRIRRETEInyeeqlSKIVVEKQELEWQKETLQHQTDTLQQQNKEA 95
Cdd:pfam15921 246 QLEALKSESQNKIELLLQ--------QHQDRIEQLISEHEVEI------TGLTEKASSARSQANSIQSQLEIIQEQARNQ 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 96 MAAFKKQL--------QARMfAMEEEKGKYQLAVEIKEKEIDGLKETLKELQISKHTLQKKLNEMDQKLQ-----MH--- 159
Cdd:pfam15921 312 NSMYMRQLsdlestvsQLRS-ELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQklladLHkre 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 160 --LTGREEHNKKL----------------------NEVERCYATIACQFGIVKGVHEKLEHSVQEAIQLNKKLTSVNKRQ 215
Cdd:pfam15921 391 keLSLEKEQNKRLwdrdtgnsitidhlrrelddrnMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQL 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 216 ETEisnlKEELKKVTTDLIRSKVT---SQHRVGEENINLAAKEK------------------QFQELQQkIRMETAISKR 274
Cdd:pfam15921 471 EST----KEMLRKVVEELTAKKMTlesSERTVSDLTASLQEKERaieatnaeitklrsrvdlKLQELQH-LKNEGDHLRN 545
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 275 VQEENANIKEEKLEILSSLQCVQKQLQQITQ--------------TNVRMESELNALREEYQTLERDNELQREKAKENEE 340
Cdd:pfam15921 546 VQTECEALKLQMAEKDKVIEILRQQIENMTQlvgqhgrtagamqvEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEA 625
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 2024503276 341 ----------KFLNLQNEHEKALRIWKKDEENLRREMDTIKNELNSLKK 379
Cdd:pfam15921 626 rvsdlelekvKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSE 674
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
142-429 |
1.71e-06 |
|
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: 52.37 E-value: 1.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 142 KHTLQKKLNEMDQKLQMHLTGREEHNKKLNEVERcYATIACQFgivKGVHEKLEH-----SVQEAIQLNKKLTSVN---K 213
Cdd:TIGR02168 174 RKETERKLERTRENLDRLEDILNELERQLKSLER-QAEKAERY---KELKAELRElelalLVLRLEELREELEELQeelK 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 214 RQETEISNLKEELKKVTTDL--IRSKVTS--------QHRVGEENINLAAKEKQFQELQQKIRMETAISKRVQEENANIK 283
Cdd:TIGR02168 250 EAEEELEELTAELQELEEKLeeLRLEVSEleeeieelQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELE 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 284 EEKLEILSSLQCVQKQLQQITQTNVRMESELNALREEYQTLERDNELQREKAKENEEKFLNLQNEHEKAlriwKKDEENL 363
Cdd:TIGR02168 330 SKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASL----NNEIERL 405
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024503276 364 RREMDTIKNELNSLKKTQ-GHLDDCHPPQGNQHSEQVENL--QIHSTVHPVIRNSGQEQSKGSEIQAIQ 429
Cdd:TIGR02168 406 EARLERLEDRRERLQQEIeELLKKLEEAELKELQAELEELeeELEELQEELERLEEALEELREELEEAE 474
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
5-383 |
4.77e-06 |
|
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: 50.89 E-value: 4.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 5 DRQVLKMDEDLKMQALDSALQSPSETllsiRLLDFKTSLLETIEELRiRRETEINYEEQLSKIVVEKQELEWQKEtLQHQ 84
Cdd:pfam15921 376 DDQLQKLLADLHKREKELSLEKEQNK----RLWDRDTGNSITIDHLR-RELDDRNMEVQRLEALLKAMKSECQGQ-MERQ 449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 85 TDTLQQQNK--EAMAAFKKQLQAR---MFAMEEEKGKYQLAVEIKEKEIDGLKETLKE----LQISKHTLQKKLNEMDQK 155
Cdd:pfam15921 450 MAAIQGKNEslEKVSSLTAQLESTkemLRKVVEELTAKKMTLESSERTVSDLTASLQEkeraIEATNAEITKLRSRVDLK 529
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 156 LQ--MHLTGREEHnkkLNEVERCYATIACQFGIVKGVHEKLEHSVQEAIQLNKKLTSVNKRQETEISNLKEELKKVTTDL 233
Cdd:pfam15921 530 LQelQHLKNEGDH---LRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLEL 606
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 234 IRSKVTSQhrvgEENINLAAKEKQFQELQ-QKIRMETAISKRVQEENaNIKEEKLEILSSLQCVQkqlqqitqtnvrmeS 312
Cdd:pfam15921 607 QEFKILKD----KKDAKIRELEARVSDLElEKVKLVNAGSERLRAVK-DIKQERDQLLNEVKTSR--------------N 667
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024503276 313 ELNALREEYQTLERDnelqrekakeneekFLNLQNEHEKALRIWKKDEENLRREMDTIKNELNSLKKTQGH 383
Cdd:pfam15921 668 ELNSLSEDYEVLKRN--------------FRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGH 724
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
61-280 |
1.69e-05 |
|
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: 48.61 E-value: 1.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 61 EEQLSKIVVEKQELEWQKETLQHQTDTLQQQnkeamaafKKQLQARMFAMEEEKGKYQLAVEIKEKEIDGLKETLKELQI 140
Cdd:COG4942 26 EAELEQLQQEIAELEKELAALKKEEKALLKQ--------LAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 141 SKHTLQKKLNEMDQKLQMHltGREE------HNKKLNEVERCYATIACQFGIVKGVHEKLEHSVQEAIQLNKKLTSVNKR 214
Cdd:COG4942 98 ELEAQKEELAELLRALYRL--GRQPplalllSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 215 QETEISNLKEELKKVTTDLIRSKVTS---QHRVGEENINLAAKEKQFQELQQKI-RMETAISKRVQEENA 280
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLarlEKELAELAAELAELQQEAEELEALIaRLEAEAAAAAERTPA 245
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
37-385 |
1.72e-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: 48.95 E-value: 1.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 37 LDFKTSLLETIEELRIRRETEInyeEQLSKIVVEKQELEWQKETLQHQTDTLQQQNKEAMAAfkkqLQARmfameeekgk 116
Cdd:pfam05483 386 LQKKSSELEEMTKFKNNKEVEL---EELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFL----LQAR---------- 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 117 yqlaveikEKEIDGLKETLKELQISKHTLQKKLNEMDQKLQmhltgreehNKKLNEVERCYATIACQFGIVKGVHEKLEH 196
