|
Name |
Accession |
Description |
Interval |
E-value |
| CCDC73 |
pfam15818 |
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil ... |
1-1000 |
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: 928.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024410660 1 MAAFKKQLQARMFAMEEEKGKYQLAVEIKEKEIDGLKETLKELQISKHTLQKKLNEMDQKLQMHLTVREEHNKKLNEVER 80
Cdd:pfam15818 62 MAVFKKQLQMKMCALEEEKGKYQLATEIKEKEIEGLKETLKALQVSKYSLQKKVSEMEQKLQLHLLAKEDHHKQLNEIEK 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024410660 81 CYATIACQFGIVKGVHEKLEHSVQEAIQLNKKLTSVNKRQETEISNLKEELKKVTTDLIRSKVTSQHRVGEENINLAAKE 160
Cdd:pfam15818 142 YYATITGQFGLVKENHGKLEQNVQEAIQLNKRLSALNKKQESEICSLKKELKKVTSDLIKSKVTCQYKMGEENINLTIKE 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024410660 161 KQFQELQQKIRMETAISKRVQEENANIKEEKLEILSSLQCVQKQLQQITQTNVRMESELNALREEYQTLERDNELQREKA 240
Cdd:pfam15818 222 QKFQELQERLNMELELNKKINEEITHIQEEKQDIIISFQHMQQLLQQQTQANTEMEAELKALKENNQTLERDNELQREKV 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024410660 241 KENEEKFLNLQNEHEKALRIWKKDEENLRREMDTIKNELNSLKKTQGHLDDCHPPQGNQ----HSEQVENLQIHSTVHpi 316
Cdd:pfam15818 302 KENEEKFLNLQNEHEKALGTWKKHVEELNGEINEIKNELSSLKETHIKLQEHYNKLCNQkkfeEDKKFQNVPEVNNEN-- 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024410660 317 irnsGQEQSKGSEIQAIQKENDcmpsilrkdnnfghEDEIEVKNTVSFSLSTEELQIEQK------------LQVLENGF 384
Cdd:pfam15818 380 ----SEMSTEKSENLIIQKYNS--------------EQEIREENTKSFCSDTEYRETEKKkgppveeiiiedLQVLEKSF 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024410660 385 KDEINVASPLEGKEREVSPRNTLCTDTDLITQGQNseMHVTECKEAENLETTCRVLLEGNSANLQQKLQDSTGPAAPHHT 464
Cdd:pfam15818 442 KNEIDTSVPQDKNQSEISLSKTLCTDKDLISQGQT--LNVTDFRKSVTTEIKDKLCLEKDNGCSEFKSPNNLFLVADQSI 519
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024410660 465 ETSKVLLNAADRVIVSDKNAIQEMNSSNQELCSTTHESICTKvdknssiiELNSSVLTTKASKKESEAAVCTEKSAVCER 544
Cdd:pfam15818 520 ETEKIHLESTEGLGLHHADIHLETESNRSSFNGTLNEMAHNT--------NHNKDVSENEPFKQQFRLLLCTQENATEKR 591
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024410660 545 NTDNHQVSEFHFGILSYPKENCQtgYQKCSLLNSDN-NVDNRLCRIERslLNLSGLPRDKFPFKQTHIDAEDKNYNDNAA 623
Cdd:pfam15818 592 ITNSDQTKAGLDSSLDVKKNPVQ--CQKYSLQDSSNvSLDDKQCKIEQ--LLNKKSECSTLPLKQTSSFQQLCNDTSEKP 667
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024410660 624 NINRSGALrhigfpAMDAQNVLAIYCDNASTD-KAAKEHSSNMPFTGTYNLCPEKINKGINVDDVHSKQPE-HDSTEQSG 701
Cdd:pfam15818 668 GLTIPCDT------VVSHPISPAAFSDNLKADlKNSDNNVNIMPMLVKPNSSPGKRTTRKNLDDMQSSQFKnCLGGLENG 741
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024410660 702 GDESMCTLNAEAMSPVKAHDLDTTVQKVPADGIDVDKL----NEEIQIQSIKNGHSLDINDDSINNSMLK--QEKDSVHS 775
Cdd:pfam15818 742 VTISHLQVNNENSHASQAKDLKTAVHPKTSTEIQFSSKesqiDENQITEATKNDLFLLVNVNERQHTLLNntEKTESLND 821
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024410660 776 TVPGRKFAEGHLKESCSLPMRTSGNLVNVSGRSSFDLSNSDKKAEKTSVCFKFLGLSSCSRVNQMRSQATWTSSSQEPSV 855
Cdd:pfam15818 822 IVSGKIYSEGQLEESHSFHIKPSGDLVNRSGRSAFDLSTSDKKTEKTPVYLNFLDPSPWSKVNQTEGQTVSTSTSSIPLL 901
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024410660 856 LKEKLPCLVENKKVPSRELFQNVSENVGRKETGPGSTSSNRAADTLNTSRIHRDPQGDPTEEWNAIAKTFYDSSFPTEHV 935
Cdd:pfam15818 902 LKEKPIGPSENTKIISVTLCKNVGVDDVRKDIGPDTTSISRVADTLNNSSIHPDPKGEPSEERNATAKTFYDSSFPTEHV 981
|
970 980 990 1000 1010 1020
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024410660 936 KEGFTALNEQKSSPMTVTSAQSERTLGDEDRFPTHNSTVQSQIEEIEKYLNLETLCSSRKRKYED 1000
Cdd:pfam15818 982 KTEPLKSTVLQSHFQTVKIKDSPDLLKSSPGEDDWQSLITNQITEIEKLLSLENDNQPKKRKAEE 1046
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
6-282 |
1.45e-10 |
|
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: 65.46 E-value: 1.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024410660 6 KQLQARMFAMEEEKGKYQLAVEIKEKEIDGLKETLKELQISKHTLQKKLNEMDQKLQmhlTVREEHNKKLNEVERCYATI 85
Cdd:TIGR02168 680 EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLA---RLEAEVEQLEERIAQLSKEL 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024410660 86 ACQFGIVKGVHEKLEHSVQEAIQLNKKLTSVNKRQET---EISNLKEELKKVTTDLIRSKV---TSQHRVGEENINLAAK 159
Cdd:TIGR02168 757 TELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQlkeELKALREALDELRAELTLLNEeaaNLRERLESLERRIAAT 836
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024410660 160 EKQFQELQQKIRMETAISKRVQEENANIKEEKLEILSSLQCVQKQLQQitqtnvrMESELNALREEYQTLERDNELQREK 239
Cdd:TIGR02168 837 ERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERAS-------LEEALALLRSELEELSEELRELESK 909
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 2024410660 240 AKENEEKFLNLQNEHEKAlriwKKDEENLRREMDTIKNELNSL 282
Cdd:TIGR02168 910 RSELRRELEELREKLAQL----ELRLEGLEVRIDNLQERLSEE 948
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
16-283 |
2.37e-10 |
|
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: 64.69 E-value: 2.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024410660 16 EEEKGKYQLAVEIKE--KEIDGLKETLKELQISKHTLQKKLNEMDQKLqmhltvrEEHNKKLNEVERCYATIACQFGIVK 93
Cdd:TIGR02168 222 LRELELALLVLRLEElrEELEELQEELKEAEEELEELTAELQELEEKL-------EELRLEVSELEEEIEELQKELYALA 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024410660 94 GVHEKLEHSVQEAIQLNKKLTSVNKRQETEISNLKEELKKVTTDLIRSKVtsqhRVGEENINLAAKEKQFQELQQKIR-M 172
Cdd:TIGR02168 295 NEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEE----KLEELKEELESLEAELEELEAELEeL 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024410660 173 ETAIS---KRVQEENANIKEEKLEILS---SLQCVQKQLQQITQTNVRMESELNALREEYQTLERDnELQREKAKENEEK 246
Cdd:TIGR02168 371 ESRLEeleEQLETLRSKVAQLELQIASlnnEIERLEARLERLEDRRERLQQEIEELLKKLEEAELK-ELQAELEELEEEL 449
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 2024410660 247 FlNLQNEHE---KALRIWKKDEENLRREMDTIKNELNSLK 283
Cdd:TIGR02168 450 E-ELQEELErleEALEELREELEEAEQALDAAERELAQLQ 488
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1-291 |
5.93e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 63.42 E-value: 5.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024410660 1 MAAFKKQLQARMFAMEEEKGKYQLAVEIKEKEIDGLKETLKELQISKHTLQKKLNEMDQKLQmhltvreEHNKKLNEVER 80
Cdd:COG1196 230 LLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEY-------ELLAELARLEQ 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024410660 81 cyatiacqfgivkgvheKLEHSVQEAIQLNKKLtsvnKRQETEISNLKEELKKVTTDLIRSKVTSQhrvgEENINLAAKE 160
Cdd:COG1196 303 -----------------DIARLEERRRELEERL----EELEEELAELEEELEELEEELEELEEELE----EAEEELEEAE 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024410660 161 KQFQELQQKIRMETAISKRVQEENANIKEEKLEILSSLQCVQKQLQQITQTNVRMESELNALREEYQTLERDNELQREKA 240
Cdd:COG1196 358 AELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEE 437
