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Conserved domains on  [gi|1720408942|ref|XP_030109448|]
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leucine zipper protein 1 isoform X2 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Smc super family cl34174
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
19-354 1.84e-14

Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];


The actual alignment was detected with superfamily member COG1196:

Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 78.22  E-value: 1.84e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942   19 KLQSLSRRLDELEEATKNLQRAEDELLDLQDKviqaegsdsstLAEIEVLRQRVL--KIEGKDEEIKRAEDlchtmkekl 96
Cdd:COG1196    187 NLERLEDLLEELEKQLEKLERQAEKAERYQEL-----------KAELRELELALLlaKLKELRKELEELEE--------- 246
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942   97 eEEENLTRELKSEIERLQKRMVDLEKLEEALSRSKNECSQLCLSLNEERNLTKKISSELEMLRVKVKELESSEDRLDKTE 176
Cdd:COG1196    247 -ELSRLEEELEELQEELEEAEKEIEELKSELEELREELEELQEELLELKEEIEELEGEISLLRERLEELENELEELEERL 325
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  177 QSLVSELEKLKSLTLSFVNERKYLNEKEKENEKIIKELTQKLEQNKKMNRDHM---RNASTFLERNDLRIEDGISSTLSS 253
Cdd:COG1196    326 EELKEKIEALKEELEERETLLEELEQLLAELEEAKEELEEKLSALLEELEELFealREELAELEAELAEIRNELEELKRE 405
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  254 KESKRKGSLDYLKQVENETRDKSENEKNRNQEDNKVKDLNQEIEKLKTQIKHFESLEEELKKMRAKNNDLQDNYLTELNR 333
Cdd:COG1196    406 IESLEERLERLSERLEDLKEELKELEAELEELQTELEELNEELEELEEQLEELRDRLKELERELAELQEELQRLEKELSS 485
                          330       340
                   ....*....|....*....|.
gi 1720408942  334 NRSLASQLEEIKLQVRKQKEL 354
Cdd:COG1196    486 LEARLDRLEAEQRASQGVRAV 506
 
Name Accession Description Interval E-value
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
19-354 1.84e-14

Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 78.22  E-value: 1.84e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942   19 KLQSLSRRLDELEEATKNLQRAEDELLDLQDKviqaegsdsstLAEIEVLRQRVL--KIEGKDEEIKRAEDlchtmkekl 96
Cdd:COG1196    187 NLERLEDLLEELEKQLEKLERQAEKAERYQEL-----------KAELRELELALLlaKLKELRKELEELEE--------- 246
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942   97 eEEENLTRELKSEIERLQKRMVDLEKLEEALSRSKNECSQLCLSLNEERNLTKKISSELEMLRVKVKELESSEDRLDKTE 176
Cdd:COG1196    247 -ELSRLEEELEELQEELEEAEKEIEELKSELEELREELEELQEELLELKEEIEELEGEISLLRERLEELENELEELEERL 325
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  177 QSLVSELEKLKSLTLSFVNERKYLNEKEKENEKIIKELTQKLEQNKKMNRDHM---RNASTFLERNDLRIEDGISSTLSS 253
Cdd:COG1196    326 EELKEKIEALKEELEERETLLEELEQLLAELEEAKEELEEKLSALLEELEELFealREELAELEAELAEIRNELEELKRE 405
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  254 KESKRKGSLDYLKQVENETRDKSENEKNRNQEDNKVKDLNQEIEKLKTQIKHFESLEEELKKMRAKNNDLQDNYLTELNR 333
Cdd:COG1196    406 IESLEERLERLSERLEDLKEELKELEAELEELQTELEELNEELEELEEQLEELRDRLKELERELAELQEELQRLEKELSS 485
                          330       340
                   ....*....|....*....|.
gi 1720408942  334 NRSLASQLEEIKLQVRKQKEL 354
Cdd:COG1196    486 LEARLDRLEAEQRASQGVRAV 506
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
104-353 2.65e-12

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 71.25  E-value: 2.65e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  104 RELKSEIERLQKRMVDLEKLEEALSRSKNECSQLCLSLNEERNLTKKISSELEMLRVKVKELESSEDRLDKTEQSLVSEL 183
Cdd:PRK03918   172 KEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLE 251
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  184 EKLKSLTLSFVNERKYLNEKEKEN---EKIIKELTQ---------KLEQNKKMNRDHMRNASTFLERNDLRIEdGISSTL 251
Cdd:PRK03918   252 GSKRKLEEKIRELEERIEELKKEIeelEEKVKELKElkekaeeyiKLSEFYEEYLDELREIEKRLSRLEEEIN-GIEERI 330
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  252 SSKESKrKGSLDYLKQVENETRDKSENEKNRNQEDNKVKDLNQEIEKLKTQIKHF--ESLEEELKKMRAKNNDLQDNYLT 329
Cdd:PRK03918   331 KELEEK-EERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLtpEKLEKELEELEKAKEEIEEEISK 409
                          250       260
                   ....*....|....*....|....
gi 1720408942  330 ELNRNRSLASQLEEIKLQVRKQKE 353
Cdd:PRK03918   410 ITARIGELKKEIKELKKAIEELKK 433
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
103-362 1.53e-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: 65.47  E-value: 1.53e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  103 TRELKSEIERLQKRMVDLEKLEEAL----SRSKNECSQLCLSLNEERNLTKKISSELEML---RVKVKE-LESSEDRLDK 174
Cdd:TIGR02169  669 SRSEPAELQRLRERLEGLKRELSSLqselRRIENRLDELSQELSDASRKIGEIEKEIEQLeqeEEKLKErLEELEEDLSS 748
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  175 TEQSLVSELEKLKSLTLSFVNERKYLNEKEKENEKIIKELTQKLEQNKkmnRDHMRNASTFLERNDLRIEDgISSTLSSK 254
Cdd:TIGR02169  749 LEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEI---QAELSKLEEEVSRIEARLRE-IEQKLNRL 824
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  255 ESKRKGSLDYLKQVENETRDKSENEKNRNQE----DNKVKDLNQEIEKLKTQIKHFES----LEEELKKMRAKNNDLQDN 326
Cdd:TIGR02169  825 TLEKEYLEKEIQELQEQRIDLKEQIKSIEKEienlNGKKEELEEELEELEAALRDLESrlgdLKKERDELEAQLRELERK 904
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 1720408942  327 Y---LTELNRNRSLASQLEEiKLQVRKQ--KELGNGDIEGE 362
Cdd:TIGR02169  905 IeelEAQIEKKRKRLSELKA-KLEALEEelSEIEDPKGEDE 944
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N-terminus of SMC proteins. The ...
61-353 5.17e-07

RecF/RecN/SMC N terminal domain; This domain is found at the N-terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 53.82  E-value: 5.17e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942   61 TLAEIEVLRQRVLKIEGKDEEIKRAEDlchtmKEKLEEEENLTRELKSEIERLQKRMVDLEKLEEALSRSKNECSQLCLS 140
Cdd:pfam02463  174 ALKKLIEETENLAELIIDLEELKLQEL-----KLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRD 248
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  141 LNEERNLTKKI---SSELEMLRVKVKELESSEDRLDKTEQSLVSELEKLKSLTLSFVNERKYLNEKEKENEKIIKELTQK 217
Cdd:pfam02463  249 EQEEIESSKQEiekEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEK 328
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  218 LEQNKKMNRDHMRNASTFLERNDLRIEDGISSTLSS--KESKRKGSLDYLKQVENETRDKSENEKN-----RNQEDNKVK 290
Cdd:pfam02463  329 ELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLqeKLEQLEEELLAKKKLESERLSSAAKLKEeelelKSEEEKEAQ 408
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720408942  291 DLNQEIEKLKTQIKHFESLEEELKKMRAKNNDLQDNYLTELNRNRSLASQLEEIKLQVRKQKE 353
Cdd:pfam02463  409 LLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSE 471
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
262-346 4.66e-03

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 40.39  E-value: 4.66e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942   262 LDYLKQVENETRDKSENEKNRNQEdnKVKDLNQEIEKLKTQIKHFESLEEELKKMRAKNNDLQDNYLTELNrnrSLASQL 341
Cdd:smart00787  188 LRQLKQLEDELEDCDPTELDRAKE--KLKKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIA---EAEKKL 262

                    ....*
gi 1720408942   342 EEIKL 346
Cdd:smart00787  263 EQCRG 267
 
Name Accession Description Interval E-value
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
19-354 1.84e-14

Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 78.22  E-value: 1.84e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942   19 KLQSLSRRLDELEEATKNLQRAEDELLDLQDKviqaegsdsstLAEIEVLRQRVL--KIEGKDEEIKRAEDlchtmkekl 96
Cdd:COG1196    187 NLERLEDLLEELEKQLEKLERQAEKAERYQEL-----------KAELRELELALLlaKLKELRKELEELEE--------- 246
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942   97 eEEENLTRELKSEIERLQKRMVDLEKLEEALSRSKNECSQLCLSLNEERNLTKKISSELEMLRVKVKELESSEDRLDKTE 176
Cdd:COG1196    247 -ELSRLEEELEELQEELEEAEKEIEELKSELEELREELEELQEELLELKEEIEELEGEISLLRERLEELENELEELEERL 325
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  177 QSLVSELEKLKSLTLSFVNERKYLNEKEKENEKIIKELTQKLEQNKKMNRDHM---RNASTFLERNDLRIEDGISSTLSS 253
Cdd:COG1196    326 EELKEKIEALKEELEERETLLEELEQLLAELEEAKEELEEKLSALLEELEELFealREELAELEAELAEIRNELEELKRE 405
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  254 KESKRKGSLDYLKQVENETRDKSENEKNRNQEDNKVKDLNQEIEKLKTQIKHFESLEEELKKMRAKNNDLQDNYLTELNR 333
Cdd:COG1196    406 IESLEERLERLSERLEDLKEELKELEAELEELQTELEELNEELEELEEQLEELRDRLKELERELAELQEELQRLEKELSS 485
                          330       340
                   ....*....|....*....|.
gi 1720408942  334 NRSLASQLEEIKLQVRKQKEL 354
Cdd:COG1196    486 LEARLDRLEAEQRASQGVRAV 506
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
14-351 2.28e-13

Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 74.75  E-value: 2.28e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942   14 RHLRFKLQSLSRRLDELEEATKNLQRAEDELLDLQDKVIQAEGSDSSTLAEIEVLRQRVL-KIEGKDEEIKRAEDLCHTM 92
Cdd:COG1196    691 KSLKNELRSLEDLLEELRRQLEELERQLEELKRELAALEEELEQLQSRLEELEEELEELEeELEELQERLEELEEELESL 770
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942   93 KEKLEEEENLTRELKSEIERLQKRmvdLEKLEEALSRSKNECSQLCLSLNEERNLTKKISSELEMLRVKVKELESSEDRL 172
Cdd:COG1196    771 EEALAKLKEEIEELEEKRQALQEE---LEELEEELEEAERRLDALERELESLEQRRERLEQEIEELEEEIEELEEKLDEL 847
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  173 DKTEQSLVSELEKLKSLTLSFVNERKYLNEKEKENEKIIKELTQKLEQnkkmnrdhmrnastfLERNDLRIEDGISSTLS 252
Cdd:COG1196    848 EEELEELEKELEELKEELEELEAEKEELEDELKELEEEKEELEEELRE---------------LESELAELKEEIEKLRE 912
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  253 SKESKRKgsldyLKQVENETRDKSENEKNRNQEDNKVKDLNQEIEKLKTQIKHFE-----SLEE--ELKKMRAKNNDLQD 325
Cdd:COG1196    913 RLEELEA-----KLERLEVELPELEEELEEEYEDTLETELEREIERLEEEIEALGpvnlrAIEEyeEVEERYEELKSQRE 987
                          330       340
                   ....*....|....*....|....*.
gi 1720408942  326 NYLTELNRNRSLASQLEEIKLQVRKQ 351
Cdd:COG1196    988 DLEEAKEKLLEVIEELDKEKRERFKE 1013
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
104-379 3.45e-13

Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 73.98  E-value: 3.45e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  104 RELKSEIERLQKRMVDLEKLEEALSRSKNECSQLCLSLNEERNLTKKISSELEMLRVKVKELESSEDRLDKTEQSLVSEL 183
Cdd:COG1196    667 RELKELEEELAELEAQLEKLEEELKSLKNELRSLEDLLEELRRQLEELERQLEELKRELAALEEELEQLQSRLEELEEEL 746
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  184 EKLKS---LTLSFVNERKYLNEKEKENEKIIKELTQKLEQNKKMNRDHMRNASTFLERNDLRiedgISSTLSSKESKRKG 260
Cdd:COG1196    747 EELEEeleELQERLEELEEELESLEEALAKLKEEIEELEEKRQALQEELEELEEELEEAERR----LDALERELESLEQR 822
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  261 SLDYLKQVENETRDKSENEKNRNQEDNKVKDLNQEIEKLKTQIKHFE----SLEEELKKMRAKNNDLQdnyltelNRNRS 336
Cdd:COG1196    823 RERLEQEIEELEEEIEELEEKLDELEEELEELEKELEELKEELEELEaekeELEDELKELEEEKEELE-------EELRE 895
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 1720408942  337 LASQLEEIKLQVRKQKELGNgDIEGEDAFLLGRGRHERTKLKG 379
Cdd:COG1196    896 LESELAELKEEIEKLRERLE-ELEAKLERLEVELPELEEELEE 937
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
7-356 1.12e-12

Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 72.44  E-value: 1.12e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942    7 YKDAASNRHLRFKLQSLSRRLDELEEatkNLQRAEDELLDLQDKVIQAEGsdsstlaEIEVLRQRVLKIEGKDEEIKRAE 86
Cdd:COG1196    656 SRNKRSSLAQKRELKELEEELAELEA---QLEKLEEELKSLKNELRSLED-------LLEELRRQLEELERQLEELKREL 725
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942   87 dlchtmkekleeeenltRELKSEIERLQKRmvdLEKLEEALSRSKNECSQLCLSLNEERNLTKKISSELEMLRVKVKELE 166
Cdd:COG1196    726 -----------------AALEEELEQLQSR---LEELEEELEELEEELEELQERLEELEEELESLEEALAKLKEEIEELE 785
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  167 SSEDRLDKTEQSLVSELEKLKSLTLSFVNERKYLNEKEKENEKIIKELTQKLEQNKKmnrdhmrnastflERNDLRIEdg 246
Cdd:COG1196    786 EKRQALQEELEELEEELEEAERRLDALERELESLEQRRERLEQEIEELEEEIEELEE-------------KLDELEEE-- 850
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  247 ISSTLSSKESKRKGSLDYLKQVENETRDKSENEKNRNQEDNKVKDLNQEIEKLKTQIK----HFESLEEELKKMRAKNND 322
Cdd:COG1196    851 LEELEKELEELKEELEELEAEKEELEDELKELEEEKEELEEELRELESELAELKEEIEklreRLEELEAKLERLEVELPE 930
                          330       340       350
                   ....*....|....*....|....*....|....
gi 1720408942  323 LQDNYLTELNRNRSLASQlEEIKLQVRKQKELGN 356
Cdd:COG1196    931 LEEELEEEYEDTLETELE-REIERLEEEIEALGP 963
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
104-353 2.65e-12