Cdd:pfam05483 449 --------EKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELE---------KEKLKNIELTAHCDKLLLENKELTQEASDM 511
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 197 SV-----QEAIQLNKK-----LTSVNKRQETEIsNLKEELKKVTTDLI--RSKVTSQHRVGEENINLAAKEKQFQELQQK 264
Cdd:pfam05483 512 TLelkkhQEDIINCKKqeermLKQIENLEEKEM-NLRDELESVREEFIqkGDEVKCKLDKSEENARSIEYEVLKKEKQMK 590
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 265 IRMETAISKRVQEENANIKEEKLeilsslqcvQKQLQQITQTNVRMESELNALREEYQTLErdneLQREKAKEneeKFLN 344
Cdd:pfam05483 591 ILENKCNNLKKQIENKNKNIEEL---------HQENKALKKKGSAENKQLNAYEIKVNKLE----LELASAKQ---KFEE 654
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 2024503276 345 LQNEHEKALRIWKKDEENLRREMDTIKNELNSLKKTQGHLD 385
Cdd:pfam05483 655 IIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEID 695
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
45-386 |
2.93e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.14 E-value: 2.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 45 ETIEELRIRRETEINYEEQLSKIVVEKQELEWQKETLQHQTDTLQQQNKEaMAAFKKQLQARMFAMEEEKGKYQLAVEIK 124
Cdd:PRK03918 304 EYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKR-LEELEERHELYEEAKAKKEELERLKKRLT 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 125 EKEIDGLKETLKELQISKHTLQKKLNEMDQKLQMHLTGREEHNKKLNEVERCYATI-ACQFGIVKGVHEKLEHSVQEAIq 203
Cdd:PRK03918 383 GLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCpVCGRELTEEHRKELLEEYTAEL- 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 204 lnKKLTSVNKRQETEISNLKEELKKVTTDLIR-SKVTSQHRVGEENINLAAKEKQF--QELQQKirmetaiskrvQEENA 280
Cdd:PRK03918 462 --KRIEKELKEIEEKERKLRKELRELEKVLKKeSELIKLKELAEQLKELEEKLKKYnlEELEKK-----------AEEYE 528
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 281 NIKEEKLEILSSLQCVQKQLqqitqtnvrmeSELNALREEYQTLERD-NELQREKA--------------KENEEKFLNL 345
Cdd:PRK03918 529 KLKEKLIKLKGEIKSLKKEL-----------EKLEELKKKLAELEKKlDELEEELAellkeleelgfesvEELEERLKEL 597
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 2024503276 346 QNEHEKALRIwKKDEENLRREMDTIKNELNSLKKTQGHLDD 386
Cdd:PRK03918 598 EPFYNEYLEL-KDAEKELEREEKELKKLEEELDKAFEELAE 637
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
125-354 |
3.09e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.52 E-value: 3.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 125 EKEIDGLKETLKELQISKHTLQKKLNEMDQKLqmhltgrEEHNKKLNEVErcyatiacqfgivkgvhEKLEHSVQEAIQL 204
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAEL-------EELNEEYNELQ-----------------AELEALQAEIDKL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 205 NKKLTsvnkRQETEISNLKEELKKvttdLIRSKVTSQHRVGEENINLAAKEkqFQELQQKIRMETAISKRVQEENANIKE 284
Cdd:COG3883 71 QAEIA----EAEAEIEERREELGE----RARALYRSGGSVSYLDVLLGSES--FSDFLDRLSALSKIADADADLLEELKA 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024503276 285 EKLEILSSLQCVQKQLQQITQTNVRMES---ELNALREEYQTLERDNELQREKAKENEEKFLNLQNEHEKALR 354
Cdd:COG3883 141 DKAELEAKKAELEAKLAELEALKAELEAakaELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAA 213
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
29-628 |
3.32e-05 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 48.04 E-value: 3.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 29 ETLLSIRLLDFKTSLLETIEELRIRRETEINYEEQLSKIVVEKQELEWQKETLQHQTDTLQQQNKEAMA-AFKKQLQARM 107
Cdd:pfam02463 180 EETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDeQEEIESSKQE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 108 FAMEEEKGKYQLAVEIKEKEIDGLKETLKELQISKhtLQKKLNEMDQKLQMHLTGREEHNKKLNEVERcyatiaCQFGIV 187
Cdd:pfam02463 260 IEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKE--EEELKSELLKLERRKVDDEEKLKESEKEKKK------AEKELK 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 188 KGVHEKLEHSVQEAIQLNKKLTSVNKRQETEISNLKEELKKvtTDLIRSKVTSQHRVGEENINLAAKEKQFQELQQKIRM 267
Cdd:pfam02463 332 KEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLE--EELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQL 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 268 ETAISKRVQEENANIKEEKLEILSSLQCVQkQLQQITQTNVRMESELNALREeyqtLERDNELQREKAKENEEKFLNLQN 347
Cdd:pfam02463 410 LLELARQLEDLLKEEKKEELEILEEEEESI-ELKQGKLTEEKEELEKQELKL----LKDELELKKSEDLLKETQLVKLQE 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 348 EHEKALRIWKKDEENLRREMDT---IKNELNSLKKTQGHLDDCHPPQGNQHSEQVENLQIHSTVHPVirnsgQEQSKGSE 424
Cdd:pfam02463 485 QLELLLSRQKLEERSQKESKARsglKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIV-----EVSATADE 559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 425 IQAIQKKNDCMPSILRKDNNSGHEDEIEVKNTVSFS-LSTEELQIEQKLQVLENGFKDEINVASPLEGKEREVSPRNTLC 503
Cdd:pfam02463 560 VEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAvLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKE 639
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 504 TDTDLITQGQNSEMHVTECKEAENLETTCRVLLEGNSANLQQKLQDSTGPAAPHHTETSKVLLDAADRVIVSDKNAIQEM 583
Cdd:pfam02463 640 SAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEA 719
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 2024503276 584 NSSNQELCSTTHESICTKVDKNSSIIELNSSVLTTKASKKESEAA 628
