|
Name |
Accession |
Description |
Interval |
E-value |
| CCDC73 |
pfam15818 |
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil ... |
24-1040 |
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: 950.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 24 ETLQHQTDTLQQQNKEAMAAFKKQLQARMFAMEEEKGKYQLAVEIKEKEIDGLKETLKELQISKHTLQKKLNEMDQKLQM 103
Cdd:pfam15818 45 ETLQNQKETLAKQHKEAMAVFKKQLQMKMCALEEEKGKYQLATEIKEKEIEGLKETLKALQVSKYSLQKKVSEMEQKLQL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 104 HLTGREEHNKKLNEVERCYATIACQFGIVKGVHEKLEHSVQEAIQLNKKLTSVNKRQETEISNLKEELKKVTTDLIRSKV 183
Cdd:pfam15818 125 HLLAKEDHHKQLNEIEKYYATITGQFGLVKENHGKLEQNVQEAIQLNKRLSALNKKQESEICSLKKELKKVTSDLIKSKV 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 184 TSQHRVGEENINLAAKEKQFQELQQKIRMETAISKRVQEENANIKEEKLEILSSLQCVQKQLQQITQTNVRMESELNALR 263
Cdd:pfam15818 205 TCQYKMGEENINLTIKEQKFQELQERLNMELELNKKINEEITHIQEEKQDIIISFQHMQQLLQQQTQANTEMEAELKALK 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 264 EEYQTLERDNELQREKAKENEEKFLNLQNEHEKALRIWKKDEENLRREMDTIKNELNSLKKTQGHLDDCHPPQGNQ---- 339
Cdd:pfam15818 285 ENNQTLERDNELQREKVKENEEKFLNLQNEHEKALGTWKKHVEELNGEINEIKNELSSLKETHIKLQEHYNKLCNQkkfe 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 340 HSEQVENLQIHSTVHpvirnsGQEQSKGSEIQAIQKKNDcmpsilrkdnnsghEDEIEVKNTVSFSLSTEELQIEQK--- 416
Cdd:pfam15818 365 EDKKFQNVPEVNNEN------SEMSTEKSENLIIQKYNS--------------EQEIREENTKSFCSDTEYRETEKKkgp 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 417 ---------LQVLENGFKDEINVASPLEGKEREVSPRNTLCTDTDLITQGQNseMHVTECKEAENLETTCRVLLEGNSAN 487
Cdd:pfam15818 425 pveeiiiedLQVLEKSFKNEIDTSVPQDKNQSEISLSKTLCTDKDLISQGQT--LNVTDFRKSVTTEIKDKLCLEKDNGC 502
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 488 LQQKLQDSTGPAAPHHTETSKVLLDAADRVIVSDKNAIQEMNSSNQELCSTTHESICTKvdknssiiELNSSVLTTKASK 567
Cdd:pfam15818 503 SEFKSPNNLFLVADQSIETEKIHLESTEGLGLHHADIHLETESNRSSFNGTLNEMAHNT--------NHNKDVSENEPFK 574
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 568 KESEAAVCTEKSAVCERNTDNHQVSEFHFGILSYPKENCQtgYQKCSLLNSDN-NVDNRLCRIERslLNLSDLPRDKFPF 646
Cdd:pfam15818 575 QQFRLLLCTQENATEKRITNSDQTKAGLDSSLDVKKNPVQ--CQKYSLQDSSNvSLDDKQCKIEQ--LLNKKSECSTLPL 650
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 647 KQTHIDAEDKNYNDNAA--NINRSGALRHIGFPpmdaqnvlAIYCDNASTD-KAAKEQSSNMPFTGTYNLCPEKINKGIN 723
Cdd:pfam15818 651 KQTSSFQQLCNDTSEKPglTIPCDTVVSHPISP--------AAFSDNLKADlKNSDNNVNIMPMLVKPNSSPGKRTTRKN 722
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 724 VDDVHSKQPE-HDSTEQSGGDESMCTLNAEAMSPVKAHDLDTTVQKVPADGIDVDKL----NEEIQIQSIKNEHSLDIND 798
Cdd:pfam15818 723 LDDMQSSQFKnCLGGLENGVTISHLQVNNENSHASQAKDLKTAVHPKTSTEIQFSSKesqiDENQITEATKNDLFLLVNV 802
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 799 DSINNSMLK--QEKDSVHSTVPGRKFAEGHLKESCSLPMRTSGNLVNASGRSSFDLSNSDKKAEKTSVCFKFLGLSSCSR 876
Cdd:pfam15818 803 NERQHTLLNntEKTESLNDIVSGKIYSEGQLEESHSFHIKPSGDLVNRSGRSAFDLSTSDKKTEKTPVYLNFLDPSPWSK 882
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 877 VNQMRSQATWTSSSQEPSVLKEKLPCLVENKKVPSRELFQNVSENVGRKETGPGSTSSNRAADTLNTSRIHRDPQGDPTE 956
Cdd:pfam15818 883 VNQTEGQTVSTSTSSIPLLLKEKPIGPSENTKIISVTLCKNVGVDDVRKDIGPDTTSISRVADTLNNSSIHPDPKGEPSE 962
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 957 EWNAIAKTFYDSSFPTEHVKEGFTALNEQKSSPMTVTSAQSERTLGDEDRFPTHNSTVQSQIEEIEKYLNLETLCSSRKR 1036
Cdd:pfam15818 963 ERNATAKTFYDSSFPTEHVKTEPLKSTVLQSHFQTVKIKDSPDLLKSSPGEDDWQSLITNQITEIEKLLSLENDNQPKKR 1042
|
....
gi 2024503300 1037 KYED 1040
Cdd:pfam15818 1043 KAEE 1046
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
23-322 |
5.20e-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: 67.00 E-value: 5.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 23 LETLQHQTDTLQQQNKEAMAAfKKQLQARMFAMEEEKGKYQLAVEIKEKEIDGLKETLKELQISKHTLQKKLNEMDQKLQ 102
Cdd:TIGR02168 700 LAELRKELEELEEELEQLRKE-LEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELA 778
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 103 MHLTGREEHNKKLNEVERCYATIACQFGIVKGVHEKLEHSVQEAIQLNKKLTSVNKRQETEISNLKEELKKVTTDLIRSk 182
Cdd:TIGR02168 779 EAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESL- 857
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 183 vtsQHRVGEENINLAAKEKQFQELQQKirmetaisKRVQEENANIKEEKLEILSslqcvqKQLQQITQTNVRMESELNAL 262
Cdd:TIGR02168 858 ---AAEIEELEELIEELESELEALLNE--------RASLEEALALLRSELEELS------EELRELESKRSELRRELEEL 920
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024503300 263 REEYQTLERD-----NELQREKAKENEEKFLNLQNEHEKALRIwKKDEENLRREMDTIKNELNSL 322
Cdd:TIGR02168 921 REKLAQLELRlegleVRIDNLQERLSEEYSLTLEEAEALENKI-EDDEEEARRRLKRLENKIKEL 984
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
16-330 |
6.11e-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: 67.00 E-value: 6.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 16 ISVLCLVLETLQHQTDTLQQQnKEAMAAFKKQLQARMFAMEEEKGKYQLAVEIKEKEIDGLKETLKELQISKHTLQKKLN 95
Cdd:TIGR02168 227 LALLVLRLEELREELEELQEE-LKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQ 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 96 EMDQKLQMHLTGREEHNKKLNEVERcyatiacqfgivkgvheKLEHSVQEAIQLNKKLTSVNKRQEtEISNLKEELKKVT 175
Cdd:TIGR02168 306 ILRERLANLERQLEELEAQLEELES-----------------KLDELAEELAELEEKLEELKEELE-SLEAELEELEAEL 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 176 TDLIRSKVTSQHRVGEENINLAAKEKQFQELQQKI-RMETAISkRVQEENANIKEEKLEILSSLQCVQKQLQQitQTNVR 254
Cdd:TIGR02168 368 EELESRLEELEEQLETLRSKVAQLELQIASLNNEIeRLEARLE-RLEDRRERLQQEIEELLKKLEEAELKELQ--AELEE 444
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024503300 255 MESELNALREEYQTLERDNELQREKAKENEEKFLNLQNEHEKA---LRIWKKDEENLRREMDTIKNELNSLKKTQGHLD 330
Cdd:TIGR02168 445 LEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLqarLDSLERLQENLEGFSEGVKALLKNQSGLSGILG 523
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
46-322 |