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 2024410660 241 KENEEKFLNLQNEHEKALRiwkkDEENLRREMDTIKNELNSLKKTQGHLDD 291
Cdd:COG1196 438 EEEEEALEEAAEEEAELEE----EEEALLELLAELLEEAALLEAALAELLE 484
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
5-290 |
2.53e-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: 2.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024410660 5 KKQLQARMFAMEEEKGKYQLAVEIKEKEIDGLKETLKELQISKHTLQKKLNEMDQKLQmHLTVR-EEHNKKLNEVERCYA 83
Cdd:TIGR02168 241 LEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEIS-RLEQQkQILRERLANLERQLE 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024410660 84 TIACQFGIVKgvhEKLEHSVQEAIQLNKKLTSVNKRQEtEISNLKEELKKVTTDLIRSKVTSQHRVGEENINLAAKEKQF 163
Cdd:TIGR02168 320 ELEAQLEELE---SKLDELAEELAELEEKLEELKEELE-SLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQI 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024410660 164 QELQQKI-RMETAISkRVQEENANIKEEKLEILSSLQCVQKQLQQitQTNVRMESELNALREEYQTLERDNELQREKAKE 242
Cdd:TIGR02168 396 ASLNNEIeRLEARLE-RLEDRRERLQQEIEELLKKLEEAELKELQ--AELEELEEELEELQEELERLEEALEELREELEE 472
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 2024410660 243 NEEKFLNLQNEHEKA---LRIWKKDEENLRREMDTIKNELNSLKKTQGHLD 290
Cdd:TIGR02168 473 AEQALDAAERELAQLqarLDSLERLQENLEGFSEGVKALLKNQSGLSGILG 523
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
7-282 |
3.35e-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: 61.23 E-value: 3.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024410660 7 QLQARMFAMEEEKGKYQLAVEIKEKEIDGLKETLKELQISKHTLQKKLNEMDQKLQMHLTVREEHNKKLNEVERCYATIA 86
Cdd:TIGR02168 723 ELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALR 802
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024410660 87 CQFGIVKGVHEKLEHSVQEAIQLNKKLTSVNKRQETEISNLKEELKKVTTDLIRSkvtsQHRVGEENINLAAKEKQFQEL 166
Cdd:TIGR02168 803 EALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESL----AAEIEELEELIEELESELEAL 878
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024410660 167 QQKirmetaisKRVQEENANIKEEKLEILSslqcvqKQLQQITQTNVRMESELNALREEYQTLERD-----NELQREKAK 241
Cdd:TIGR02168 879 LNE--------RASLEEALALLRSELEELS------EELRELESKRSELRRELEELREKLAQLELRlegleVRIDNLQER 944
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 2024410660 242 ENEEKFLNLQNEHEKALRIwKKDEENLRREMDTIKNELNSL 282
Cdd:TIGR02168 945 LSEEYSLTLEEAEALENKI-EDDEEEARRRLKRLENKIKEL 984
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
17-291 |
3.57e-09 |
|
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: 60.85 E-value: 3.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024410660 17 EEKGKYQLAVEIKEKEIDGLKETLKELQISKHT------LQKKLNEMDQKLqmHLTVREEHNKKLNEVERCYATIACQfg 90
Cdd:TIGR02169 177 EELEEVEENIERLDLIIDEKRQQLERLRREREKaeryqaLLKEKREYEGYE--LLKEKEALERQKEAIERQLASLEEE-- 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024410660 91 iVKGVHEKLEHSVQEAIQLNKKLTSVNKR----QETEISNLKEELKKVTTDLIRSKVtsqhrvgeeniNLAAKEKQFQEL 166
Cdd:TIGR02169 253 -LEKLTEEISELEKRLEEIEQLLEELNKKikdlGEEEQLRVKEKIGELEAEIASLER-----------SIAEKERELEDA 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024410660 167 QQKIRmetaiskRVQEENANIKEEKLEILSSLQCVQKQLQQITQTNVRMESELNALREEYQTLERDNELQREKAKENEEK 246
Cdd:TIGR02169 321 EERLA-------KLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREK 393
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 2024410660 247 FLNLQNEHEKALRIWKKDEENLRR---EMDTIKNELNSLKKTQGHLDD 291
Cdd:TIGR02169 394 LEKLKREINELKRELDRLQEELQRlseELADLNAAIAGIEAKINELEE 441
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
5-246 |
1.15e-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: 59.31 E-value: 1.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024410660 5 KKQLQARMFAMEEEKGKYQLAVE------------IKEKEIDGLKETLKELQISKHTLQKKLNEMDQKLQMhltVREEHN 72
Cdd:TIGR02169 760 LKELEARIEELEEDLHKLEEALNdlearlshsripEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEY---LEKEIQ 836
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024410660 73 KKLNEVERCYATIAcqfgivkgvheklehSVQEAIQLNK----KLTSVNKRQETEISNLKEELKKVTTDliRSKVTSQHR 148
Cdd:TIGR02169 837 ELQEQRIDLKEQIK---------------SIEKEIENLNgkkeELEEELEELEAALRDLESRLGDLKKE--RDELEAQLR 899
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024410660 149 VGEENINLAAKEKQFQELQQKIRMETAisKRVQEENANIKEEKLEILS------SLQCVQKQLQQITQTNVRMESELNAL 222
Cdd:TIGR02169 900 ELERKIEELEAQIEKKRKRLSELKAKL--EALEEELSEIEDPKGEDEEipeeelSLEDVQAELQRVEEEIRALEPVNMLA 977
|
250 260
....*....|....*....|....*
gi 2024410660 223 REEYQ-TLERDNELQREKAKENEEK 246
Cdd:TIGR02169 978 IQEYEeVLKRLDELKEKRAKLEEER 1002
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
5-284 |
3.30e-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: 57.77 E-value: 3.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024410660 5 KKQLQARMFAMEEEKGKYQLAVEIKEKEIDGLKETLKEL--QISKHT------LQKKLNEMDQKLQMHLTVREEHNKKLN 76
Cdd:TIGR02169 239 KEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELnkKIKDLGeeeqlrVKEKIGELEAEIASLERSIAEKERELE 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024410660 77 EVERCYATIACQFGIVKGVHEKLEHSVQEaiqLNKKLTSVnkrqETEISNLKEELkkvttDLIRSKvtsqhrvgeeninL 156
Cdd:TIGR02169 319 DAEERLAKLEAEIDKLLAEIEELEREIEE---ERKRRDKL----TEEYAELKEEL-----EDLRAE-------------L 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024410660 157 AAKEKQFQELQQKirmetaiSKRVQEENANIKEEKLEILSSLQCVQKQLQQITQTNVRMESELNALREEYQTLERDNELQ 236
Cdd:TIGR02169 374 EEVDKEFAETRDE-------LKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDK 446
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 2024410660 237 REKAKENEEKFLNLQNEHEKAlriwKKDEENLRREMDTIKNELNSLKK 284
Cdd:TIGR02169 447 ALEIKKQEWKLEQLAADLSKY----EQELYDLKEEYDRVEKELSKLQR 490
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
36-286 |
4.30e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 57.25 E-value: 4.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024410660 36 LKETLKELQISKhtLQKKLNEMDQKLQMHLTVREEHNKKLNEVERCYATIAcqfgivkgvhEKLEHSVQEAIQLNKKLts 115
Cdd:COG1196 218 LKEELKELEAEL--LLLKLRELEAELEELEAELEELEAELEELEAELAELE----------AELEELRLELEELELEL-- 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024410660 116 vNKRQEtEISNLKEELKKVTTDLIRSKVTSQhrvgEENINLAAKEKQFQELQQKIRMETAISKRVQEENANIKEEKLEIL 195
Cdd:COG1196 284 -EEAQA-EEYELLAELARLEQDIARLEERRR----ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAE 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024410660 196 SSLQCVQKQLQQITQTNVRMESELNALREEYQTLERDNELQREKAKENEEKFLNLQNEHEKALRIWKKDEENLRREMDTI 275
Cdd:COG1196 358 AELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEE 437
|
250
....*....|.