Cdd:pfam02463 720 EELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEE 764
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
60-374 |
3.91e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.75 E-value: 3.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 60 YEEQLSKIVVEKQELEWQKETLQHQTDTLQQQ-NKEAMAAFKKQLQARMFAMEEEKGKYQLA-VEIKEKEIDGLKETLKE 137
Cdd:PRK03918 457 YTAELKRIEKELKEIEEKERKLRKELRELEKVlKKESELIKLKELAEQLKELEEKLKKYNLEeLEKKAEEYEKLKEKLIK 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 138 LQISKHTLQKKLNemdqKLQMHLTGREEHNKKLNEVERCYATIACQFGIVK-GVHEKLEHSVQEAIQLNKKLTSVnKRQE 216
Cdd:PRK03918 537 LKGEIKSLKKELE----KLEELKKKLAELEKKLDELEEELAELLKELEELGfESVEELEERLKELEPFYNEYLEL-KDAE 611
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 217 TEISNLKEELKKVTTDLIRSKVtsqhrvgeeniNLAAKEKQFQELQQKIrmETAISKRVQEENANIKEEKLEILSSLQCV 296
Cdd:PRK03918 612 KELEREEKELKKLEEELDKAFE-----------ELAETEKRLEELRKEL--EELEKKYSEEEYEELREEYLELSRELAGL 678
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024503276 297 QKQLQQITQTNVRMESELNALREEYQTlerdnelqREKAKENEEKFlnlqnehEKALriwkKDEENLRREMDTIKNEL 374
Cdd:PRK03918 679 RAELEELEKRREEIKKTLEKLKEELEE--------REKAKKELEKL-------EKAL----ERVEELREKVKKYKALL 737
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
30-353 |
5.93e-05 |
|
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: 47.27 E-value: 5.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 30 TLLSIRLLDFKTSLLETIEELRIRRETEINYEEQL------SKIVVEKQE---LEWQKETLQHQtDTLQQQNKEAMAAFK 100
Cdd:TIGR00618 179 TQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMpdtyheRKQVLEKELkhlREALQQTQQSH-AYLTQKREAQEEQLK 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 101 KQLQARMFAMEEEKGKYQLA-VEIKEKEIDGLKETLKELQISKHTLQ--KKLNEMDQKLQMHLTGREEHNKKLNEVERCY 177
Cdd:TIGR00618 258 KQQLLKQLRARIEELRAQEAvLEETQERINRARKAAPLAAHIKAVTQieQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQ 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 178 ATIACQFGIVKGVHEKLEHsvqeaiqlnkkltsvNKRQETEISNLKEELKKVTTDLIRSKVTSQHR-VGEENINLAAKEK 256
Cdd:TIGR00618 338 SSIEEQRRLLQTLHSQEIH---------------IRDAHEVATSIREISCQQHTLTQHIHTLQQQKtTLTQKLQSLCKEL 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 257 -QFQELQQKIRMETAISKRVQEENANIK-EEKLEILSSLQC---VQKQLQQITQTNVRMESELNALREEYQTL-ERDNEL 330
Cdd:TIGR00618 403 dILQREQATIDTRTSAFRDLQGQLAHAKkQQELQQRYAELCaaaITCTAQCEKLEKIHLQESAQSLKEREQQLqTKEQIH 482
|
330 340
....*....|....*....|....
gi 2024503276 331 QREKAKEN-EEKFLNLQNEHEKAL 353
Cdd:TIGR00618 483 LQETRKKAvVLARLLELQEEPCPL 506
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
42-384 |
6.12e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.07 E-value: 6.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 42 SLLETIEELRIRRETEINYEEQLSKIVVEKQELEWQKETLQHQTDTLQQQNKEAMAAFKKQLQARMFAMEEEKGKYQLAV 121
Cdd:COG4717 143 ELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEEL 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 122 EIKEKEIDGLKETLKELQiskhtLQKKLNEMDQkLQMHLTGREEHNKKLNEVERCYATIACQFGIVKGVhekleHSVQEA 201
Cdd:COG4717 223 EELEEELEQLENELEAAA-----LEERLKEARL-LLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGL-----LALLFL 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 202 IQLNKKLTSVNKRQETEISNLKEELKKVTTDLIRSKVtsqhrvgeeNINLAAKEKQFQELQQKIRmetaiskRVQEENAN 281
Cdd:COG4717 292 LLAREKASLGKEAEELQALPALEELEEEELEELLAAL---------GLPPDLSPEELLELLDRIE-------ELQELLRE 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 282 IKEEKLEILssLQCVQKQLQQI-TQTNVRMESELNALREEYQTLERdnelQREKAKENEEKFLNLQNEHEKALRIWKKDE 360
Cdd:COG4717 356 AEELEEELQ--LEELEQEIAALlAEAGVEDEEELRAALEQAEEYQE----LKEELEELEEQLEELLGELEELLEALDEEE 429
|
330 340
....*....|....*....|....*....
gi 2024503276 361 -----ENLRREMDTIKNELNSLKKTQGHL 384
Cdd:COG4717 430 leeelEELEEELEELEEELEELREELAEL 458
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
4-378 |
1.09e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.57 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 4 KDRQVLKMDEDLKMQALDSALQSPSETLLSIRLLDFKTSLLETIEELRIRRETEINYEEQLSKIVVEKQELEWQKETLQH 83
Cdd:PRK02224 284 LRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELRE 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 84 QTDTLQQQNKEAMAAFKKQlQARMFAMEEEKGKYQLAVEIKEKEIDGLKETLKELQISKHTLQKKLNEMDQKLQmHLTGR 163
Cdd:PRK02224 364 EAAELESELEEAREAVEDR-REEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLR-TARER 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 164 EEHNKKLNEVERC--------YATIACQFGIVKGVHEKLEHSVQEA----IQLNKKLTSVN--KRQETEISNLKEELKKV 229
Cdd:PRK02224 442 VEEAEALLEAGKCpecgqpveGSPHVETIEEDRERVEELEAELEDLeeevEEVEERLERAEdlVEAEDRIERLEERREDL 521
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 230 TtDLIRSKVTsqhRVGEENINLAAKEKQFQELQQKIRM--ETAISKR-----VQEENANIKEEKLEILSSLQCVQKqLQQ 302
Cdd:PRK02224 522 E-ELIAERRE---TIEEKRERAEELRERAAELEAEAEEkrEAAAEAEeeaeeAREEVAELNSKLAELKERIESLER-IRT 596
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 303 ITQTNVRMESELNALREEYQTLERDNELQREKAKE------------NEEKFLNLQNEHEKA----------LRIWKKDE 360
Cdd:PRK02224 597 LLAAIADAEDEIERLREKREALAELNDERRERLAEkrerkreleaefDEARIEEAREDKERAeeyleqveekLDELREER 676
|
410
....*....|....*...