1.54e-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: 1.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 46 KQLQARMFAMEEEKGKYQLAVEIKEKEIDGLKETLKELQISKHTLQKKLNEMDQKLQMHltgREEHNKKLNEVERCYATI 125
Cdd:TIGR02168 680 EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARL---EAEVEQLEERIAQLSKEL 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 126 ACQFGIVKGVHEKLEHSVQEAIQLNKKLTSVNKRQET---EISNLKEELKKVTTDLIRSKV---TSQHRVGEENINLAAK 199
Cdd:TIGR02168 757 TELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQlkeELKALREALDELRAELTLLNEeaaNLRERLESLERRIAAT 836
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 200 EKQFQELQQKIRMETAISKRVQEENANIKEEKLEILSSLQCVQKQLQQitqtnvrMESELNALREEYQTLERDNELQREK 279
Cdd:TIGR02168 837 ERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERAS-------LEEALALLRSELEELSEELRELESK 909
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 2024503300 280 AKENEEKFLNLQNEHEKAlriwKKDEENLRREMDTIKNELNSL 322
Cdd:TIGR02168 910 RSELRRELEELREKLAQL----ELRLEGLEVRIDNLQERLSEE 948
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
15-324 |
3.56e-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: 64.32 E-value: 3.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 15 NISVLCLVLETLQHQTDTLQQQNKEAMA--AFKKQLQARMF--------AMEEEKGKYQLAVEIKEKEIDGLKETLKELQ 84
Cdd:TIGR02169 185 NIERLDLIIDEKRQQLERLRREREKAERyqALLKEKREYEGyellkekeALERQKEAIERQLASLEEELEKLTEEISELE 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 85 ISKHTLQKKLNEMDQKLqmhltgreehnKKLNEVErcYATIACQFGIVKGVHEKLEHSVQEAIQLNKKLTSVNKRQETEI 164
Cdd:TIGR02169 265 KRLEEIEQLLEELNKKI-----------KDLGEEE--QLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEI 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 165 SNLKEELKKVTTDLIRSKVtSQHRVGEENINLAAK-EKQFQELQQ---KIRMETAISKRVQEENANIKEEKLEILSSLQC 240
Cdd:TIGR02169 332 DKLLAEIEELEREIEEERK-RRDKLTEEYAELKEElEDLRAELEEvdkEFAETRDELKDYREKLEKLKREINELKRELDR 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 241 VQKQLQQITQTNVRMESELNALREEYQTLERDNELQREKAKENEEKFLNLQNEHEKAlriwKKDEENLRREMDTIKNELN 320
Cdd:TIGR02169 411 LQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKY----EQELYDLKEEYDRVEKELS 486
|
....
gi 2024503300 321 SLKK 324
Cdd:TIGR02169 487 KLQR 490
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
23-286 |
1.06e-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: 62.78 E-value: 1.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 23 LETLQHQTDTLQQQnKEAMAAFKKQLQARMFAMEEEKGKYQLAVE------------IKEKEIDGLKETLKELQISKHTL 90
Cdd:TIGR02169 739 LEELEEDLSSLEQE-IENVKSELKELEARIEELEEDLHKLEEALNdlearlshsripEIQAELSKLEEEVSRIEARLREI 817
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 91 QKKLNEMDQKLQMhltGREEHNKKLNEVERCYATIAcqfgivkgvheklehSVQEAIQLNK----KLTSVNKRQETEISN 166
Cdd:TIGR02169 818 EQKLNRLTLEKEY---LEKEIQELQEQRIDLKEQIK---------------SIEKEIENLNgkkeELEEELEELEAALRD 879
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 167 LKEELKKVTTDliRSKVTSQHRVGEENINLAAKEKQFQELQQKIRMETAisKRVQEENANIKEEKLEILS------SLQC 240
Cdd:TIGR02169 880 LESRLGDLKKE--RDELEAQLRELERKIEELEAQIEKKRKRLSELKAKL--EALEEELSEIEDPKGEDEEipeeelSLED 955
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 2024503300 241 VQKQLQQITQTNVRMESELNALREEYQ-TLERDNELQREKAKENEEK 286
Cdd:TIGR02169 956 VQAELQRVEEEIRALEPVNMLAIQEYEeVLKRLDELKEKRAKLEEER 1002
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
57-331 |
2.68e-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: 61.62 E-value: 2.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 57 EEKGKYQLAVEIKEKEIDGLKETLKELQISKHT------LQKKLNEMDQKLqmHLTGREEHNKKLNEVERCYATIACQfg 130
Cdd:TIGR02169 177 EELEEVEENIERLDLIIDEKRQQLERLRREREKaeryqaLLKEKREYEGYE--LLKEKEALERQKEAIERQLASLEEE-- 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 131 iVKGVHEKLEHSVQEAIQLNKKLTSVNKR----QETEISNLKEELKKVTTDLIRSKVtsqhrvgeeniNLAAKEKQFQEL 206
Cdd:TIGR02169 253 -LEKLTEEISELEKRLEEIEQLLEELNKKikdlGEEEQLRVKEKIGELEAEIASLER-----------SIAEKERELEDA 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 207 QQKIRmetaiskRVQEENANIKEEKLEILSSLQCVQKQLQQITQTNVRMESELNALREEYQTLERDNELQREKAKENEEK 286
Cdd:TIGR02169 321 EERLA-------KLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREK 393
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 2024503300 287 FLNLQNEHEKALRIWKKDEENLRR---EMDTIKNELNSLKKTQGHLDD 331
Cdd:TIGR02169 394 LEKLKREINELKRELDRLQEELQRlseELADLNAAIAGIEAKINELEE 441
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
61-326 |
3.78e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 57.64 E-value: 3.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 61 KYQ-LAVEIKEKEIDGLKETLKELQISKHTLQKKLNEMDQKLQMHLTGREEHNKKLNEVERcyatiacqfgivkgVHEKL 139
Cdd:COG1196 214 RYReLKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRL--------------ELEEL 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 140 EHSVQEAIQLNKKLTSVNKRQETEISNLKEELKkvttdlirskvtsqhrvgEENINLAAKEKQFQELQQKIRMETAISKR 219
Cdd:COG1196 280 ELELEEAQAEEYELLAELARLEQDIARLEERRR------------------ELEERLEELEEELAELEEELEELEEELEE 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 220 VQEENANIKEEKLEILSSLQCVQKQLQQITQTNVRMESELNALREEYQTLERDNELQREKAKENEEKFLNLQNEHEKALR 299
Cdd:COG1196 342 LEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEE 421
|
250 260
....*....|....*....|....*..
gi 2024503300 300 IWKKDEENLRREMDTIKNELNSLKKTQ 326
Cdd:COG1196 422 ELEELEEALAELEEEEEEEEEALEEAA 448
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
158-331 |
2.23e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 55.33 E-value: 2.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 158 KRQETEISNLKEELKKVTTDLIRSKVTSQH---RVGEENINLAAKEKQFQELQQKIRMETAISKRVQEENANIKEEKLEI 234
Cdd:COG1196 235 RELEAELEELEAELEELEAELEELEAELAEleaELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRREL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 235 LSSLQCVQKQLQQITQTNVRMESELNALREEYQTLERDNELQREKAKENEEKFLNLQNEHEKALRIWKKDEENLRREMDT 314
Cdd:COG1196 315 EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRA 394
|
170
....*....|....*..
