|
Name |
Accession |
Description |
Interval |
E-value |
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
104-353 |
4.42e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 70.48 E-value: 4.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 104 RELKSEIERLQKRMVDLEKLEEALSRSKNECSQLCLSLNEERNLTKKISSELEMLRVKVKELESSEDRLDKTEQSLVSEL 183
Cdd:PRK03918 172 KEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 184 EKLKSLTLSFVNERKYLNEKEKEN---EKIIKELTQ---------KLEQNKKMNRDHMRNASTFLERNDLRIEdGISSTL 251
Cdd:PRK03918 252 GSKRKLEEKIRELEERIEELKKEIeelEEKVKELKElkekaeeyiKLSEFYEEYLDELREIEKRLSRLEEEIN-GIEERI 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 252 SSKESKrKGSLDYLKQVENETRDKSENEKNRNQEDNKVKDLNQEIEKLKTQIKHF--ESLEEELKKMRAKNNDLQDNYLT 329
Cdd:PRK03918 331 KELEEK-EERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLtpEKLEKELEELEKAKEEIEEEISK 409
|
250 260
....*....|....*....|....
gi 119433663 330 ELNRNRSLASQLEEIKLQVRKQKE 353
Cdd:PRK03918 410 ITARIGELKKEIKELKKAIEELKK 433
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
7-406 |
6.08e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 66.88 E-value: 6.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 7 YKDAASNRHLRFKLQSLSRRLDELEEATKNLQRAEDELLDLQDKVIQAEgsdsstlAEIEVLRQRVLKIEGKDEEIKRAE 86
Cdd:COG1196 218 LKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELE-------AELEELRLELEELELELEEAQAEE 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 87 dlchtmkekleeeenltRELKSEIERLQKRMVDLEKLEEALSRSKNECSQLCLSLNEER-NLTKKISSELEMLRVKVKEL 165
Cdd:COG1196 291 -----------------YELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELeELEEELEELEEELEEAEEEL 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 166 ESSEDRLDKTEQSLVSELEKLKSLtlsfvnerkyLNEKEKENEKIIKELTQKLEQNKKMNRdhmrnastfLERNDLRIED 245
Cdd:COG1196 354 EEAEAELAEAEEALLEAEAELAEA----------EEELEELAEELLEALRAAAELAAQLEE---------LEEAEEALLE 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 246 GISSTLSSKESKRKGSLDYLKQVENETRDKSENEKNRNQEDNKVKDLNQEIEKLKTQIkhfESLEEELKKMRAKNNDLQD 325
Cdd:COG1196 415 RLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEA---ALLEAALAELLEELAEAAA 491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 326 NYLTELNRNRSLASQLEEIKlqvRKQKELGNGDIEGEDAFLLGRGRHERTKLKGHGSEASVSKHTSRELSPQHKRERLRN 405
Cdd:COG1196 492 RLLLLLEAEADYEGFLEGVK---AALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKA 568
|
.
gi 119433663 406 R 406
Cdd:COG1196 569 A 569
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
103-362 |
1.83e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 65.47 E-value: 1.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 103 TRELKSEIERLQKRMVDLEKLEEAL----SRSKNECSQLCLSLNEERNLTKKISSELEML---RVKVKE-LESSEDRLDK 174
Cdd:TIGR02169 669 SRSEPAELQRLRERLEGLKRELSSLqselRRIENRLDELSQELSDASRKIGEIEKEIEQLeqeEEKLKErLEELEEDLSS 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 175 TEQSLVSELEKLKSLTLSFVNERKYLNEKEKENEKIIKELTQKLEQNKkmnRDHMRNASTFLERNDLRIEDgISSTLSSK 254
Cdd:TIGR02169 749 LEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEI---QAELSKLEEEVSRIEARLRE-IEQKLNRL 824
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 255 ESKRKGSLDYLKQVENETRDKSENEKNRNQE----DNKVKDLNQEIEKLKTQIKHFES----LEEELKKMRAKNNDLQDN 326
Cdd:TIGR02169 825 TLEKEYLEKEIQELQEQRIDLKEQIKSIEKEienlNGKKEELEEELEELEAALRDLESrlgdLKKERDELEAQLRELERK 904
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 119433663 327 Y---LTELNRNRSLASQLEEiKLQVRKQ--KELGNGDIEGE 362
Cdd:TIGR02169 905 IeelEAQIEKKRKRLSELKA-KLEALEEelSEIEDPKGEDE 944
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
28-345 |
2.04e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 65.09 E-value: 2.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 28 DELEEATKNLQRAEDELLDLQDKVIQAEGSDSSTLAEIEVLRQRVLKIEGKDEEIKRAEDLCHTMKEKLEEEENLTRELK 107
Cdd:PRK03918 193 ELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELK 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 108 SEIERLQKRMVDLEKLEE------ALSRSKNEcsqlclSLNEERNLTK---KISSELEMLRVKVKELESSEDRLDKTEQS 178
Cdd:PRK03918 273 KEIEELEEKVKELKELKEkaeeyiKLSEFYEE------YLDELREIEKrlsRLEEEINGIEERIKELEEKEERLEELKKK 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 179 LvSELEKLKSLTLSFVNERKYLNEKEKENEKIIKELTQKLEQNKKMNRDHMRNASTFLERNDLRIEDGISStLSSKESKR 258
Cdd:PRK03918 347 L-KELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGE-LKKEIKEL 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 259 KGSLDYLKQVENET----RDKSENEKnrnqeDNKVKDLNQEIEKLKTQIKHFESLEEELKKmRAKNNDLQDNYLTELNRN 334
Cdd:PRK03918 425 KKAIEELKKAKGKCpvcgRELTEEHR-----KELLEEYTAELKRIEKELKEIEEKERKLRK-ELRELEKVLKKESELIKL 498
|
330
....*....|.