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 71.25  E-value: 2.65e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  104 RELKSEIERLQKRMVDLEKLEEALSRSKNECSQLCLSLNEERNLTKKISSELEMLRVKVKELESSEDRLDKTEQSLVSEL 183
Cdd:PRK03918   172 KEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLE 251
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  184 EKLKSLTLSFVNERKYLNEKEKEN---EKIIKELTQ---------KLEQNKKMNRDHMRNASTFLERNDLRIEdGISSTL 251
Cdd:PRK03918   252 GSKRKLEEKIRELEERIEELKKEIeelEEKVKELKElkekaeeyiKLSEFYEEYLDELREIEKRLSRLEEEIN-GIEERI 330
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  252 SSKESKrKGSLDYLKQVENETRDKSENEKNRNQEDNKVKDLNQEIEKLKTQIKHF--ESLEEELKKMRAKNNDLQDNYLT 329
Cdd:PRK03918   331 KELEEK-EERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLtpEKLEKELEELEKAKEEIEEEISK 409
                          250       260
                   ....*....|....*....|....
gi 1720408942  330 ELNRNRSLASQLEEIKLQVRKQKE 353
Cdd:PRK03918   410 ITARIGELKKEIKELKKAIEELKK 433
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
3-353 2.16e-11

DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];


Pssm-ID: 223496 [Multi-domain]  Cd Length: 908  Bit Score: 68.25  E-value: 2.16e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942    3 ELTNYKDAASNRHLRFKLQSLSRRLDELEEATKNLQRAEDELLDLQDKVIQAEGSDSSTLAEIEVLrqrvlkIEGKDEEI 82
Cdd:COG0419    217 KLEEIQEEQEEEELEQEIEALEERLAELEEEKERLEELKARLLEIESLELEALKIREEELRELERL------LEELEEKI 290
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942   83 KRAEDLchtmkekleeeENLTRELKSEIERLQKRMVDLEKLEEALSRSKNECSQLCLSLNEERNLTKKISSELEMLRVKV 162
Cdd:COG0419    291 ERLEEL-----------EREIEELEEELEGLRALLEELEELLEKLKSLEERLEKLEEKLEKLESELEELAEEKNELAKLL 359
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  163 KELESS-EDRLDKTEQSLVSELE--------------KLKSLTLSFVNERKYLNEKEKENEKIIKELTQKLEQNKKMNRD 227
Cdd:COG0419    360 EERLKElEERLEELEKELEKALErlkqleeaiqelkeELAELSAALEEIQEELEELEKELEELERELEELEEEIKKLEEQ 439
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  228 HMRNASTFLERNDLRIEDGISSTLSSK--ESKRKGSLDYLKQVENETRDKSENEKNRNQEDNKVKDLNQEIEKLKTQIKH 305
Cdd:COG0419    440 INQLESKELMIAELAGAGEKCPVCGQElpEEHEKELLELYELELEELEEELSREKEEAELREEIEELEKELRELEEELIE 519
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1720408942  306 --------FESLEEELKKMRAKNNDLQDNYL-TELNRNRSLASQLEEIKLQVRKQKE 353
Cdd:COG0419    520 lleleealKEELEEKLEKLENLLEELEELKEkLQLQQLKEELRQLEDRLQELKELLE 576
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
19-356 2.50e-11

DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];


Pssm-ID: 223496 [Multi-domain]  Cd Length: 908  Bit Score: 67.86  E-value: 2.50e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942   19 KLQSLSRRLDELEEATKNLQRAEDELLDLQDKVIQAEGSDS---------STLAEIEVLRQRVLKIEGKDEEIKRAEDLC 89
Cdd:COG0419    418 ELEELERELEELEEEIKKLEEQINQLESKELMIAELAGAGEkcpvcgqelPEEHEKELLELYELELEELEEELSREKEEA 497
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942   90 HTMKEKLEEEENLTRELKSEIERLQKRMVDLEKLEEALSRSKNECSQLCLslNEERNLTKKISSELEMLRVKVKELESSE 169
Cdd:COG0419    498 ELREEIEELEKELRELEEELIELLELEEALKEELEEKLEKLENLLEELEE--LKEKLQLQQLKEELRQLEDRLQELKELL 575
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  170 DRLDKTEQSLvSELEKLksltlsfvnerkylNEKEKENEKIIKELTQKLEQ-NKKMNRDHMRNASTFLERNDLRIEDgIS 248
Cdd:COG0419    576 EELRLLRTRK-EELEEL--------------RERLKELKKKLKELEERLSQlEELLQSLELSEAENELEEAEEELES-EL 639
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  249 STLSSKESKRKGSLDYLKQVEN---ETRDKSENEKNRNQEDNKVKDLNQEIEKLKTQIKHFESLEEELKKMRAKNNDLQD 325
Cdd:COG0419    640 EKLNLQAELEELLQAALEELEEkveELEAEIRRELQRIENEEQLEEKLEELEQLEEELEQLREELEELLKKLGEIEQLIE 719
                          330       340       350
                   ....*....|....*....|....*....|.
gi 1720408942  326 NYLTELNRNRSLASQLEEIKLQVRKQKELGN 356
Cdd:COG0419    720 ELESRKAELEELKKELEKLEKALELLEELRE 750
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
28-360 3.08e-11

Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 67.82  E-value: 3.08e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942   28 DELEEATKNLQRAEDELLDLQDKviqaegsdsstlaeIEVLRQRVLKIEgkdEEIKRAEDlchtmkekleeeenlTRELK 107
Cdd:COG1196    172 ERKEEAERKLERTEENLERLEDL--------------LEELEKQLEKLE---RQAEKAER---------------YQELK 219
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  108 SEIERLQKRMV--DLEKLEEALSRSKNECSQLCLSLNEERNLTKKISSELEMLRVKVKELESSEDRLDKTEQSLVSELEK 185
Cdd:COG1196    220 AELRELELALLlaKLKELRKELEELEEELSRLEEELEELQEELEEAEKEIEELKSELEELREELEELQEELLELKEEIEE 299
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  186 LKSLTLSFVNERKYLNEKEKENEKIIKELTQKLEQNKKMnrdhmrnastFLERNDLRIE-----DGISSTLSSKESKRKG 260
Cdd:COG1196    300 LEGEISLLRERLEELENELEELEERLEELKEKIEALKEE----------LEERETLLEEleqllAELEEAKEELEEKLSA 369
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  261 SLDYLKQVENETRDK-SENEKNRNQEDNKVKDLNQEIEKLKTQIKHFESLEEELKKMRAKNNDLQDNYLTELNRNRSLAS 339
Cdd:COG1196    370 LLEELEELFEALREElAELEAELAEIRNELEELKREIESLEERLERLSERLEDLKEELKELEAELEELQTELEELNEELE 449
                          330       340
                   ....*....|....*....|.
gi 1720408942  340 QLEEIKLQVRKQKELGNGDIE 360
Cdd:COG1196    450 ELEEQLEELRDRLKELERELA 470
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
28-345 1.34e-10

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 65.47  E-value: 1.34e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942   28 DELEEATKNLQRAEDELLDLQDKVIQAEGSDSSTLAEIEVLRQRVLKIEGKDEEIKRAEDLCHTMKEKLEEEENLTRELK 107
Cdd:PRK03918   193 ELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELK 272
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  108 SEIERLQKRMVDLEKLEE------ALSRSKNEcsqlclSLNEERNLTK---KISSELEMLRVKVKELESSEDRLDKTEQS 178
Cdd:PRK03918   273 KEIEELEEKVKELKELKEkaeeyiKLSEFYEE------YLDELREIEKrlsRLEEEINGIEERIKELEEKEERLEELKKK 346
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  179 LvSELEKLKSLTLSFVNERKYLNEKEKENEKIIKELTQKLEQNKKMNRDHMRNASTFLERNDLRIEDGISStLSSKESKR 258
Cdd:PRK03918   347 L-KELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGE-LKKEIKEL 424
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  259 KGSLDYLKQVENET----RDKSENEKnrnqeDNKVKDLNQEIEKLKTQIKHFESLEEELKKmRAKNNDLQDNYLTELNRN 334
Cdd:PRK03918   425 KKAIEELKKAKGKCpvcgRELTEEHR-----KELLEEYTAELKRIEKELKEIEEKERKLRK-ELRELEKVLKKESELIKL 498
                          330
                   ....*....|.
gi 1720408942  335 RSLASQLEEIK 345
Cdd:PRK03918   499 KELAEQLKELE 509
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
103-362 1.53e-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: 65.47  E-value: 1.53e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  103 TRELKSEIERLQKRMVDLEKLEEAL----SRSKNECSQLCLSLNEERNLTKKISSELEML---RVKVKE-LESSEDRLDK 174
Cdd:TIGR02169  669 SRSEPAELQRLRERLEGLKRELSSLqselRRIENRLDELSQELSDASRKIGEIEKEIEQLeqeEEKLKErLEELEEDLSS 748
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  175 TEQSLVSELEKLKSLTLSFVNERKYLNEKEKENEKIIKELTQKLEQNKkmnRDHMRNASTFLERNDLRIEDgISSTLSSK 254
Cdd:TIGR02169  749 LEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEI---QAELSKLEEEVSRIEARLRE-IEQKLNRL 824
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  255 ESKRKGSLDYLKQVENETRDKSENEKNRNQE----DNKVKDLNQEIEKLKTQIKHFES----LEEELKKMRAKNNDLQDN 326
Cdd:TIGR02169  825 TLEKEYLEKEIQELQEQRIDLKEQIKSIEKEienlNGKKEELEEELEELEAALRDLESrlgdLKKERDELEAQLRELERK 904
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 1720408942  327 Y---LTELNRNRSLASQLEEiKLQVRKQ--KELGNGDIEGE 362
Cdd:TIGR02169  905 IeelEAQIEKKRKRLSELKA-KLEALEEelSEIEDPKGEDE 944
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
14-314 1.97e-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: 65.09  E-value: 1.97e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942   14 RHLRFKLQSLSRRLDELEEATKNLQ----RAEDELLDLQDKVIQAEGSDSSTLAEIEVLRQRVLKIEGKDEEIKRAEDLC 89
Cdd:TIGR02169  670 RSEPAELQRLRERLEGLKRELSSLQselrRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSL 749
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942   90 htmkekleeeENLTRELKSEIERLQKRmvdLEKLEEALSRSKNECSQLCLSLNEERnlTKKISSELEMLRVKVKELESSE 169
Cdd:TIGR02169  750 ----------EQEIENVKSELKELEAR---IEELEEDLHKLEEALNDLEARLSHSR--IPEIQAELSKLEEEVSRIEARL 814
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  170 DRLDKTEQSLVSELEKLKSLTLSFVNERKYLNEKEKENEKIIKELTQKLEqnkKMNRDhmrnastfLERNDLRIEDgiss 249
Cdd:TIGR02169  815 REIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKE---ELEEE--------LEELEAALRD---- 879
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720408942  250 tLSSKESKRKgsldylKQVENETRDKSENEKNRNQEDNKVKDLNQEIEKLKTQIkhfESLEEELK 314
Cdd:TIGR02169  880 -LESRLGDLK------KERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKL---EALEEELS 934
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
27-348 2.10e-10

Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 65.12  E-value: 2.10e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942   27 LDELEEATKNLQRAEDELLDLQDKVIQAEGSDSSTLAEIEVLRQRVLKIegkDEEIKRAEdlchtmkekleeeenltrel 106
Cdd:COG1196    231 LAKLKELRKELEELEEELSRLEEELEELQEELEEAEKEIEELKSELEEL---REELEELQ-------------------- 287
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  107 kseiERLQKRMVDLEKLEEALSRSKNECSQLCLSLNEERNLTKKISSELEMLRVKVKELESSEDRLDKTEQSLVSELEKL 186
Cdd:COG1196    288 ----EELLELKEEIEELEGEISLLRERLEELENELEELEERLEELKEKIEALKEELEERETLLEELEQLLAELEEAKEEL 363
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  187 KSLTLSFVNERKYLNEKEKENEKIIKELTQKLEQNKKMNRDHMRNASTFLERNDLRIEDgISSTLSSKESKRKGSLDYLK 266
Cdd:COG1196    364 EEKLSALLEELEELFEALREELAELEAELAEIRNELEELKREIESLEERLERLSERLED-LKEELKELEAELEELQTELE 442
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  267 QVENETrdkSENEKNRNQEDNKVKDLNQEIEKLKTQIKHFESLEEELKKMRAKNNDLQDNYLTELNRNRSLASQLEEIKL 346
Cdd:COG1196    443 ELNEEL---EELEEQLEELRDRLKELERELAELQEELQRLEKELSSLEARLDRLEAEQRASQGVRAVLEALESGLPGVYG 519

                   ..
gi 1720408942  347 QV 348
Cdd:COG1196    520 PV 521
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
3-319 2.28e-10

Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 64.74  E-value: 2.28e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942    3 ELTNYKDAASNRHLRFKLQSLSRRLDELEEATKNLQRAEDELL----DLQDKVIQAEGSDSSTLAEIEVLRQRVL----K 74
Cdd:COG1196    217 ELKAELRELELALLLAKLKELRKELEELEEELSRLEEELEELQeeleEAEKEIEELKSELEELREELEELQEELLelkeE 296
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942   75 IEGKDEEIKRAEDLCHTMKEKLEEEENLTRELKSEIERLQKRMVDLEKLEEALSRSKNECSQLCLSLNEERnltkkiSSE 154
Cdd:COG1196    297 IEELEGEISLLRERLEELENELEELEERLEELKEKIEALKEELEERETLLEELEQLLAELEEAKEELEEKL------SAL 370
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  155 LEMLRVKVKELESSEDRLDKTEQSLVSELEKLKSLTLSFVNERKYLNEKEKENEKIIKELTQKLEQNKKmnrdhmrnast 234
Cdd:COG1196    371 LEELEELFEALREELAELEAELAEIRNELEELKREIESLEERLERLSERLEDLKEELKELEAELEELQT----------- 439
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  235 flERNDLRIEdgisstLSSKESKRKGSLDYLKQVENETRDKSENEKNRNQEdnkVKDLNQEIEKLKTQIKHFESLEEELK 314
Cdd:COG1196    440 --ELEELNEE------LEELEEQLEELRDRLKELERELAELQEELQRLEKE---LSSLEARLDRLEAEQRASQGVRAVLE 508

                   ....*
gi 1720408942  315 KMRAK 319
Cdd:COG1196    509 ALESG 513
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
104-410 2.68e-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: 2.68e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  104 RELKSEIERLQKRM--VDLEKLEEALSRSKNECSQLCLSLNEERNLTKKISSELEMLRVKVKELESSEDRLDKTEQSLVS 181
Cdd:TIGR02168  216 KELKAELRELELALlvLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALAN 295
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  182 ELEKLKSLTLSFVNERKYLNEKEKENEKIIKELTQKLEQnkkmnrdhmrnastfLERNDLRIEDGISSTLSSKESkrkgs 261
Cdd:TIGR02168  296 EISRLEQQKQILRERLANLERQLEELEAQLEELESKLDE---------------LAEELAELEEKLEELKEELES----- 355
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  262 ldyLKQVENETRDKSENEKNRNQE-DNKVKDLNQEIEKLKTQIkhfESLEEELKKMRAKNNDLQDNYLTELNRNRSLASQ 340
Cdd:TIGR02168  356 ---LEAELEELEAELEELESRLEElEEQLETLRSKVAQLELQI---ASLNNEIERLEARLERLEDRRERLQQEIEELLKK 429
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  341 LEEIKLQvRKQKELGNGDIEGEDAfllgRGRHERTKLKGHGSEASVSKHTSRELSPQHKRERLRNREFAL 410
Cdd:TIGR02168  430 LEEAELK-ELQAELEELEEELEEL----QEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSL 494
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
30-350 4.03e-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: 64.31  E-value: 4.03e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942   30 LEEATKNLQRAED---------ELLDLQDKV------IQAEGSDSSTLAEIEVLRQRVLKIEGKDEEIKRAEDLCHTMKE 94
Cdd:TIGR02168  181 LERTRENLDRLEDilnelerqlKSLERQAEKaerykeLKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTA 260
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942   95 KLEEEENLTRELKSEIERLQKRMVDLEKLEEALSRSKNECSQLCLSLNEERnltKKISSELEMLRVKVKELESSEDRLDK 174
Cdd:TIGR02168  261 ELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERL---ANLERQLEELEAQLEELESKLDELAE 337
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  175 TEQSLVSELEKLKSLTLSFVNERKYLNEKEKENEKIIKELTQKLEQNKKmnrdhmRNASTFLERNDLRIEdgISSTLSSK 254
Cdd:TIGR02168  338 ELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRS------KVAQLELQIASLNNE--IERLEARL 409
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  255 ESKrKGSLDYLKQvENETRDKSENEKNRNQEDNKVKDLNQEIEKLKTQIKHFESLEEELKKMRAKNNDLQDNYLTELNRN 334
Cdd:TIGR02168  410 ERL-EDRRERLQQ-EIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQL 487
                          330
                   ....*....|....*.
gi 1720408942  335 RSLASQLEEIKLQVRK 350
Cdd:TIGR02168  488 QARLDSLERLQENLEG 503
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
30-345 1.13e-09

DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];


Pssm-ID: 223496 [Multi-domain]  Cd Length: 908  Bit Score: 62.47  E-value: 1.13e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942   30 LEEATKNLQRAEDELLDLQ--DKVIQAEGSDSSTL-AEIEVLRQRV-LKIEGKDEEIKRAED-LCHTMKEKLEEEENLTR 104
Cdd:COG0419    149 LKSKPKERKEILDELFGLEkyEKLSELLKEVIKEAkAKIEELEGQLsELLEDIEDLLEALEEeLKELKKLEEIQEEQEEE 228
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  105 ELKSEIERLQKRMVDLEKLEEALSRSKNecsqlclslneerNLTKKISSELEMLRVKVKELESSEDRLDKTEQSLvSELE 184
Cdd:COG0419    229 ELEQEIEALEERLAELEEEKERLEELKA-------------RLLEIESLELEALKIREEELRELERLLEELEEKI-ERLE 294
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  185 KLKSLTLSFVNERKYLNEKEKENEKIIKELTQKLEQNKKMNRDhMRNASTFLERNDLRIEDGiSSTLSSKESKRKGSLDY 264
Cdd:COG0419    295 ELEREIEELEEELEGLRALLEELEELLEKLKSLEERLEKLEEK-LEKLESELEELAEEKNEL-AKLLEERLKELEERLEE 372
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  265 L-KQVENETRDKSENEKNRNQEDNKVKDLNQEIEK----LKTQIKHFESLEEELKKMRAKNNDLQDnyltELNRNRSLAS 339
Cdd:COG0419    373 LeKELEKALERLKQLEEAIQELKEELAELSAALEEiqeeLEELEKELEELERELEELEEEIKKLEE----QINQLESKEL 448

                   ....*.
gi 1720408942  340 QLEEIK 345
Cdd:COG0419    449 MIAELA 454
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
16-345 2.86e-09

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 61.23  E-value: 2.86e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942   16 LRFKLQSLSRRLDELEEATKNLQRAEDELLDLQDKVIQAEGsDSSTLAEIEVLRQRV--LKIEGKDEEIKRAEDLCHTMK 93
Cdd:PRK03918   319 LEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEE-RHELYEEAKAKKEELerLKKRLTGLTPEKLEKELEELE 397
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942   94 EKLEEEENLTRELKSEIERLQKRMVDLEKLEEALSRSKNECSqLC---LSLNEERNLTKKISSELEMLRVKVKELESSED 170
Cdd:PRK03918   398 KAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCP-VCgreLTEEHRKELLEEYTAELKRIEKELKEIEEKER 476
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  171 RLDKTEQSLVSELEKLKSLTlsfvnerkylneKEKENEKIIKELTQKLeqnKKMNRDHMRNASTFLE--RNDLRIEDGIS 248
Cdd:PRK03918   477 KLRKELRELEKVLKKESELI------------KLKELAEQLKELEEKL---KKYNLEELEKKAEEYEklKEKLIKLKGEI 541
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  249 STLSSKESKRKGSLDYLKQVENETRDKSENEKNRNQEDNK-----VKDLNQEIE----------KLKTQIKHFESLEEEL 313
Cdd:PRK03918   542 KSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEElgfesVEELEERLKelepfyneylELKDAEKELEREEKEL 621
                          330       340       350
                   ....*....|....*....|....*....|..
gi 1720408942  314 KKMRAKNNDLQDNYLTELNRNRSLASQLEEIK 345
Cdd:PRK03918   622 KKLEEELDKAFEELAETEKRLEELRKELEELE 653
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
104-439 9.07e-09

Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 59.73  E-value: 9.07e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  104 RELKSEIERLQKRMVDLEKLEEALSRSKNEcSQLCLSLNEERNLTkkissELEMLRVKVKELESSEDRLDKTEQSLVSEL 183
Cdd:COG1196    182 ERTEENLERLEDLLEELEKQLEKLERQAEK-AERYQELKAELREL-----ELALLLAKLKELRKELEELEEELSRLEEEL 255
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  184 EKLKSLTLSFVNERKYLNEKEKENEKIIKELTQKLEQNKK------MNRDHMRNASTFLERNDLRIEDGISSTLSSKESK 257
Cdd:COG1196    256 EELQEELEEAEKEIEELKSELEELREELEELQEELLELKEeieeleGEISLLRERLEELENELEELEERLEELKEKIEAL 335
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  258 RKGSLDYLKQVENETRDKSENEKNRNQEDNKVKDLNQEIEKLKTQIKhfESLEEELKKMRAKNNDLQDNyLTELNRNRSL 337
Cdd:COG1196    336 KEELEERETLLEELEQLLAELEEAKEELEEKLSALLEELEELFEALR--EELAELEAELAEIRNELEEL-KREIESLEER 412
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  338 ASQLEEIKLQVRKQKELGNGDIEGEDAFLLGRGRHERTKLKGHGSEASVSKHTSRELSP-QHKRERLRNREFALSNEHYS 416
Cdd:COG1196    413 LERLSERLEDLKEELKELEAELEELQTELEELNEELEELEEQLEELRDRLKELERELAElQEELQRLEKELSSLEARLDR 492
                          330       340
                   ....*....|....*....|...
gi 1720408942  417 LSSKQASSPVFTNKRAAKASNMG 439
Cdd:COG1196    493 LEAEQRASQGVRAVLEALESGLP 515
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
19-353 1.59e-08

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: 58.49  E-value: 1.59e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942   19 KLQSLSRRLDELEEATKNLQRaedELLDLQDKVIQAEGSDSSTLAEIEVLRQRVLKIEGKdeeIKRAEDLCHTMKEKLEE 98
Cdd:TIGR04523  343 QISQLKKELTNSESENSEKQR---ELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESK---IQNQEKLNQQKDEQIKK 416
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942   99 EENLTRELKSEIERLQKrmvDLEKLEEALSRSKNECSQLCLSLNEERNLTKKISSELEMLRVKVKELESSedrLDKTEQS 178
Cdd:TIGR04523  417 LQQEKELLEKEIERLKE---TIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQN---LEQKQKE 490
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  179 LVSELEKLKSLTlsfvNERKYLNEKEKENEKIIKELTQKLEQnkkmnrdhmrnastfLERNDLRIEDGISST----LSSK 254
Cdd:TIGR04523  491 LKSKEKELKKLN----EEKKELEEKVKDLTKKISSLKEKIEK---------------LESEKKEKESKISDLedelNKDD 551
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  255 ESKRKGSLDYLKQVENETRDKSENE-----KNRNQEDNKVKDLNQEIEKLKTQI----KHFESLEEELKKMRAKNNDLQD 325
Cdd:TIGR04523  552 FELKKENLEKEIDEKNKEIEELKQTqkslkKKQEEKQELIDQKEKEKKDLIKEIeekeKKISSLEKELEKAKKENEKLSS 631
                          330       340
                   ....*....|....*....|....*...
gi 1720408942  326 NYLTELNRNRSLASQLEEIKLQVRKQKE 353
Cdd:TIGR04523  632 IIKNIKSKKNKLKQEVKQIKETIKEIRN 659
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
7-315 3.43e-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: 57.76  E-value: 3.43e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942    7 YKDAASNRHLRFKLQSLSRRLDELEEATKNLQRAEDELLDLQDKVIQAEGSDSSTLAEIEVLRQRVLKIEGKDEEIKRAe 86
Cdd:TIGR02168  218 LKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANE- 296
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942   87 dlchtmkekleeeenlTRELKSEIERLQKRMVDLEKLEEALSRSKNECSQlclSLNEERNLTKKISSELEMLRVKVKELE 166
Cdd:TIGR02168  297 ----------------ISRLEQQKQILRERLANLERQLEELEAQLEELES---KLDELAEELAELEEKLEELKEELESLE 357
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  167 SSEDRLDKTEQSLVSELEKLKSLTLSFVNERKYLNEKEKENEKIIKELTQKLEQNKKMNRDHMRNASTFLERNDLRIEDG 246
Cdd:TIGR02168  358 AELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKE 437
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720408942  247 ISSTLsskESKRKGSLDYLKQVENETRDKSENEKNRNQEDNKVKDLNQEIEKLKTQIKHFESLEEELKK 315
Cdd:TIGR02168  438 LQAEL---EELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEG 503
PTZ00121 PTZ00121
MAEBL; Provisional
16-334 4.36e-08

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 57.46  E-value: 4.36e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942   16 LRFKLQSLSRRLDELEEATKNLQRAeDELLDLQDKVIQAEGSDSSTLAEIEVLRqrvlkiegKDEEIKRAEDLCHTMKEK 95
Cdd:PTZ00121  1488 AKKKAEEAKKKADEAKKAAEAKKKA-DEAKKAEEAKKADEAKKAEEAKKADEAK--------KAEEKKKADELKKAEELK 1558
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942   96 LEEEENLTRELKSEIERlqkRMVDLEKLEEALSRSKNECSQLCLSLNEERNLTKKISSELEMLRVKVKELESSED----- 170
Cdd:PTZ00121  1559 KAEEKKKAEEAKKAEED---KNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEekkkv 1635
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  171 -RLDKTEQSLVSELEKLKSLTLSFVNERKYLNEKEKENEKIIKELTQKLEQNKKMNRDHMRNASTFLERNDLRI----ED 245
Cdd:PTZ00121  1636 eQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKkeaeEK 1715
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  246 GISSTLSSKESKRKGSLDYLKQVENETRDKSENEKNRNQEDNKVKDLNQEIEKLKTQIKHFES--LEEELKKMRAKNNDL 323
Cdd:PTZ00121  1716 KKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEavIEEELDEEDEKRRME 1795
                          330
                   ....*....|.
gi 1720408942  324 QDNYLTELNRN 334
Cdd:PTZ00121  1796 VDKKIKDIFDN 1806
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
105-354 4.31e-07

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: 53.87  E-value: 4.31e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  105 ELKSEIERLQKRMVDLEKLEEALSRSKNECSQLCLSLNEERNLTKKISSELEMLRVKVKELESSEDRLDKTEQSLVSELE 184
Cdd:TIGR04523  156 KLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIE 235
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  185 KLKS----LTLSFVNERKYLNEKEKENEKIIKELTQK---LEQNKKMNRDhmrnastfLERNDLRIEDGISSTlssKESK 257
Cdd:TIGR04523  236 KKQQeineKTTEISNTQTQLNQLKDEQNKIKKQLSEKqkeLEQNNKKIKE--------LEKQLNQLKSEISDL---NNQK 304
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  258 RKGSLDYLK-QVENETRDKSENEKNRNQEDNKVKDLNQEIEKLKTQIKHFESLEEELKK-MRAKNNDLQ------DNYLT 329
Cdd:TIGR04523  305 EQDWNKELKsELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQReLEEKQNEIEklkkenQSYKQ 384
                          250       260
                   ....*....|....*....|....*
gi 1720408942  330 ELNrnrSLASQLEEIKLQVRKQKEL 354
Cdd:TIGR04523  385 EIK---NLESQINDLESKIQNQEKL 406
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N-terminus of SMC proteins. The ...
61-353 5.17e-07

RecF/RecN/SMC N terminal domain; This domain is found at the N-terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 53.82  E-value: 5.17e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942   61 TLAEIEVLRQRVLKIEGKDEEIKRAEDlchtmKEKLEEEENLTRELKSEIERLQKRMVDLEKLEEALSRSKNECSQLCLS 140
Cdd:pfam02463  174 ALKKLIEETENLAELIIDLEELKLQEL-----KLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRD 248
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  141 LNEERNLTKKI---SSELEMLRVKVKELESSEDRLDKTEQSLVSELEKLKSLTLSFVNERKYLNEKEKENEKIIKELTQK 217
Cdd:pfam02463  249 EQEEIESSKQEiekEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEK 328
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  218 LEQNKKMNRDHMRNASTFLERNDLRIEDGISSTLSS--KESKRKGSLDYLKQVENETRDKSENEKN-----RNQEDNKVK 290
Cdd:pfam02463  329 ELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLqeKLEQLEEELLAKKKLESERLSSAAKLKEeelelKSEEEKEAQ 408
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720408942  291 DLNQEIEKLKTQIKHFESLEEELKKMRAKNNDLQDNYLTELNRNRSLASQLEEIKLQVRKQKE 353
Cdd:pfam02463  409 LLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSE 471
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
3-325 5.35e-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: 53.91  E-value: 5.35e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942    3 ELTNYKDAAsnRHLRFKLQSLSRRLDELEE----ATKNLQRAEDELLDLQDKVIQAEGSDSSTLAEIEVLRQRVLKIEGK 78
Cdd:TIGR02168  706 ELEELEEEL--EQLRKELEELSRQISALRKdlarLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAE 783
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942   79 ----DEEIKRAEDLCHTMKEKLEEEENLTRELKSEIERLQKRMVDLEKLEEALSRSKNECSQLCLSLNEERnltKKISSE 154
Cdd:TIGR02168  784 ieelEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDI---ESLAAE 860
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  155 LEMLRVKVKELESSEDRLDKTEQSLVSELEKLKSLTLSFVNERKYLNEKEKENEKIIKELTQKLEQnkkmnrdhmrnAST 234
Cdd:TIGR02168  861 IEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQ-----------LEL 929
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  235 FLERNDLRIeDGISSTLSSKESKrkgSLDYLKQVENETRDKSENEKNRnqednkVKDLNQEIEKLK----TQIKHFESLE 310
Cdd:TIGR02168  930 RLEGLEVRI-DNLQERLSEEYSL---TLEEAEALENKIEDDEEEARRR------LKRLENKIKELGpvnlAAIEEYEELK 999
                          330
                   ....*....|....*
gi 1720408942  311 EELKKMRAKNNDLQD 325
Cdd:TIGR02168 1000 ERYDFLTAQKEDLTE 1014
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
16-415 7.75e-07