gi 2024503300 315 IKNELNSLKKTQGHLDD 331
Cdd:COG1196 395 AAELAAQLEELEEAEEA 411
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
87-374 |
4.28e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 54.29 E-value: 4.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 87 KHTLQKKLNEMDQKLQMHLTGREEHNKKLNEVERcYATIACQFgivKGVHEKLEH-----SVQEAIQLNKKLTSVN---K 158
Cdd:TIGR02168 174 RKETERKLERTRENLDRLEDILNELERQLKSLER-QAEKAERY---KELKAELRElelalLVLRLEELREELEELQeelK 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 159 RQETEISNLKEELKKVTTDL--IRSKVTS--------QHRVGEENINLAAKEKQFQELQQKIRMETAISKRVQEENANIK 228
Cdd:TIGR02168 250 EAEEELEELTAELQELEEKLeeLRLEVSEleeeieelQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELE 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 229 EEKLEILSSLQCVQKQLQQITQTNVRMESELNALREEYQTLERDNELQREKAKENEEKFLNLQNEHEKAlriwKKDEENL 308
Cdd:TIGR02168 330 SKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASL----NNEIERL 405
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024503300 309 RREMDTIKNELNSLKKTQ-GHLDDCHPPQGNQHSEQVENL--QIHSTVHPVIRNSGQEQSKGSEIQAIQ 374
Cdd:TIGR02168 406 EARLERLEDRRERLQQEIeELLKKLEEAELKELQAELEELeeELEELQEELERLEEALEELREELEEAE 474
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
25-324 |
1.18e-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: 1.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 25 TLQHQTDTLQQQNKEAMAAFKKQL--------QARMfAMEEEKGKYQLAVEIKEKEIDGLKETLKELQISKHTLQKKLNE 96
Cdd:pfam15921 296 SIQSQLEIIQEQARNQNSMYMRQLsdlestvsQLRS-ELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGN 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 97 MDQKLQ-----MH-----LTGREEHNKKL----------------------NEVERCYATIACQFGIVKGVHEKLEHSVQ 144
Cdd:pfam15921 375 LDDQLQklladLHkrekeLSLEKEQNKRLwdrdtgnsitidhlrrelddrnMEVQRLEALLKAMKSECQGQMERQMAAIQ 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 145 EAIQLNKKLTSVNKRQETEisnlKEELKKVTTDLIRSKVT---SQHRVGEENINLAAKEK------------------QF 203
Cdd:pfam15921 455 GKNESLEKVSSLTAQLEST----KEMLRKVVEELTAKKMTlesSERTVSDLTASLQEKERaieatnaeitklrsrvdlKL 530
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 204 QELQQkIRMETAISKRVQEENANIKEEKLEILSSLQCVQKQLQQITQ--------------TNVRMESELNALREEYQTL 269
Cdd:pfam15921 531 QELQH-LKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQlvgqhgrtagamqvEKAQLEKEINDRRLELQEF 609
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024503300 270 ERDNELQREKAKENEE----------KFLNLQNEHEKALRIWKKDEENLRREMDTIKNELNSLKK 324
Cdd:pfam15921 610 KILKDKKDAKIRELEArvsdlelekvKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSE 674
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
70-299 |
7.95e-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: 7.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 70 EKEIDGLKETLKELQISKHTLQKKLNEMDQKLqmhltgrEEHNKKLNEVErcyatiacqfgivkgvhEKLEHSVQEAIQL 149
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAEL-------EELNEEYNELQ-----------------AELEALQAEIDKL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 150 NKKLTsvnkRQETEISNLKEELKKvttdLIRSKVTSQHRVGEENINLAAKEkqFQELQQKIRMETAISKRVQEENANIKE 229
Cdd:COG3883 71 QAEIA----EAEAEIEERREELGE----RARALYRSGGSVSYLDVLLGSES--FSDFLDRLSALSKIADADADLLEELKA 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024503300 230 EKLEILSSLQCVQKQLQQITQTNVRMES---ELNALREEYQTLERDNELQREKAKENEEKFLNLQNEHEKALR 299
Cdd:COG3883 141 DKAELEAKKAELEAKLAELEALKAELEAakaELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAA 213
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
56-323 |
9.44e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 49.68 E-value: 9.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 56 EEEKG----KYQLAVEIKEKEIDGLKETLKELQISKHTLQKKLNEMDQKLQMHLTGRE--EHNKKLNEVERcyatiacqf 129
Cdd:PRK03918 447 EEHRKelleEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQlkELEEKLKKYNL--------- 517
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 130 givkgvhEKLEHSVQEAIQLNKKLTSVnkrqETEISNLKEELKKVtTDLIRSKVTSQHRVGEENINLAAKEKQFQELQQK 209
Cdd:PRK03918 518 -------EELEKKAEEYEKLKEKLIKL----KGEIKSLKKELEKL-EELKKKLAELEKKLDELEEELAELLKELEELGFE 585
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 210 IRMEtaISKRVQE---------ENANIKEEKLEILSSLQCVQKQLQQITQTNVRMESELNALREEYQTLERdnELQREKA 280
Cdd:PRK03918 586 SVEE--LEERLKElepfyneylELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEK--KYSEEEY 661
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 2024503300 281 KENEEKFLNLQNEHEKAlriwKKDEENLRREMDTIKNELNSLK 323
Cdd:PRK03918 662 EELREEYLELSRELAGL----RAELEELEKRREEIKKTLEKLK 700
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
18-250 |
1.38e-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: 1.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 18 VLCLVLETLQHQTDTLQQQNKEAMAAFK--KQLQARMFAMEEEKGKYQLAVEIKEKEIDGLKETLKELQISKHTLQKKLN 95
Cdd:COG4942 7 LALLLALAAAAQADAAAEAEAELEQLQQeiAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 96 EMDQKLQMHLTGREEHNKKLNEVERCYATIACQFGIVKGVHEKlehSVQEAIQLNKKLTSVNKRQETEIsnlkEELKKVT 175
Cdd:COG4942 87 ELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPE---DFLDAVRRLQYLKYLAPARREQA----EELRADL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024503300 176 TDLIRSKVTSQHRVGEENINLAAKEKQFQELQQKIRMETAISKRVQEENANIKEEKLEILSSLQCVQKQLQQITQ 250
Cdd:COG4942 160 AELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEA 234
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
37-270 |
2.00e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 48.91 E-value: 2.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 37 NKEAMAAFKKQLQARMFAMEEEKGKYQLAVEIKEKEIDGLKETLKEL--QISKHT------LQKKLNEMDQKLQMHLTGR 108
Cdd:TIGR02169 231 EKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELnkKIKDLGeeeqlrVKEKIGELEAEIASLERSI 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 109 EEHNKKLNEVERCYATIACQFGIVKGVHEKLEHSVQEAIQLNKKLTSVNKRQETEISNLKEELKKVTTDLIRSKVTS--- 185
Cdd:TIGR02169 311 AEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELkdy 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 186 -------QHRVGEENINLAAKEKQFQELQQKIRMETAISKRVQEENANIKEEKLEI----------LSSLQC----VQKQ 244
Cdd:TIGR02169 391 rekleklKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKaleikkqewkLEQLAAdlskYEQE 470
|
250 260
....*....|....*....|....*.
gi 2024503300 245 LQQITQTNVRMESELNALREEYQTLE 270
Cdd:TIGR02169 471 LYDLKEEYDRVEKELSKLQRELAEAE 496
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
22-298 |
3.59e-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: 48.04 E-value: 3.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 22 VLETLQHQTDTLQQQNKEAMAAFKKQLQARMFAMEEEKGKYQLA-VEIKEKEIDGLKETLKELQISKHTLQ--KKLNEMD 98
Cdd:TIGR00618 234 ALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAvLEETQERINRARKAAPLAAHIKAVTQieQQAQRIH 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 99 QKLQMHLTGREEHNKKLNEVERCYATIACQFGIVKGVHEKLEHsvqeaiqlnkkltsvNKRQETEISNLKEELKKVTTDL 178
Cdd:TIGR00618 314 TELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIH---------------IRDAHEVATSIREISCQQHTLT 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 179 IRSKVTSQHR-VGEENINLAAKEK-QFQELQQKIRMETAISKRVQEENANIK-EEKLEILSSLQC---VQKQLQQITQTN 252
Cdd:TIGR00618 379 QHIHTLQQQKtTLTQKLQSLCKELdILQREQATIDTRTSAFRDLQGQLAHAKkQQELQQRYAELCaaaITCTAQCEKLEK 458
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 2024503300 253 VRMESELNALREEYQTL-ERDNELQREKAKEN-EEKFLNLQNEHEKAL 298
Cdd:TIGR00618 459 IHLQESAQSLKEREQQLqTKEQIHLQETRKKAvVLARLLELQEEPCPL 506
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
25-281 |
3.75e-05 |
|
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: 48.13 E-value: 3.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 25 TLQHQTDTLQQQNKEAMAAFKKQLQARMFAMEEEKGKYQLAVEIKEKEIDGLKETLKELQISKHTLQKKLNEMDQKLQMH 104
Cdd:TIGR02168 750 AQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESL 829
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 105 LTGREEHNKKLNEVERCYATIACQFGIVKGVHEKLEHSVQEAIQLNKKLTSVNKRQETEISNLKEELKKVTTDL--IRSK 182
Cdd:TIGR02168 830 ERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELreLESK 909
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 183 VT--------SQHRVGEENINLAAKEKQFQELQQKIRMETAISKRVQEENANIKEEKLEIL-SSLQCVQKQLQQITQTNV 253
Cdd:TIGR02168 910 RSelrreleeLREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEArRRLKRLENKIKELGPVNL 989
|
250 260
....*....|....*....|....*....