gi 119433663 335 RSLASQLEEIK 345
Cdd:PRK03918 499 KELAEQLKELE 509
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
14-314 |
2.31e-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: 2.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 14 RHLRFKLQSLSRRLDELEEATKNLQ----RAEDELLDLQDKVIQAEGSDSSTLAEIEVLRQRVLKIEGKDEEIKRAEDLC 89
Cdd:TIGR02169 670 RSEPAELQRLRERLEGLKRELSSLQselrRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSL 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 90 htmkekleeeENLTRELKSEIERLQKRmvdLEKLEEALSRSKNECSQLCLSLNEERnlTKKISSELEMLRVKVKELESSE 169
Cdd:TIGR02169 750 ----------EQEIENVKSELKELEAR---IEELEEDLHKLEEALNDLEARLSHSR--IPEIQAELSKLEEEVSRIEARL 814
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 170 DRLDKTEQSLVSELEKLKSLTLSFVNERKYLNEKEKENEKIIKELTQKLEqnkKMNRDhmrnastfLERNDLRIEDgiss 249
Cdd:TIGR02169 815 REIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKE---ELEEE--------LEELEAALRD---- 879
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119433663 250 tLSSKESKRKgsldylKQVENETRDKSENEKNRNQEDNKVKDLNQEIEKLKTQIkhfESLEEELK 314
Cdd:TIGR02169 880 -LESRLGDLK------KERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKL---EALEEELS 934
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
104-410 |
2.88e-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: 2.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 104 RELKSEIERLQKRM--VDLEKLEEALSRSKNECSQLCLSLNEERNLTKKISSELEMLRVKVKELESSEDRLDKTEQSLVS 181
Cdd:TIGR02168 216 KELKAELRELELALlvLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALAN 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 182 ELEKLKSLTLSFVNERKYLNEKEKENEKIIKELTQKLEQnkkmnrdhmrnastfLERNDLRIEDGISSTLSSKESkrkgs 261
Cdd:TIGR02168 296 EISRLEQQKQILRERLANLERQLEELEAQLEELESKLDE---------------LAEELAELEEKLEELKEELES----- 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 262 ldyLKQVENETRDKSENEKNRNQE-DNKVKDLNQEIEKLKTQIkhfESLEEELKKMRAKNNDLQDNYLTELNRNRSLASQ 340
Cdd:TIGR02168 356 ---LEAELEELEAELEELESRLEElEEQLETLRSKVAQLELQI---ASLNNEIERLEARLERLEDRRERLQQEIEELLKK 429
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 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 |
4.15e-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: 4.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 30 LEEATKNLQRAED---------ELLDLQDKV------IQAEGSDSSTLAEIEVLRQRVLKIEGKDEEIKRAEDLCHTMKE 94
Cdd:TIGR02168 181 LERTRENLDRLEDilnelerqlKSLERQAEKaerykeLKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTA 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 95 KLEEEENLTRELKSEIERLQKRMVDLEKLEEALSRSKNECSQLCLSLNEERnltKKISSELEMLRVKVKELESSEDRLDK 174
Cdd:TIGR02168 261 ELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERL---ANLERQLEELEAQLEELESKLDELAE 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 175 TEQSLVSELEKLKSLTLSFVNERKYLNEKEKENEKIIKELTQKLEQNKKmnrdhmRNASTFLERNDLRIEdgISSTLSSK 254
Cdd:TIGR02168 338 ELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRS------KVAQLELQIASLNNE--IERLEARL 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 255 ESKrKGSLDYLKQvENETRDKSENEKNRNQEDNKVKDLNQEIEKLKTQIKHFESLEEELKKMRAKNNDLQDNYLTELNRN 334
Cdd:TIGR02168 410 ERL-EDRRERLQQ-EIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQL 487
|
330
....*....|....*.
gi 119433663 335 RSLASQLEEIKLQVRK 350
Cdd:TIGR02168 488 QARLDSLERLQENLEG 503
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
25-371 |
2.58e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 61.49 E-value: 2.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 25 RRLDELEEatkNLQRAED---EL---LD-LQDKVIQAEgsDSSTLAEIEVLRQ---RVLKIEGKDEEIKRAEDlchtmke 94
Cdd:COG1196 179 RKLEATEE---NLERLEDilgELerqLEpLERQAEKAE--RYRELKEELKELEaelLLLKLRELEAELEELEA------- 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 95 kleeeenLTRELKSEIERLQKRmvdLEKLEEALSRSKNECSQLCLSLNE----ERNLTKKISSELEMLRVKVKELESSED 170
Cdd:COG1196 247 -------ELEELEAELEELEAE---LAELEAELEELRLELEELELELEEaqaeEYELLAELARLEQDIARLEERRRELEE 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 171 RLDKTEQSLVSELEKLKSLTlsfvNERKYLNEKEKENEKIIKELTQKLEQNKKMNRDHMRNASTfLERNDLRIEDGISST 250
Cdd:COG1196 317 RLEELEEELAELEEELEELE----EELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAE-AEEELEELAEELLEA 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 251 LSSKESKRKGSLDYLKQVENETRDKSENEKNRNQEDNKVKDLNQEIEKLKTQIKHFESLEEELKKMRAKNNDLQDNYLTE 330
Cdd:COG1196 392 LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEE 471
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 119433663 331 LNRNRSLASQLEEIKLQVRKQKELGNGDIEGEDAFLLGRGR 371
Cdd:COG1196 472 AALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKA 512
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
16-345 |
5.00e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 60.46 E-value: 5.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 16 LRFKLQSLSRRLDELEEATKNLQRAEDELLDLQDKVIQAEGsDSSTLAEIEVLRQRV--LKIEGKDEEIKRAEDLCHTMK 93
Cdd:PRK03918 319 LEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEE-RHELYEEAKAKKEELerLKKRLTGLTPEKLEKELEELE 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 94 EKLEEEENLTRELKSEIERLQKRMVDLEKLEEALSRSKNECSqLC---LSLNEERNLTKKISSELEMLRVKVKELESSED 170
Cdd:PRK03918 398 KAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCP-VCgreLTEEHRKELLEEYTAELKRIEKELKEIEEKER 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 171 RLDKTEQSLVSELEKLKSLTlsfvnerkylneKEKENEKIIKELTQKLeqnKKMNRDHMRNASTFLE--RNDLRIEDGIS 248
Cdd:PRK03918 477 KLRKELRELEKVLKKESELI------------KLKELAEQLKELEEKL---KKYNLEELEKKAEEYEklKEKLIKLKGEI 541
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 249 STLSSKESKRKGSLDYLKQVENETRDKSENEKNRNQEDNK-----VKDLNQEIE----------KLKTQIKHFESLEEEL 313
Cdd:PRK03918 542 KSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEElgfesVEELEERLKelepfyneylELKDAEKELEREEKEL 621
|
330 340 350
....*....|....*....|....*....|..