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: 53.51  E-value: 7.75e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942   16 LRFKLQSLSRRLDELEEATKNLQRAEDELLDL---QDKVIQAEgsdsstLAEIEVLRQRVLKIEGKDEEIKRAEDLCHTM 92
Cdd:TIGR00606  700 LQSKLRLAPDKLKSTESELKKKEKRRDEMLGLapgRQSIIDLK------EKEIPELRNKLQKVNRDIQRLKNDIEEQETL 773
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942   93 KEKLEEEENLTRELKSE---IERLQKRMVDLEKLEEALSrSKNECSQLCLSLNEERNLTKKISSELEMLRVKVKELESSE 169
Cdd:TIGR00606  774 LGTIMPEEESAKVCLTDvtiMERFQMELKDVERKIAQQA-AKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLI 852
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  170 DRLDKTEQSLVSELEKLKSLTLSFVNERKYLNEKEKENEKIIKELtQKLEQNKKMNRDHMRNASTFLERNDLRIEDGISS 249
Cdd:TIGR00606  853 QDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEV-QSLIREIKDAKEQDSPLETFLEKDQQEKEELISS 931
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  250 TLSSK----------ESKRKGSLDYLKQVENETRDKSENEKnrNQEDNKVKDLNQEIEKLKtqiKHFESLEEELKKMRaK 319
Cdd:TIGR00606  932 KETSNkkaqdkvndiKEKVKNIHGYMKDIENKIQDGKDDYL--KQKETELNTVNAQLEECE---KHQEKINEDMRLMR-Q 1005
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  320 NNDLQDNYLTELNRNRSLASQLEEIKlQVRKQKELGNGDIeGEDAFLLGRGRH----ERTKLKGHGSEASVSKHTSRELS 395
Cdd:TIGR00606 1006 DIDTQKIQERWLQDNLTLRKRENELK-EVEEELKQHLKEM-GQMQVLQMKQEHqkleENIDLIKRNHVLALGRQKGYEKE 1083
                          410       420
                   ....*....|....*....|
gi 1720408942  396 PQHKRERLRNREFALSNEHY 415
Cdd:TIGR00606 1084 IKHFKKELREPQFRDAEEKY 1103
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
80-353 8.17e-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: 53.14  E-value: 8.17e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942   80 EEIKRAEDLCHTMKEKLEeeenltrELKSEIERLQKRMVDLEKLEEALSRSKNECS-QLCLSLNEERNLTKKISSELEML 158
Cdd:TIGR02168  684 EKIEELEEKIAELEKALA-------ELRKELEELEEELEQLRKELEELSRQISALRkDLARLEAEVEQLEERIAQLSKEL 756
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  159 RVKVKELESSEDRLDKTEQSLVSELEKLKSLTLSFVNerkyLNEKEKENEKIIKELTQKLeQNKKMNRDHMRNASTFLER 238
Cdd:TIGR02168  757 TELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQ----LKEELKALREALDELRAEL-TLLNEEAANLRERLESLER 831
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  239 NDLRIEDGISSTLSSKESKRKGSLDYLKQVENETRDKSENEKNRNQEDNKVKDLNQEIEKLKtqiKHFESLEEELKKMRA 318
Cdd:TIGR02168  832 RIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLR---SELEELSEELRELES 908
                          250       260       270
                   ....*....|....*....|....*....|....*
gi 1720408942  319 KNNDLQDNYLTELNRNRSLASQLEEIKLQVRKQKE 353
Cdd:TIGR02168  909 KRSELRRELEELREKLAQLELRLEGLEVRIDNLQE 943
PTZ00121 PTZ00121
MAEBL; Provisional
64-322 8.47e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 53.22  E-value: 8.47e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942   64 EIEVLRQRVLKIEGKDEEIKRAEDlchTMKEKLEEEENLTRELKSEIERLQKRMVDLEKLEEALSRSKNE---CSQLCLS 140
Cdd:PTZ00121  1634 KVEQLKKKEAEEKKKAEELKKAEE---ENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEakkAEELKKK 1710
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  141 LNEERNLTKKISSELEMLRVKVKELESSEDRLDKTEQSLVSELEKLKSLTLSFVNERKYLNEKEKENEKIIKELTQKLEQ 220
Cdd:PTZ00121  1711 EAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDE 1790
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  221 NKKMNRDhmRNASTFLERNDLRIEDGISSTL---SSKE---SKRKGSLDYLKQVENETRDKSENEKNRNQEDNKVKDLNQ 294
Cdd:PTZ00121  1791 KRRMEVD--KKIKDIFDNFANIIEGGKEGNLvinDSKEmedSAIKEVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEA 1868
                          250       260
                   ....*....|....*....|....*...
gi 1720408942  295 EIEKLKTQIKHFESLEEELKKMRAKNND 322
Cdd:PTZ00121  1869 DFNKEKDLKEDDEEEIEEADEIEKIDKD 1896
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
21-280 9.02e-07

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 53.15  E-value: 9.02e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942   21 QSLSRRLDELEEATKNLQR-AEDELLDLQDKVIQAEGSDSSTLAEIEVLRQRVlkiEGKDEEIKRAEDLCHtmkEKLEEE 99
Cdd:TIGR02169  265 KRLEEIEQLLEELNKKIKDlGEEEQLRVKEKIGELEAEIASLERSIAEKEREL---EDAEERLAKLEAEID---KLLAEI 338
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  100 ENLTRELKSEIERLQKRMVDLEKLEEALSRSKNECSQLCLSLNEERNLTKKISSELEMLRVKVKELESSEDRLDKTEQSL 179
Cdd:TIGR02169  339 EELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRL 418
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  180 VSELEKLKSLTLSFVNERKYLNEKEKENEKIIKELTQKLEQNKKMNRDHmrNASTFLERNDLRIedgISSTLSSKESKRK 259
Cdd:TIGR02169  419 SEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKY--EQELYDLKEEYDR---VEKELSKLQRELA 493
                          250       260
                   ....*....|....*....|.
gi 1720408942  260 GSLDYLKQVENETRDKSENEK 280
Cdd:TIGR02169  494 EAEAQARASEERVRGGRAVEE 514
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
2-349 2.21e-06

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 51.96  E-value: 2.21e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942    2 AELTNYKDAASNRhlRFKLQSLSRRLDELEEATKN----LQRAEDELLDLQDKVIQAEGSDSSTLAEIEVLRQRV----- 72
Cdd:PRK02224   370 SELEEAREAVEDR--REEIEELEEEIEELRERFGDapvdLGNAEDFLEELREERDELREREAELEATLRTARERVeeaea 447
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942   73 LKIEGK---------DEEIKRAEDLCHTMKEKLEEEENLTRELKSEIERLQKRMVDLEKLEEALSRSKNECSQLCLSLNE 143
Cdd:PRK02224   448 LLEAGKcpecgqpveGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEERREDLEELIAE 527
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  144 ERNLTKKISSELEMLRVKVKELESSEDRLDKTEQSLVSELEKLKSLTLSFVNERKYLNEKEKENEKI------------- 210
Cdd:PRK02224   528 RRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIrtllaaiadaede 607
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  211 IKELTQKLEQNKKMNRDHMRNASTFLERNDLRIEDGISSTLSSKESKRKGSLDYLKQVENETRDKSEneknrnQEDnkvk 290
Cdd:PRK02224   608 IERLREKREALAELNDERRERLAEKRERKRELEAEFDEARIEEAREDKERAEEYLEQVEEKLDELRE------ERD---- 677
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1720408942  291 DLNQEIEKLKTQIKHFESLEEELKKMRAKNNDLQDNYltelnrnrSLASQLEEIKLQVR 349
Cdd:PRK02224   678 DLQAEIGAVENELEELEELRERREALENRVEALEALY--------DEAEELESMYGDLR 728
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N-terminus of SMC proteins. The ...
19-323 2.24e-06

RecF/RecN/SMC N terminal domain; This domain is found at the N-terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 51.90  E-value: 2.24e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942   19 KLQSLSRRLDELEEATKNLQRAEDELLDLQDKVIQAEGSDSSTLAEIEVLRQRVLKIEGKDEEIKRAEDLCHTMKEKLEE 98
Cdd:pfam02463  723 LADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEE 802
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942   99 EENLTRELKSEIERLQKRMVDLEKLEEALSRSKNECSQLCL-SLNEERNLTKKISSELEMLRVKVKELESSEDRLDKTEQ 177
Cdd:pfam02463  803 LRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKeEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQ 882
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  178 SLVSELEK-----------LKSLTLSFVNERKYLNEKEKENEKIIKELTQKLEQNKKMnRDHMRNASTFLERNDLRIEDG 246
Cdd:pfam02463  883 KLKDELESkeekekeekkeLEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEEL-LLEEADEKEKEENNKEEEEER 961
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720408942  247 ISSTLSSKESKRKGSLDYLKQVENETRDKSENEKNRNQEDNKVKDLNQEIEKLKTQIKhfeslEEELKKMRAKNNDL 323
Cdd:pfam02463  962 NKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRL-----KEFLELFVSINKGW 1033
PRK10929 PRK10929
putative mechanosensitive channel protein; Provisional
21-378 2.78e-06

putative mechanosensitive channel protein; Provisional


Pssm-ID: 236798 [Multi-domain]  Cd Length: 1109  Bit Score: 51.59  E-value: 2.78e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942   21 QSLSRRLDELEEATKNLQRAED-----------------ELLDLQDKVIQAEGSDSStlAEIEvlrQRVLKIEGK----- 78
Cdd:PRK10929    48 EALQSALNWLEERKGSLERAKQyqqvidnfpklsaelrqQLNNERDEPRSVPPNMST--DALE---QEILQVSSQlleks 122
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942   79 ---DEEIKRAEDLCHTMKEKLEEEENLTRELkSEIERlqkRMVDLEKLEEALSRSKNecsqlcLSLNEERNLTKKISSEL 155
Cdd:PRK10929   123 rqaQQEQDRAREISDSLSQLPQQQTEARRQL-NEIER---RLQTLGTPNTPLAQAQL------TALQAESAALKALVDEL 192
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  156 EM-----------LRVKVKELESSEDRLDKTEQSLVSELEKLKSLTLSFVNERKYLNEKEKENekIIKELTQKLEQNkkm 224
Cdd:PRK10929   193 ELaqlsannrqelARLRSELAKKRSQQLDAYLQALRNQLNSQRQREAERALESTELLAEQSGD--LPKSIVAQFKIN--- 267
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  225 nrdhmRNASTFLERNDLRIEDgisstLSSKESKRKGSLDYLKQVENETRDKSE--------NEKNRNQ-----EDNKVKD 291
Cdd:PRK10929   268 -----RELSQALNQQAQRMDL-----IASQQRQAASQTLQVRQALNTLREQSQwlgvsnalGEALRAQvarlpEMPKPQQ 337
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  292 LNQEIEKLKTQIKHFESLEEELKKMRAKNNDlqDNYLTELNRNRSLASQLeeiklqvRKQKELGNGDIEGEDAFLLgrgr 371
Cdd:PRK10929   338 LDTEMAQLRVQRLRYEDLLNKQPQLRQIRQA--DGQPLTAEQNRILDAQL-------RTQRELLNSLLSGGDTLIL---- 404

                   ....*..
gi 1720408942  372 hERTKLK 378
Cdd:PRK10929   405 -ELTKLK 410
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
19-214 9.08e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 49.68  E-value: 9.08e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942   19 KLQSLSRRLDELEEATKNLQRAEDELLD-LQDKVIQAEGSDSSTLAEIEVLRQRVLKIEGKDEEIKRAEDLCHTMKEKLE 97
Cdd:PRK03918   550 KLEELKKKLAELEKKLDELEEELAELLKeLEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELD 629
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942   98 EEENLTRELKSEIERLQKRmvdLEKLEEALSRSKNEcsqlclslnEERNLTKKISSELEMLRVKVKELESSEDRLDKTeq 177
Cdd:PRK03918   630 KAFEELAETEKRLEELRKE---LEELEKKYSEEEYE---------ELREEYLELSRELAGLRAELEELEKRREEIKKT-- 695
                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1720408942  178 slvseLEKLKsltlsfvNERKYLNEKEKENEKIIKEL 214
Cdd:PRK03918   696 -----LEKLK-------EELEEREKAKKELEKLEKAL 720
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
14-319 1.29e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 49.29  E-value: 1.29e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942   14 RHLRFKLQSLSRRLDELEEATKNLQRAED-------ELLDLQDKVIQAEGSdsstlAEIEVLRQRVLKIEGKDEEIK-RA 85
Cdd:PRK03918   408 SKITARIGELKKEIKELKKAIEELKKAKGkcpvcgrELTEEHRKELLEEYT-----AELKRIEKELKEIEEKERKLRkEL 482
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942   86 EDLCHTMKEKLEEEENLT-----RELKSE-----IERLQKRMVDLEKLEEALSRSKNECSQLCLSLNEERNLTKKIS--- 152
Cdd:PRK03918   483 RELEKVLKKESELIKLKElaeqlKELEEKlkkynLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAele 562
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  153 ----------------------SELEMLRVKVKELESSEDR---LDKTEQSLVSELEKLKSLTLSFVNERKYLNEKEKEN 207
Cdd:PRK03918   563 kkldeleeelaellkeleelgfESVEELEERLKELEPFYNEyleLKDAEKELEREEKELKKLEEELDKAFEELAETEKRL 642
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  208 EKIIKELTqklEQNKKMNRDHMRNASTFLERndlriedgISSTLSSKESKRKGSLDYLKQVENETRDKSENEKNRnqedn 287
Cdd:PRK03918   643 EELRKELE---ELEKKYSEEEYEELREEYLE--------LSRELAGLRAELEELEKRREEIKKTLEKLKEELEER----- 706
                          330       340       350
                   ....*....|....*....|....*....|..
gi 1720408942  288 kvKDLNQEIEKLKTQIKHFESLEEELKKMRAK 319
Cdd:PRK03918   707 --EKAKKELEKLEKALERVEELREKVKKYKAL 736
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
19-353 1.49e-05

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: 49.27  E-value: 1.49e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942   19 KLQSLSRRLDELEEATKNLQRAEDELLDLQDKV-IQAEGSDSSTLAEIEVLRQRVLKIE----GKDEEIKRAEDLCHTMK 93
Cdd:TIGR00606  320 ELVDCQRELEKLNKERRLLNQEKTELLVEQGRLqLQADRHQEHIRARDSLIQSLATRLEldgfERGPFSERQIKNFHTLV 399
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942   94 EKLEEEENLTrelkseIERLQKRMVDLEKL-EEALSRSKNECSQLCLSLNEERNLTKKISSELEMLRVKVKELESSEDRL 172
Cdd:TIGR00606  400 IERQEDEAKT------AAQLCADLQSKERLkQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRI 473
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  173 DKTEQSLVSELEKL-----KSLTLSFVNERKYLNEKEKENEKIIKELTQKLEQ--NKKMNRDHMRNASTFLERNDLRIED 245
Cdd:TIGR00606  474 LELDQELRKAERELskaekNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQlnHHTTTRTQMEMLTKDKMDKDEQIRK 553
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  246 gISSTLSSKESKRKGSLDYLKQVENETRDKSeneKNRNQEDNKVKDLNQEIEKLKTQIKHFeslEEELKKMRAKNNDLQD 325
Cdd:TIGR00606  554 -IKSRHSDELTSLLGYFPNKKQLEDWLHSKS---KEINQTRDRLAKLNKELASLEQNKNHI---NNELESKEEQLSSYED 626
                          330       340
                   ....*....|....*....|....*...
gi 1720408942  326 NyLTELNRNRSLASQLEEIKLQVRKQKE 353
Cdd:TIGR00606  627 K-LFDVCGSQDEESDLERLKEEIEKSSK 653
PRK01156 PRK01156
chromosome segregation protein; Provisional
106-359 2.01e-05

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 48.74  E-value: 2.01e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  106 LKSEIERLQKRMVDLEKLEEALSRSKNECSQLCLSLNEERNLTKKISSELEMLRVKVKELESSEDRLDKTEQSLVSELEK 185
Cdd:PRK01156   171 LKDVIDMLRAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDM 250
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  186 LKSLTLSFVNERKYLNEKEKENEKI--IKELTQKLEQNKKM-NRDHMRNasTFLERNDLRIEDGISSTLSSKESKRKGSL 262
Cdd:PRK01156   251 KNRYESEIKTAESDLSMELEKNNYYkeLEERHMKIINDPVYkNRNYIND--YFKYKNDIENKKQILSNIDAEINKYHAII 328
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  263 DYLKQVENETRDKSENEKNRNQEDNKVKDLNQEIEKLKTQIKHFESLEEELKKMRAKNNDLQDNYLTELNRNRSLASQLE 342
Cdd:PRK01156   329 KKLSVLQKDYNDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIK 408
                          250
                   ....*....|....*..
gi 1720408942  343 EIKLQVRKQKELGNGDI 359
Cdd:PRK01156   409 KELNEINVKLQDISSKV 425
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
109-342 2.10e-05

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 48.39  E-value: 2.10e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  109 EIERLqKRMVDLEKLEEALSRSkNECSQLCLSLNEERNLTKKISSELEmlRVKVKELESSEDRLDKTEQSLVSELEKLks 188
Cdd:PRK05771    32 HIEDL-KEELSNERLRKLRSLL-TKLSEALDKLRSYLPKLNPLREEKK--KVSVKSLEELIKDVEEELEKIEKEIKEL-- 105
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  189 ltlsfVNERKYLNEKEKENEKIIKELTQ--------KLEQNKKmnrdhmrNASTFLERNDLRIEDGISSTLSSK----ES 256
Cdd:PRK05771   106 -----EEEISELENEIKELEQEIERLEPwgnfdldlSLLLGFK-------YVSVFVGTVPEDKLEELKLESDVEnveyIS 173
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  257 KRKGSLDYLKQVENETRDKSENE--KN--RNQEDNKVKDLNQEIEKLKTQI----KHFESLEEELKKMRAKNNDL---QD 325
Cdd:PRK05771   174 TDKGYVYVVVVVLKELSDEVEEElkKLgfERLELEEEGTPSELIREIKEELeeieKERESLLEELKELAKKYLEEllaLY 253
                          250
                   ....*....|....*...
gi 1720408942  326 NYL-TELNRNRSLASQLE 342
Cdd:PRK05771   254 EYLeIELERAEALSKFLK 271
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
82-356 4.23e-05

reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.