gi 2024503300 254 RMESELNALREEYQTLER-DNELQREKAK 281
Cdd:TIGR02168 990 AAIEEYEELKERYDFLTAqKEDLTEAKET 1018
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
22-480 |
8.84e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 46.65 E-value: 8.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 22 VLETLQHQTDTLQQQNKEAMAAFKKQ----------LQARMFAMEEEKgkyQLAVEIKEKEI-------DGLKETLKELQ 84
Cdd:pfam15921 79 VLEEYSHQVKDLQRRLNESNELHEKQkfylrqsvidLQTKLQEMQMER---DAMADIRRRESqsqedlrNQLQNTVHELE 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 85 ISKHTLQKKLNEMDQKLQMHLTGREEHNKKLNEVErcyaTIACQFGIVKG--VHEKLEHSVQEAIQLNKKLTSVNKRQET 162
Cdd:pfam15921 156 AAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIR----SILVDFEEASGkkIYEHDSMSTMHFRSLGSAISKILRELDT 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 163 EISNLKEELKKVTTDLIRSKVTSQHRVgeeninlaakEKQFQELQQkiRMETAISKR------VQEENANIKEEKLEILS 236
Cdd:pfam15921 232 EISYLKGRIFPVEDQLEALKSESQNKI----------ELLLQQHQD--RIEQLISEHeveitgLTEKASSARSQANSIQS 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 237 SLQCVQKQLQQITQTNVR----MESELNALREEYqtlerdnelqREKAKENEEKFlnlqNEHEKALRIWKKDEENLRREM 312
Cdd:pfam15921 300 QLEIIQEQARNQNSMYMRqlsdLESTVSQLRSEL----------REAKRMYEDKI----EELEKQLVLANSELTEARTER 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 313 DTIKNELNSL-KKTQGHLDDCHPPQGNQHSEQVENLQIHS-------TVHPVIRNSGQEQSKGSEIQAIQK--KNDCMPS 382
Cdd:pfam15921 366 DQFSQESGNLdDQLQKLLADLHKREKELSLEKEQNKRLWDrdtgnsiTIDHLRRELDDRNMEVQRLEALLKamKSECQGQ 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 383 ILRKDNN-SGHEDEIEVKNTVSFSL-STEEL------QIEQKLQVLENGFKDEINVASPLEGKEREVSPRNTLCTD--TD 452
Cdd:pfam15921 446 MERQMAAiQGKNESLEKVSSLTAQLeSTKEMlrkvveELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKlrSR 525
|
490 500
....*....|....*....|....*...
gi 2024503300 453 LITQGQNSEMHVTECKEAENLETTCRVL 480
Cdd:pfam15921 526 VDLKLQELQHLKNEGDHLRNVQTECEAL 553
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
17-330 |
9.17e-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: 46.64 E-value: 9.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 17 SVLCLVLETLQHQTDTLQQqNKEAMAAFKKQLQARMFAMEE-EKGKYQLAVEIKE-KEIDGLKETLKELQISKHTLQKKL 94
Cdd:pfam05483 356 ATTCSLEELLRTEQQRLEK-NEDQLKIITMELQKKSSELEEmTKFKNNKEVELEElKKILAEDEKLLDEKKQFEKIAEEL 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 95 NEMDQKLQMHLTGREEHNKKLnEVERCYATIACQFGI--VKGVHEKLEHSVQEAIQLN---KKLTSVNKRQETEISNLKE 169
Cdd:pfam05483 435 KGKEQELIFLLQAREKEIHDL-EIQLTAIKTSEEHYLkeVEDLKTELEKEKLKNIELTahcDKLLLENKELTQEASDMTL 513
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 170 ELKKVTTDLIRSKvTSQHRVGEENINLAAKEKQFQELQQKIRMETaISKRVQ--------EENAN------IKEEKLEIL 235
Cdd:pfam05483 514 ELKKHQEDIINCK-KQEERMLKQIENLEEKEMNLRDELESVREEF-IQKGDEvkckldksEENARsieyevLKKEKQMKI 591
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 236 SSLQC--VQKQLQQITQTNVRMESELNALREE----------YQTLERDNELQREKAKEneeKFLNLQNEHEKALRIWKK 303
Cdd:pfam05483 592 LENKCnnLKKQIENKNKNIEELHQENKALKKKgsaenkqlnaYEIKVNKLELELASAKQ---KFEEIIDNYQKEIEDKKI 668
|
330 340
....*....|....*....|....*..
gi 2024503300 304 DEENLRREMDTIKNELNSLKKTQGHLD 330
Cdd:pfam05483 669 SEEKLLEEVEKAKAIADEAVKLQKEID 695
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
71-324 |
1.06e-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: 45.91 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 71 KEIDGLKETLKELQISKHTLQKKLNEMDQKLQMHLTGREEHNKKLNEVERcyatiacqfgivkgvheKLEHSVQEAIQLN 150
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALAR-----------------RIRALEQELAALE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 151 KKLTSVNKRQETeisnLKEELKKVTTDLIRSKVTSQHRVGEENINLAAKEKQFQELQQKIRMETAISKRVQEENANIKEE 230
Cdd:COG4942 83 AELAELEKEIAE----LRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRAD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 231 kleilsslqcvQKQLQQITQtnvrmesELNALREEYQTLERDNELQREKAKENEEKFLNLQNEHEKALRIWKKDEENLRR 310
Cdd:COG4942 159 -----------LAELAALRA-------ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQ 220
|
250
....*....|....
gi 2024503300 311 EMDTIKNELNSLKK 324
Cdd:COG4942 221 EAEELEALIARLEA 234
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
26-328 |
1.33e-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: 1.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 26 LQHQTDTLQQQNK--EAMAAFKKQLQAR---MFAMEEEKGKYQLAVEIKEKEIDGLKETLKE----LQISKHTLQKKLNE 96
Cdd:pfam15921 446 MERQMAAIQGKNEslEKVSSLTAQLESTkemLRKVVEELTAKKMTLESSERTVSDLTASLQEkeraIEATNAEITKLRSR 525
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 97 MDQKLQ--MHLTGREEHNKKLN-EVERCYATIACQFGIVKGVHEKLEHSVQEAIQLNKKLTS--VNKRQ-ETEISNLKEE 170
Cdd:pfam15921 526 VDLKLQelQHLKNEGDHLRNVQtECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAmqVEKAQlEKEINDRRLE 605
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 171 LKKVTtdLIRSKVTSQHRvgeeniNLAAKEKQFQelQQKIRMETAISKRVQEENaNIKEEKLEILSSLQCVQkqlqqitq 250
Cdd:pfam15921 606 LQEFK--ILKDKKDAKIR------ELEARVSDLE--LEKVKLVNAGSERLRAVK-DIKQERDQLLNEVKTSR-------- 666
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024503300 251 tnvrmeSELNALREEYQTLERDnelqrekakeneekFLNLQNEHEKALRIWKKDEENLRREMDTIKNELNSLKKTQGH 328
Cdd:pfam15921 667 ------NELNSLSEDYEVLKRN--------------FRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGH 724
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
53-326 |
1.35e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.21 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 53 FAMEEEKGKYQLAVEIKEK------EIDGLKETLKELQiskhTLQKKLNEMDQKLQMHLTGREEHNKKLNEVercyatia 126
Cdd:PRK03918 515 YNLEELEKKAEEYEKLKEKliklkgEIKSLKKELEKLE----ELKKKLAELEKKLDELEEELAELLKELEEL-------- 582
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 127 cQFGIVKGVHEKLEhSVQEAiqLNKKLTSVNKRQETEIsnLKEELKKVTTDLIRSKVtsqhrvgeeniNLAAKEKQFQEL 206
Cdd:PRK03918 583 -GFESVEELEERLK-ELEPF--YNEYLELKDAEKELER--EEKELKKLEEELDKAFE-----------ELAETEKRLEEL 645
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 207 QQKIrmETAISKRVQEENANIKEEKLEILSSLQCVQKQLQQITQTNVRMESELNALREEYQTlerdnelqREKAKENEEK 286
Cdd:PRK03918 646 RKEL--EELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEE--------REKAKKELEK 715
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 2024503300 287 FlnlqnehEKALriwkKDEENLRREMDTIKNEL--NSLKKTQ 326
Cdd:PRK03918 716 L-------EKAL----ERVEELREKVKKYKALLkeRALSKVG 746
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
26-278 |
1.59e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.78 E-value: 1.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 26 LQHQTDTLQQQNKEAMAAFKKQLQarmfameeekgKYQLAVEIKEKEIDGLKETLKELQISKHT--LQKKLNEMDQKLQM 103
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQLP-----------ELRKELEEAEAALEEFRQKNGLVDLSEEAklLLQQLSELESQLAE 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 104 HLTGREEHNKKLNEVERcyatiacqfgivkgvheKLEHSVQEAIQLNkkltsvnkrQETEISNLKEELKKVTTDL--IRS 181
Cdd:COG3206 231 ARAELAEAEARLAALRA-----------------QLGSGPDALPELL---------QSPVIQQLRAQLAELEAELaeLSA 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 182 KVTSQHRvgeeninlaakekQFQELQQKIR-METAISKRVQEENANIKEEKLEILSSLQCVQKQLQQITQtnvRMeSELN 260
Cdd:COG3206 285 RYTPNHP-------------DVIALRAQIAaLRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEA---RL-AELP 347
|
250
....*....|....*...