gi 2024503276 361 ENLRREMDTIKNELNSLK 378
Cdd:PRK02224 677 DDLQAEIGAVENELEELE 694
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
45-278 |
1.22e-04 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 46.17 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 45 ETIEELRIRRETEInyeeqlskivvekqelewqkETLQHQTDTLQQQnKEAMAAFKKQLQARMFAMEEEKGKYQLAVEIK 124
Cdd:pfam05667 324 ETEEELQQQREEEL--------------------EELQEQLEDLESS-IQELEKEIKKLESSIKQVEEELEELKEQNEEL 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 125 EKEIDGLKETLKEL-----QISKhtLQKKLNEMDQKLQmHLTG----------------REEHNKKLNEVERCYATIacq 183
Cdd:pfam05667 383 EKQYKVKKKTLDLLpdaeeNIAK--LQALVDASAQRLV-ELAGqwekhrvplieeyralKEAKSNKEDESQRKLEEI--- 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 184 fgivKGVHEKLEHSVQEAiqlnkkltsvnKRQETEISNLKEELKKVTTDLIRSKVTSqhRVGE--ENInlaakEKQFQEL 261
Cdd:pfam05667 457 ----KELREKIKEVAEEA-----------KQKEELYKQLVAEYERLPKDVSRSAYTR--RILEivKNI-----KKQKEEI 514
|
250
....*....|....*..
gi 2024503276 262 qQKIRMETaisKRVQEE 278
Cdd:pfam05667 515 -TKILSDT---KSLQKE 527
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
7-325 |
1.44e-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: 46.26 E-value: 1.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 7 QVLKMDEDLKMQALDSALQSPSETL-----LSIRLLDFKTSLLETIEELRIRRETEINYEEQLSKIVVEKQELEWQKET- 80
Cdd:pfam15921 436 KAMKSECQGQMERQMAAIQGKNESLekvssLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEAt 515
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 81 -----------------LQH-----------QTD----TLQQQNKEAMAAFKKQLQARMFAMEEEKGKYQLAVEIK---- 124
Cdd:pfam15921 516 naeitklrsrvdlklqeLQHlknegdhlrnvQTEcealKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEkaql 595
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 125 EKEIDGLKETLKELQISKHTLQKKLNEMD--------QKLQMHLTGRE----------EHNKKLNEVERCyatiacqfgi 186
Cdd:pfam15921 596 EKEINDRRLELQEFKILKDKKDAKIRELEarvsdlelEKVKLVNAGSErlravkdikqERDQLLNEVKTS---------- 665
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 187 vkgvHEKLEHSVQEAIQLNKKLTSVNKRQETEISNLKEELKKVTTDLIRSKVTSQHRVGEE----------NINLAAKEK 256
Cdd:pfam15921 666 ----RNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDghamkvamgmQKQITAKRG 741
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024503276 257 QFQELQQKIRMETAISKRVQEENANIKEEKLEILSSLQCVQkqlqqiTQTNvRMESELNALREEYQTLE 325
Cdd:pfam15921 742 QIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVA------TEKN-KMAGELEVLRSQERRLK 803
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
126-379 |
2.52e-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: 2.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 126 KEIDGLKETLKELQISKHTLQKKLNEMDQKLQMHLTGREEHNKKLNEVERcyatiacqfgivkgvheKLEHSVQEAIQLN 205
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALAR-----------------RIRALEQELAALE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 206 KKLTSVNKRQETeisnLKEELKKVTTDLIRSKVTSQHRVGEENINLAAKEKQFQELQQKIRMETAISKRVQEENANIKEE 285
Cdd:COG4942 83 AELAELEKEIAE----LRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRAD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 286 kleilsslqcvQKQLQQITQtnvrmesELNALREEYQTLERDNELQREKAKENEEKFLNLQNEHEKALRIWKKDEENLRR 365
Cdd:COG4942 159 -----------LAELAALRA-------ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQ 220
|
250
....*....|....
gi 2024503276 366 EMDTIKNELNSLKK 379
Cdd:COG4942 221 EAEELEALIARLEA 234
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
77-305 |
2.83e-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: 2.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 77 QKETLQHQTDTLQQQnkeamaafKKQLQARMFAMEEEKGKYQLAVEIKEKEIDGLKETLKELQISKHTLQKKLNEMDQKL 156
Cdd:COG4942 21 AAAEAEAELEQLQQE--------IAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 157 QMHLTGREEHNKKLNEVERCYATIACQFGIVKGVHEKlehSVQEAIQLNKKLTSVNKRQETEIsnlkEELKKVTTDLIRS 236
Cdd:COG4942 93 AELRAELEAQKEELAELLRALYRLGRQPPLALLLSPE---DFLDAVRRLQYLKYLAPARREQA----EELRADLAELAAL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024503276 237 KVTSQHRVGEENINLAAKEKQFQELQQKIRMETAISKRVQEENANIKEEKLEILSSLQCVQKQLQQITQ 305
Cdd:COG4942 166 RAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEA 234
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
71-378 |
3.05e-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: 45.11 E-value: 3.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 71 KQELEWQKETLQHQTDTLQQQNKEAMAAFKKQ----------LQARMFAMEEEKgkyQLAVEIKEKEI-------DGLKE 133
Cdd:pfam15921 73 KEHIERVLEEYSHQVKDLQRRLNESNELHEKQkfylrqsvidLQTKLQEMQMER---DAMADIRRRESqsqedlrNQLQN 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 134 TLKELQISKHTLQKKLNEMDQKLQMHLTGREEHNKKLNEVERCYATIACQFGivKGVHEKLEHSVQEAIQLNKKLTSVNK 213
Cdd:pfam15921 150 TVHELEAAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSILVDFEEASG--KKIYEHDSMSTMHFRSLGSAISKILR 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 214 RQETEISNLKEELKKVTTDLIRSKVTSQHR---------------VGEENINLA--------------AKEKQFQELQQK 264
Cdd:pfam15921 228 ELDTEISYLKGRIFPVEDQLEALKSESQNKielllqqhqdrieqlISEHEVEITgltekassarsqanSIQSQLEIIQEQ 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 265 IRMETAISKR-VQEENANIKEEKLEILSSLQCVQKQLQQITQTNVRMESELNALREEYQTLER-----DNELQREKAK-E 337
Cdd:pfam15921 308 ARNQNSMYMRqLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQesgnlDDQLQKLLADlH 387
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 2024503276 338 NEEKFLNLQNEHEKalRIWKKDEEN------LRREMDTIKNELNSLK 378
Cdd:pfam15921 388 KREKELSLEKEQNK--RLWDRDTGNsitidhLRRELDDRNMEVQRLE 432