gi 119433663 314 KKMRAKNNDLQDNYLTELNRNRSLASQLEEIK 345
Cdd:PRK03918 622 KKLEEELDKAFEELAETEKRLEELRKELEELE 653
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
19-353 |
1.21e-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: 59.26 E-value: 1.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 19 KLQSLSRRLDELEEATKNLQRaedELLDLQDKVIQAEGSDSSTLAEIEVLRQRVLKIEGKdeeIKRAEDLCHTMKEKLEE 98
Cdd:TIGR04523 343 QISQLKKELTNSESENSEKQR---ELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESK---IQNQEKLNQQKDEQIKK 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 99 EENLTRELKSEIERLQKrmvDLEKLEEALSRSKNECSQLCLSLNEERNLTKKISSELEMLRVKVKELESSedrLDKTEQS 178
Cdd:TIGR04523 417 LQQEKELLEKEIERLKE---TIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQN---LEQKQKE 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 179 LVSELEKLKSLTlsfvNERKYLNEKEKENEKIIKELTQKLEQnkkmnrdhmrnastfLERNDLRIEDGISST----LSSK 254
Cdd:TIGR04523 491 LKSKEKELKKLN----EEKKELEEKVKDLTKKISSLKEKIEK---------------LESEKKEKESKISDLedelNKDD 551
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 255 ESKRKGSLDYLKQVENETRDKSENE-----KNRNQEDNKVKDLNQEIEKLKTQI----KHFESLEEELKKMRAKNNDLQD 325
Cdd:TIGR04523 552 FELKKENLEKEIDEKNKEIEELKQTqkslkKKQEEKQELIDQKEKEKKDLIKEIeekeKKISSLEKELEKAKKENEKLSS 631
|
330 340
....*....|....*....|....*...
gi 119433663 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 |
3.53e-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: 3.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 7 YKDAASNRHLRFKLQSLSRRLDELEEATKNLQRAEDELLDLQDKVIQAEGSDSSTLAEIEVLRQRVLKIEGKDEEIKRAe 86
Cdd:TIGR02168 218 LKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANE- 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 87 dlchtmkekleeeenlTRELKSEIERLQKRMVDLEKLEEALSRSKNECSQlclSLNEERNLTKKISSELEMLRVKVKELE 166
Cdd:TIGR02168 297 ----------------ISRLEQQKQILRERLANLERQLEELEAQLEELES---KLDELAEELAELEEKLEELKEELESLE 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 167 SSEDRLDKTEQSLVSELEKLKSLTLSFVNERKYLNEKEKENEKIIKELTQKLEQNKKMNRDHMRNASTFLERNDLRIEDG 246
Cdd:TIGR02168 358 AELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKE 437
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119433663 247 ISSTLsskESKRKGSLDYLKQVENETRDKSENEKNRNQEDNKVKDLNQEIEKLKTQIKHFESLEEELKK 315
Cdd:TIGR02168 438 LQAEL---EELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEG 503
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
16-334 |
5.84e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 57.46 E-value: 5.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 16 LRFKLQSLSRRLDELEEATKNLQRAeDELLDLQDKVIQAEGSDSSTLAEIEVLRqrvlkiegKDEEIKRAEDLCHTMKEK 95
Cdd:PTZ00121 1488 AKKKAEEAKKKADEAKKAAEAKKKA-DEAKKAEEAKKADEAKKAEEAKKADEAK--------KAEEKKKADELKKAEELK 1558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 96 LEEEENLTRELKSEIERlqkRMVDLEKLEEALSRSKNECSQLCLSLNEERNLTKKISSELEMLRVKVKELESSED----- 170
Cdd:PTZ00121 1559 KAEEKKKAEEAKKAEED---KNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEekkkv 1635
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 171 -RLDKTEQSLVSELEKLKSLTLSFVNERKYLNEKEKENEKIIKELTQKLEQNKKMNRDHMRNASTFLERNDLRI----ED 245
Cdd:PTZ00121 1636 eQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKkeaeEK 1715
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 246 GISSTLSSKESKRKGSLDYLKQVENETRDKSENEKNRNQEDNKVKDLNQEIEKLKTQIKHFES--LEEELKKMRAKNNDL 323
Cdd:PTZ00121 1716 KKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEavIEEELDEEDEKRRME 1795
|
330
....*....|.