gi 2024503300 261 ALREEYQTLERDNELQRE 278
Cdd:COG3206 348 ELEAELRRLEREVEVARE 365
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
22-330 |
2.15e-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: 45.34 E-value: 2.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 22 VLETLQHQTDT-------LQQQNKEAMAAFKKQLQARMFAMEEEKGKYQLAVEIKeKEIDGLKETLKELQISKHTLQKKL 94
Cdd:TIGR00618 543 SEEDVYHQLTSerkqrasLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQ-DLTEKLSEAEDMLACEQHALLRKL 621
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 95 NEMDQKLQMHLTGR---EEHNKKLNEVERCYATIAcqfgivkgvHEKLEHSVQEAIQLNKKLTSVNKRQETEISNLKEEL 171
Cdd:TIGR00618 622 QPEQDLQDVRLHLQqcsQELALKLTALHALQLTLT---------QERVREHALSIRVLPKELLASRQLALQKMQSEKEQL 692
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 172 K--KVTTDLIRSKVTSQHRVGEENinlaakEKQFQELQQKirMETAISKRVQEENA-NIKEEKLEILSSLQCvqKQLQQI 248
Cdd:TIGR00618 693 TywKEMLAQCQTLLRELETHIEEY------DREFNEIENA--SSSLGSDLAAREDAlNQSLKELMHQARTVL--KARTEA 762
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 249 TQTNVRMESELNALREEYQTLERDNELQREKAKENEEKFLNLQNEHEKALR----IWKKDEENLRREMDTIKNELNSLKK 324
Cdd:TIGR00618 763 HFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPsdedILNLQCETLVQEEEQFLSRLEEKSA 842
|
....*.
gi 2024503300 325 TQGHLD 330
Cdd:TIGR00618 843 TLGEIT 848
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
23-223 |
2.30e-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: 45.02 E-value: 2.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 23 LETLQHQTDTLQQQnKEAMAAFKKQLQARMFAMEEEKGKYQLAVEIKEKEIDGLKETLKEL-----QISKhtLQKKLNEM 97
Cdd:pfam05667 337 LEELQEQLEDLESS-IQELEKEIKKLESSIKQVEEELEELKEQNEELEKQYKVKKKTLDLLpdaeeNIAK--LQALVDAS 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 98 DQKLQmHLTG----------------REEHNKKLNEVERCYATIacqfgivKGVHEKLEHSVQEAiqlnkkltsvnKRQE 161
Cdd:pfam05667 414 AQRLV-ELAGqwekhrvplieeyralKEAKSNKEDESQRKLEEI-------KELREKIKEVAEEA-----------KQKE 474
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024503300 162 TEISNLKEELKKVTTDLIRSKVTSqhRVGE--ENInlaakEKQFQELqQKIRMETaisKRVQEE 223
Cdd:pfam05667 475 ELYKQLVAEYERLPKDVSRSAYTR--RILEivKNI-----KKQKEEI-TKILSDT---KSLQKE 527
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
196-329 |
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 2024503300 196 LAAKEKQFQELQQKIRMETAISKRVQEENANIKEEKLEILSSLQCVQKQLQQITQTNVRMESELNALREEYQTLERDNEL 275
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEA 101
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024503300 276 QREKAKE-----------NEEKFLNLQ---NEHEKALRIWKKDEENLRREMDTIKNELNSLKKTQGHL 329
Cdd:COG4942 102 QKEELAEllralyrlgrqPPLALLLSPedfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAEL 169
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
22-270 |
3.02e-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: 3.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 22 VLETLQHQTDTLQQ------QNKEAMAAFKKQLQARMFAMEEEKGKYQLAVEIKEKEIDGLKETLKELQISKHTLqkkLN 95
Cdd:pfam15921 563 VIEILRQQIENMTQlvgqhgRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKL---VN 639
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 96 EMDQKLQMHLTGREEHNKKLNEVERCyatiacqfgivkgvHEKLEHSVQEAIQLNKKLTSVNKRQETEISNLKEELKKVT 175
Cdd:pfam15921 640 AGSERLRAVKDIKQERDQLLNEVKTS--------------RNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQ 705
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 176 TDLIRSKVTSQHRVGEE----------NINLAAKEKQFQELQQKIRMETAISKRVQEENANIKEEKLEILSSLQCVQkql 245
Cdd:pfam15921 706 SELEQTRNTLKSMEGSDghamkvamgmQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVA--- 782
|
250 260
....*....|....*....|....*
gi 2024503300 246 qqiTQTNvRMESELNALREEYQTLE 270
Cdd:pfam15921 783 ---TEKN-KMAGELEVLRSQERRLK 803
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
42-251 |
3.12e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.76 E-value: 3.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 42 AAFKKQLQARMFAMEEEKGKyqlAVEIKEKEIDGLKETLKELQISKHTLQKKLNEMDQkLQMHLTGREEHNKKLNEVERC 121
Cdd:COG4717 45 AMLLERLEKEADELFKPQGR---KPELNLKELKELEEELKEAEEKEEEYAELQEELEE-LEEELEELEAELEELREELEK 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 122 YATIACQFGIVKGVHE---KLEHSVQEAIQLNKKLTSVnKRQETEISNLKEELKKVTTDLIRSKVTSQHRVGEEninLAA 198
Cdd:COG4717 121 LEKLLQLLPLYQELEAleaELAELPERLEELEERLEEL-RELEEELEELEAELAELQEELEELLEQLSLATEEE---LQD 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2024503300 199 KEKQFQELQQKIRMETAISKRVQEENANIKEEkLEILSSLQCVQKQLQQITQT 251
Cdd:COG4717 197 LAEELEELQQRLAELEEELEEAQEELEELEEE-LEQLENELEAAALEERLKEA 248
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
136-330 |
4.41e-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: 4.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 136 HEKLEHSVQEAIQLNKKLTSVNKRQ-----ETEISNLKEELKKVTTDLirskvtsqhrvgeeninlAAKEKQFQELQQKI 210
Cdd:COG4913 264 YAAARERLAELEYLRAALRLWFAQRrlellEAELEELRAELARLEAEL------------------ERLEARLDALREEL 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 211 R-METAISKRVQEENANIKEEkleilssLQCVQKQLQQITQTNVRMESELNALREEYQTLERDNELQREKAKENEEKFLN 289
Cdd:COG4913 326 DeLEAQIRGNGGDRLEQLERE-------IERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEE 398
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2024503300 290 LQNEHEKALRIWKKDEENLRREMDTIKNELNSLKKTQGHLD 330
Cdd:COG4913 399 ELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIP 439
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
43-326 |
6.52e-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: 6.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 43 AFKKQLQARMFAMEEEKGKYQLAVEIKEKEIDGLKETLKELQISKHTLQKKLNEMDQKLQMHltgreehnKKLNEVERCY 122
Cdd:TIGR00618 198 LLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQ--------QLLKQLRARI 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 123 ATIACQFGIVKGVHEKLEHSVQEA--IQLNKKLTSVNKRQETEISNLKEELKKVTTDLIRSKVTSQHRvgeeninlAAKE 200
Cdd:TIGR00618 270 EELRAQEAVLEETQERINRARKAAplAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQ--------SSIE 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 201 KQFQELQQKIRMETAIsKRVQEENANIKEEKLEILSSLQCVQKQLQQIT---QTNVRMESELNALREEYQTLE----RDN 273
Cdd:TIGR00618 342 EQRRLLQTLHSQEIHI-RDAHEVATSIREISCQQHTLTQHIHTLQQQKTtltQKLQSLCKELDILQREQATIDtrtsAFR 420
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 2024503300 274 ELQREKAK-----ENEEKFLNLQNEH-EKALRIWKKDEENLRREMDTIKNELNSLKKTQ 326
Cdd:TIGR00618 421 DLQGQLAHakkqqELQQRYAELCAAAiTCTAQCEKLEKIHLQESAQSLKEREQQLQTKE 479
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
144-331 |
7.39e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.60 E-value: 7.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 144 QEAIQLNKKLTSVNKRQETEISNLKEELK--KVTTDLIRSKVTSQHRVGEEninLAAKEKQFQELQQKIR-METAISKR- 219
Cdd:COG4717 53 KEADELFKPQGRKPELNLKELKELEEELKeaEEKEEEYAELQEELEELEEE---LEELEAELEELREELEkLEKLLQLLp 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 220 VQEENANIKEEKLEILSSLQCVQKQLQQITQtnvrMESELNALREEYQTLERD-NELQREKAKENEEKFLNLQNEHE--- 295
Cdd:COG4717 130 LYQELEALEAELAELPERLEELEERLEELRE----LEEELEELEAELAELQEElEELLEQLSLATEEELQDLAEELEelq 205
|
170 180 190
....*....|....*....|....*....|....*.