Pssm-ID: 130673 [Multi-domain]  Cd Length: 2757  Bit Score: 47.74  E-value: 4.23e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942   82 IKRAEDLCHTMKEKLEEEENLTRELKSEIE-RLQKRMvdLEKLEEALSRSKNecsqlclSLNEERNLTKKISSELEMLRV 160
Cdd:TIGR01612  502 MKDFKDIIDFMELYKPDEVPSKNIIGFDIDqNIKAKL--YKEIEAGLKESYE-------LAKNWKKLIHEIKKELEEENE 572
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  161 KVKELESSEDRLDKTEQSLVSELEKLKSLTLSFVNERKYLNEKekeNEKIIKELT-QKLEQNKKMNRDHMRNASTFLERN 239
Cdd:TIGR01612  573 DSIHLEKEIKDLFDKYLEIDDEIIYINKLKLELKEKIKNISDK---NEYIKKAIDlKKIIENNNAYIDELAKISPYQVPE 649
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  240 DLRIEDGISSTLSSKESK-RKGSLDYLKqveNETRD-KSENEKNRNQEDNKVKDLNQEIEKLKTQIKHFE--SLEEELKK 315
Cdd:TIGR01612  650 HLKNKDKIYSTIKSELSKiYEDDIDALY---NELSSiVKENAIDNTEDKAKLDDLKSKIDKEYDKIQNMEtaTVELHLSN 726
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 1720408942  316 MRAKNNDLQDNyLTELNR------NRSLASQLEEIKlqvRKQKELGN 356
Cdd:TIGR01612  727 IENKKNELLDI-IVEIKKhihgeiNKDLNKILEDFK---NKEKELSN 769
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
62-349 4.76e-05

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 47.37  E-value: 4.76e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942   62 LAEIEVLRQRVLKIEGKDEEIK---------RAEDLCHTMKEKLEEEENLT------RELKSEIERLQKRMVDLEKLEEA 126
Cdd:TIGR02169  176 LEELEEVEENIERLDLIIDEKRqqlerlrreREKAERYQALLKEKREYEGYellkekEALERQKEAIERQLASLEEELEK 255
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  127 LSRSKNECSQLCLSLNEERN-LTKKIS--SELEMLRVKVK--ELESSEDRLDKTEQSLVSELEKL-KSLTLSFVNERKYL 200
Cdd:TIGR02169  256 LTEEISELEKRLEEIEQLLEeLNKKIKdlGEEEQLRVKEKigELEAEIASLERSIAEKERELEDAeERLAKLEAEIDKLL 335
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  201 NEKEKENEKIikeLTQKLEQNKKMNRDHMRNASTFLERNDLRIEDGISSTLSSKESKRKGSLDYLKQVENE---TRDKSE 277
Cdd:TIGR02169  336 AEIEELEREI---EEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINElkrELDRLQ 412
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  278 NEKNRNQEdnKVKDLNQEIEKLKTQIKHFES-----------LEEELKKMRAKNNDLQDNYL---TELN----RNRSLAS 339
Cdd:TIGR02169  413 EELQRLSE--ELADLNAAIAGIEAKINELEEekedkaleikkQEWKLEQLAADLSKYEQELYdlkEEYDrvekELSKLQR 490
                          330
                   ....*....|
gi 1720408942  340 QLEEIKLQVR 349
Cdd:TIGR02169  491 ELAEAEAQAR 500
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
19-189 5.20e-05

Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 47.40  E-value: 5.20e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942   19 KLQSLSRRLDELEEATKNLQRAEDELLDLQDKVIQAEGSDSSTLAEIEVLRQRvlKIEGKDEEIKRAEDLCHTMKEKLEE 98
Cdd:COG1196    345 LLEELEQLLAELEEAKEELEEKLSALLEELEELFEALREELAELEAELAEIRN--ELEELKREIESLEERLERLSERLED 422
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942   99 EENLTRELKSEIERLQKRMVD----LEKLEEALSRSKNECSQLCLSLNEERNLTKKISSELEMLRVKVKELESSEDRLDK 174
Cdd:COG1196    423 LKEELKELEAELEELQTELEElneeLEELEEQLEELRDRLKELERELAELQEELQRLEKELSSLEARLDRLEAEQRASQG 502
                          170
                   ....*....|....*
gi 1720408942  175 TEQSLVSELEKLKSL 189
Cdd:COG1196    503 VRAVLEALESGLPGV 517
PRK01156 PRK01156
chromosome segregation protein; Provisional
20-353 6.16e-05

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 47.20  E-value: 6.16e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942   20 LQSLSRRLDELEEATKNLQRAEDELLDLQDKVIQAEGSDSSTLAEIEVLRQRVLKIEGKDEEIKRAEDLCHTMKEKLEEE 99
Cdd:PRK01156   175 IDMLRAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRY 254
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  100 ENLTRELKSEIERLQKRMVDLEKLEEALSRSKNecSQLCLSLNEER---NLTKKISSELEMLRVKVKELESSEDRLDKTE 176
Cdd:PRK01156   255 ESEIKTAESDLSMELEKNNYYKELEERHMKIIN--DPVYKNRNYINdyfKYKNDIENKKQILSNIDAEINKYHAIIKKLS 332
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  177 --QSLVSELEKLKSLTLSFVNERKYLNEKEKENEKIIKELTQ---KLEQNKKMNRDHMRNASTFLERNDL------RIED 245
Cdd:PRK01156   333 vlQKDYNDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESlkkKIEEYSKNIERMSAFISEILKIQEIdpdaikKELN 412
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  246 GISSTL---SSKESKRKGSLDYLKQVENETRDKSE-------------------NEKNRNQEDNKVKDLNQEIEKLKTQI 303
Cdd:PRK01156   413 EINVKLqdiSSKVSSLNQRIRALRENLDELSRNMEmlngqsvcpvcgttlgeekSNHIINHYNEKKSRLEEKIREIEIEV 492
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1720408942  304 KHFESLEEELKKMRAKNNDLQDN-YLTELNRNRSLASQLEEIKLQVRKQKE 353
Cdd:PRK01156   493 KDIDEKIVDLKKRKEYLESEEINkSINEYNKIESARADLEDIKIKINELKD 543
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
197-353 7.42e-05

DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];


Pssm-ID: 223496 [Multi-domain]  Cd Length: 908  Bit Score: 46.68  E-value: 7.42e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  197 RKYLNEKEKENEKIIKELTQkLEQNKKMnrdhmrnaSTFLERNDLRIEDGISSTLSSKESKRKGSLDYLKQVENETrdKS 276
Cdd:COG0419    146 DAFLKSKPKERKEILDELFG-LEKYEKL--------SELLKEVIKEAKAKIEELEGQLSELLEDIEDLLEALEEEL--KE 214
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720408942  277 ENEKNRNQEDNKVKDLNQEIEKLKTQIKHFESLEEELKKMRAKNNDLQDNYLTELNRNRSLASQLEEIKLQVRKQKE 353
Cdd:COG0419    215 LKKLEEIQEEQEEEELEQEIEALEERLAELEEEKERLEELKARLLEIESLELEALKIREEELRELERLLEELEEKIE 291
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
68-354 8.10e-05

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 435022 [Multi-domain]  Cd Length: 1112  Bit Score: 46.63  E-value: 8.10e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942   68 LRQRVLKIEGKDEEIKRAEDLchtmkekleeeenlTRELKSEIERLQKRMVDLEKLEEALSRSKNECSQLCLSLNEERNL 147
Cdd:pfam15921  446 MERQMAAIQGKNESLEKVSSL--------------TAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERA 511
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  148 TKKISSELEMLRVKVkELESSEdrldktEQSLVSELEKLKSLTlsfvNERKYLNEKEKENEKIIKELTQKLEQNKKMNRD 227
Cdd:pfam15921  512 IEATNAEITKLRSRV-DLKLQE------LQHLKNEGDHLRNVQ----TECEALKLQMAEKDKVIEILRQQIENMTQLVGQ 580
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  228 HMRNASTFL--------ERNDLRIEDGISSTLSSKESKRKGSLDylKQVENETRDKSENEKNRNQEDNKVKDLNQEIEKL 299
Cdd:pfam15921  581 HGRTAGAMQvekaqlekEINDRRLELQEFKILKDKKDAKIRELE--ARVSDLELEKVKLVNAGSERLRAVKDIKQERDQL 658
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720408942  300 KTQIKHFESleeELKKMRAKNNDLQDNYlteLNRNRSLASQLEEIKLQVRK-QKEL 354
Cdd:pfam15921  659 LNEVKTSRN---ELNSLSEDYEVLKRNF---RNKSEEMETTTNKLKMQLKSaQSEL 708
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N-terminus of SMC proteins. The ...
103-363 8.57e-05

RecF/RecN/SMC N terminal domain; This domain is found at the N-terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 46.89  E-value: 8.57e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  103 TRELKSEIERLQKRMVDLEKLEEALSRSKNECSQLCLSLNEER------NLTKKISSELEMLRV--KVKELESSEDRLDK 174
Cdd:pfam02463  165 SRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKkaleyyQLKEKLELEEEYLLYldYLKLNEERIDLLQE 244
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  175 TEQSLVSELEKLKSL------TLSFVNERKYLNEKEKENEKIIKELTQKLEQNKKMNRDHMRNASTFLERNDLRIEDGIS 248
Cdd:pfam02463  245 LLRDEQEEIESSKQEiekeeeKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKK 324
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  249 STLSSKESKRKGSLDYLKQVENETRDKSENE-KNRNQEDNKVKDLNQEIEKLKTQIKHFESLEEELKKmRAKNNDLQDNY 327
Cdd:pfam02463  325 KAEKELKKEKEEIEELEKELKELEIKREAEEeEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKL-KEEELELKSEE 403
                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 1720408942  328 LTELNRNRSLASQLEEIkLQVRKQKELGNGDIEGED 363
Cdd:pfam02463  404 EKEAQLLLELARQLEDL-LKEEKKEELEILEEEEES 438
PTZ00440 PTZ00440
reticulocyte binding protein 2-like protein; Provisional
27-332 1.31e-04

reticulocyte binding protein 2-like protein; Provisional


Pssm-ID: 240419 [Multi-domain]  Cd Length: 2722  Bit Score: 46.36  E-value: 1.31e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942   27 LDELEEATKNLQRAEDELLDLQDKVIQAEGSDSST--LAEIEVLRQRvlkIEGKDEEIKRAEDLCHTMkekleeeenltr 104
Cdd:PTZ00440   690 IKNLKKELQNLLSLKENIIKKQLNNIEQDISNSLNqyTIKYNDLKSS---IEEYKEEEEKLEVYKHQI------------ 754
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  105 elkseIERLQKRMVDLEKLEEALSRSKNECSQLCLSLNEERNLTKKISSELEMLRVKVK----ELESSEDRLDKTEQSLV 180
Cdd:PTZ00440   755 -----INRKNEFILHLYENDKDLPDGKNTYEEFLQYKDTILNKENKISNDINILKENKKnnqdLLNSYNILIQKLEAHTE 829
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  181 SELEKLKSLTLSFVNERKYLNEKEKENE-----KIIKELTQKLEQ-NKKMNRDHMRNASTFLERNDLRIedgISSTLSSK 254
Cdd:PTZ00440   830 KNDEELKQLLQKFPTEDENLNLKELEKEfnennQIVDNIIKDIENmNKNINIIKTLNIAINRSNSNKQL---VEHLLNNK 906
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  255 ESKRKGSLDYLKQVENET----RDKSENEKNRNQEDNKV-KDLNQE-IEKLKTQIkhfESLEEELKKMRAKNNDLQDNYL 328
Cdd:PTZ00440   907 IDLKNKLEQHMKIINTDNiiqkNEKLNLLNNLNKEKEKIeKQLSDTkINNLKMQI---EKTLEYYDKSKENINGNDGTHL 983

                   ....
gi 1720408942  329 TELN 332
Cdd:PTZ00440   984 EKLD 987
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
16-353 1.41e-04

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 435022 [Multi-domain]  Cd Length: 1112  Bit Score: 45.86  E-value: 1.41e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942   16 LRFKLQSLSRRLDELEEATKNLQRAEDELLD-LQDKVIQAEGS---------DSSTlaEIEVLRQRVLKIEGKDEEIKR- 84
Cdd:pfam15921  115 LQTKLQEMQMERDAMADIRRRESQSQEDLRNqLQNTVHELEAAkclkedmlnDSNT--QIEQLRKMMLSHEGVLQEIRSi 192
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942   85 -------------AEDLCHTM--KEKLEEEENLTRELKSEIERLQKRMVDLEKLEEAL-SRSKNECSQLclsLNEERNLT 148
Cdd:pfam15921  193 lvdfeeasgkkiyEHDSMSTIhfRSLGSAISKILRELDTEISYLKGRIFPVEDQLEALkSESQNKIELL---LQQHQDRI 269
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  149 KKISSELEmlrVKVKELESSEDRLDKTEQSLVSELEKLKSLTLsfvNERKYLNEKEKENEKIIKELTQKLEQNKKMNRDH 228
Cdd:pfam15921  270 EQLISEHE---VEITGLTEKASSARSQANSIQSQLEIIQEQAR---NQNSMYMRQLSDLESTVSQLRSELREAKRMYEDK 343
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  229 MRNastfLERNDLRIEDGISSTLSSKE--SKRKGSLDYLKQVENETRDKSENEKNRNQEDNK------------------ 288
Cdd:pfam15921  344 IEE----LEKQLVLANSELTEARTERDqfSQESGNLDDQLQKLLADLHKREKELSLEKEQNKrlwdrdtgnsitidhlrr 419
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720408942  289 -VKDLNQEIEKLKTQIKHFES-----LEEELKKMRAKNNDLQdnyltelnRNRSLASQLEEIKLQVRKQKE 353
Cdd:pfam15921  420 eLDDRNMEVQRLEALLKAMKSecqgqMERQMAAIQGKNESLE--------KVSSLTAQLESTKEMLRKVVE 482
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
79-345 1.94e-04