gi 119433663 324 QDNYLTELNRN 334
Cdd:PTZ00121 1796 VDKKIKDIFDN 1806
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
19-198 |
3.13e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.39 E-value: 3.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 19 KLQSLSRRLDELEEATKNLQRAEDELLDLQDKVIQAEgsdsstlAEIEVLRQRVLKIEgkdeEIKRAEDLCHTMKEKLEE 98
Cdd:COG4717 72 ELKELEEELKEAEEKEEEYAELQEELEELEEELEELE-------AELEELREELEKLE----KLLQLLPLYQELEALEAE 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 99 EENLT---RELKSEIERLQKRMVDLEKLEEALSRSKNECSQLC--LSLNEERNLtKKISSELEMLRVKVKELESSEDRLD 173
Cdd:COG4717 141 LAELPerlEELEERLEELRELEEELEELEAELAELQEELEELLeqLSLATEEEL-QDLAEELEELQQRLAELEEELEEAQ 219
|
170 180
....*....|....*....|....*
gi 119433663 174 KTEQSLVSELEKLKSLTLSFVNERK 198
Cdd:COG4717 220 EELEELEEELEQLENELEAAALEER 244
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
105-354 |
3.55e-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: 54.26 E-value: 3.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 105 ELKSEIERLQKRMVDLEKLEEALSRSKNECSQLCLSLNEERNLTKKISSELEMLRVKVKELESSEDRLDKTEQSLVSELE 184
Cdd:TIGR04523 156 KLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIE 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 185 KLKS----LTLSFVNERKYLNEKEKENEKIIKELTQK---LEQNKKMNRDhmrnastfLERNDLRIEDGISSTlssKESK 257
Cdd:TIGR04523 236 KKQQeineKTTEISNTQTQLNQLKDEQNKIKKQLSEKqkeLEQNNKKIKE--------LEKQLNQLKSEISDL---NNQK 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 258 RKGSLDYLK-QVENETRDKSENEKNRNQEDNKVKDLNQEIEKLKTQIKHFESLEEELKK-MRAKNNDLQ------DNYLT 329
Cdd:TIGR04523 305 EQDWNKELKsELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQReLEEKQNEIEklkkenQSYKQ 384
|
250 260
....*....|....*....|....*
gi 119433663 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 |
4.97e-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: 54.21 E-value: 4.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 61 TLAEIEVLRQRVLKIEGKDEEIKRAEDlchtmKEKLEEEENLTRELKSEIERLQKRMVDLEKLEEALSRSKNECSQLCLS 140
Cdd:pfam02463 174 ALKKLIEETENLAELIIDLEELKLQEL-----KLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRD 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 141 LNEERNLTKKI---SSELEMLRVKVKELESSEDRLDKTEQSLVSELEKLKSLTLSFVNERKYLNEKEKENEKIIKELTQK 217
Cdd:pfam02463 249 EQEEIESSKQEiekEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEK 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 218 LEQNKKMNRDHMRNASTFLERNDLRIEDGISSTLSS--KESKRKGSLDYLKQVENETRDKSENEKN-----RNQEDNKVK 290
Cdd:pfam02463 329 ELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLqeKLEQLEEELLAKKKLESERLSSAAKLKEeelelKSEEEKEAQ 408
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119433663 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 |
5.69e-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: 5.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 3 ELTNYKDAAsnRHLRFKLQSLSRRLDELEE----ATKNLQRAEDELLDLQDKVIQAEGSDSSTLAEIEVLRQRVLKIEGK 78
Cdd:TIGR02168 706 ELEELEEEL--EQLRKELEELSRQISALRKdlarLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAE 783
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 79 ----DEEIKRAEDLCHTMKEKLEEEENLTRELKSEIERLQKRMVDLEKLEEALSRSKNECSQLCLSLNEERnltKKISSE 154
Cdd:TIGR02168 784 ieelEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDI---ESLAAE 860
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 155 LEMLRVKVKELESSEDRLDKTEQSLVSELEKLKSLTLSFVNERKYLNEKEKENEKIIKELTQKLEQnkkmnrdhmrnAST 234
Cdd:TIGR02168 861 IEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQ-----------LEL 929
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 235 FLERNDLRIeDGISSTLSSKESKrkgSLDYLKQVENETRDKSENEKNRnqednkVKDLNQEIEKLK----TQIKHFESLE 310
Cdd:TIGR02168 930 RLEGLEVRI-DNLQERLSEEYSL---TLEEAEALENKIEDDEEEARRR------LKRLENKIKELGpvnlAAIEEYEELK 999
|
330
....*....|....*
gi 119433663 311 EELKKMRAKNNDLQD 325
Cdd:TIGR02168 1000 ERYDFLTAQKEDLTE 1014
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
13-220 |
6.02e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 53.48 E-value: 6.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 13 NRHLRFKLQSLSRRLD----ELEEATKNLQRAEDELLDLQDK--VIQAEGSDSSTLAEIEVLRQRVLKIEgkdEEIKRAE 86
Cdd:COG3206 163 EQNLELRREEARKALEfleeQLPELRKELEEAEAALEEFRQKngLVDLSEEAKLLLQQLSELESQLAEAR---AELAEAE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 87 DLCHTMKEKLEEEENLTRELKS--EIERLQKRMVDLE-KLEEALSRSKNECSQLcLSLNEER-NLTKKISSELEMLRVkv 162
Cdd:COG3206 240 ARLAALRAQLGSGPDALPELLQspVIQQLRAQLAELEaELAELSARYTPNHPDV-IALRAQIaALRAQLQQEAQRILA-- 316
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119433663 163 kELESSEDRLDKTEQSLVSELEKLKSLTLSFVNERKYLNEKEKE---NEKIIKELTQKLEQ 220
Cdd:COG3206 317 -SLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREvevARELYESLLQRLEE 376
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
16-415 |
7.78e-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: 7.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 16 LRFKLQSLSRRLDELEEATKNLQRAEDELLDL---QDKVIQAEgsdsstLAEIEVLRQRVLKIEGKDEEIKRAEDLCHTM 92
Cdd:TIGR00606 700 LQSKLRLAPDKLKSTESELKKKEKRRDEMLGLapgRQSIIDLK------EKEIPELRNKLQKVNRDIQRLKNDIEEQETL 773