gi 2024503300 296 KALRIWKKDEENLRREMDTIKNELNSLKKTQGHLDD 331
Cdd:COG4717 206 QRLAELEEELEEAQEELEELEEELEQLENELEAAAL 241
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
229-331 |
8.17e-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: 8.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 229 EEKLEILSSLQCVQKQLQQITQTNVRMESELNALREEYQTLERDNELQREKAKENEEKFLNLQNEHEKALRIWKKDEENL 308
Cdd:COG1579 3 PEDLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQL 82
|
90 100
....*....|....*....|....*...
gi 2024503300 309 R-----REMDTIKNELNSLKKTQGHLDD 331
Cdd:COG1579 83 GnvrnnKEYEALQKEIESLKRRISDLED 110
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
24-324 |
8.37e-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: 43.56 E-value: 8.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 24 ETLQHQTDTLQQQNKEAMAAFKKQLQARM---FAMEEEKGKYQLAVEIKEKEIDGLKETLKELQISKHTLQKKLNEMDQK 100
Cdd:pfam05483 317 EDLQIATKTICQLTEEKEAQMEELNKAKAahsFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEM 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 101 LQMHlTGREEHNKKLNEVERCYATIACQFGIVKGVHEKLEHSVQEaiqlnkkLTSVNKRQETEISNLKEELKKVTTD--- 177
Cdd:pfam05483 397 TKFK-NNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQE-------LIFLLQAREKEIHDLEIQLTAIKTSeeh 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 178 ---LIRSKVTSQHRVGEENINLAAKEKQF----QELQQKIRMETAISKRVQEENANIKEEKLEILsslqcvqKQLQQITQ 250
Cdd:pfam05483 469 ylkEVEDLKTELEKEKLKNIELTAHCDKLllenKELTQEASDMTLELKKHQEDIINCKKQEERML-------KQIENLEE 541
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024503300 251 TNVRMESELNALREEYQTLERDNELQREKAKENEEKFLNLQNEHEKALRIWKKDEENLRREMDTIKNELNSLKK 324
Cdd:pfam05483 542 KEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQ 615
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
186-329 |
8.79e-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: 8.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 186 QHRVGEENINLAAKEKQFQELQQKIrmeTAISKRVQEENANIKEEKLEILSslqcVQKQLQQIT--QTNVRMESELNALR 263
Cdd:COG1579 23 EHRLKELPAELAELEDELAALEARL---EAAKTELEDLEKEIKRLELEIEE----VEARIKKYEeqLGNVRNNKEYEALQ 95
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024503300 264 EEYQTLERDNELQREKAKENEEKFLNLQNEHEKALRIWKKDEENLRREMDTIKNELNSLKKTQGHL 329
Cdd:COG1579 96 KEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEEL 161
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
191-305 |
1.01e-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: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 191 EENINLAAKEKQFQELQQKIrmetaisKRVQEENANIK---EEKLEILSSLQCVQKQLQQITQTNVRMESELNALREEYQ 267
Cdd:COG2433 403 HEERELTEEEEEIRRLEEQV-------ERLEAEVEELEaelEEKDERIERLERELSEARSEERREIRKDREISRLDREIE 475
|
90 100 110
....*....|....*....|....*....|....*...
gi 2024503300 268 TLERdnELQREKaKENEEkflnLQNEHEKALRIWKKDE 305
Cdd:COG2433 476 RLER--ELEEER-ERIEE----LKRKLERLKELWKLEH 506
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
65-324 |
1.15e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.13 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 65 AVEIKEKEIDGLKETLKELQISKHTLQKKLNEMDQKLQMHLTGREEHNKKLNEVERcyatIACQFGIVKGVHEKLEHSVQ 144
Cdd:PRK03918 225 KLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEE----KVKELKELKEKAEEYIKLSE 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 145 EAIQLNKKLTSVNKRQET---EISNLKEELKKVTTDLIRSKVTSQHRVGEEN--INLAAKEKQFQELQQKI-RMETAISK 218
Cdd:PRK03918 301 FYEEYLDELREIEKRLSRleeEINGIEERIKELEEKEERLEELKKKLKELEKrlEELEERHELYEEAKAKKeELERLKKR 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 219 RVQEENANIKEEKLEILSSLQCVQKQLQQITQTNVRMESELNALREEYQTLER--------DNELQREKAKENEEKFLNL 290
Cdd:PRK03918 381 LTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKakgkcpvcGRELTEEHRKELLEEYTAE 460
|
250 260 270
....*....|....*....|....*....|....
gi 2024503300 291 QNEHEKALRIWKKDEENLRREMDTIKNELNSLKK 324
Cdd:PRK03918 461 LKRIEKELKEIEEKERKLRKELRELEKVLKKESE 494
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
38-174 |
1.35e-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: 39.52 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 38 KEAMAAFKKQLQARMFAMEEEKGKYQLAVEIKEKEIDGLKETLKELQISKHTLQKKLNEMDQKLQmhltgREEHNKKLNE 117
Cdd:pfam20492 1 REEAEREKQELEERLKQYEEETKKAQEELEESEETAEELEEERRQAEEEAERLEQKRQEAEEEKE-----RLEESAEMEA 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 2024503300 118 VERcyatiacqfgivkgvhEKLEHSVQEAIQLNKKLTSVNKRQETEISNLKEELKKV 174
Cdd:pfam20492 76 EEK----------------EQLEAELAEAQEEIARLEEEVERKEEEARRLQEELEEA 116
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
12-330 |
1.48e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 42.58 E-value: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 12 LPTNISVLCLVLETLQHQTDTLQQQNKEAmaafkKQLQARMFAMEEEKGKYQLAVEIKEKEIDGLKETLKELQiSKHTLQ 91
Cdd:PRK01156 178 LRAEISNIDYLEEKLKSSNLELENIKKQI-----ADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELS-SLEDMK 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 92 KKLNEMDQKLQMHLTGREEHNKKLNEVE------------------RCYATIACQFGIVKGVHEKLEHSVQEAIQLNKKL 153
Cdd:PRK01156 252 NRYESEIKTAESDLSMELEKNNYYKELEerhmkiindpvyknrnyiNDYFKYKNDIENKKQILSNIDAEINKYHAIIKKL 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 154 TSVNK--RQETEISNLKEELKKVTTDLIRSKVTSQHRVGE-ENINLaaKEKQFQELQQKIRMETAISKRVQEENAN-IKE 229
Cdd:PRK01156 332 SVLQKdyNDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSiESLKK--KIEEYSKNIERMSAFISEILKIQEIDPDaIKK 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 230 EKLEILSSLQCVQKQLQQITQTNVRMESELNALREEYQTLERDNELQREKAKENEEKFLNLQNEHEKALRIWKKDEENLR 309
Cdd:PRK01156 410 ELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSVCPVCGTTLGEEKSNHIINHYNEKKSRLEEKIREIE 489
|
330 340
....*....|....*....|.