gi 2024410660 276 KNELNSLKKTQ 286
Cdd:COG1196 438 EEEEEALEEAA 448
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
47-336 |
7.16e-08 |
|
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: 56.60 E-value: 7.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024410660 47 KHTLQKKLNEMDQKLQMHLTVREEHNKKLNEVERcYATIACQFgivKGVHEKLEH-----SVQEAIQLNKKLTSVN---K 118
Cdd:TIGR02168 174 RKETERKLERTRENLDRLEDILNELERQLKSLER-QAEKAERY---KELKAELRElelalLVLRLEELREELEELQeelK 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024410660 119 RQETEISNLKEELKKVTTDL--IRSKVTS--------QHRVGEENINLAAKEKQFQELQQKIRMETAISKRVQEENANIK 188
Cdd:TIGR02168 250 EAEEELEELTAELQELEEKLeeLRLEVSEleeeieelQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELE 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024410660 189 EEKLEILSSLQCVQKQLQQITQTNVRMESELNALREEYQTLERDNELQREKAKENEEKFLNLQNEHEKAlriwKKDEENL 268
Cdd:TIGR02168 330 SKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASL----NNEIERL 405
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024410660 269 RREMDTIKNELNSLKKTQ-GHLDDCHPPQGNQHSEQVENL--QIHSTVHPIIRNSGQEQSKGSEIQAIQKE 336
Cdd:TIGR02168 406 EARLERLEDRRERLQQEIeELLKKLEEAELKELQAELEELeeELEELQEELERLEEALEELREELEEAEQA 476
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
6-263 |
1.72e-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: 1.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024410660 6 KQLQARMFAMEEEkgkyqlaVEIKEKEIDGLKETLKELQISKHTLQKKLNEMDQKLQMHLTVREEHNKKLNEVErcyati 85
Cdd:COG1196 284 EEAQAEEYELLAE-------LARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAE------ 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024410660 86 acqfgivkgvhEKLEHSVQEAIQLNKKLTSVNKRQETEISNLKEELkkvttdliRSKVTSQHRVGEENINLAAKEKQFQE 165
Cdd:COG1196 351 -----------EELEEAEAELAEAEEALLEAEAELAEAEEELEELA--------EELLEALRAAAELAAQLEELEEAEEA 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024410660 166 LQQKIRMETAISKRVQEENANIKEEKLEILSSLQCVQKQLQQITQTNVRMESELNALREEYQTLER---DNELQREKAKE 242
Cdd:COG1196 412 LLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAalaELLEELAEAAA 491
|
250 260
....*....|....*....|.
gi 2024410660 243 NEEKFLNLQNEHEKALRIWKK 263
Cdd:COG1196 492 RLLLLLEAEADYEGFLEGVKA 512
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
29-279 |
3.56e-06 |
|
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: 50.53 E-value: 3.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024410660 29 KEKEIDGLKETLKElqiskhtLQKKLNEMDQKLQMHLTVREEHNKKLNEVERcyatiacqfgivkgvheKLEHSVQEAIQ 108
Cdd:COG4942 25 AEAELEQLQQEIAE-------LEKELAALKKEEKALLKQLAALERRIAALAR-----------------RIRALEQELAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024410660 109 LNKKLTSVNKRQETeisnLKEELKKVTTDLIRSKVTSQHRVGEENINLAAKEKQFQELQQKIRMETAISKRVQEENANIK 188
Cdd:COG4942 81 LEAELAELEKEIAE----LRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024410660 189 EEKLEIlsslqcvQKQLQQITQTNVRMESELNALREEYQTLERDNELQREKAKENEEKflnlQNEHEKALRIWKKDEENL 268
Cdd:COG4942 157 ADLAEL-------AALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKE----LAELAAELAELQQEAEEL 225
|
250
....*....|.
gi 2024410660 269 RREMDTIKNEL 279
Cdd:COG4942 226 EALIARLEAEA 236
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
30-259 |
7.26e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.44 E-value: 7.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024410660 30 EKEIDGLKETLKELQISKHTLQKKLNEMDQKLqmhltvrEEHNKKLNEVErcyatiacqfgivkgvhEKLEHSVQEAIQL 109
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAEL-------EELNEEYNELQ-----------------AELEALQAEIDKL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024410660 110 NKKLTsvnkRQETEISNLKEELKKvttdLIRSKVTSQHRVGEENINLAAKEkqFQELQQKIRMETAISKRVQEENANIKE 189
Cdd:COG3883 71 QAEIA----EAEAEIEERREELGE----RARALYRSGGSVSYLDVLLGSES--FSDFLDRLSALSKIADADADLLEELKA 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024410660 190 EKLEILSSLQCVQKQLQQITQTNVRMES---ELNALREEYQTLERDNELQREKAKENEEKFLNLQNEHEKALR 259
Cdd:COG3883 141 DKAELEAKKAELEAKLAELEALKAELEAakaELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAA 213
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
15-284 |
1.06e-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: 49.73 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024410660 15 MEEEKGKYQLAVEIKEKEIDGLKETLKELQISKHTLQKKLNEMDQKLQ-----MH-----LTVREEHNKKL--------- 75
Cdd:pfam15921 333 LREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQklladLHkrekeLSLEKEQNKRLwdrdtgnsi 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024410660 76 -------------NEVERCYATIACQFGIVKGVHEKLEHSVQEAIQLNKKLTSVNKRQETEisnlKEELKKVTTDLIRSK 142
Cdd:pfam15921 413 tidhlrrelddrnMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLEST----KEMLRKVVEELTAKK 488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024410660 143 VT---SQHRVGEENINLAAKEK------------------QFQELQQkIRMETAISKRVQEENANIKEEKLEILSSLQCV 201
Cdd:pfam15921 489 MTlesSERTVSDLTASLQEKERaieatnaeitklrsrvdlKLQELQH-LKNEGDHLRNVQTECEALKLQMAEKDKVIEIL 567
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024410660 202 QKQLQQITQ--------------TNVRMESELNALREEYQTLERDNELQREKAKENEE----------KFLNLQNEHEKA 257
Cdd:pfam15921 568 RQQIENMTQlvgqhgrtagamqvEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEArvsdlelekvKLVNAGSERLRA 647
|
330 340
....*....|....*....|....*..