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 93 KEKLEEEENLTRELKSE---IERLQKRMVDLEKLEEALSrSKNECSQLCLSLNEERNLTKKISSELEMLRVKVKELESSE 169
Cdd:TIGR00606 774 LGTIMPEEESAKVCLTDvtiMERFQMELKDVERKIAQQA-AKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLI 852
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 170 DRLDKTEQSLVSELEKLKSLTLSFVNERKYLNEKEKENEKIIKELtQKLEQNKKMNRDHMRNASTFLERNDLRIEDGISS 249
Cdd:TIGR00606 853 QDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEV-QSLIREIKDAKEQDSPLETFLEKDQQEKEELISS 931
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 250 TLSSK----------ESKRKGSLDYLKQVENETRDKSENEKnrNQEDNKVKDLNQEIEKLKtqiKHFESLEEELKKMRaK 319
Cdd:TIGR00606 932 KETSNkkaqdkvndiKEKVKNIHGYMKDIENKIQDGKDDYL--KQKETELNTVNAQLEECE---KHQEKINEDMRLMR-Q 1005
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 320 NNDLQDNYLTELNRNRSLASQLEEIKlQVRKQKELGNGDIeGEDAFLLGRGRH----ERTKLKGHGSEASVSKHTSRELS 395
Cdd:TIGR00606 1006 DIDTQKIQERWLQDNLTLRKRENELK-EVEEELKQHLKEM-GQMQVLQMKQEHqkleENIDLIKRNHVLALGRQKGYEKE 1083
|
410 420
....*....|....*....|
gi 119433663 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 |
8.33e-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: 53.52 E-value: 8.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 80 EEIKRAEDLCHTMKEKLEeeenltrELKSEIERLQKRMVDLEKLEEALSRSKNECS-QLCLSLNEERNLTKKISSELEML 158
Cdd:TIGR02168 684 EKIEELEEKIAELEKALA-------ELRKELEELEEELEQLRKELEELSRQISALRkDLARLEAEVEQLEERIAQLSKEL 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 159 RVKVKELESSEDRLDKTEQSLVSELEKLKSLTLSFVNerkyLNEKEKENEKIIKELTQKLeQNKKMNRDHMRNASTFLER 238
Cdd:TIGR02168 757 TELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQ----LKEELKALREALDELRAEL-TLLNEEAANLRERLESLER 831
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 239 NDLRIEDGISSTLSSKESKRKGSLDYLKQVENETRDKSENEKNRNQEDNKVKDLNQEIEKLKtqiKHFESLEEELKKMRA 318
Cdd:TIGR02168 832 RIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLR---SELEELSEELRELES 908
|
250 260 270
....*....|....*....|....*....|....*
gi 119433663 319 KNNDLQDNYLTELNRNRSLASQLEEIKLQVRKQKE 353
Cdd:TIGR02168 909 KRSELRRELEELREKLAQLELRLEGLEVRIDNLQE 943
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
21-280 |
1.01e-06 |
|
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: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 21 QSLSRRLDELEEATKNLQR-AEDELLDLQDKVIQAEGSDSSTLAEIEVLRQRVlkiEGKDEEIKRAEDLCHtmkEKLEEE 99
Cdd:TIGR02169 265 KRLEEIEQLLEELNKKIKDlGEEEQLRVKEKIGELEAEIASLERSIAEKEREL---EDAEERLAKLEAEID---KLLAEI 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 100 ENLTRELKSEIERLQKRMVDLEKLEEALSRSKNECSQLCLSLNEERNLTKKISSELEMLRVKVKELESSEDRLDKTEQSL 179
Cdd:TIGR02169 339 EELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRL 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 180 VSELEKLKSLTLSFVNERKYLNEKEKENEKIIKELTQKLEQNKKMNRDHmrNASTFLERNDLRIedgISSTLSSKESKRK 259
Cdd:TIGR02169 419 SEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKY--EQELYDLKEEYDR---VEKELSKLQRELA 493
|
250 260
....*....|....*....|.
gi 119433663 260 GSLDYLKQVENETRDKSENEK 280
Cdd:TIGR02169 494 EAEAQARASEERVRGGRAVEE 514
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
64-322 |
1.12e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 53.22 E-value: 1.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 64 EIEVLRQRVLKIEGKDEEIKRAEDlchTMKEKLEEEENLTRELKSEIERLQKRMVDLEKLEEALSRSKNE---CSQLCLS 140
Cdd:PTZ00121 1634 KVEQLKKKEAEEKKKAEELKKAEE---ENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEakkAEELKKK 1710
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 141 LNEERNLTKKISSELEMLRVKVKELESSEDRLDKTEQSLVSELEKLKSLTLSFVNERKYLNEKEKENEKIIKELTQKLEQ 220
Cdd:PTZ00121 1711 EAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDE 1790
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 221 NKKMNRDhmRNASTFLERNDLRIEDGISSTL---SSKE---SKRKGSLDYLKQVENETRDKSENEKNRNQEDNKVKDLNQ 294
Cdd:PTZ00121 1791 KRRMEVD--KKIKDIFDNFANIIEGGKEGNLvinDSKEmedSAIKEVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEA 1868
|
250 260
....*....|....*....|....*...
gi 119433663 295 EIEKLKTQIKHFESLEEELKKMRAKNND 322
Cdd:PTZ00121 1869 DFNKEKDLKEDDEEEIEEADEIEKIDKD 1896
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
19-323 |
2.30e-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: 2.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 19 KLQSLSRRLDELEEATKNLQRAEDELLDLQDKVIQAEGSDSSTLAEIEVLRQRVLKIEGKDEEIKRAEDLCHTMKEKLEE 98
Cdd:pfam02463 723 LADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEE 802
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 99 EENLTRELKSEIERLQKRMVDLEKLEEALSRSKNECSQLCL-SLNEERNLTKKISSELEMLRVKVKELESSEDRLDKTEQ 177
Cdd:pfam02463 803 LRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKeEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQ 882
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 178 SLVSELEK-----------LKSLTLSFVNERKYLNEKEKENEKIIKELTQKLEQNKKMnRDHMRNASTFLERNDLRIEDG 246
Cdd:pfam02463 883 KLKDELESkeekekeekkeLEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEEL-LLEEADEKEKEENNKEEEEER 961
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119433663 247 ISSTLSSKESKRKGSLDYLKQVENETRDKSENEKNRNQEDNKVKDLNQEIEKLKTQIKhfeslEEELKKMRAKNNDL 323