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
125-333 |
4.93e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.24 E-value: 4.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 125 EKEIDGLKETLKELQ--ISKHTLQKKLNEMDQKLQMHLTGREEHNKKLNEVERCYATIacqfgivkgvhEKLEHSVQEAI 202
Cdd:COG3206 181 EEQLPELRKELEEAEaaLEEFRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEA-----------EARLAALRAQL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 203 QLNKKlTSVNKRQETEISNLKEELKKVTTDL--IRSKVTSQHRvgeeninlaakekQFQELQQKIR-METAISKRVQEEN 279
Cdd:COG3206 250 GSGPD-ALPELLQSPVIQQLRAQLAELEAELaeLSARYTPNHP-------------DVIALRAQIAaLRAQLQQEAQRIL 315
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2024503276 280 ANIKEEKLEILSSLQCVQKQLQQITQTNvrmeSELNALREEYQTLERDNELQRE 333
Cdd:COG3206 316 ASLEAELEALQAREASLQAQLAQLEARL----AELPELEAELRRLEREVEVARE 365
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
251-384 |
5.37e-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: 43.60 E-value: 5.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 251 LAAKEKQFQELQQKIRMETAISKRVQEENANIKEEKLEILSSLQCVQKQLQQITQTNVRMESELNALREEYQTLERDNEL 330
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEA 101
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024503276 331 QREKAKE-----------NEEKFLNLQ---NEHEKALRIWKKDEENLRREMDTIKNELNSLKKTQGHL 384
Cdd:COG4942 102 QKEELAEllralyrlgrqPPLALLLSPedfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAEL 169
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
17-232 |
5.51e-04 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 44.12 E-value: 5.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 17 MQALDSALQSPSETLLSIRLLDFKTSLLE-TIEELRIRReteINYEEQLSKIVVEKQELEWQK-ETLQHQTDTLQQQNKE 94
Cdd:PLN02939 242 IQFLKAELIEVAETEERVFKLEKERSLLDaSLRELESKF---IVAQEDVSKLSPLQYDCWWEKvENLQDLLDRATNQVEK 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 95 AMAAFKKQLQARmfameeekgkyqlaveikeKEIDGLKETLKELQISKHTLQkKLNEMDQKLQMhltgREEHnkklneve 174
Cdd:PLN02939 319 AALVLDQNQDLR-------------------DKVDKLEASLKEANVSKFSSY-KVELLQQKLKL----LEER-------- 366
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2024503276 175 rcyatiacqfgivkgvHEKLEHSVQEAIQLNKKltSVNKRQETeISNLKEELKKVTTD 232
Cdd:PLN02939 367 ----------------LQASDHEIHSYIQLYQE--SIKEFQDT-LSKLKEESKKRSLE 405
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
40-386 |
5.87e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.88 E-value: 5.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 40 KTSLLETIEELRIRRETEINYEEQLSKIVVEKQELEWQKETLQHQTDTLQQQ--------------------NKEAMAAF 99
Cdd:PRK02224 236 RDEADEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERleeleeerddllaeaglddaDAEAVEAR 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 100 KKQLQARMFAMEEEKGKYQLAVEIKEKEIDGLKETLKELQISKHTLQKKLNEMDQKLQMHLTGREEHNKKLNEVERCYAT 179
Cdd:PRK02224 316 REELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEE 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 180 IACQFGIVKGVHEKLEHSVQEAiqlnkkltsvnkrqETEISNLKEELKKVTTDLirskVTSQHRVgEENINLAAKEK--- 256
Cdd:PRK02224 396 LRERFGDAPVDLGNAEDFLEEL--------------REERDELREREAELEATL----RTARERV-EEAEALLEAGKcpe 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 257 QFQELQQKIRMETAISKRvqEENANIKEEKLEILSSLQCVQKQLQQITQTnVRMESELNALREEYQTLERDNELQREKAK 336
Cdd:PRK02224 457 CGQPVEGSPHVETIEEDR--ERVEELEAELEDLEEEVEEVEERLERAEDL-VEAEDRIERLEERREDLEELIAERRETIE 533
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 2024503276 337 ENEEKFLNLQ---NEHEKALRIWKKDEENLRREMDTIKNELNSLKKTQGHLDD 386
Cdd:PRK02224 534 EKRERAEELReraAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKE 586
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
57-231 |
6.02e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 44.05 E-value: 6.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 57 EINYEEQLSKIVVEKQELEWQKETLQHQTDTLQQQNKEAMAAFKKqlqarmfameeekgKYQLAVEIKEKEIDGLKETLK 136
Cdd:PRK00409 529 ERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEK--------------EAQQAIKEAKKEADEIIKELR 594
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 137 ELQISKHTLQK---------KLNEMDQKLQMHLTGREEHNKKLNEVERCYATIACQFGIVKGVHEKLEHSVQEAI-QLNK 206
Cdd:PRK00409 595 QLQKGGYASVKaheliearkRLNKANEKKEKKKKKQKEKQEELKVGDEVKYLSLGQKGEVLSIPDDKEAIVQAGImKMKV 674
|
170 180
....*....|....*....|....*
gi 2024503276 207 KLTSVNKRQETEisnlKEELKKVTT 231
Cdd:PRK00409 675 PLSDLEKIQKPK----KKKKKKPKT 695
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
48-340 |
7.13e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 44.01 E-value: 7.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 48 EELRIRRETEINYEEQLSKIVVEKQELEWQKETLQHQTDTLQQQNKEA------MAAFKKQLQARMFAME-----EEKGK 116
Cdd:pfam01576 12 EELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAeemrarLAARKQELEEILHELEsrleeEEERS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 117 YQLAVEIK--EKEIDGLKETLKE-------LQISKHTLQKKLNEMDQKLQMhltgREEHNKKLNEVERcyatiacqfgIV 187
Cdd:pfam01576 92 QQLQNEKKkmQQHIQDLEEQLDEeeaarqkLQLEKVTTEAKIKKLEEDILL----LEDQNSKLSKERK----------LL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 188 KGVHEKLEHSVQEAIQLNKKLTSVNKRQETEISNLKEELKK-----------------VTTDLIRSKVTSQHRVGEENIN 250
Cdd:pfam01576 158 EERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKeekgrqelekakrklegESTDLQEQIAELQAQIAELRAQ 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 251 LAAKEKQFQELQQKIRMETAISKRVQEENANIKEEKLEILSSLQCVQKQLQQITQTNVRMESELNALREEYQ-TLERDNE 329
Cdd:pfam01576 238 LAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEdTLDTTAA 317
|
330
....*....|.