gi 2024410660 258 LRIWKKDEENLRREMDTIKNELNSLKK 284
Cdd:pfam15921 648 VKDIKQERDQLLNEVKTSRNELNSLSE 674
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2-291 |
4.30e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.75 E-value: 4.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024410660 2 AAFKKQLQARMFAMEEEKGKYQLAVEIKEKEIDGLKETLKELQISKHTLQKKLNEMDQKLQMHLTVREEHNKKLNEVERC 81
Cdd:PRK03918 355 EELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKA 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024410660 82 YATI-ACQFGIVKGVHEKLEHSVQEAIqlnKKLTSVNKRQETEISNLKEELKKVTTDLIR-SKVTSQHRVGEENINLAAK 159
Cdd:PRK03918 435 KGKCpVCGRELTEEHRKELLEEYTAEL---KRIEKELKEIEEKERKLRKELRELEKVLKKeSELIKLKELAEQLKELEEK 511
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024410660 160 EKQF--QELQQKirmetaiskrvQEENANIKEEKLEILSSLQCVQKQLQQITQTNVR---MESELNALREEYQTLERD-N 233
Cdd:PRK03918 512 LKKYnlEELEKK-----------AEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKlaeLEKKLDELEEELAELLKElE 580
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 2024410660 234 ELQREKAKENEEKFLNLQNEHEKALRIwKKDEENLRREMDTIKNELNSLKKTQGHLDD 291
Cdd:PRK03918 581 ELGFESVEELEERLKELEPFYNEYLEL-KDAEKELEREEKELKKLEEELDKAFEELAE 637
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
31-284 |
7.86e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.60 E-value: 7.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024410660 31 KEIDGLKETLKELQISKHTLQKKLNEMDQKLQMHLTVREEHNKKLNEVERcyatiacQFGIVKGVHEKLEHSVQEAIQLN 110
Cdd:PRK03918 172 KEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELRE-------ELEKLEKEVKELEELKEEIEELE 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024410660 111 KKLTSVNKRQ---ETEISNLK---EELKKVTTDL--IRSKVTSQHRVGEENINLAAKEKQFQELQQKIRMETAiskRVQE 182
Cdd:PRK03918 245 KELESLEGSKrklEEKIRELEeriEELKKEIEELeeKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLS---RLEE 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024410660 183 ENANIkEEKLEILSSLQcvqKQLQQITQTNVRMESELNALREEYQTLER----DNELQREKAK---ENEEKFLNLQNEHE 255
Cdd:PRK03918 322 EINGI-EERIKELEEKE---ERLEELKKKLKELEKRLEELEERHELYEEakakKEELERLKKRltgLTPEKLEKELEELE 397
|
250 260
....*....|....*....|....*....
gi 2024410660 256 KALRIWKKDEENLRREMDTIKNELNSLKK 284
Cdd:PRK03918 398 KAKEEIEEEISKITARIGELKKEIKELKK 426
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
31-284 |
9.35e-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: 45.91 E-value: 9.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024410660 31 KEIDGLKETLKELQISKHTLQKKLNEMDQKLQMHLTVREEHNKKLNEVERcyatiacqfgivkgvheKLEHSVQEAIQLN 110
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALAR-----------------RIRALEQELAALE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024410660 111 KKLTSVNKRQETeisnLKEELKKVTTDLIRSKVTSQHRVGEENINLAAKEKQFQELQQKIRMETAISKRVQEENANIKEE 190
Cdd:COG4942 83 AELAELEKEIAE----LRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRAD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024410660 191 kleilsslqcvQKQLQQITQtnvrmesELNALREEYQTLERDNELQREKAKENEEKFLNLQNEHEKALRIWKKDEENLRR 270
Cdd:COG4942 159 -----------LAELAALRA-------ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQ 220
|
250
....*....|....
gi 2024410660 271 EMDTIKNELNSLKK 284
Cdd:COG4942 221 EAEELEALIARLEA 234
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
30-238 |
1.03e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.16 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024410660 30 EKEIDGLKETLKELQ--ISKHTLQKKLNEMDQKLQMHLTVREEHNKKLNEVERCYATIACQFGIVKgvhEKLEHSVQEAI 107
Cdd:COG3206 181 EEQLPELRKELEEAEaaLEEFRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALR---AQLGSGPDALP 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024410660 108 QLNkkltsvnkrQETEISNLKEELKKVTTDL--IRSKVTSQHRvgeeninlaakekQFQELQQKIR-METAISKRVQEEN 184
Cdd:COG3206 258 ELL---------QSPVIQQLRAQLAELEAELaeLSARYTPNHP-------------DVIALRAQIAaLRAQLQQEAQRIL 315
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2024410660 185 ANIKEEKLEILSSLQCVQKQLQQITQtnvRMeSELNALREEYQTLERDNELQRE 238
Cdd:COG3206 316 ASLEAELEALQAREASLQAQLAQLEA---RL-AELPELEAELRRLEREVEVARE 365
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2-211 |
1.14e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.91 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024410660 2 AAFKKQLQARMFAMEEEKGKyqlAVEIKEKEIDGLKETLKELQISKHTLQKKLNEMDQKLQMHLTVREEHNKKLNEVERC 81
Cdd:COG4717 45 AMLLERLEKEADELFKPQGR---KPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024410660 82 YATIACQFGIVKGVH--EKLEHSVQEAIQLNKKLTSVnKRQETEISNLKEELKKVTTDLIRSKVTSQHRVGEEninLAAK 159
Cdd:COG4717 122 EKLLQLLPLYQELEAleAELAELPERLEELEERLEEL-RELEEELEELEAELAELQEELEELLEQLSLATEEE---LQDL 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2024410660 160 EKQFQELQQKIRMETAISKRVQEENANIKEEkLEILSSLQCVQKQLQQITQT 211
Cdd:COG4717 198 AEELEELQQRLAELEEELEEAQEELEELEEE-LEQLENELEAAALEERLKEA 248
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
6-291 |
1.32e-04 |
|
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: 45.78 E-value: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024410660 6 KQLQARMFAMEEEKGKYQLAVEIKEKEIDGLKETLKELQISKHTLQKKLNEMDQKLQMHLTVREEHNKKLNEVERCYATI 85
Cdd:TIGR04523 214 KSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024410660 86 ACQF---------GIVKGVHEKLEHSVQEAIQLNKKLTSVNKRqeteISNLKEELKKVTTDLIRSKVTSQhrvgeeninl 156
Cdd:TIGR04523 294 KSEIsdlnnqkeqDWNKELKSELKNQEKKLEEIQNQISQNNKI----ISQLNEQISQLKKELTNSESENS---------- 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024410660 157 aAKEKQFQELQQKIRMETAISKRVQEENANIKEEKLEILSSLQCVQKQLQQITQTNVRMESELNALREEYQTLERDNELQ 236
Cdd:TIGR04523 360 -EKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKN 438
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 2024410660 237 REKAKENEEKFLNLQNEHEKALRIWKKDEENLRREMDTIKNELNSLKKTQGHLDD 291
Cdd:TIGR04523 439 NSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKS 493
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
13-279 |
1.53e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.83 E-value: 1.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024410660 13 FAMEEEKGKYQLAVEIKEK------EIDGLKETLKELQiskhTLQKKLNEMDQKLQmhlTVREEHNKKLNEVERCyatia 86
Cdd:PRK03918 515 YNLEELEKKAEEYEKLKEKliklkgEIKSLKKELEKLE----ELKKKLAELEKKLD---ELEEELAELLKELEEL----- 582
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024410660 87 cQFGIVKGVHEKLEhSVQEAiqLNKKLTSVNKRQETEIsnLKEELKKVTTDLIRSKVtsqhrvgeeniNLAAKEKQFQEL 166
Cdd:PRK03918 583 -GFESVEELEERLK-ELEPF--YNEYLELKDAEKELER--EEKELKKLEEELDKAFE-----------ELAETEKRLEEL 645
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024410660 167 QQKIrmETAISKRVQEENANIKEEKLEILSSLQCVQKQLQQITQTNVRMESELNALREEYQTlerdnelqREKAKENEEK 246
Cdd:PRK03918 646 RKEL--EELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEE--------REKAKKELEK 715
|
250 260 270
....*....|....*....|....*....|...