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: 45.44  E-value: 1.94e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942   79 DEEIKRAEDLCHTMKEKLEEEENLTRELKSEIERLQKRMVDLEKLEeALSRSKNECSQLCLSLNEERNLT--KKISSELE 156
Cdd:TIGR02169  169 DRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQ-ALLKEKREYEGYELLKEKEALERqkEAIERQLA 247
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  157 MLRvkvKELESSEDRLDKTEQSLVSELEKLKSLT--LSFVNERKYLNEKEKenekiIKELTQKLEQNKKMNRDHMRNAST 234
Cdd:TIGR02169  248 SLE---EELEKLTEEISELEKRLEEIEQLLEELNkkIKDLGEEEQLRVKEK-----IGELEAEIASLERSIAEKERELED 319
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  235 fLERNDLRIEDGISSTLSSKESKRKGSLDYLKQVENETrdkSENEKNRNQEDNKVKDLNQEIEKLKTQIKHFESLEEELK 314
Cdd:TIGR02169  320 -AEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLT---EEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLE 395
                          250       260       270
                   ....*....|....*....|....*....|.
gi 1720408942  315 KMRAKNNDLQDNYLTELNRNRSLASQLEEIK 345
Cdd:TIGR02169  396 KLKREINELKRELDRLQEELQRLSEELADLN 426
YloA COG1293
Predicted component of the ribosome quality control (RQC) complex, YloA/Tae2 family, contains ...
109-353 2.20e-04

Predicted component of the ribosome quality control (RQC) complex, YloA/Tae2 family, contains fibronectin-binding (FbpA) and DUF814 domains [Translation, ribosomal structure and biogenesis];


Pssm-ID: 224212 [Multi-domain]  Cd Length: 564  Bit Score: 45.08  E-value: 2.20e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  109 EIERLQKRMVDLEKL--EEALSRSKNECSQLCLSLNEERNLTKKISSELEMLRVKVKELESSEDRLDKTEQSLVSELEKL 186
Cdd:COG1293    187 DIVRLLARFLGLGGLlaEELLSRAGLDKKVPAKDLFEEEIKKVREALEELLNPLKPNYYYKDEKYLDVVPLKAYADLEKL 266
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  187 KSLTLSFVNER----KYLNEKEKENEKIIKELTQKLEQNKKMNRDHMRNASTFLERNDL------RIEDGISS-TLSSKE 255
Cdd:COG1293    267 FNEALDEKFERdkikQLASELEKKLEKELKKLENKLEKQEDELEELEKAAEELRQKGELlyanlqLIEEGLKSvRLADFY 346
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  256 SKRKGSLDylkqvENETRDKSENEKNRNQEDNKVKDLNQEIEKLKTQIKHFESLEEELKKMRAKNNDLQDnylTELNRNR 335
Cdd:COG1293    347 GNEEIKIE-----LDKSKTPSENAQRYFKKYKKLKGAKVNLDRQLSELKEAIAYYESAKTALEKAEGKKA---IEEIREE 418
                          250
                   ....*....|....*...
gi 1720408942  336 SLASQLEEIKLQVRKQKE 353
Cdd:COG1293    419 LIEEGLLKSKKKKRKKKE 436
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
16-366 2.71e-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: 45.10  E-value: 2.71e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942   16 LRFKLQSLSRRLDELE-EATKNLQRAEDELLDLQDKVIQAEGSDSSTLAEIEVLRQRVLKIEGK----DEEIKRAEDLCH 90
Cdd:pfam05483  213 MHFKLKEDHEKIQHLEeEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKtklqDENLKELIEKKD 292
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942   91 TMkekleeeenlTRELKSEIERLQKRMVDLEKLEEALSRSKNECSQLC-------LSLNEERNLTKKISSEL-------- 155
Cdd:pfam05483  293 HL----------TKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTeekeaqmEELNKAKAAHSFVVTEFeattcsle 362
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  156 EMLRVKVKELESSEDRLDKTEQSLVSELEKLKSLTlsfvnerKYLNEKEKENEKIIKELTQK---LEQNKKMNRdhmrna 232
Cdd:pfam05483  363 ELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMT-------KFKNNKEVELEELKKILAEDeklLDEKKQFEK------ 429
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  233 stflerndlriedgISSTLSSKESKRKGSLdylkqvenETRDKseneknrnqednKVKDLNQEIEKLKTQIKHF----ES 308
Cdd:pfam05483  430 --------------IAEELKGKEQELIFLL--------QAREK------------EIHDLEIQLTAIKTSEEHYlkevED 475
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720408942  309 LEEELKKMRAKNNDLQDNYLTELNRNRSLASQLEEIKLQVRKQKELGNGDIEGEDAFL 366
Cdd:pfam05483  476 LKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERML 533
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
121-353 3.09e-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: 44.63  E-value: 3.09e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  121 EKLEEALSRSKNECSQLCLSL-NEERNLTKKISsELEMLRVKVKELESSEDRLDKTEQSLVSELEKLKSLTLSFVNERKY 199
Cdd:TIGR04523   36 KQLEKKLKTIKNELKNKEKELkNLDKNLNKDEE-KINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKN 114
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  200 LNEKEKENEKIIKELTQKLEQNKKmnrdhmrNASTFLerNDLRIEDGISSTLSSKES---KRKGSL-DYLKQVENETRDK 275
Cdd:TIGR04523  115 DKEQKNKLEVELNKLEKQKKENKK-------NIDKFL--TEIKKKEKELEKLNNKYNdlkKQKEELeNELNLLEKEKLNI 185
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720408942  276 SENEKNRNQEDNKvkdLNQEIEKLKTQIKHFESLEEELKKMRAKNNDLQDNYLTELNRNRSLASQLEEIKLQVRKQKE 353
Cdd:TIGR04523  186 QKNIDKIKNKLLK---LELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKD 260
PRK01156 PRK01156
chromosome segregation protein; Provisional
29-360 3.51e-04

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 44.51  E-value: 3.51e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942   29 ELEEATKNLQRAEDELLDLQDKVIQAEGSDSSTLAEIEVLR-QRVLKIEGKDEEIKRAEDLCHTMKEKLEEEENLTRELK 107
Cdd:PRK01156   410 ELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNgQSVCPVCGTTLGEEKSNHIINHYNEKKSRLEEKIREIE 489
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  108 SEIERLQKRMVDLEKLEEALSRSKNEcsqlclSLNEERNLTKKISSELEMLRVKVKELESSEDRLDKTEQSLVS-ELEKL 186
Cdd:PRK01156   490 IEVKDIDEKIVDLKKRKEYLESEEIN------KSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRYKSlKLEDL 563
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  187 KSLTLSFVNERKYLNEKEKENEKiikelTQKLEQNKKMNRdhmrnastfLERNDLRIEDGISSTLSSKESkrkgsldYLK 266
Cdd:PRK01156   564 DSKRTSWLNALAVISLIDIETNR-----SRSNEIKKQLND---------LESRLQEIEIGFPDDKSYIDK-------SIR 622
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  267 QVENETRDkSENEKNRNQEDNKVKD-LNQEIEKLKTQIKHFESLEEELKKMRAKNNDLQDNY------LTELNRNRSLAS 339
Cdd:PRK01156   623 EIENEANN-LNNKYNEIQENKILIEkLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLkksrkaLDDAKANRARLE 701
                          330       340
                   ....*....|....*....|.
gi 1720408942  340 QLEEIKLQVRKQKELGNGDIE 360
Cdd:PRK01156   702 STIEILRTRINELSDRINDIN 722
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
15-347 7.58e-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: 7.58e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942   15 HLRFKLQSLSRRLDELEEATKNLQRAEDELLDLQDKViqaeGSDSSTLAEIEVLRQRVLKIEGKDEEI--------KRAE 86
Cdd:pfam05483  378 QLKIITMELQKKSSELEEMTKFKNNKEVELEELKKIL----AEDEKLLDEKKQFEKIAEELKGKEQELifllqareKEIH 453
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942   87 DL---CHTMKEKLEEEENLTRELKSEIERLQKRMVDLEKLEEALSRSK----NECSQLCLSL-NEERNLTKKISSELEML 158
Cdd:pfam05483  454 DLeiqLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENkeltQEASDMTLELkKHQEDIINCKKQEERML 533
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  159 rvkvKELESsedrLDKTEQSLVSELEKLKSLTLSFVNERKYLNEKEKENEKIIKELTQKLEQNKKMNRDHMRNASTFLER 238
Cdd:pfam05483  534 ----KQIEN----LEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIEN 605
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  239 NDLRIEDgisstlsskeskrkgsldyLKQVENETRDKSENE-KNRNQEDNKVKDLNQEIEKLKTQikhFESLEEELKKMR 317
Cdd:pfam05483  606 KNKNIEE-------------------LHQENKALKKKGSAEnKQLNAYEIKVNKLELELASAKQK---FEEIIDNYQKEI 663
                          330       340       350
                   ....*....|....*....|....*....|
gi 1720408942  318 AKNNDLQDNYLTELNRNRSLASqlEEIKLQ 347
Cdd:pfam05483  664 EDKKISEEKLLEEVEKAKAIAD--EAVKLQ 691
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
4-226 7.99e-04

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 225288 [Multi-domain]  Cd Length: 652  Bit Score: 43.15  E-value: 7.99e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942    4 LTNYKDAASNRHLRFKLQSLSRRLDELEEATKNLQR-AEDELLDLQDKVIQAEGSDSSTLAEieVLRQRVLKIEGKDEEI 82
Cdd:COG2433    331 LRTLKISVSDDHERDALAAAYKAYLAYKPKLEKVERkLPELGIWKDVERIKALVIRGYPLAE--ALSKVKEEERPREKEG 408
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942   83 KRAEDlchtmKEKLEEEENLTRELKSEIERLQKRMVDLEKLEEALSRsknecsqlclslneernltkkissELEMLRVKV 162
Cdd:COG2433    409 TEEEE-----RREITVYEKRIKKLEETVERLEEENSELKRELEELKR------------------------EIEKLESEL 459
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720408942  163 KEL---ESSEDRLDKTEQSLVSELEKLksltlsfvnERKYLNEKEKenekiIKELTQKLEQNKKMNR 226
Cdd:COG2433    460 ERFrreVRDKVRKDREIRARDRRIERL---------EKELEEKKKR-----VEELERKLAELRKMRK 512
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
3-223 8.16e-04

Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 43.55  E-value: 8.16e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942    3 ELTNYKDAASNRHLRFKLQSLSRRLDELEEATKNLQRAEDELLDLQDKVIQAEGSDSSTLAEIEVLRQRVLKIEgkdEEI 82
Cdd:COG1196    803 EEAERRLDALERELESLEQRRERLEQEIEELEEEIEELEEKLDELEEELEELEKELEELKEELEELEAEKEELE---DEL 879
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942   83 KRAEDLCHTMKEKLEEEENLTRELKSEIERLQKRMVDLEKLEEALsrsKNECSQLCLSLNEERNLTkkISSELEMlrvKV 162
Cdd:COG1196    880 KELEEEKEELEEELRELESELAELKEEIEKLRERLEELEAKLERL---EVELPELEEELEEEYEDT--LETELER---EI 951
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720408942  163 KELESSEDRLDKTEQSLVSELEKLKsltlsfvNERKYLNEKEKENEKI---IKELTQKLEQNKK 223
Cdd:COG1196    952 ERLEEEIEALGPVNLRAIEEYEEVE-------ERYEELKSQREDLEEAkekLLEVIEELDKEKR 1008
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
73-374 8.24e-04

reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.


Pssm-ID: 130673 [Multi-domain]  Cd Length: 2757  Bit Score: 43.50  E-value: 8.24e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942   73 LKIEGKDEEIKRAEDLCHTMKEKLEEEENlTRELKSEIERLQKRMVDLEKLEEALSRSKNECSQL-CLSLNEERNLTKKI 151
Cdd:TIGR01612 1226 LFLEKIDEEKKKSEHMIKAMEAYIEDLDE-IKEKSPEIENEMGIEMDIKAEMETFNISHDDDKDHhIISKKHDENISDIR 1304
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  152 SSELEMLRVKVKEleSSEDRLDKTEQSLVSELEKLKSLTLSFVNERKYLNEKEKEN--EKII---KELTQKLEQNKKMNR 226
Cdd:TIGR01612 1305 EKSLKIIEDFSEE--SDINDIKKELQKNLLDAQKHNSDINLYLNEIANIYNILKLNkiKKIIdevKEYTKEIEENNKNIK 1382
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  227 DHMRNASTFLE--RNDLRIED---GISSTLSSKE-----SKRKGSLDYL--KQVENETRDKSENEKNRN----------- 283
Cdd:TIGR01612 1383 DELDKSEKLIKkiKDDINLEEcksKIESTLDDKDideciKKIKELKNHIlsEESNIDTYFKNADENNENvlllfkniema 1462
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  284 ----------QEDNKVKDLNQEIEKLKTQIKHFESLEEEL---KKMRAKNNDLQDNYLTELNR--NRSLASQLEEIKLQV 348
Cdd:TIGR01612 1463 dnksqhilkiKKDNATNDHDFNINELKEHIDKSKGCKDEAdknAKAIEKNKELFEQYKKDVTEllNKYSALAIKNKFAKT 1542
                          330       340
                   ....*....|....*....|....*..
gi 1720408942  349 RKQKELGNGDI-EGEDAFLLGRGRHER 374
Cdd:TIGR01612 1543 KKDSEIIIKEIkDAHKKFILEAEKSEQ 1569
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
154-354 9.72e-04

DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];


Pssm-ID: 223496 [Multi-domain]  Cd Length: 908  Bit Score: 43.21  E-value: 9.72e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  154 ELEMLRVKVKELESS-EDRLDKTEQSLVSELEKLKSLTLSFVNERKYLNEKEKENEKIIKELTQKLEQNKKMNRDHMRNA 232
Cdd:COG0419    168 KYEKLSELLKEVIKEaKAKIEELEGQLSELLEDIEDLLEALEEELKELKKLEEIQEEQEEEELEQEIEALEERLAELEEE 247
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  233 STFLERNDLRIEDGISStlsskeskrkgsldylkqvenetrdKSENEKNRNQEDNKVKDLNQEIEKLKTQIKHFESLEEE 312
Cdd:COG0419    248 KERLEELKARLLEIESL-------------------------ELEALKIREEELRELERLLEELEEKIERLEELEREIEE 302
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1720408942  313 LKKMRAKNNDLQDNYLTELNRNRSLASQLEEIKLQVRKQKEL 354
Cdd:COG0419    303 LEEELEGLRALLEELEELLEKLKSLEERLEKLEEKLEKLESE 344
COG5022 COG5022
Myosin heavy chain [General function prediction only];
14-347 1.03e-03