gi 2024503276 330 LQREKAKENEE 340
Cdd:pfam01576 318 QQELRSKREQE 328
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
191-385 |
1.03e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.37 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 191 HEKLEHSVQEAIQLNKKLTSVNKRQ-----ETEISNLKEELKKVTTDLirskvtsqhrvgeeninlAAKEKQFQELQQKI 265
Cdd:COG4913 264 YAAARERLAELEYLRAALRLWFAQRrlellEAELEELRAELARLEAEL------------------ERLEARLDALREEL 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 266 R-METAISKRVQEENANIKEEkleilssLQCVQKQLQQITQTNVRMESELNALREEYQTLERDNELQREKAKENEEKFLN 344
Cdd:COG4913 326 DeLEAQIRGNGGDRLEQLERE-------IERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEE 398
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2024503276 345 LQNEHEKALRIWKKDEENLRREMDTIKNELNSLKKTQGHLD 385
Cdd:COG4913 399 ELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIP 439
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
40-379 |
1.08e-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: 43.09 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 40 KTSLLETIEELRIRREteiNYEEQLSKIVVEKQELEWQKETLQHQTDTLQQQNKEaMAAFKKQLQARMFAMEEEKGKYQL 119
Cdd:TIGR04523 379 NQSYKQEIKNLESQIN---DLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIER-LKETIIKNNSEIKDLTNQDSVKEL 454
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 120 AVEIKEKEIDGLKETLKELQIS----KHTLQKKLNEMDQKLQMHLTGREEHNKKLNEVErcyatiacqfgivkgvheKLE 195
Cdd:TIGR04523 455 IIKNLDNTRESLETQLKVLSRSinkiKQNLEQKQKELKSKEKELKKLNEEKKELEEKVK------------------DLT 516
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 196 HSVQEAIQLNKKLTSVNKRQETEISNLKEELKKVTTDLIRSKVtsqhrvgeeninlaakEKQFQELQQKIrmetaiskrv 275
Cdd:TIGR04523 517 KKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENL----------------EKEIDEKNKEI---------- 570
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 276 qeenANIKEEKLEILSSLQCVQKQLQQITQTNVRMESELNALREEYQTLERDNELQREKAKENEEKFLNLQNEHEKAlri 355
Cdd:TIGR04523 571 ----EELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKL--- 643
|
330 340
....*....|....*....|....
gi 2024503276 356 wKKDEENLRREMDTIKNELNSLKK 379
Cdd:TIGR04523 644 -KQEVKQIKETIKEIRNKWPEIIK 666
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
97-306 |
1.25e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.83 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 97 AAFKKQLQARMFAMEEEKGKyqlAVEIKEKEIDGLKETLKELQISKHTLQKKLNEMDQKLQMHLTGREEHNKKLNEVERC 176
Cdd:COG4717 45 AMLLERLEKEADELFKPQGR---KPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 177 YATIACQFGIVKGVH--EKLEHSVQEAIQLNKKLTSVnKRQETEISNLKEELKKVTTDLIRSKVTSQHRVGEEninLAAK 254
Cdd:COG4717 122 EKLLQLLPLYQELEAleAELAELPERLEELEERLEEL-RELEEELEELEAELAELQEELEELLEQLSLATEEE---LQDL 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2024503276 255 EKQFQELQQKIRMETAISKRVQEENANIKEEkLEILSSLQCVQKQLQQITQT 306
Cdd:COG4717 198 AEELEELQQRLAELEEELEEAQEELEELEEE-LEQLENELEAAALEERLKEA 248
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
55-334 |
1.50e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.02 E-value: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 55 ETEINYEEQLSkIVVEKQElewQKETLQHQTDTLQQQNKEAmaafKKQL---QARMFAMEEEKGKYQLAVEIKEK----- 126
Cdd:PRK04863 359 ELEERLEEQNE-VVEEADE---QQEENEARAEAAEEEVDEL----KSQLadyQQALDVQQTRAIQYQQAVQALERakqlc 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 127 -----EIDGLKETLKELQISKHTLQKKLNEMDQKLQMHLTGREEHNKKLN-------EVERCYA---------------T 179
Cdd:PRK04863 431 glpdlTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQlvrkiagEVSRSEAwdvarellrrlreqrH 510
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 180 IACQFGIVKGVHEKLEHSVQEAIQLNKKLTSVNKRQETEISNlKEELKKVTTDL---IRSKVTSQHRVGEENINLAAKEK 256
Cdd:PRK04863 511 LAEQLQQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDD-EDELEQLQEELearLESLSESVSEARERRMALRQQLE 589
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 257 QfqeLQQKIRMETAISKR---VQEENANIKEEKLEILSSLQCVQKQLQQiTQTNVRmesELNALREEYQTLERDNELQRE 333
Cdd:PRK04863 590 Q---LQARIQRLAARAPAwlaAQDALARLREQSGEEFEDSQDVTEYMQQ-LLERER---ELTVERDELAARKQALDEEIE 662
|
.
gi 2024503276 334 K 334
Cdd:PRK04863 663 R 663
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
246-360 |
1.96e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 42.15 E-value: 1.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 246 EENINLAAKEKQFQELQQKIrmetaisKRVQEENANIK---EEKLEILSSLQCVQKQLQQITQTNVRMESELNALREEYQ 322
Cdd:COG2433 403 HEERELTEEEEEIRRLEEQV-------ERLEAEVEELEaelEEKDERIERLERELSEARSEERREIRKDREISRLDREIE 475
|
90 100 110
....*....|....*....|....*....|....*...
gi 2024503276 323 TLERdnELQREKaKENEEkflnLQNEHEKALRIWKKDE 360
Cdd:COG2433 476 RLER--ELEEER-ERIEE----LKRKLERLKELWKLEH 506
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
284-386 |
1.97e-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: 1.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 284 EEKLEILSSLQCVQKQLQQITQTNVRMESELNALREEYQTLERDNELQREKAKENEEKFLNLQNEHEKALRIWKKDEENL 363
Cdd:COG1579 3 PEDLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQL 82
|
90 100
....*....|....*....|....*...