gi 2024410660 247 FlnlqnehEKALriwkKDEENLRREMDTIKNEL 279
Cdd:PRK03918 716 L-------EKAL----ERVEELREKVKKYKALL 737
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
156-289 |
2.39e-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: 2.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024410660 156 LAAKEKQFQELQQKIRMETAISKRVQEENANIKEEKLEILSSLQCVQKQLQQITQTNVRMESELNALREEYQTLERDNEL 235
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEA 101
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024410660 236 QREKAKE-----------NEEKFLNLQ---NEHEKALRIWKKDEENLRREMDTIKNELNSLKKTQGHL 289
Cdd:COG4942 102 QKEELAEllralyrlgrqPPLALLLSPedfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAEL 169
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
30-385 |
2.48e-04 |
|
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: 45.01 E-value: 2.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024410660 30 EKEIDGLKETLKELQISKHTLQKKLNEMDQKLQmhlTVREEHNKKLNEVERcyatiacqfgivkgVHEKLEHSVQEAIQL 109
Cdd:TIGR04523 217 ESQISELKKQNNQLKDNIEKKQQEINEKTTEIS---NTQTQLNQLKDEQNK--------------IKKQLSEKQKELEQN 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024410660 110 NKKLTSVNKR---QETEISNLKEELKKVTTDLIRSKVTSQHRVGEENIN-LAAKEKQFQELQQKIRMETAISKRVQEENA 185
Cdd:TIGR04523 280 NKKIKELEKQlnqLKSEISDLNNQKEQDWNKELKSELKNQEKKLEEIQNqISQNNKIISQLNEQISQLKKELTNSESENS 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024410660 186 NIKEEKLEILSSLQCVQKQLQQITQTNVRMESELNALREEYQTLERDNELQREKAKENEEKFLNLQNEHE--KALRIWKK 263
Cdd:TIGR04523 360 EKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIErlKETIIKNN 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024410660 264 DE-ENLRREMDTIKNELNSLKKTQGHLddchppqgnQHSEQVENLQIHSTVHPIIRNSGQEQSKGSEIQAIQKENdcmps 342
Cdd:TIGR04523 440 SEiKDLTNQDSVKELIIKNLDNTRESL---------ETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEK----- 505
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 2024410660 343 ILRKDNNFGHEDEIEVKNTVSFSLSTEELQIEQKLQVLENGFK 385
Cdd:TIGR04523 506 KELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELN 548
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
16-290 |
3.53e-04 |
|
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: 44.71 E-value: 3.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024410660 16 EEEKGKYQ---LAVEIKEKEIDGLKETLKELQISKHTLQKKLNEMDQKLQmhltvreehNKKLNEVERCYATIACQFGIV 92
Cdd:pfam05483 432 EELKGKEQeliFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELE---------KEKLKNIELTAHCDKLLLENK 502
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024410660 93 KGVHEKLEHSV-----QEAIQLNKK-----LTSVNKRQETEIsNLKEELKKVTTDLI--RSKVTSQHRVGEENINLAAKE 160
Cdd:pfam05483 503 ELTQEASDMTLelkkhQEDIINCKKqeermLKQIENLEEKEM-NLRDELESVREEFIqkGDEVKCKLDKSEENARSIEYE 581
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024410660 161 KQFQELQQKIRMETAISKRVQEENANIKEEKLeilsslqcvQKQLQQITQTNVRMESELNAlreeYQTLERDNELQREKA 240
Cdd:pfam05483 582 VLKKEKQMKILENKCNNLKKQIENKNKNIEEL---------HQENKALKKKGSAENKQLNA----YEIKVNKLELELASA 648
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 2024410660 241 KEneeKFLNLQNEHEKALRIWKKDEENLRREMDTIKNELNSLKKTQGHLD 290
Cdd:pfam05483 649 KQ---KFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEID 695
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
6-210 |
3.96e-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: 43.98 E-value: 3.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024410660 6 KQLQARMFAMEEEKGKYQLAVEIKEKEIDGLKETLKELQISKHTLQKKLNEMDQKLQMHLTVREEHNKKLNEVERCYATI 85
Cdd:COG4942 37 AELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024410660 86 ACQFGIVKGVHEKlehSVQEAIQLNKKLTSVNKRQETEIsnlkEELKKVTTDLIRSKVTSQHRVGEENINLAAKEKQFQE 165
Cdd:COG4942 117 GRQPPLALLLSPE---DFLDAVRRLQYLKYLAPARREQA----EELRADLAELAALRAELEAERAELEALLAELEEERAA 189
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2024410660 166 LQQKIRMETAISKRVQEENANIKEEKLEILSSLQCVQKQLQQITQ 210
Cdd:COG4942 190 LEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEA 234
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
96-290 |
4.21e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.52 E-value: 4.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024410660 96 HEKLEHSVQEAIQLNKKLTSVNKRQ-----ETEISNLKEELKKVTTDLirskvtsqhrvgeeninlAAKEKQFQELQQKI 170
Cdd:COG4913 264 YAAARERLAELEYLRAALRLWFAQRrlellEAELEELRAELARLEAEL------------------ERLEARLDALREEL 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024410660 171 R-METAISKRVQEENANIKEEkleilssLQCVQKQLQQITQTNVRMESELNALREEYQTLERDNELQREKAKENEEKFLN 249
Cdd:COG4913 326 DeLEAQIRGNGGDRLEQLERE-------IERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEE 398
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2024410660 250 LQNEHEKALRIWKKDEENLRREMDTIKNELNSLKKTQGHLD 290
Cdd:COG4913 399 ELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIP 439
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
3-286 |
4.32e-04 |
|
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: 44.19 E-value: 4.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024410660 3 AFKKQLQARMFAMEEEKGKYQLAVEIKEKEIDGLKETLKELQISKHTLQKKLNEMDQKLQMHltvreehnKKLNEVERCY 82
Cdd:TIGR00618 198 LLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQ--------QLLKQLRARI 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024410660 83 ATIACQFGIVKGVHEKLEHSVQEA--IQLNKKLTSVNKRQETEISNLKEELKKVTTDLIRSKVTSQHRvgeeninlAAKE 160
Cdd:TIGR00618 270 EELRAQEAVLEETQERINRARKAAplAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQ--------SSIE 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024410660 161 KQFQELQQKIRMETAIsKRVQEENANIKEEKLEILSSLQCVQKQLQQIT---QTNVRMESELNALREEYQTLE----RDN 233
Cdd:TIGR00618 342 EQRRLLQTLHSQEIHI-RDAHEVATSIREISCQQHTLTQHIHTLQQQKTtltQKLQSLCKELDILQREQATIDtrtsAFR 420
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 2024410660 234 ELQREKAK-----ENEEKFLNLQNEH-EKALRIWKKDEENLRREMDTIKNELNSLKKTQ 286
Cdd:TIGR00618 421 DLQGQLAHakkqqELQQRYAELCAAAiTCTAQCEKLEKIHLQESAQSLKEREQQLQTKE 479
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
37-289 |
6.07e-04 |
|
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: 43.80 E-value: 6.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024410660 37 KETLKELQISKHTLQKKLNEMDQKLQMHlTVREEHNKKLNEVERCYATIACQFGIVKGVHEKLEHSVQEAIQ-------- 108
Cdd:TIGR00618 166 KELLMNLFPLDQYTQLALMEFAKKKSLH-GKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQqtqqshay 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024410660 109 LNKKLTSVNKRQ--ETEISNLKEELKKVTTDLIRskvtsqHRVGEENINLAAKEKQFQELQQKIrmeTAISKRVQEENAN 186
Cdd:TIGR00618 245 LTQKREAQEEQLkkQQLLKQLRARIEELRAQEAV------LEETQERINRARKAAPLAAHIKAV---TQIEQQAQRIHTE 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024410660 187 IKEEKLEILSSLQCVQKQLQQiTQTNVRMESELNALREEYQTLERDNELQR------EKAKENEEKFLNLQNEHEKA--- 257
Cdd:TIGR00618 316 LQSKMRSRAKLLMKRAAHVKQ-QSSIEEQRRLLQTLHSQEIHIRDAHEVATsireisCQQHTLTQHIHTLQQQKTTLtqk 394
|
250 260 270
....*....|....*....|....*....|..