Cdd:pfam02463 962 NKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRL-----KEFLELFVSINKGW 1033
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
137-354 |
2.57e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.92 E-value: 2.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 137 LCLSLNEERNLTKKISSELEMLRVKVKELESSEDRLDKTEQSLVSELEKLK---SLTLSFVN----ERKYLNEKEKENEK 209
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALErriAALARRIRaleqELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 210 IIKELTQKLEQNKKMNRDHMRNASTFLERNDLRIedgISSTLSSKESKRkgSLDYLKQVENETRDKSENEKNRNQEDNKV 289
Cdd:COG4942 91 EIAELRAELEAQKEELAELLRALYRLGRQPPLAL---LLSPEDFLDAVR--RLQYLKYLAPARREQAEELRADLAELAAL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119433663 290 K-DLNQEIEKLKTQIKHFESLEEELKKMRAKNNDLqdnyLTELNRNrsLASQLEEIKLQVRKQKEL 354
Cdd:COG4942 166 RaELEAERAELEALLAELEEERAALEALKAERQKL----LARLEKE--LAELAAELAELQQEAEEL 225
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2-349 |
3.54e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 51.19 E-value: 3.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 2 AELTNYKDAASNRhlRFKLQSLSRRLDELEEATKN----LQRAEDELLDLQDKVIQAEGSDSSTLAEIEVLRQRV----- 72
Cdd:PRK02224 370 SELEEAREAVEDR--REEIEELEEEIEELRERFGDapvdLGNAEDFLEELREERDELREREAELEATLRTARERVeeaea 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 73 LKIEGK---------DEEIKRAEDLCHTMKEKLEEEENLTRELKSEIERLQKRMVDLEKLEEALSRSKNECSQLCLSLNE 143
Cdd:PRK02224 448 LLEAGKcpecgqpveGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEERREDLEELIAE 527
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 144 ERNLTKKISSELEMLRVKVKELESSEDRLDKTEQSLVSELEKLKSLTLSFVNERKYLNEKEKENEKI------------- 210
Cdd:PRK02224 528 RRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIrtllaaiadaede 607
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 211 IKELTQKLEQNKKMNRDHMRNASTFLERNDLRIEDGISSTLSSKESKRKGSLDYLKQVENETRDKSEneknrnQEDnkvk 290
Cdd:PRK02224 608 IERLREKREALAELNDERRERLAEKRERKRELEAEFDEARIEEAREDKERAEEYLEQVEEKLDELRE------ERD---- 677
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 119433663 291 DLNQEIEKLKTQIKHFESLEEELKKMRAKNNDLQDNYltelnrnrSLASQLEEIKLQVR 349
Cdd:PRK02224 678 DLQAEIGAVENELEELEELRERREALENRVEALEALY--------DEAEELESMYGDLR 728
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
19-223 |
4.68e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 49.15 E-value: 4.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 19 KLQSLSRRLDELEEATKNLQRaedELLDLQDKVIQAEgsdsstlAEIEVLRQRVLKIEgkdEEIKRAEdlchtmkeklee 98
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPA---ELAELEDELAALE-------ARLEAAKTELEDLE---KEIKRLE------------ 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 99 eenltrelkSEIERLQKRmvdLEKLEEALSRSKNecsqlclslNEERnltKKISSELEMLRVKVKELESSEDRLDKTEQS 178
Cdd:COG1579 66 ---------LEIEEVEAR---IKKYEEQLGNVRN---------NKEY---EALQKEIESLKRRISDLEDEILELMERIEE 121
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 119433663 179 LVSELEKLKSLtlsFVNERKYLNEKEKENEKIIKELTQKLEQNKK 223
Cdd:COG1579 122 LEEELAELEAE---LAELEAELEEKKAELDEELAELEAELEELEA 163
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
19-214 |
1.36e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 49.29 E-value: 1.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 19 KLQSLSRRLDELEEATKNLQRAEDELLD-LQDKVIQAEGSDSSTLAEIEVLRQRVLKIEGKDEEIKRAEDLCHTMKEKLE 97
Cdd:PRK03918 550 KLEELKKKLAELEKKLDELEEELAELLKeLEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELD 629
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 98 EEENLTRELKSEIERLQKRmvdLEKLEEALSRSKNEcsqlclslnEERNLTKKISSELEMLRVKVKELESSEDRLDKTeq 177
Cdd:PRK03918 630 KAFEELAETEKRLEELRKE---LEELEKKYSEEEYE---------ELREEYLELSRELAGLRAELEELEKRREEIKKT-- 695
|
170 180 190
....*....|....*....|....*....|....*..
gi 119433663 178 slvseLEKLKsltlsfvNERKYLNEKEKENEKIIKEL 214
Cdd:PRK03918 696 -----LEKLK-------EELEEREKAKKELEKLEKAL 720
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
19-353 |
1.42e-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: 1.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 19 KLQSLSRRLDELEEATKNLQRAEDELLDLQDKV-IQAEGSDSSTLAEIEVLRQRVLKIE----GKDEEIKRAEDLCHTMK 93
Cdd:TIGR00606 320 ELVDCQRELEKLNKERRLLNQEKTELLVEQGRLqLQADRHQEHIRARDSLIQSLATRLEldgfERGPFSERQIKNFHTLV 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 94 EKLEEEENLTrelkseIERLQKRMVDLEKL-EEALSRSKNECSQLCLSLNEERNLTKKISSELEMLRVKVKELESSEDRL 172
Cdd:TIGR00606 400 IERQEDEAKT------AAQLCADLQSKERLkQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRI 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 173 DKTEQSLVSELEKL-----KSLTLSFVNERKYLNEKEKENEKIIKELTQKLEQ--NKKMNRDHMRNASTFLERNDLRIED 245
Cdd:TIGR00606 474 LELDQELRKAERELskaekNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQlnHHTTTRTQMEMLTKDKMDKDEQIRK 553
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 246 gISSTLSSKESKRKGSLDYLKQVENETRDKSeneKNRNQEDNKVKDLNQEIEKLKTQIKHFeslEEELKKMRAKNNDLQD 325
Cdd:TIGR00606 554 -IKSRHSDELTSLLGYFPNKKQLEDWLHSKS---KEINQTRDRLAKLNKELASLEQNKNHI---NNELESKEEQLSSYED 626
|
330 340
....*....|....*....|....*...