gi 2024503276 364 R-----REMDTIKNELNSLKKTQGHLDD 386
Cdd:COG1579 83 GnvrnnKEYEALQKEIESLKRRISDLED 110
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
78-379 |
2.30e-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: 42.02 E-value: 2.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 78 KETLQHQTDTLQQQNKEAMAAFKKQLQARM---FAMEEEKGKYQLAVEIKEKEIDGLKETLKELQISKHTLQKKLNEMDQ 154
Cdd:pfam05483 316 EEDLQIATKTICQLTEEKEAQMEELNKAKAahsFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEE 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 155 KLQMHlTGREEHNKKLNEVERCYATIACQFGIVKGVHEKLEHSVQEaiqlnkkLTSVNKRQETEISNLKEELKKVTTD-- 232
Cdd:pfam05483 396 MTKFK-NNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQE-------LIFLLQAREKEIHDLEIQLTAIKTSee 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 233 ----LIRSKVTSQHRVGEENINLAAKEKQF----QELQQKIRMETAISKRVQEENANIKEEKLEILsslqcvqKQLQQIT 304
Cdd:pfam05483 468 hylkEVEDLKTELEKEKLKNIELTAHCDKLllenKELTQEASDMTLELKKHQEDIINCKKQEERML-------KQIENLE 540
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024503276 305 QTNVRMESELNALREEYQTLERDNELQREKAKENEEKFLNLQNEHEKALRIWKKDEENLRREMDTIKNELNSLKK 379
Cdd:pfam05483 541 EKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQ 615
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
241-384 |
2.43e-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: 40.68 E-value: 2.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 241 QHRVGEENINLAAKEKQFQELQQKIrmeTAISKRVQEENANIKEEKLEILSslqcVQKQLQQIT--QTNVRMESELNALR 318
Cdd:COG1579 23 EHRLKELPAELAELEDELAALEARL---EAAKTELEDLEKEIKRLELEIEE----VEARIKKYEeqLGNVRNNKEYEALQ 95
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024503276 319 EEYQTLERDNELQREKAKENEEKFLNLQNEHEKALRIWKKDEENLRREMDTIKNELNSLKKTQGHL 384
Cdd:COG1579 96 KEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEEL 161
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
98-355 |
2.88e-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: 2.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 98 AFKKQLQARMFAMEEEKGKYQLAVEIKEKEIDGLKETLKELQISKHTLQKKLNEMDQKLQMHltgreehnKKLNEVERCY 177
Cdd:TIGR00618 198 LLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQ--------QLLKQLRARI 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 178 ATIACQFGIVKGVHEKLEHSVQEA--IQLNKKLTSVNKRQETEISNLKEELKKVTTDLIRSKVTSQHRvgeeninlAAKE 255
Cdd:TIGR00618 270 EELRAQEAVLEETQERINRARKAAplAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQ--------SSIE 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 256 KQFQELQQKIRMETAIsKRVQEENANIKEEKLEILSSLQCVQKQLQQIT---QTNVRMESELNALREEYQTLE----RDN 328
Cdd:TIGR00618 342 EQRRLLQTLHSQEIHI-RDAHEVATSIREISCQQHTLTQHIHTLQQQKTtltQKLQSLCKELDILQREQATIDtrtsAFR 420
|
250 260
....*....|....*....|....*..
gi 2024503276 329 ELQREKAKENEEKFLNLQNEHEKALRI 355
Cdd:TIGR00618 421 DLQGQLAHAKKQQELQQRYAELCAAAI 447
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
199-386 |
3.32e-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: 41.29 E-value: 3.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 199 QEAIQLNKKLTSVNKrqetEISNLKEELKKVTTDliRSKVTSQHRVGEENINLAAK-----EKQFQELQQKIRmetAISK 273
Cdd:COG4942 20 DAAAEAEAELEQLQQ----EIAELEKELAALKKE--EKALLKQLAALERRIAALARriralEQELAALEAELA---ELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 274 RVQEENANIKEEKLEILSSLQCVQKQ------------------------LQQITQTNVRMESELNALREEYQTLERDNE 329
Cdd:COG4942 91 EIAELRAELEAQKEELAELLRALYRLgrqpplalllspedfldavrrlqyLKYLAPARREQAEELRADLAELAALRAELE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2024503276 330 LQREKAKENEEKFLNLQNEHEKALRIWKKDEENLRREMDTIKNELNSLKKTQGHLDD 386
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEA 227
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
199-386 |
3.49e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.29 E-value: 3.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 199 QEAIQLNKKLTSVNKRQETEISNLKEELK--KVTTDLIRSKVTSQHRVGEEninLAAKEKQFQELQQKIR-METAISKR- 274
Cdd:COG4717 53 KEADELFKPQGRKPELNLKELKELEEELKeaEEKEEEYAELQEELEELEEE---LEELEAELEELREELEkLEKLLQLLp 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 275 VQEENANIKEEKLEILSSLQCVQKQLQQITQtnvrMESELNALREEYQTLERD-NELQREKAKENEEKFLNLQNEHE--- 350
Cdd:COG4717 130 LYQELEALEAELAELPERLEELEERLEELRE----LEEELEELEAELAELQEElEELLEQLSLATEEELQDLAEELEelq 205
|
170 180 190
....*....|....*....|....*....|....*.
gi 2024503276 351 KALRIWKKDEENLRREMDTIKNELNSLKKTQGHLDD 386
Cdd:COG4717 206 QRLAELEEELEEAQEELEELEEELEQLENELEAAAL 241
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
48-381 |
3.76e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.67 E-value: 3.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 48 EELRIRRETEINYEEQLSKIVVEKQELEWQKETLQH--QTDTLQQQNKEAmaafKKQLQARMFAMEEEKGKYQLAVEIKE 125
Cdd:PTZ00121 1394 DEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEkkKADEAKKKAEEA----KKADEAKKKAEEAKKAEEAKKKAEEA 1469
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 126 KEIDGLKETLKELQISKHtLQKKLNEMDQKLQmHLTGREEHNKKLNEVERcyATIACQFGIVKGVHEKLEHSVQEAIQLN 205
Cdd:PTZ00121 1470 KKADEAKKKAEEAKKADE-AKKKAEEAKKKAD-EAKKAAEAKKKADEAKK--AEEAKKADEAKKAEEAKKADEAKKAEEK 1545
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 206 KKLTSVNKRQETEISnlkEELKKVttdlirskvtSQHRVGEENINLAAKEKQFQELQQKIRMETAISKRVQE-------- 277
Cdd:PTZ00121 1546 KKADELKKAEELKKA---EEKKKA----------EEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEkkmkaeea 1612
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 278 ---ENANIKEEKLEILSSLQCVQKQLQQITQTNVRMESELNALREEYQTLERDNELQREKAKENEEKFLNLQNEHEKALR 354
Cdd:PTZ00121 1613 kkaEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAE 1692
|
330 340
....*....|....*....|....*..