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 43.14  E-value: 1.03e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942   14 RHLRFKLQSLSRRLDELEEATKNL---QRAEDELLDLQDKVIQAEGSDSSTLAEievLRQRVLKIEGKDEEIKRAEDLCH 90
Cdd:COG5022    758 RYLRRRYLQALKRIKKIQVIQHGFrlrRLVDYELKWRLFIKLQPLLSLLGSRKE---YRSYLACIIKLQKTIKREKKLRE 834
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942   91 TMKEKLEEEENLTRELKSEIERLQKRMVDLEKlEEALSRSKNEcsqlclSLNEERNLT--KKISSELEMLRVKVKELESS 168
Cdd:COG5022    835 TEEVEFSLKAEVLIQKFGRSLKAKKRFSLLKK-ETIYLQSAQR------VELAERQLQelKIDVKSISSLKLVNLELESE 907
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  169 EDRLDKTEQSlvSELEKLKSLTLSFVNERKYLNEKEKENEKIIKeltqkLEQNKKMNRDHMRNAS---TFLERNDLRIED 245
Cdd:COG5022    908 IIELKKSLSS--DLIENLEFKTELIARLKKLLNNIDLEEGPSIE-----YVKLPELNKLHEVESKlkeTSEEYEDLLKKS 980
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  246 GIS-STLSSKESKRKGSLDYLKQVENETRDKSENEKNRNQEDNKVKDLNQEIEKLKTQIKHFESLEEELKKMRA---KNN 321
Cdd:COG5022    981 TILvREGNKANSELKNFKKELAELSKQYGALQESTKQLKELPVEVAELQSASKIISSESTELSILKPLQKLKGLlllENN 1060
                          330       340
                   ....*....|....*....|....*.
gi 1720408942  322 DLQDNYLTELNRNRSLASQLEEIKLQ 347
Cdd:COG5022   1061 QLQARYKALKLRRENSLLDDKQLYQL 1086
PTZ00440 PTZ00440
reticulocyte binding protein 2-like protein; Provisional
81-413 1.08e-03

reticulocyte binding protein 2-like protein; Provisional


Pssm-ID: 240419 [Multi-domain]  Cd Length: 2722  Bit Score: 43.28  E-value: 1.08e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942   81 EIKRAEDLCHTMKE---KLEEEENLTRELKSEIERLQKRMVDLEKLEEALSRSKNECSQLCLSLNEERNLTKKISSELEM 157
Cdd:PTZ00440   496 YQEKVDELLQIINSikeKNNIVNNNFKNIEDYYITIEGLKNEIEGLIELIKYYLQSIETLIKDEKLKRSMKNDIKNKIKY 575
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  158 LR---VKVKELESSEDRLDKTEQslvsELEKLKSLTLSfvNERKYLNEKEKENEKIIKELTQKLEQNKKMNRDHMrnaST 234
Cdd:PTZ00440   576 IEenvDHIKDIISLNDEIDNIIQ----QIEELINEALF--NKEKFINEKNDLQEKVKYILNKFYKGDLQELLDEL---SH 646
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  235 FLERNdlriedgisstlsSKESKRKGSLDYLKQVENETRDKSENEKNRNQEDNkvkdlNQEIEKLKTQIKHFESLEEELK 314
Cdd:PTZ00440   647 FLDDH-------------KYLYHEAKSKEDLQTLLNTSKNEYEKLEFMKSDNI-----DNIIKNLKKELQNLLSLKENII 708
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  315 KMRAKN--NDLQDNYLTELNRNRSLASQLEEIKLQVRKQKELGNGDIEGEDAFLLGRGRHERTKLKGHGSEASVSKHtsr 392
Cdd:PTZ00440   709 KKQLNNieQDISNSLNQYTIKYNDLKSSIEEYKEEEEKLEVYKHQIINRKNEFILHLYENDKDLPDGKNTYEEFLQY--- 785
                          330       340
                   ....*....|....*....|.
gi 1720408942  393 elspqhkRERLRNREFALSNE 413
Cdd:PTZ00440   786 -------KDTILNKENKISND 799
PTZ00121 PTZ00121
MAEBL; Provisional
25-364 1.19e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.21  E-value: 1.19e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942   25 RRLDELEEATKNLQRAEDELLDLQDKVIQAEGSDSSTLAE-----------IEVLRQRVLKiegKDEEIKRAEDLCHTMK 93
Cdd:PTZ00121  1134 RKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEdakkaeaarkaEEVRKAEELR---KAEDARKAEAARKAEE 1210
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942   94 EKLEEEENLTRELK--SEIERLQKRMVDLEKLEEALSRSKNECSQLCLSLNEERNLTKKISSELEMLRvKVKELESSEDR 171
Cdd:PTZ00121  1211 ERKAEEARKAEDAKkaEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEAR-KADELKKAEEK 1289
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  172 LDKTEQSLVSELEKLKSLtlsfvnerkylnEKEKENEKIIKELTQKLEQNKKMNRDHMRNASTFLERNDLRIEDGISSTL 251
Cdd:PTZ00121  1290 KKADEAKKAEEKKKADEA------------KKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAAD 1357
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  252 SSKESKRKGSLDYLKQveNETRDKSENEKNRNQEDNKVKDLNQEIEKLKTQIKHFESLEEELKKM-RAKNNDLQDNYLTE 330
Cdd:PTZ00121  1358 EAEAAEEKAEAAEKKK--EEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKAdEAKKKAEEKKKADE 1435
                          330       340       350
                   ....*....|....*....|....*....|....
gi 1720408942  331 LNRNRSLASQLEEIKLQVRKQKELGNGDIEGEDA 364
Cdd:PTZ00121  1436 AKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEA 1469
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
27-345 1.29e-03

Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation.


Pssm-ID: 428797 [Multi-domain]  Cd Length: 542  Bit Score: 42.53  E-value: 1.29e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942   27 LDELEEATK--NLQRAEDELLDLQDKVIQAEGSDSSTLAEIEVLrqrvLKIEGKD-EEIKRAEDLchtmkekleeeenlT 103
Cdd:pfam06160   69 LFEAEELNDkyRFKKAKKALDEIEELLDDIEEDIKQILEELDEL----LESEEKNrEEVEELKDK--------------Y 130
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  104 RELKSEIerLQKRM---VDLEKLEEALSRSKNECSQLcLSLNEE------RNLTKKISSELEMLRVKVKELEsseDRLDK 174
Cdd:pfam06160  131 RELRKTL--LANRFsygPAIDELEKQLAEIEEEFSQF-EELTESgdyleaREVLEKLEEETDALEELMEDIP---PLYEE 204
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  175 TEQSLVSELEKLKSLTLSFVNERKYLNEKEKENEkiIKELTQKLEQNKKM-NRDHMRNASTFLERNDLRIeDGISSTL-- 251
Cdd:pfam06160  205 LKTELPDQLEELKEGYREMEEEGYALEHLNVDKE--IQQLEEQLEENLALlENLELDEAEEALEEIEERI-DQLYDLLek 281
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  252 --SSK---ESKRKGSLDYLKQVENETRD-KSENE---KN---RNQEDNKVKDLNQEIEKLKTQikhFESLEEELKKMRAK 319
Cdd:pfam06160  282 evDAKkyvEKNLPEIEDYLEHAEEQNKElKEELErvqQSytlNENELERVRGLEKQLEELEKR---YDEIVERLEEKEVA 358
                          330       340
                   ....*....|....*....|....*.
gi 1720408942  320 NNDLQDNYLTELNRNRSLASQLEEIK 345
Cdd:pfam06160  359 YSELQEELEEILEQLEEIEEEQEEFK 384
PRK12704 PRK12704
phosphodiesterase; Provisional
108-220 1.36e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 42.46  E-value: 1.36e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  108 SEIERLQKRMVDLEKLE------EALSRSKNECSQLCLSLNEERNLTKKISSELEmLRVKVKE--LESSEDRLDKTEQSL 179
Cdd:PRK12704    34 KEAEEEAKRILEEAKKEaeaikkEALLEAKEEIHKLRNEFEKELRERRNELQKLE-KRLLQKEenLDRKLELLEKREEEL 112
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1720408942  180 VSELEKLKsltlsfvNERKYLNEKEKENEKIIKELTQKLEQ 220
Cdd:PRK12704   113 EKKEKELE-------QKQQELEKKEEELEELIEEQLQELER 146
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
28-349 1.47e-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: 42.73  E-value: 1.47e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942   28 DELEEATKNLQRAEDELLDLQDKVIQAEGSDSSTLAEIEVLRQRVLKIEGKDEEIKRAEDLchtmkekleeeENLTRELK 107
Cdd:TIGR00606  577 DWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSQDE-----------ESDLERLK 645
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  108 SEIERLQKRMVDL-------EKLEEALSRSKNECSQLC----LSLNEERNLTKKISSELEMLRVKVKELESSEDRLDKTE 176
Cdd:TIGR00606  646 EEIEKSSKQRAMLagatavySQFITQLTDENQSCCPVCqrvfQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRR 725
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  177 QSLVSELEKLKSLTLSFVNERKYLNEKEKENEKIIKELTQKLEQNKKMNRDHM-RNASTFLERNDLRIEDGISSTLSSKE 255
Cdd:TIGR00606  726 DEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMpEEESAKVCLTDVTIMERFQMELKDVE 805
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  256 SKRKGSLDYLKQVENEtRDKSENEKNRNQEDNKVKDLNQEIEKLKtqiKHFESLEEELKKMRAKNNDLQDNYL---TELN 332
Cdd:TIGR00606  806 RKIAQQAAKLQGSDLD-RTVQQVNQEKQEKQHELDTVVSKIELNR---KLIQDQQEQIQHLKSKTNELKSEKLqigTNLQ 881
                          330
                   ....*....|....*..
gi 1720408942  333 RNRSLASQLEEIKLQVR 349
Cdd:TIGR00606  882 RRQQFEEQLVELSTEVQ 898
PTZ00121 PTZ00121
MAEBL; Provisional
25-315 1.61e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.82  E-value: 1.61e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942   25 RRLDELEEATKNLQRAEDELLDLQDKVIQAEGSDSSTLAEIEVLRQRVLKIE--GKDEEIKRAEDLCHTMKEKLEEEENL 102
Cdd:PTZ00121  1230 KKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADelKKAEEKKKADEAKKAEEKKKADEAKK 1309
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  103 TRELKSEIERLQKRMVDLEKLEEALSRSKNEcsqlclslNEERNLTKKISSELEMLRVKVKELESSEDRLDKTEQSLVSE 182
Cdd:PTZ00121  1310 KAEEAKKADEAKKKAEEAKKKADAAKKKAEE--------AKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKAD 1381
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  183 LEKLKSLTLSFVNERKylnEKEKENEKIIKELTQKLEQNKKMnrDHMRNASTFLERND---LRIEDGISSTLSSKESKRK 259
Cdd:PTZ00121  1382 AAKKKAEEKKKADEAK---KKAEEDKKKADELKKAAAAKKKA--DEAKKKAEEKKKADeakKKAEEAKKADEAKKKAEEA 1456
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720408942  260 GSLDYLKQVENETRdKSENEKNRNQEDNKVKDLNQEIEKLKTQIKHFESLEEELKK 315
Cdd:PTZ00121  1457 KKAEEAKKKAEEAK-KADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKK 1511
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
21-361 1.77e-03

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 435022 [Multi-domain]  Cd Length: 1112  Bit Score: 42.40  E-value: 1.77e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942   21 QSLSRRLDELEEATKNLQRAEDELLDLQDKVIQAEGSDSSTLAEIEVLRQRV---------LKIEGkdEEIKRAEDLCHT 91
Cdd:pfam15921  475 EMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVdlklqelqhLKNEG--DHLRNVQTECEA 552
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942   92 MKEKLEEEENLTRELKSEIERLQK------RMVDLEKLEEAlsRSKNECSQLCLSLNEERNLTKKISSELEMLRVKVKEL 165
Cdd:pfam15921  553 LKLQMAEKDKVIEILRQQIENMTQlvgqhgRTAGAMQVEKA--QLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDL 630
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  166 ESSEDRLDKTEQSLVSELEKLKSLTLSFVNE----RKYLNEKEKENEKIIKELTQKLEQNKKMN---RDHMRNASTFLE- 237
Cdd:pfam15921  631 ELEKVKLVNAGSERLRAVKDIKQERDQLLNEvktsRNELNSLSEDYEVLKRNFRNKSEEMETTTnklKMQLKSAQSELEq 710
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  238 -RNDLRIEDG-------ISSTLSSKESKRKGSLDYLKQ--------VENETRDKSENEKNRNQEDNKVKDLNQEIEKLKT 301
Cdd:pfam15921  711 tRNTLKSMEGsdghamkVAMGMQKQITAKRGQIDALQSkiqfleeaMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAG 790
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  302 QIKHFESLEEELKKMRAKNNDLQDNYLTELNRNRSLASQLEEIKLQVRKQKELGNGDIEG 361
Cdd:pfam15921  791 ELEVLRSQERRLKEKVANMEVALDKASLQFAECQDIIQRQEQESVRLKLQHTLDVKELQG 850
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
16-353 2.02e-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: 42.34  E-value: 2.02e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942   16 LRFKLQSLSRRLDELEEATKNLQRAEDELLDLQDKVIQAEGSDSSTL-------AEIEVLRQRVLKIEGKDEEIKRAEDL 88
Cdd:TIGR00606  191 LRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSReivksyeNELDPLKNRLKEIEHNLSKIMKLDNE 270
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942   89 CHTMKEKLEEEENLTRELKSEIERL----QKRMVDLEKLEEALSRSKNE----CSQLCLSLNEERNLTKKISSELEmlrV 160
Cdd:TIGR00606  271 IKALKSRKKQMEKDNSELELKMEKVfqgtDEQLNDLYHNHQRTVREKERelvdCQRELEKLNKERRLLNQEKTELL---V 347
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  161 KVKELESSEDRLDktEQSLVSELEKLKSLTLSFVNERKYLNEKEKENEKIIKELTQKLEQNKKMNRDHMrnastflernd 240
Cdd:TIGR00606  348 EQGRLQLQADRHQ--EHIRARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQLC----------- 414
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  241 lriedgisSTLSSKESKRKGSLDYLKQVENETRDKSENEKNR-NQEDNKVKDLNQEIEKLKTQIKHFESLEEELKKMRAK 319
Cdd:TIGR00606  415 --------ADLQSKERLKQEQADEIRDEKKGLGRTIELKKEIlEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERE 486
                          330       340       350
                   ....*....|....*....|....*....|....
gi 1720408942  320 NNDLQDNYLTELNRNRSLASQLEEIKLQVRKQKE 353
Cdd:TIGR00606  487 LSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKL 520
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
19-354 2.53e-03

rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 41.96  E-value: 2.53e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942   19 KLQSLSRRLDELEEATKNLQRAEDELLDlqdkviQAEGSDSSTLAEIEVLRQRVLKIEGKDEEIKRAEDLCHTMKEKLEE 98
Cdd:TIGR00606  406 EAKTAAQLCADLQSKERLKQEQADEIRD------EKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQE 479
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942   99 EENLTREL-----KSEIERLQKRMVDLEKLEEALSRSKNECSQLclslNEERNLTKKISSELEML-RVKVKELESSEDRL 172
Cdd:TIGR00606  480 LRKAERELskaekNSLTETLKKEVKSLQNEKADLDRKLRKLDQE----MEQLNHHTTTRTQMEMLtKDKMDKDEQIRKIK 555
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  173 DKTEQSLVSELEKL---KSLTLSFVNERKYLNEKEKENEKIIKELtQKLEQNKkmnrDHMRNASTFLERNDLRIEDGISS 249
Cdd:TIGR00606  556 SRHSDELTSLLGYFpnkKQLEDWLHSKSKEINQTRDRLAKLNKEL-ASLEQNK----NHINNELESKEEQLSSYEDKLFD 630
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  250 TLSSKESKRK-------------------GSLDYLKQVENETRDKSENEKNRNQEDNKVK-DLNQEIEKLKTQIKHF--- 306
Cdd:TIGR00606  631 VCGSQDEESDlerlkeeieksskqramlaGATAVYSQFITQLTDENQSCCPVCQRVFQTEaELQEFISDLQSKLRLApdk 710
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720408942  307 -ESLEEELKK-------------MRAKNNDLQDNYLTEL-NRNRSLASQLEEIKLQVRKQKEL 354
Cdd:TIGR00606  711 lKSTESELKKkekrrdemlglapGRQSIIDLKEKEIPELrNKLQKVNRDIQRLKNDIEEQETL 773
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
28-423 3.20e-03

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 41.75  E-value: 3.20e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942   28 DELEEATKNLQRAEDELLDLQDKVIQAEGSDSSTLAEIEVLRQRVLKIEGKDEEIKR----------------------- 84
Cdd:pfam12128  471 ERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELqlfpqagtllhflrkeapdweqs 550
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942   85 ------AEDLCHTMKEKLEEEENLTRELKSEIERLQKRMVDLEK---LEEALsrsKNECSQLCLSLNEERNLTKKISSEL 155
Cdd:pfam12128  551 igkvisPELLHRTDLDPEVWDGSVGGELNLYGVKLDLKRIDVPEwaaSEEEL---RERLDKAEEALQSAREKQAAAEEQL 627
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  156 EMLRVKVKELESSEDRldkTEQSLVSELEKLKSLTLSFVNERKYLNEKEKENEKIIKELTQKLEQNKKMNRDHMRNASTF 235
Cdd:pfam12128  628 VQANGELEKASREETF---ARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEE 704
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  236 LERNDLRIEDGISSTLSSKESKRKGSLDYLKQVENETRDKSENEKNRNQEDNKvKDLN------QEIEKLKTQIKHFESL 309
Cdd:pfam12128  705 QKEQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRSGAKAELKALETWYK-RDLAslgvdpDVIAKLKREIRTLERK 783
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  310 EEELKKMRAKNNDLQDNYL-TELNRNRSLASQLEEIKLQVRkqkelgngDIEGEdaflLGRGRHE-RTKLKGHGSEASVS 387
Cdd:pfam12128  784 IERIAVRRQEVLRYFDWYQeTWLQRRPRLATQLSNIERAIS--------ELQQQ----LARLIADtKLRRAKLEMERKAS 851
                          410       420       430
                   ....*....|....*....|....*....|....*.
gi 1720408942  388 KHTSRELSPQHKRERLRNREFALSNEHYSLSSKQAS 423
Cdd:pfam12128  852 EKQQVRLSENLRGLRCEMSKLATLKEDANSEQAQGS 887
Tropomyosin pfam00261
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ...
28-245 3.80e-03

Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organisation and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.