gi 119433663 326 NyLTELNRNRSLASQLEEIKLQVRKQKE 353
Cdd:TIGR00606 627 K-LFDVCGSQDEESDLERLKEEIEKSSK 653
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
105-324 |
1.56e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 47.98 E-value: 1.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 105 ELKSEIERLQKRmvdLEKLEEALSRSKNECSQLCLSLNEERNLTKKISSELEMLRVKVKELESSEDRLDKTEQSLVSELE 184
Cdd:COG1340 19 ELREEIEELKEK---RDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELREELD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 185 KLKSLTLSFVNERKYLNEKEKENEKI--------------------IKELTQKLEQNKKMNRDHMRNASTFLERNDLRIE 244
Cdd:COG1340 96 ELRKELAELNKAGGSIDKLRKEIERLewrqqtevlspeeekelvekIKELEKELEKAKKALEKNEKLKELRAELKELRKE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 245 -DGIS---STLSSKESKRKGSLDYLKQVENETRDKSENEKNRNQE-DNKVKDLNQEIEKLKTQIKhfeSLEEELKKMRAK 319
Cdd:COG1340 176 aEEIHkkiKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEaQEKADELHEEIIELQKELR---ELRKELKKLRKK 252
|
....*
gi 119433663 320 NNDLQ 324
Cdd:COG1340 253 QRALK 257
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1-299 |
1.85e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 48.36 E-value: 1.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 1 MAELTNYKDAASNRHLRFKLQSLSRRLDELEEATKNLQRAEDELLDLQDKVIQAEgsdsstlAEIEVLRQRVLKIEgkdE 80
Cdd:COG4372 18 LRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQAR-------SELEQLEEELEELN---E 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 81 EIKRAEDLCHTMKEKLEEEENLTRELKSEIERLQKRMVDLEKLEEALSRSKnecSQLCLSLNEERNLTKKISSELEMLRV 160
Cdd:COG4372 88 QLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQI---AELQSEIAEREEELKELEEQLESLQE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 161 KVKELESSEDRLDKTEqsLVSELEKLKSLTLSFVNERKYLNEKEKENEKIIKELTQKLEQNKKMNRDHMRNASTFLERND 240
Cdd:COG4372 165 ELAALEQELQALSEAE--AEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDAL 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 119433663 241 LRIEDGISSTLSSKESKRKGSLDYLKQVENETRDKSENEKNRNQEDNKVKDLNQEIEKL 299
Cdd:COG4372 243 ELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALL 301
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
106-359 |
2.12e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 48.74 E-value: 2.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 106 LKSEIERLQKRMVDLEKLEEALSRSKNECSQLCLSLNEERNLTKKISSELEMLRVKVKELESSEDRLDKTEQSLVSELEK 185
Cdd:PRK01156 171 LKDVIDMLRAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDM 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 186 LKSLTLSFVNERKYLNEKEKENEKI--IKELTQKLEQNKKM-NRDHMRNasTFLERNDLRIEDGISSTLSSKESKRKGSL 262
Cdd:PRK01156 251 KNRYESEIKTAESDLSMELEKNNYYkeLEERHMKIINDPVYkNRNYIND--YFKYKNDIENKKQILSNIDAEINKYHAII 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 263 DYLKQVENETRDKSENEKNRNQEDNKVKDLNQEIEKLKTQIKHFESLEEELKKMRAKNNDLQDNYLTELNRNRSLASQLE 342
Cdd:PRK01156 329 KKLSVLQKDYNDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIK 408
|
250
....*....|....*..
gi 119433663 343 EIKLQVRKQKELGNGDI 359
Cdd:PRK01156 409 KELNEINVKLQDISSKV 425
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
109-342 |
2.27e-05 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 48.39 E-value: 2.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 109 EIERLqKRMVDLEKLEEALSRSkNECSQLCLSLNEERNLTKKISSELEmlRVKVKELESSEDRLDKTEQSLVSELEKLks 188
Cdd:PRK05771 32 HIEDL-KEELSNERLRKLRSLL-TKLSEALDKLRSYLPKLNPLREEKK--KVSVKSLEELIKDVEEELEKIEKEIKEL-- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 189 ltlsfVNERKYLNEKEKENEKIIKELTQ--------KLEQNKKmnrdhmrNASTFLERNDLRIEDGISSTLSSK----ES 256
Cdd:PRK05771 106 -----EEEISELENEIKELEQEIERLEPwgnfdldlSLLLGFK-------YVSVFVGTVPEDKLEELKLESDVEnveyIS 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 257 KRKGSLDYLKQVENETRDKSENE--KN--RNQEDNKVKDLNQEIEKLKTQI----KHFESLEEELKKMRAKNNDL---QD 325
Cdd:PRK05771 174 TDKGYVYVVVVVLKELSDEVEEElkKLgfERLELEEEGTPSELIREIKEELeeieKERESLLEELKELAKKYLEEllaLY 253
|
250
....*....|....*...
gi 119433663 326 NYL-TELNRNRSLASQLE 342
Cdd:PRK05771 254 EYLeIELERAEALSKFLK 271
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
14-319 |
2.61e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.52 E-value: 2.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 14 RHLRFKLQSLSRRLDELEEATKNLQRAED-------ELLDLQDKVIQAEGSdsstlAEIEVLRQRVLKIEGKDEEIK-RA 85
Cdd:PRK03918 408 SKITARIGELKKEIKELKKAIEELKKAKGkcpvcgrELTEEHRKELLEEYT-----AELKRIEKELKEIEEKERKLRkEL 482
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 86 EDLCHTMKEKLEEEENLT-----RELKSE-----IERLQKRMVDLEKLEEALSRSKNECSQLCLSLNEERNLTKKIS--- 152
Cdd:PRK03918 483 RELEKVLKKESELIKLKElaeqlKELEEKlkkynLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAele 562
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 153 ----------------------SELEMLRVKVKELESSEDR---LDKTEQSLVSELEKLKSLTLSFVNERKYLNEKEKEN 207
Cdd:PRK03918 563 kkldeleeelaellkeleelgfESVEELEERLKELEPFYNEyleLKDAEKELEREEKELKKLEEELDKAFEELAETEKRL 642
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 208 EKIIKELTqklEQNKKMNRDHMRNASTFLERndlriedgISSTLSSKESKRKGSLDYLKQVENETRDKSENEKNRnqedn 287
Cdd:PRK03918 643 EELRKELE---ELEKKYSEEEYEELREEYLE--------LSRELAGLRAELEELEKRREEIKKTLEKLKEELEER----- 706
|
330 340 350
....*....|....*....|....*....|..