gi 2024503300 310 REMDTIKNELNSLKKTQGHLD 330
Cdd:PRK01156 490 IEVKDIDEKIVDLKKRKEYLE 510
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
158-331 |
1.73e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.81 E-value: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 158 KRQETEISNLKEELKKVTTDLIRSKVTSQhrvgEENINLAAKEKQFQELQQKIRMETAISKRVQEENANIKEEKLEILSS 237
Cdd:COG4372 41 DKLQEELEQLREELEQAREELEQLEEELE----QARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 238 LQCVQKQLQQITQTNVRMESELNALREEYQTLERDNELQREKAKENEEKFLNLQNEHEKAlriwkkDEENLRREMDTIKN 317
Cdd:COG4372 117 LEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQAL------SEAEAEQALDELLK 190
|
170
....*....|....
gi 2024503300 318 ELNSLKKTQGHLDD 331
Cdd:COG4372 191 EANRNAEKEEELAE 204
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
24-277 |
1.86e-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: 42.19 E-value: 1.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 24 ETLQHQTDTLQQQNKEAMAAFKKQLQARmfamEEEKGKYQLAVEIKEKEIDGLKETLKELQISKHTLQKKLNEMDQKLQm 103
Cdd:pfam07888 30 ELLQNRLEECLQERAELLQAQEAANRQR----EKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYK- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 104 hltgreehnkklnEVERCYATIACQFGIVKGVHEKLEHSVQEAIQLNKKLTSVNKRQETEISNLKEELKKVTTDLirskv 183
Cdd:pfam07888 105 -------------ELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQR----- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 184 tsqhrvGEENinlaAKEKQFQ-ELQQKIRMETAISKRVQEENANIKEEKLEILsSLQCVQKQLQQITQTNVRMESELNAL 262
Cdd:pfam07888 167 ------KEEE----AERKQLQaKLQQTEEELRSLSKEFQELRNSLAQRDTQVL-QLQDTITTLTQKLTTAHRKEAENEAL 235
|
250
....*....|....*.
gi 2024503300 263 REEYQTL-ERDNELQR 277
Cdd:pfam07888 236 LEELRSLqERLNASER 251
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
38-331 |
2.51e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.97 E-value: 2.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 38 KEAMAAFKKQLQARMFAMEEEKGKYQLAVEIKEKEIDGLKETLKELQISKHTLQKKLNEMDQKLQMHLTGREEHNKKLNE 117
Cdd:PRK03918 351 EKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEE 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 118 VERcyATIACQF-GIVKGVHEKLEHSVQEAIQLnKKLTSVNKRQETEISNLKEELKKVTTDLIR-SKVTSQHRVGEENIN 195
Cdd:PRK03918 431 LKK--AKGKCPVcGRELTEEHRKELLEEYTAEL-KRIEKELKEIEEKERKLRKELRELEKVLKKeSELIKLKELAEQLKE 507
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 196 LAAKEKQF--QELQQKirmetaiskrvQEENANIKEEKLEILSSLQCVQKQLqqitqtnvrmeSELNALREEYQTLERD- 272
Cdd:PRK03918 508 LEEKLKKYnlEELEKK-----------AEEYEKLKEKLIKLKGEIKSLKKEL-----------EKLEELKKKLAELEKKl 565
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024503300 273 NELQREKA--------------KENEEKFLNLQNEHEKALRIwKKDEENLRREMDTIKNELNSLKKTQGHLDD 331
Cdd:PRK03918 566 DELEEELAellkeleelgfesvEELEERLKELEPFYNEYLEL-KDAEKELEREEKELKKLEEELDKAFEELAE 637
|
|
| ANIS5_cation-bd |
pfam02520 |
SXP/RAL-2 family protein Ani s 5-like, metal-binding domain; This domain is found in proteins ... |
192-266 |
3.00e-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: 3.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 192 ENINLAAKEKQFQELQQKIRMETAIS---KRVQEENANIKEEKLEILSSLQCVQKQLQQI----TQTNVRMESELNALRE 264
Cdd:pfam02520 12 ETLTIAEKEEQLAAWAEKYGVTDQYKefqANVTALKEEVKKNVTAVISNLSSVLNQLSAIldnkNQTRAQQHEAIDALKQ 91
|
..
gi 2024503300 265 EY 266
Cdd:pfam02520 92 QY 93
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
23-176 |
3.29e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 41.35 E-value: 3.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 23 LETLQHQTDTLQQQNKEAMAAFKKQLQArmfAMEEEKGKYQLAVEIKEKEIDGLKETLKELQISKHTLQK---------K 93
Cdd:PRK00409 539 AEALLKEAEKLKEELEEKKEKLQEEEDK---LLEEAEKEAQQAIKEAKKEADEIIKELRQLQKGGYASVKaheliearkR 615
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 94 LNEMDQKLQMHLTGREEHNKKLNEVERCYATIACQFGIVKGVHEKLEHSVQEAI-QLNKKLTSVNKRQETEisnlKEELK 172
Cdd:PRK00409 616 LNKANEKKEKKKKKQKEKQEELKVGDEVKYLSLGQKGEVLSIPDDKEAIVQAGImKMKVPLSDLEKIQKPK----KKKKK 691
|
....
gi 2024503300 173 KVTT 176
Cdd:PRK00409 692 KPKT 695
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
180-300 |
3.34e-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: 3.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 180 RSKVTSQHRVGEENIN-LAAKEKQFQELQQKIRMETAISKRVQEENANIkEEKLEILSSLQCV----------------- 241
Cdd:COG4913 595 RRRIRSRYVLGFDNRAkLAALEAELAELEEELAEAEERLEALEAELDAL-QERREALQRLAEYswdeidvasaereiael 673
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024503300 242 QKQLQQITQTNV---RMESELNALREEYQTLERDNELQREKAKENEEKFLNLQNEHEKALRI 300
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 ... |
51-285 |
4.01e-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: 4.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 51 RMFAMEEEKGKYQLAVEIKEKEIDGLKETLKELQISKHTLQKKLNEMDQKLQMhltgREEHNKKLNEvERcyatiacqfg 130
Cdd:pfam01576 90 RSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILL----LEDQNSKLSK-ER---------- 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 131 ivKGVHEKL---EHSVQEAIQLNKKLTSVNKRQETEISNLKEELKK-----------------VTTDLIRSKVTSQHRVG 190
Cdd:pfam01576 155 --KLLEERIsefTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKeekgrqelekakrklegESTDLQEQIAELQAQIA 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 191 EENINLAAKEKQFQELQQKIRMETAISKRVQEENANIKEEKLEILSSLQCVQKQLQQITQTNVRMESELNALREEYQ-TL 269
Cdd:pfam01576 233 ELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEdTL 312
|
250
....*....|....*.