gi 2024410660 258 LRIWKKDEENLRREMDTIKNELNSLKKTQGHL 289
Cdd:TIGR00618 395 LQSLCKELDILQREQATIDTRTSAFRDLQGQL 426
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
104-291 |
6.48e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.60 E-value: 6.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024410660 104 QEAIQLNKKLTSVNKRQETEISNLKEELK--KVTTDLIRSKVTSQHRVGEEninLAAKEKQFQELQQKIR-METAISKR- 179
Cdd:COG4717 53 KEADELFKPQGRKPELNLKELKELEEELKeaEEKEEEYAELQEELEELEEE---LEELEAELEELREELEkLEKLLQLLp 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024410660 180 VQEENANIKEEKLEILSSLQCVQKQLQQITQtnvrMESELNALREEYQTLERD-NELQREKAKENEEKFLNLQNEHE--- 255
Cdd:COG4717 130 LYQELEALEAELAELPERLEELEERLEELRE----LEEELEELEAELAELQEElEELLEQLSLATEEELQDLAEELEelq 205
|
170 180 190
....*....|....*....|....*....|....*.
gi 2024410660 256 KALRIWKKDEENLRREMDTIKNELNSLKKTQGHLDD 291
Cdd:COG4717 206 QRLAELEEELEEAQEELEELEEELEQLENELEAAAL 241
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
17-288 |
6.73e-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: 43.95 E-value: 6.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024410660 17 EEKGKYQLAVEIKEKEIDGLKETLKE----LQISKHTLQKKLNEMDQKLQ--MHLTVREEHNKKLN-EVERCYATIACQF 89
Cdd:pfam15921 482 EELTAKKMTLESSERTVSDLTASLQEkeraIEATNAEITKLRSRVDLKLQelQHLKNEGDHLRNVQtECEALKLQMAEKD 561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024410660 90 GIVKGVHEKLEHSVQEAIQLNKKLTS--VNKRQ-ETEISNLKEELKKVTtdLIRSKVTSQHRvgeeniNLAAKEKQFQel 166
Cdd:pfam15921 562 KVIEILRQQIENMTQLVGQHGRTAGAmqVEKAQlEKEINDRRLELQEFK--ILKDKKDAKIR------ELEARVSDLE-- 631
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024410660 167 QQKIRMETAISKRVQEENaNIKEEKLEILSSLQCVQkqlqqitqtnvrmeSELNALREEYQTLERDnelqrekakeneek 246
Cdd:pfam15921 632 LEKVKLVNAGSERLRAVK-DIKQERDQLLNEVKTSR--------------NELNSLSEDYEVLKRN-------------- 682
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 2024410660 247 FLNLQNEHEKALRIWKKDEENLRREMDTIKNELNSLKKTQGH 288
Cdd:pfam15921 683 FRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGH 724
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
189-291 |
8.03e-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: 8.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024410660 189 EEKLEILSSLQCVQKQLQQITQTNVRMESELNALREEYQTLERDNELQREKAKENEEKFLNLQNEHEKALRIWKKDEENL 268
Cdd:COG1579 3 PEDLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQL 82
|
90 100
....*....|....*....|....*...
gi 2024410660 269 R-----REMDTIKNELNSLKKTQGHLDD 291
Cdd:COG1579 83 GnvrnnKEYEALQKEIESLKRRISDLED 110
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
23-339 |
8.18e-04 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 43.19 E-value: 8.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024410660 23 QLAVEIKEKEIDGlKETLKELQISKHTLQKKLN---EMDQKLQMHLTVRE----EHNKKLNE-VERCYATIACQFGIVKG 94
Cdd:pfam05557 13 QLQNEKKQMELEH-KRARIELEKKASALKRQLDresDRNQELQKRIRLLEkreaEAEEALREqAELNRLKKKYLEALNKK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024410660 95 VHEKlEHSVQEAIQLNKKLTSVNKRQETEISNLKEELKKVTTDLIRSkvtsQHRVGEENINLAAKEKQFQELQQKIRMET 174
Cdd:pfam05557 92 LNEK-ESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEEL----QERLDLLKAKASEAEQLRQNLEKQQSSLA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024410660 175 AISKRVQEenaniKEEKLEILSSLQCVQKQLQQITQTNVRMESELNALREE---YQTLERDNELQREKAKENEEKFLNLQ 251
Cdd:pfam05557 167 EAEQRIKE-----LEFEIQSQEQDSEIVKNSKSELARIPELEKELERLREHnkhLNENIENKLLLKEEVEDLKRKLEREE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024410660 252 NEHEKALriwkkdeeNLRREMDTIKNELNSLKKT-QGHLDDCHPPQgnQHSEQVENLQIHSTVHPIIRNSGQEQSKGSEI 330
Cdd:pfam05557 242 KYREEAA--------TLELEKEKLEQELQSWVKLaQDTGLNLRSPE--DLSRRIEQLQQREIVLKEENSSLTSSARQLEK 311
|
....*....
gi 2024410660 331 QAIQKENDC 339
Cdd:pfam05557 312 ARRELEQEL 320
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
146-289 |
8.72e-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: 8.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024410660 146 QHRVGEENINLAAKEKQFQELQQKIrmeTAISKRVQEENANIKEEKLEILSslqcVQKQLQQIT--QTNVRMESELNALR 223
Cdd:COG1579 23 EHRLKELPAELAELEDELAALEARL---EAAKTELEDLEKEIKRLELEIEE----VEARIKKYEeqLGNVRNNKEYEALQ 95
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024410660 224 EEYQTLERDNELQREKAKENEEKFLNLQNEHEKALRIWKKDEENLRREMDTIKNELNSLKKTQGHL 289
Cdd:COG1579 96 KEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEEL 161
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
104-291 |
1.00e-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: 42.44 E-value: 1.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024410660 104 QEAIQLNKKLTSVNKrqetEISNLKEELKKVTTDliRSKVTSQHRVGEENINLAAK-----EKQFQELQQKIRmetAISK 178
Cdd:COG4942 20 DAAAEAEAELEQLQQ----EIAELEKELAALKKE--EKALLKQLAALERRIAALARriralEQELAALEAELA---ELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024410660 179 RVQEENANIKEEKLEILSSLQCVQKQ------------------------LQQITQTNVRMESELNALREEYQTLERDNE 234
Cdd:COG4942 91 EIAELRAELEAQKEELAELLRALYRLgrqpplalllspedfldavrrlqyLKYLAPARREQAEELRADLAELAALRAELE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2024410660 235 LQREKAKENEEKFLNLQNEHEKALRIWKKDEENLRREMDTIKNELNSLKKTQGHLDD 291
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEA 227
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
151-265 |
1.17e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 42.92 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024410660 151 EENINLAAKEKQFQELQQKIrmetaisKRVQEENANIK---EEKLEILSSLQCVQKQLQQITQTNVRMESELNALREEYQ 227
Cdd:COG2433 403 HEERELTEEEEEIRRLEEQV-------ERLEAEVEELEaelEEKDERIERLERELSEARSEERREIRKDREISRLDREIE 475
|
90 100 110
....*....|....*....|....*....|....*...
gi 2024410660 228 TLERdnELQREKaKENEEkflnLQNEHEKALRIWKKDE 265
Cdd:COG2433 476 RLER--ELEEER-ERIEE----LKRKLERLKELWKLEH 506
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
29-235 |
1.45e-03 |
|
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
Pssm-ID: 310534 [Multi-domain] Cd Length: 258 Bit Score: 41.63 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024410660 29 KEKEIDGLKETLKELQISKHTLQKKLNEMDQKLQmhlTVREEHNKKLNEVERCYATIacqfgivKGVHEKLEHSVQEAIQ 108
Cdd:pfam06008 38 HKIQIEILEKELSSLAQETEELQKKATQTLAKAQ---QVNAESERTLGHAKELAEAI-------KNLIDNIKEINEKVAT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024410660 109 LNKKLtsvNKRQETEISNLKEELKKVtTDLIRSKVTSQHRVGEENINLAAKE--KQFQELQQKIRMETAISKRVQEENAN 186
Cdd:pfam06008 108 LGEND---FALPSSDLSRMLAEAQRM-LGEIRSRDFGTQLQNAEAELKAAQDllSRIQTWFQSPQEENKALANALRDSLA 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2024410660 187 IKEEKLEIL-SSLQCVQKQLQQITQTNVRMESELNALREEYQTLERDNEL 235
Cdd:pfam06008 184 EYEAKLSDLrELLREAAAKTRDANRLNLANQANLREFQRKKEEVSEQKNQ 233
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
118-291 |
1.52e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.20 E-value: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024410660 118 KRQETEISNLKEELKKVTTDLIRSKVTSQhrvgEENINLAAKEKQFQELQQKIRMETAISKRVQEENANIKEEKLEILSS 197
Cdd:COG4372 41 DKLQEELEQLREELEQAREELEQLEEELE----QARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024410660 198 LQCVQKQLQQITQTNVRMESELNALREEYQTLERDNELQREKAKENEEKFLNLQNEHEKAlriwkkDEENLRREMDTIKN 277
Cdd:COG4372 117 LEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQAL------SEAEAEQALDELLK 190
|
170
....*....|....