gi 2024503276 355 IWKKDEENLRREMDTIKNELNSLKKTQ 381
Cdd:PTZ00121 1693 ALKKEAEEAKKAEELKKKEAEEKKKAE 1719
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
43-385 |
4.14e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 41.43 E-value: 4.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 43 LLETIEELRIRRETEINYEEQLSKIVVEKQELEWQKETLQHQTDTLQQQNKEAmaafkKQLQARMFAMEEEKGKYQLAVE 122
Cdd:PRK01156 154 ILDEILEINSLERNYDKLKDVIDMLRAEISNIDYLEEKLKSSNLELENIKKQI-----ADDEKSHSITLKEIERLSIEYN 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 123 IKEKEIDGLKETLKELQiSKHTLQKKLNEMDQKLQMHLTGREEHNKKLNEVE------------------RCYATIACQF 184
Cdd:PRK01156 229 NAMDDYNNLKSALNELS-SLEDMKNRYESEIKTAESDLSMELEKNNYYKELEerhmkiindpvyknrnyiNDYFKYKNDI 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 185 GIVKGVHEKLEHSVQEAIQLNKKLTSVNK--RQETEISNLKEELKKVTTDLIRSKVTSQHRVGE-ENINLaaKEKQFQEL 261
Cdd:PRK01156 308 ENKKQILSNIDAEINKYHAIIKKLSVLQKdyNDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSiESLKK--KIEEYSKN 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 262 QQKIRMETAISKRVQEENAN-IKEEKLEILSSLQCVQKQLQQITQTNVRMESELNALREEYQTLERDNELQREKAKENEE 340
Cdd:PRK01156 386 IERMSAFISEILKIQEIDPDaIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSVCPVCGTTLGEE 465
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 2024503276 341 KFLNLQNEHEKALRIWKKDEENLRREMDTIKNELNSLKKTQGHLD 385
Cdd:PRK01156 466 KSNHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLE 510
|
|
| ANIS5_cation-bd |
pfam02520 |
SXP/RAL-2 family protein Ani s 5-like, metal-binding domain; This domain is found in proteins ... |
247-321 |
5.19e-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: 37.56 E-value: 5.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 247 ENINLAAKEKQFQELQQKIRMETAIS---KRVQEENANIKEEKLEILSSLQCVQKQLQQI----TQTNVRMESELNALRE 319
Cdd:pfam02520 12 ETLTIAEKEEQLAAWAEKYGVTDQYKefqANVTALKEEVKKNVTAVISNLSSVLNQLSAIldnkNQTRAQQHEAIDALKQ 91
|
..
gi 2024503276 320 EY 321
Cdd:pfam02520 92 QY 93
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
109-386 |
6.17e-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: 40.81 E-value: 6.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 109 AMEEEKGKYQLAVEIKEKEIDGLKET-LKELQIS---KHTLQKKLNEMDQKL-QMHLTGREEHNkklNEVERCYATIACQ 183
Cdd:TIGR01612 932 SIEKFHNKQNILKEILNKNIDTIKESnLIEKSYKdkfDNTLIDKINELDKAFkDASLNDYEAKN---NELIKYFNDLKAN 1008
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 184 FGIVKG--------VHEKLEHSV-QEAIQLNKKLTSVNKRQETEISNLKEELKKVTTDLIRSKVTSQHRVGEENINlaak 254
Cdd:TIGR01612 1009 LGKNKEnmlyhqfdEKEKATNDIeQKIEDANKNIPNIEIAIHTSIYNIIDEIEKEIGKNIELLNKEILEEAEINIT---- 1084
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 255 ekQFQELQQKIRMETaISKRVQEENANIKEE----KLEILSSLQCVQKQLQQITQTNVRMESELNALREEYQTLER--DN 328
Cdd:TIGR01612 1085 --NFNEIKEKLKHYN-FDDFGKEENIKYADEinkiKDDIKNLDQKIDHHIKALEEIKKKSENYIDEIKAQINDLEDvaDK 1161
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 2024503276 329 ELQREKAKENEEKFLNLQNEHEKalriwkkdEENLRREMDTIKNELNSLKKTQGHLDD 386
Cdd:TIGR01612 1162 AISNDDPEEIEKKIENIVTKIDK--------KKNIYDEIKKLLNEIAEIEKDKTSLEE 1211
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
235-355 |
7.05e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.67 E-value: 7.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 235 RSKVTSQHRVGEENIN-LAAKEKQFQELQQKIRMETAISKRVQEENANIkEEKLEILSSLQCV----------------- 296
Cdd:COG4913 595 RRRIRSRYVLGFDNRAkLAALEAELAELEEELAEAEERLEALEAELDAL-QERREALQRLAEYswdeidvasaereiael 673
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024503276 297 QKQLQQITQTNV---RMESELNALREEYQTLERDNELQREKAKENEEKFLNLQNEHEKALRI 355
Cdd:COG4913 674 EAELERLDASSDdlaALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDR 735
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
79-332 |
8.33e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 39.88 E-value: 8.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 79 ETLQHQTDTLQQQNKEAMAAFKKQLQARmfamEEEKGKYQLAVEIKEKEIDGLKETLKELQISKHTLQKKLNEMDQKLQm 158
Cdd:pfam07888 30 ELLQNRLEECLQERAELLQAQEAANRQR----EKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYK- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 159 hltgreehnkklnEVERCYATIACQFGIVKGVHEKLEHSVQEAIQLNKKLTSVNKRQETEISNLKEELKKVTTDLirskv 238
Cdd:pfam07888 105 -------------ELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQR----- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 239 tsqhrvGEENinlaAKEKQFQ-ELQQKIRMETAISKRVQEENANIKEEKLEILsSLQCVQKQLQQITQTNVRMESELNAL 317
Cdd:pfam07888 167 ------KEEE----AERKQLQaKLQQTEEELRSLSKEFQELRNSLAQRDTQVL-QLQDTITTLTQKLTTAHRKEAENEAL 235
|
250
....*....|....*.
gi 2024503276 318 REEYQTL-ERDNELQR 332
Cdd:pfam07888 236 LEELRSLqERLNASER 251
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
93-229 |
9.05e-03 |
|
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.
Pssm-ID: 466641 [Multi-domain] Cd Length: 120 Bit Score: 37.21 E-value: 9.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503276 93 KEAMAAFKKQLQARMFAMEEEKGKYQLAVEIKEKEIDGLKETLKELQISKHTLQKKLNEMDQKLQmhltgREEHNKKLNE 172
Cdd:pfam20492 1 REEAEREKQELEERLKQYEEETKKAQEELEESEETAEELEEERRQAEEEAERLEQKRQEAEEEKE-----RLEESAEMEA 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 2024503276 173 VERcyatiacqfgivkgvhEKLEHSVQEAIQLNKKLTSVNKRQETEISNLKEELKKV 229
Cdd:pfam20492 76 EEK----------------EQLEAELAEAQEEIARLEEEVERKEEEARRLQEELEEA 116
|
|
| |