Pssm-ID: 425563 [Multi-domain]  Cd Length: 235  Bit Score: 40.01  E-value: 3.80e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942   28 DELEEATKNLQRAEDELLDLQDKVIQAEgsdsstlAEIEVLRQRVLKIEgkdEEIKRAEDLCHTMKEKLEEEENLTrelk 107
Cdd:pfam00261    8 EELDEAEERLKEAMKKLEEAEKRAEKAE-------AEVAALNRRIQLLE---EELERTEERLAEALEKLEEAEKAA---- 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  108 SEIERLQKrmvdleKLEEALSRSKNECSQLCLSLNEERNLTKKISSELEMLRVKVK----ELESSEDRLDKTEqSLVSEL 183
Cdd:pfam00261   74 DESERGRK------VLENRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVvvegDLERAEERAELAE-SKIVEL 146
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  184 EK--------LKSLTLSfvnERKYlNEKEKENEKIIKELTQKLEQNKKMNRDHMRNASTfLERNDLRIED 245
Cdd:pfam00261  147 EEelkvvgnnLKSLEAS---EEKA-SEREDKYEEQIRFLTEKLKEAETRAEFAERSVQK-LEKEVDRLED 211
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
29-325 3.80e-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: 426331 [Multi-domain]  Cd Length: 1081  Bit Score: 41.30  E-value: 3.80e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942   29 ELEEATKNLQRAEDELLDLQDKvIQAEgsdSSTLAEIEVLRQRvlkIEGKDEEIkraEDLCHTMKEKLEEEENLTRELKS 108
Cdd:pfam01576   27 ELKELEKKHQQLCEEKNILAEQ-LQAE---TELFAEAEEMRAR---LAARKQEL---EEILHELEARLEEEEERSQQLQN 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  109 EIERLQKRMVDLE-KLEE------ALSRSKNECSQLCLSLNEERNLTKKISSELEmlrvkvKELESSEDRLDKTEQSLVS 181
Cdd:pfam01576   97 EKKKMQQHIQDLEeQLEEeeaarqKLQLEKVTTEAKIKKMEEDILLLEDQNNKLQ------KERKLLEERISEFTSNLAE 170
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  182 ELEKLKSltlsfvnerkyLNEKEKENEKIIKELTQKLEQNKKMnRDHMRNASTFLERNDLRIEDGIS----------STL 251
Cdd:pfam01576  171 EEEKSKS-----------LNKLKNKHEAMISDLEDRLKKEEKG-RQELEKAKRKLEGESSDLQEQIAelqaqiaelrAQL 238
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720408942  252 SSKESKRKGSLDylkQVENETRDKSENEKNRNQEDNKVKDLNQEIEKLKTQ----IKHFESLEEELKKMRAKNNDLQD 325
Cdd:pfam01576  239 AKKEEELQAALA---RLEEETAQKNAALKKLRELEAQLSELQEDLESERAArakaEKQRRDLGEELEALKTELEDTLD 313
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
22-223 4.00e-03

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];


Pssm-ID: 224259 [Multi-domain]  Cd Length: 294  Bit Score: 40.43  E-value: 4.00e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942   22 SLSRRLDELEEATKNLQRAEDELLDLQDKVIQaegsDSSTLAEievlrqrvlKIEGKDEEIKRAEDLCHTMKEKLEEEEN 101
Cdd:COG1340      3 AMLDKLDELELKRKQLKEEIEELKEKRDELRK----EASELAE---------KRDELNAKVRELREKAQELREERDEINE 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  102 LTRELKSEIERLQKRMVDLEKLEEALSRSKNECSQ---------------------LCLSLNEERNLTKKISSELEMLRV 160
Cdd:COG1340     70 EVQELKEKRDEINAKLQELRKEYRELKEKRNEFNLggrsikslereierlekkqqtSVLTPEEERELVQKIKELRKELED 149
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720408942  161 KVKELESSEDRldkteQSLVSELEKLKSLTLSFVNERKYLNEKEKENEKIIKELTQKLEQNKK 223
Cdd:COG1340    150 AKKALEENEKL-----KELKAEIDELKKKAREIHEKIQELANEAQEYHEEMIKLFEEADELRK 207
DUF4686 pfam15742
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ...
104-377 4.64e-03

Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins in this family are typically between 498 and 775 amino acids in length. There is a conserved DLK sequence motif.


Pssm-ID: 434900 [Multi-domain]  Cd Length: 384  Bit Score: 40.43  E-value: 4.64e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  104 RELKSEIERLQKRMVDLEKlEEALSRSKN-ECSQLCLSLNEER---------------NLTKKISS---ELEMLRVKVKE 164
Cdd:pfam15742   16 QQLRQDLQRLQILCTSAER-ELRYEREKNlDLKQHNSLLQEENikikaelkqaqqkllDSTKMCSSltaEWEHCQQKIRE 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  165 LESSEDRLDKTEQSLVS---ELEKLKS-----------------------LTLSFVNERKYLNEKEKENEKIIKELTQKL 218
Cdd:pfam15742   95 LELEVLKQAQSIKSQNSlqeKLAQEKSkvadaekkilelqqklehahkvcLTETCILEKKQLEEEIKEAQENEAKLKQQY 174
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  219 --EQNKKMNRDHMRNASTFLERNDLRIEDGISSTLSSKESKRKGSLDYLKQVENETRDKSENEKNRNQEDNKVKDLNQEI 296
Cdd:pfam15742  175 qeEQQKRKLLDQNVNELQQQVRSLQDKEAQLEMTNSQQQLRIQQQEAQLKQLENEKRKSDEHLKSNQELSEKLSSLQQEK 254
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  297 EKLKTQIKHF-ESLEEELK-----------KMRAKNNDLQDNYLTELNRNRSLASQLEEIKLQVRKQKELGNGDIEGEDA 364
Cdd:pfam15742  255 EALQEELQQVlKQLDVHVRkynekhhhhkaKLRRAKDRLVHEVEQRDERIKQLENEIRILRQQIEKEKAFQKQVTAENDT 334
                          330
                   ....*....|...
gi 1720408942  365 FLLgrgrhERTKL 377
Cdd:pfam15742  335 LLL-----EKRKL 342
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
262-346 4.66e-03

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 40.39  E-value: 4.66e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942   262 LDYLKQVENETRDKSENEKNRNQEdnKVKDLNQEIEKLKTQIKHFESLEEELKKMRAKNNDLQDNYLTELNrnrSLASQL 341
Cdd:smart00787  188 LRQLKQLEDELEDCDPTELDRAKE--KLKKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIA---EAEKKL 262

                    ....*
gi 1720408942   342 EEIKL 346
Cdd:smart00787  263 EQCRG 267
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
37-380 4.93e-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: 428520 [Multi-domain]  Cd Length: 660  Bit Score: 40.87  E-value: 4.93e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942   37 LQRAEDELLDLQDKVIQAEGSDSSTLAEIEvlRQRVLKIEGKDEEIKRAEDLCHTMKEKLEEEENLTRELKSEIERLQKR 116
Cdd:pfam05557    4 LIESKARLSQLQNEKKQMELEHKRARIELE--RKASALARQLERESDRNQELQKRIRLLEKREAEAEEALREQAELNRLK 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  117 MvdleKLEEALSRSKNECSQLCLSLNE-ERNLTKKIS--------SELEmLRVKVKELESSEDRLDKTEQSLvSELEKLK 187
Cdd:pfam05557   82 K----KNLEALNKKLNEKESQLADAREvISCLKNELSelrrqiqrQELE-LSSTNSELEELQERLDLQKAKA-QEAEQLR 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  188 SLTLSFVNERKYLNEKEKENEKIIKELTQKLEQNKKMNRDHMRNAStfLERNDLRIEDGISSTLSSKESKrkgslDYLKQ 267
Cdd:pfam05557  156 QNLEAQQSSLAEAEQRIKELEFEIQSQEQDSEIVKNSKSELARIPE--LERELERLREHNKHLNENIENK-----LLLKE 228
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  268 VENETRDKSENEKNRNQEdnkVKDLNQEIEKLKTQIKHFESLEEELKKMRAKNNDLQDNYLTELNRNRSLASQLEEIKLQ 347
Cdd:pfam05557  229 EVEDLKRKLEREEGYREE---LATLELEKEKLEQELKSWEKLAQDTGLNLRSPEDLSRRIEQLQQREITLKEENSSLTSS 305
                          330       340       350
                   ....*....|....*....|....*....|...
gi 1720408942  348 VRkQKELGNGDIEGEDAFLLGRGRHERTKLKGH 380
Cdd:pfam05557  306 AR-QLEKAQRELEQELAQYLKNIEDLNKKLKRH 337
PRK12704 PRK12704
phosphodiesterase; Provisional
197-353 5.12e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 40.53  E-value: 5.12e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  197 RKYLNEKEKENEKIIKELTQKLEQNKKmnrDHMRNASTflERNDLRIEdgisstlSSKESKRKgsLDYLKQVENETRDKS 276
Cdd:PRK12704    30 EAKIKEAEEEAKRILEEAKKEAEAIKK---EALLEAKE--EIHKLRNE-------FEKELRER--RNELQKLEKRLLQKE 95
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720408942  277 ENEKNRNQednkvkDLNQEIEKLKTQIKHFESLEEELKKMRAKNNDLQDNYLTELNRNRSLASqlEEIKLQVRKQKE 353
Cdd:PRK12704    96 ENLDRKLE------LLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTA--EEAKEILLEKVE 164
CwlO1 COG3883
Uncharacterized N-terminal domain of peptidoglycan hydrolase CwlO [Function unknown];
28-217 5.85e-03

Uncharacterized N-terminal domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 226400 [Multi-domain]  Cd Length: 265  Bit Score: 39.70  E-value: 5.85e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942   28 DELEEATKNLQRAEDELLDLQDKViqaegsdSSTLAEIEVLRQRVLKIEgkdEEIKraedlchtmkekleeeenltrELK 107
Cdd:COG3883     38 SKLSELQKEKKNIQNEIESLDNQI-------EEIQSKIDELQKEIDQSK---AEIK---------------------KLQ 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  108 SEIERLQKRMVDLEKLEEALSRS--KNECSQLCL-------SLNEERNLTKKISSELEMLRVKVKELESSEDRLDKTEQS 178
Cdd:COG3883     87 KEIAELKENIVERQELLKKRARAmqVNGTATSYIdvilnskSFSDLISRVTAISVIVDADKKILEQQKEDKKSLEEKQAA 166
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1720408942  179 LVSELEKLKSLTLSFVNERKYLNEKEKENEKIIKELTQK 217
Cdd:COG3883    167 LEDKLETLVALQNELETQLNSLNSQKAEKNALIAALAAK 205
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
15-354 7.32e-03

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 40.34  E-value: 7.32e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942   15 HLRFKLQSLSRRLDELEEATKNLQRAEDELLDLQDKVIQAEGSD-------------SSTLAEIEVLRQRVL-----KIE 76
Cdd:TIGR00618  390 TLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQelqqryaelcaaaITCTAQCEKLEKIHLqesaqSLK 469
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942   77 GKDEEIKRAEDLCHTMKEKLEEEENLTRELKSEIERLQKRMVDLEKLEEALSRSKNECSQLCLSLNEERNLTK---KISS 153
Cdd:TIGR00618  470 EREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETseeDVYH 549
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  154 ELEMLRVKVKELESSEDRLDKTEQSLVSELEKLKSL---TLSFVNERKYLNEKEKENEKIIKELTQKL------EQNKKM 224
Cdd:TIGR00618  550 QLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDipnLQNITVRLQDLTEKLSEAEDMLACEQHALlrklqpEQDLQD 629
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942  225 NRDHMRNAS-------TFLERNDL-----RIEDGISSTLSSKESKRKGSLDYLKQVENETRDKSENEKNRNQEDNKVKDL 292
Cdd:TIGR00618  630 VRLHLQQCSqelalklTALHALQLtltqeRVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLREL 709
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720408942  293 NQEIEKLKTQIKHFESLEEELKKMRAKNNDLQDNYLTELNRNRSLASQLEEIKLQVRKQKEL 354
Cdd:TIGR00618  710 ETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVT 771
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
11-223 7.80e-03

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 40.44  E-value: 7.80e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942   11 ASNRHLRFKLQSLSRRLDELEEATKNLQRAEDElLDLQDKVIQAEGSDS-----STLAEIEVLRQRVLKIEGKDEEIKRA 85
Cdd:TIGR02169  812 ARLREIEQKLNRLTLEKEYLEKEIQELQEQRID-LKEQIKSIEKEIENLngkkeELEEELEELEAALRDLESRLGDLKKE 890
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942   86 EDlchTMKEKLEEEENLTRELKSEIERLQKRMVDL-EKLEEALSRSKnecsqlclSLNEERNLTKKISSELEMLRVKVKE 164
Cdd:TIGR02169  891 RD---ELEAQLRELERKIEELEAQIEKKRKRLSELkAKLEALEEELS--------EIEDPKGEDEEIPEEELSLEDVQAE 959
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1720408942  165 LESSEDRLDKTEQSLVSELEKLKSlTLSFVNERKYLNEKEKENEKIIKELTQKLEQNKK 223
Cdd:TIGR02169  960 LQRVEEEIRALEPVNMLAIQEYEE-VLKRLDELKEKRAKLEEERKAILERIEEYEKKKR 1017
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Escherichia coli str. K-12 ...
8-188 9.40e-03

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Escherichia coli str. K-12 substr. MG1655 [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 225638 [Multi-domain]  Cd Length: 1480  Bit Score: 40.25  E-value: 9.40e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942    8 KDAASNRHLRFKLQSLSRRLDELEEATKNLQRAEDELLDL---QDKVIQAEgsdsstlaEIEVLRQRVlkiegkdeeikr 84
Cdd:COG3096    503 REGPDQRHLAEQVQPLRMRLSELEQRLRQQQSAERLLADFckrQGKNLDAE--------ELEALHQEL------------ 562
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942   85 aEDLCHTMKEKLEEEENLTRELKSEIERLQKRMVDLEKLEEALSRSKNECSQLCLSLNEERNLTKKISSELEMLRVKVKE 164
Cdd:COG3096    563 -EALIESLSDSVSNAREQRMALRQEQEQLQSRIQSLMQRAPVWLAAQNALEQLSEQSGEEFTDSQDVTEYMQQLLERERE 641
                          170       180
                   ....*....|....*....|....
gi 1720408942  165 LESSEDRLDKTEQSLVSELEKLKS 188
Cdd:COG3096    642 ATVERDELGARKNALDEEIERLSQ 665
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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