gi 2024410660 278 ELNSLKKTQGHLDD 291
Cdd:COG4372 191 EANRNAEKEEELAE 204
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
14-290 |
1.61e-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: 42.65 E-value: 1.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024410660 14 AMEEEKGKYQLAVEIKEKEIDGLKETLKELQISKHTLQKKLNEMDQKLQMHLTVR---EEHNKKLNEVERCYATIAcqfg 90
Cdd:TIGR00618 581 RSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQqcsQELALKLTALHALQLTLT---- 656
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024410660 91 ivkgvHEKLEHSVQEAIQLNKKLTSVNKRQETEISNLKEELK--KVTTDLIRSKVTSQHRVGEENinlaakEKQFQELQQ 168
Cdd:TIGR00618 657 -----QERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTywKEMLAQCQTLLRELETHIEEY------DREFNEIEN 725
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024410660 169 KirMETAISKRVQEENA-NIKEEKLEILSSLQCvqKQLQQITQTNVRMESELNALREEYQTLERDNELQREKAKENEEKF 247
Cdd:TIGR00618 726 A--SSSLGSDLAAREDAlNQSLKELMHQARTVL--KARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLL 801
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 2024410660 248 LNLQNEHEKALR----IWKKDEENLRREMDTIKNELNSLKKTQGHLD 290
Cdd:TIGR00618 802 KTLEAEIGQEIPsdedILNLQCETLVQEEEQFLSRLEEKSATLGEIT 848
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1-230 |
1.94e-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: 42.41 E-value: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024410660 1 MAAFKKQLQARMFAMEEEKGKYQLAVEIKEKEIDGLKETLKELQISKHTLqkkLNEMDQKLQMHLTVREEHNKKLNEVER 80
Cdd:pfam15921 588 MQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKL---VNAGSERLRAVKDIKQERDQLLNEVKT 664
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024410660 81 CyatiacqfgivkgvHEKLEHSVQEAIQLNKKLTSVNKRQETEISNLKEELKKVTTDLIRSKVTSQHRVGEE-------- 152
Cdd:pfam15921 665 S--------------RNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDghamkvam 730
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024410660 153 --NINLAAKEKQFQELQQKIRMETAISKRVQEENANIKEEKLEILSSLQCVQkqlqqiTQTNvRMESELNALREEYQTLE 230
Cdd:pfam15921 731 gmQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVA------TEKN-KMAGELEVLRSQERRLK 803
|
|
| ANIS5_cation-bd |
pfam02520 |
SXP/RAL-2 family protein Ani s 5-like, metal-binding domain; This domain is found in proteins ... |
152-226 |
2.64e-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: 38.33 E-value: 2.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024410660 152 ENINLAAKEKQFQELQQKIRMETAIS---KRVQEENANIKEEKLEILSSLQCVQKQLQQI----TQTNVRMESELNALRE 224
Cdd:pfam02520 12 ETLTIAEKEEQLAAWAEKYGVTDQYKefqANVTALKEEVKKNVTAVISNLSSVLNQLSAIldnkNQTRAQQHEAIDALKQ 91
|
..
gi 2024410660 225 EY 226
Cdd:pfam02520 92 QY 93
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
5-134 |
3.08e-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: 38.75 E-value: 3.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024410660 5 KKQLQARMFAMEEEKGKYQLAVEIKEKEIDGLKETLKELQISKHTLQKKLNEMDQKLQmhltvREEHNKKLNEVERcyat 84
Cdd:pfam20492 8 KQELEERLKQYEEETKKAQEELEESEETAEELEEERRQAEEEAERLEQKRQEAEEEKE-----RLEESAEMEAEEK---- 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 2024410660 85 iacqfgivkgvhEKLEHSVQEAIQLNKKLTSVNKRQETEISNLKEELKKV 134
Cdd:pfam20492 79 ------------EQLEAELAEAQEEIARLEEEVERKEEEARRLQEELEEA 116
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
140-260 |
3.16e-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: 3.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024410660 140 RSKVTSQHRVGEENIN-LAAKEKQFQELQQKIRMETAISKRVQEENANIkEEKLEILSSLQCV----------------- 201
Cdd:COG4913 595 RRRIRSRYVLGFDNRAkLAALEAELAELEEELAEAEERLEALEAELDAL-QERREALQRLAEYswdeidvasaereiael 673
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024410660 202 QKQLQQITQTNV---RMESELNALREEYQTLERDNELQREKAKENEEKFLNLQNEHEKALRI 260
Cdd:COG4913 674 EAELERLDASSDdlaALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDR 735
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
11-245 |
3.35e-03 |
|
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: 41.31 E-value: 3.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024410660 11 RMFAMEEEKGKYQLAVEIKEKEIDGLKETLKELQISKHTLQKKLNEMDQKLQMhltvREEHNKKLNEvERcyatiacqfg 90
Cdd:pfam01576 90 RSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILL----LEDQNSKLSK-ER---------- 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024410660 91 ivKGVHEKL---EHSVQEAIQLNKKLTSVNKRQETEISNLKEELKK-----------------VTTDLIRSKVTSQHRVG 150
Cdd:pfam01576 155 --KLLEERIsefTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKeekgrqelekakrklegESTDLQEQIAELQAQIA 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024410660 151 EENINLAAKEKQFQELQQKIRMETAISKRVQEENANIKEEKLEILSSLQCVQKQLQQITQTNVRMESELNALREEYQ-TL 229
Cdd:pfam01576 233 ELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEdTL 312
|
250
....*....|....*.
gi 2024410660 230 ERDNELQREKAKENEE 245
Cdd:pfam01576 313 DTTAAQQELRSKREQE 328
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
6-185 |
3.38e-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: 40.90 E-value: 3.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024410660 6 KQLQARMFAMEEEKGKYQLAVEIKEKEIDGLKETLKELQISKHTLQKKLNEMDQKLQMHLTVREE----HNKKLNEVERC 81
Cdd:COG4942 58 AALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLalllSPEDFLDAVRR 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024410660 82 YATIACQFGIVKGVHEKLEHSVQEAIQLNKKLTSVNKRQETEISNLKEELKKVTTDLIRSKVTS---QHRVGEENINLAA 158
Cdd:COG4942 138 LQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLarlEKELAELAAELAE 217
|
170 180
....*....|....*....|....*...