gi 2024503300 270 ERDNELQREKAKENEE 285
Cdd:pfam01576 313 DTTAAQQELRSKREQE 328
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
54-331 |
4.04e-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: 41.58 E-value: 4.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 54 AMEEEKGKYQLAVEIKEKEIDGLKET-LKELQIS---KHTLQKKLNEMDQKL-QMHLTGREEHNkklNEVERCYATIACQ 128
Cdd:TIGR01612 932 SIEKFHNKQNILKEILNKNIDTIKESnLIEKSYKdkfDNTLIDKINELDKAFkDASLNDYEAKN---NELIKYFNDLKAN 1008
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 129 FGIVKG--------VHEKLEHSV-QEAIQLNKKLTSVNKRQETEISNLKEELKKVTTDLIRSKVTSQHRVGEENINlaak 199
Cdd:TIGR01612 1009 LGKNKEnmlyhqfdEKEKATNDIeQKIEDANKNIPNIEIAIHTSIYNIIDEIEKEIGKNIELLNKEILEEAEINIT---- 1084
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 200 ekQFQELQQKIRMETaISKRVQEENANIKEE----KLEILSSLQCVQKQLQQITQTNVRMESELNALREEYQTLER--DN 273
Cdd:TIGR01612 1085 --NFNEIKEKLKHYN-FDDFGKEENIKYADEinkiKDDIKNLDQKIDHHIKALEEIKKKSENYIDEIKAQINDLEDvaDK 1161
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 2024503300 274 ELQREKAKENEEKFLNLQNEHEKalriwkkdEENLRREMDTIKNELNSLKKTQGHLDD 331
Cdd:TIGR01612 1162 AISNDDPEEIEKKIENIVTKIDK--------KKNIYDEIKKLLNEIAEIEKDKTSLEE 1211
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
36-324 |
4.74e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.82 E-value: 4.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 36 QNKEAMAAFKKQLQARMFAMEEEKGKyqlaveiKEKEIDGLKETLKELQISKHTLQKKLNEMdqklqmhltgrEEHNKKL 115
Cdd:PRK03918 179 ERLEKFIKRTENIEELIKEKEKELEE-------VLREINEISSELPELREELEKLEKEVKEL-----------EELKEEI 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 116 NEVERcyatiacQFGIVKGVHEKLEHSVQEAIQLNKKLTSVNKRQETEISNLKEELKKVTTDLIRSKVTSQHRVGEENIn 195
Cdd:PRK03918 241 EELEK-------ELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREI- 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 196 laakEKQFQELQQKIRmetAISKRVQEenANIKEEKLEILSslqcvqKQLQQITQTNVRMESELNALREEYQTLERDNEL 275
Cdd:PRK03918 313 ----EKRLSRLEEEIN---GIEERIKE--LEEKEERLEELK------KKLKELEKRLEELEERHELYEEAKAKKEELERL 377
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 2024503300 276 QREKAKENEEKFLNLQNEHEKALRIWKKDEENLRREMDTIKNELNSLKK 324
Cdd:PRK03918 378 KKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKK 426
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
215-378 |
5.67e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 40.58 E-value: 5.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 215 AISKR-------VQEENANIKEEKLEI---LSSLQCVQKQLQQITQtnvrmesELNALREEYQTLERDNELQREKAKENE 284
Cdd:PRK00409 492 EIAKRlglpeniIEEAKKLIGEDKEKLnelIASLEELERELEQKAE-------EAEALLKEAEKLKEELEEKKEKLQEEE 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 285 EKFL-NLQNEHEKALRIWKKDEENLRREMDTIKNELNS------LKKTQGHLDDCHPP---QGNQHSEQVENLQIHSTVH 354
Cdd:PRK00409 565 DKLLeEAEKEAQQAIKEAKKEADEIIKELRQLQKGGYAsvkaheLIEARKRLNKANEKkekKKKKQKEKQEELKVGDEVK 644
|
170 180
....*....|....*....|....
gi 2024503300 355 pvIRNSGQeqsKGsEIQAIQKKND 378
Cdd:PRK00409 645 --YLSLGQ---KG-EVLSIPDDKE 662
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
148-319 |
5.85e-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: 5.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 148 QLNKKLTSVNKRQET---EISNLKEELKKVTTDLIRSKVtsqhRVGEENINLAAKEKQFQELQQKIrmetaisKRVQEEN 224
Cdd:COG1579 14 ELDSELDRLEHRLKElpaELAELEDELAALEARLEAAKT----ELEDLEKEIKRLELEIEEVEARI-------KKYEEQL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 225 ANIKEEKleilsSLQCVQKQLQQITQTNVRMESELNALREEYQTLERDNELQREKAKENEEKFLNLQNEHEKALRIWKKD 304
Cdd:COG1579 83 GNVRNNK-----EYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAE 157
|
170
....*....|....*
gi 2024503300 305 EENLRREMDTIKNEL 319
Cdd:COG1579 158 LEELEAEREELAAKI 172
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
137-295 |
7.20e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.14 E-value: 7.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 137 EKLEHSVQEAIQLNKKLTSVNKRQET---EISNLKEELKKVttDLIRSKVTSQHRVGEENINLAAKEKQFQELQQKIR-- 211
Cdd:COG4717 81 KEAEEKEEEYAELQEELEELEEELEEleaELEELREELEKL--EKLLQLLPLYQELEALEAELAELPERLEELEERLEel 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 212 --METAISKRVQE-ENANIKEEKLEILSSLQcVQKQLQQITQTNVRMESELNALREEYQTLERDNELQREKAKENEEKFL 288
Cdd:COG4717 159 reLEEELEELEAElAELQEELEELLEQLSLA-TEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELE 237
|
....*..
gi 2024503300 289 NLQNEHE 295
Cdd:COG4717 238 AAALEER 244
|
|
| BLOC1_2 |
pfam10046 |
Biogenesis of lysosome-related organelles complex-1 subunit 2; Members of this family of ... |
255-330 |
7.55e-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: 36.80 E-value: 7.55e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024503300 255 MESELNALREEYQTLERDNELQREKAKENEEKFLNLQNEHEKalrIWKKDEE--NLRREMDTIKNELNSLKKTQGHLD 330
Cdd:pfam10046 11 LEAELEATVEDYKLLEKMNEATSLKYKDMKDVAASLEKELEE---LNQKYEElqPYLQQIDQIEEQVTKLEETVYELD 85
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
33-378 |
7.89e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 39.89 E-value: 7.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 33 LQQQNKEAMAAFKKQLQARMFAMEE-EKGKYQLAVEIKEK--EIDGLKETLKELQISKHTLQKKLNEMDQKLQMHLTGRE 109
Cdd:COG4372 18 LRPKTGILIAALSEQLRKALFELDKlQEELEQLREELEQAreELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 110 EHNKKLNEVERCYATIACQFgivkgvhEKLEHSVQEAIQLNKKLTSVNKRQETEISNLKEELKKVTTDLIR-SKVTSQHR 188
Cdd:COG4372 98 QAQEELESLQEEAEELQEEL-------EELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESlQEELAALE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 189 VGEENINLAAKEKQFQELQQKIRmetaisKRVQEENANIKEEKLEILSSLQCVQKQLQQITQTNVRMESELNALREEYQT 268
Cdd:COG4372 171 QELQALSEAEAEQALDELLKEAN------RNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALEL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 269 LERDNELQREKAKENEEKFLNLQNEHEKALRIWKKDEENLRREMDTIKNELNSLKKTQGHLDDCHPPQGNQHSEQVENLQ 348
Cdd:COG4372 245 EEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLEL 324
|
330 340 350
....*....|....*....|....*....|
gi 2024503300 349 IHSTVHPVIRNSGQEQSKGSEIQAIQKKND 378
Cdd:COG4372 325 AKKLELALAILLAELADLLQLLLVGLLDND 354
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
63-379 |
7.93e-03 |
|
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: 40.11 E-value: 7.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 63 QLAVEIKEKEIDGlKETLKELQISKHTLQKKLN---EMDQKLQMHLTGRE----EHNKKLNE-VERCYATIACQFGIVKG 134
Cdd:pfam05557 13 QLQNEKKQMELEH-KRARIELEKKASALKRQLDresDRNQELQKRIRLLEkreaEAEEALREqAELNRLKKKYLEALNKK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 135 VHEKlEHSVQEAIQLNKKLTSVNKRQETEISNLKEELKKVTTDLIRSkvtsQHRVGEENINLAAKEKQFQELQQKIRMET 214
Cdd:pfam05557 92 LNEK-ESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEEL----QERLDLLKAKASEAEQLRQNLEKQQSSLA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 215 AISKRVQEenaniKEEKLEILSSLQCVQKQLQQITQTNVRMESELNALREE---YQTLERDNELQREKAKENEEKFLNLQ 291
Cdd:pfam05557 167 EAEQRIKE-----LEFEIQSQEQDSEIVKNSKSELARIPELEKELERLREHnkhLNENIENKLLLKEEVEDLKRKLEREE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024503300 292 NEHEKALriwkkdeeNLRREMDTIKNELNSLKKT-QGHLDDCHPPQgnQHSEQVENLQIHSTVHPVIRNSGQEQSKGSEI 370
Cdd:pfam05557 242 KYREEAA--------TLELEKEKLEQELQSWVKLaQDTGLNLRSPE--DLSRRIEQLQQREIVLKEENSSLTSSARQLEK 311
|
....*....
gi 2024503300 371 QAIQKKNDC 379
Cdd:pfam05557 312 ARRELEQEL 320
|
|
| |