gi 2024410660 159 KEKQFQELQQKI-RMETAISKRVQEENA 185
Cdd:COG4942 218 LQQEAEELEALIaRLEAEAAAAAERTPA 245
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
7-284 |
5.23e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.82 E-value: 5.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024410660 7 QLQARMFAMEEEKGKYQLAVEIKEKEIDGLKETLKELQiskhTLQKKLNEMDQKLQMHLTVRE---EHNKKLNEVERCYA 83
Cdd:PRK03918 242 ELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELE----EKVKELKELKEKAEEYIKLSEfyeEYLDELREIEKRLS 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024410660 84 TIACQFGIVKGVHEKLEHSVQEAIQLNKKLTSVNKRQET--EISNLKEELKKVTTDLIRSKVTSQHRVGEENIN-LAAKE 160
Cdd:PRK03918 318 RLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEEleERHELYEEAKAKKEELERLKKRLTGLTPEKLEKeLEELE 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024410660 161 KQFQELQQKIRMETA----ISKRVQEENANI------------------KEEKLEILSSLqcvQKQLQQITQTNVRMESE 218
Cdd:PRK03918 398 KAKEEIEEEISKITArigeLKKEIKELKKAIeelkkakgkcpvcgreltEEHRKELLEEY---TAELKRIEKELKEIEEK 474
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024410660 219 LNALREEYQTLERDNELQRE--KAKENEEKFLNLQNEHEK----ALRIWKKDEENLRREMDTIKNELNSLKK 284
Cdd:PRK03918 475 ERKLRKELRELEKVLKKESEliKLKELAEQLKELEEKLKKynleELEKKAEEYEKLKEKLIKLKGEIKSLKK 546
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
108-279 |
5.80e-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: 39.52 E-value: 5.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024410660 108 QLNKKLTSVNKRQET---EISNLKEELKKVTTDLIRSKVtsqhRVGEENINLAAKEKQFQELQQKIrmetaisKRVQEEN 184
Cdd:COG1579 14 ELDSELDRLEHRLKElpaELAELEDELAALEARLEAAKT----ELEDLEKEIKRLELEIEEVEARI-------KKYEEQL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024410660 185 ANIKEEKleilsSLQCVQKQLQQITQTNVRMESELNALREEYQTLERDNELQREKAKENEEKFLNLQNEHEKALRIWKKD 264
Cdd:COG1579 83 GNVRNNK-----EYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAE 157
|
170
....*....|....*
gi 2024410660 265 EENLRREMDTIKNEL 279
Cdd:COG1579 158 LEELEAEREELAAKI 172
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
14-291 |
5.89e-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: 5.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024410660 14 AMEEEKGKYQLAVEIKEKEIDGLKET-LKELQIS---KHTLQKKLNEMDQKL-QMHLTVREEHNkklNEVERCYATIACQ 88
Cdd:TIGR01612 932 SIEKFHNKQNILKEILNKNIDTIKESnLIEKSYKdkfDNTLIDKINELDKAFkDASLNDYEAKN---NELIKYFNDLKAN 1008
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024410660 89 FGIVKG--------VHEKLEHSV-QEAIQLNKKLTSVNKRQETEISNLKEELKKVTTDLIRSKVTSQHRVGEENINlaak 159
Cdd:TIGR01612 1009 LGKNKEnmlyhqfdEKEKATNDIeQKIEDANKNIPNIEIAIHTSIYNIIDEIEKEIGKNIELLNKEILEEAEINIT---- 1084
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024410660 160 ekQFQELQQKIRMETaISKRVQEENANIKEE----KLEILSSLQCVQKQLQQITQTNVRMESELNALREEYQTLER--DN 233
Cdd:TIGR01612 1085 --NFNEIKEKLKHYN-FDDFGKEENIKYADEinkiKDDIKNLDQKIDHHIKALEEIKKKSENYIDEIKAQINDLEDvaDK 1161
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 2024410660 234 ELQREKAKENEEKFLNLQNEHEKalriwkkdEENLRREMDTIKNELNSLKKTQGHLDD 291
Cdd:TIGR01612 1162 AISNDDPEEIEKKIENIVTKIDK--------KKNIYDEIKKLLNEIAEIEKDKTSLEE 1211
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
53-247 |
6.23e-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: 39.52 E-value: 6.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024410660 53 KLNEMDQKLQMHLTVREEHNKKLNEVERcyatiacqfgIVKGVHEKLEHSVQEAIQLNKKLtsvnKRQETEISNLKEELK 132
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELED----------ELAALEARLEAAKTELEDLEKEI----KRLELEIEEVEARIK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024410660 133 KVttdlirskvtsqhrvgEENINLAAKEKQFQELQQKIrmETAiskrvQEENANIKEEKLEILSSLQCVQKQLQQITQTN 212
Cdd:COG1579 77 KY----------------EEQLGNVRNNKEYEALQKEI--ESL-----KRRISDLEDEILELMERIEELEEELAELEAEL 133
|
170 180 190
....*....|....*....|....*....|....*
gi 2024410660 213 VRMESELNALREEYQTLERDNELQREKAKENEEKF 247
Cdd:COG1579 134 AELEAELEEKKAELDEELAELEAELEELEAEREEL 168
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
175-338 |
6.26e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 40.58 E-value: 6.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024410660 175 AISKR-------VQEENANIKEEKLEI---LSSLQCVQKQLQQITQtnvrmesELNALREEYQTLERDNELQREKAKENE 244
Cdd:PRK00409 492 EIAKRlglpeniIEEAKKLIGEDKEKLnelIASLEELERELEQKAE-------EAEALLKEAEKLKEELEEKKEKLQEEE 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024410660 245 EKFL-NLQNEHEKALRIWKKDEENLRREMDTIKNELNS------LKKTQGHLDDCHPP---QGNQHSEQVENLQIHSTVH 314
Cdd:PRK00409 565 DKLLeEAEKEAQQAIKEAKKEADEIIKELRQLQKGGYAsvkaheLIEARKRLNKANEKkekKKKKQKEKQEELKVGDEVK 644
|
170 180
....*....|....*....|....
gi 2024410660 315 piIRNSGQeqsKGsEIQAIQKEND 338
Cdd:PRK00409 645 --YLSLGQ---KG-EVLSIPDDKE 662
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
6-283 |
6.28e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 40.80 E-value: 6.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024410660 6 KQLQARMFAMEEEKGKYQLAVEIKEKEIDGLKETLKELQISKHTLQKKLNEMDQKLQMHLTVREEHNKKLNEVERCYA-- 83
Cdd:TIGR00606 712 KSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTdv 791
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024410660 84 TIACQFGI-VKGVHEKLEHSVQE--AIQLNKKLTSVNKRQETE------ISNLKEELKKVTTD---LIRSKVTSQHRVGE 151
Cdd:TIGR00606 792 TIMERFQMeLKDVERKIAQQAAKlqGSDLDRTVQQVNQEKQEKqheldtVVSKIELNRKLIQDqqeQIQHLKSKTNELKS 871
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024410660 152 ENINLAAKEKQFQELQQKIrmeTAISKRVQEENANIKEEKLEILSSLQCVQKQLQQITQ-------TNVRMESELNALRE 224
Cdd:TIGR00606 872 EKLQIGTNLQRRQQFEEQL---VELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEElissketSNKKAQDKVNDIKE 948
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024410660 225 EYQTLE----------RDNELQREKAKENEEKFLNLQ-NEHEKALRIWKKDEENLRREMDTIKNELNSLK 283
Cdd:TIGR00606 949 KVKNIHgymkdienkiQDGKDDYLKQKETELNTVNAQlEECEKHQEKINEDMRLMRQDIDTQKIQERWLQ 1018
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
97-255 |
6.43e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.52 E-value: 6.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024410660 97 EKLEHSVQEAIQLNKKLTSVNKRQET---EISNLKEELKKVttDLIRSKVTSQHRVGEENINLAAKEKQFQELQQKIR-- 171
Cdd:COG4717 81 KEAEEKEEEYAELQEELEELEEELEEleaELEELREELEKL--EKLLQLLPLYQELEALEAELAELPERLEELEERLEel 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024410660 172 --METAISKRVQE-ENANIKEEKLEILSSLQcVQKQLQQITQTNVRMESELNALREEYQTLERDNELQREKAKENEEKFL 248
Cdd:COG4717 159 reLEEELEELEAElAELQEELEELLEQLSLA-TEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELE 237
|
....*..
gi 2024410660 249 NLQNEHE 255
Cdd:COG4717 238 AAALEER 244
|
|
| BLOC1_2 |
pfam10046 |
Biogenesis of lysosome-related organelles complex-1 subunit 2; Members of this family of ... |
215-290 |
6.57e-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: 6.57e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024410660 215 MESELNALREEYQTLERDNELQREKAKENEEKFLNLQNEHEKalrIWKKDEE--NLRREMDTIKNELNSLKKTQGHLD 290
Cdd:pfam10046 11 LEAELEATVEDYKLLEKMNEATSLKYKDMKDVAASLEKELEE---LNQKYEElqPYLQQIDQIEEQVTKLEETVYELD 85
|
|
| |