gi 119433663 288 kvKDLNQEIEKLKTQIKHFESLEEELKKMRAK 319
Cdd:PRK03918 707 --EKAKKELEKLEKALERVEELREKVKKYKAL 736
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
14-185 |
2.83e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 46.84 E-value: 2.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 14 RHLRFKLQSLSRRLDELEE----ATKNLQRAEDELLDLQDKVIQAEgsdsstlAEIEVLRQRVLKIEGKDEEIKRAEDLc 89
Cdd:COG1579 20 DRLEHRLKELPAELAELEDelaaLEARLEAAKTELEDLEKEIKRLE-------LEIEEVEARIKKYEEQLGNVRNNKEY- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 90 htmkekleeeenltRELKSEIERLQKRMVDLEK----LEEALSRSKNECSQLclsLNEERNLTKKISSELEMLRVKVKEL 165
Cdd:COG1579 92 --------------EALQKEIESLKRRISDLEDeileLMERIEELEEELAEL---EAELAELEAELEEKKAELDEELAEL 154
|
170 180
....*....|....*....|
gi 119433663 166 ESSEDRLDKTEQSLVSELEK 185
Cdd:COG1579 155 EAELEELEAEREELAAKIPP 174
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
68-354 |
3.97e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 47.81 E-value: 3.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 68 LRQRVLKIEGKDEEIKRAEDLchtmkekleeeenlTRELKSEIERLQKRMVDLEKLEEALSRSKNECSQLCLSLNEERNL 147
Cdd:pfam15921 446 MERQMAAIQGKNESLEKVSSL--------------TAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERA 511
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 148 TKKISSELEMLRVKVkELESSEdrldktEQSLVSELEKLKSLTlsfvNERKYLNEKEKENEKIIKELTQKLEQNKKMNRD 227
Cdd:pfam15921 512 IEATNAEITKLRSRV-DLKLQE------LQHLKNEGDHLRNVQ----TECEALKLQMAEKDKVIEILRQQIENMTQLVGQ 580
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 228 HMRNASTFL--------ERNDLRIEDGISSTLSSKESKRKGSLDylKQVENETRDKSENEKNRNQEDNKVKDLNQEIEKL 299
Cdd:pfam15921 581 HGRTAGAMQvekaqlekEINDRRLELQEFKILKDKKDAKIRELE--ARVSDLELEKVKLVNAGSERLRAVKDIKQERDQL 658
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 119433663 300 KTQIKHFESleeELKKMRAKNNDLQDNYlteLNRNRSLASQLEEIKLQVRK-QKEL 354
Cdd:pfam15921 659 LNEVKTSRN---ELNSLSEDYEVLKRNF---RNKSEEMETTTNKLKMQLKSaQSEL 708
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
82-356 |
4.57e-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: 4.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 82 IKRAEDLCHTMKEKLEEEENLTRELKSEIE-RLQKRMvdLEKLEEALSRSKNecsqlclSLNEERNLTKKISSELEMLRV 160
Cdd:TIGR01612 502 MKDFKDIIDFMELYKPDEVPSKNIIGFDIDqNIKAKL--YKEIEAGLKESYE-------LAKNWKKLIHEIKKELEEENE 572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 161 KVKELESSEDRLDKTEQSLVSELEKLKSLTLSFVNERKYLNEKekeNEKIIKELT-QKLEQNKKMNRDHMRNASTFLERN 239
Cdd:TIGR01612 573 DSIHLEKEIKDLFDKYLEIDDEIIYINKLKLELKEKIKNISDK---NEYIKKAIDlKKIIENNNAYIDELAKISPYQVPE 649
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 240 DLRIEDGISSTLSSKESK-RKGSLDYLKqveNETRD-KSENEKNRNQEDNKVKDLNQEIEKLKTQIKHFE--SLEEELKK 315
Cdd:TIGR01612 650 HLKNKDKIYSTIKSELSKiYEDDIDALY---NELSSiVKENAIDNTEDKAKLDDLKSKIDKEYDKIQNMEtaTVELHLSN 726
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 119433663 316 MRAKNNDLQDNyLTELNR------NRSLASQLEEIKlqvRKQKELGN 356
Cdd:TIGR01612 727 IENKKNELLDI-IVEIKKhihgeiNKDLNKILEDFK---NKEKELSN 769
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
16-353 |
5.21e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 47.42 E-value: 5.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 16 LRFKLQSLSRRLDELEEATKNLQRAEDELLD-LQDKVIQAEGS---------DSSTlaEIEVLRQRVLKIEGKDEEIKR- 84
Cdd:pfam15921 115 LQTKLQEMQMERDAMADIRRRESQSQEDLRNqLQNTVHELEAAkclkedmleDSNT--QIEQLRKMMLSHEGVLQEIRSi 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 85 -------------AEDLCHTM--KEKLEEEENLTRELKSEIERLQKRMVDLEKLEEAL-SRSKNECSQLclsLNEERNLT 148
Cdd:pfam15921 193 lvdfeeasgkkiyEHDSMSTMhfRSLGSAISKILRELDTEISYLKGRIFPVEDQLEALkSESQNKIELL---LQQHQDRI 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 149 KKISSELEmlrVKVKELESSEDRLDKTEQSLVSELEKLKSLTLsfvNERKYLNEKEKENEKIIKELTQKLEQNKKMNRDH 228
Cdd:pfam15921 270 EQLISEHE---VEITGLTEKASSARSQANSIQSQLEIIQEQAR---NQNSMYMRQLSDLESTVSQLRSELREAKRMYEDK 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 229 MRNastfLERNDLRIEDGISSTLSSKE--SKRKGSLDYLKQVENETRDKSENEKNRNQEDNK------------------ 288
Cdd:pfam15921 344 IEE----LEKQLVLANSELTEARTERDqfSQESGNLDDQLQKLLADLHKREKELSLEKEQNKrlwdrdtgnsitidhlrr 419
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119433663 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 ... |
62-349 |
6.05e-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: 6.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 62 LAEIEVLRQRVLKIEGKDEEIK---------RAEDLCHTMKEKLEEEENLT------RELKSEIERLQKRMVDLEKLEEA 126
Cdd:TIGR02169 176 LEELEEVEENIERLDLIIDEKRqqlerlrreREKAERYQALLKEKREYEGYellkekEALERQKEAIERQLASLEEELEK 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 127 LSRSKNECSQLCLSLNEERN-LTKKIS--SELEMLRVKVK--ELESSEDRLDKTEQSLVSELEKL-KSLTLSFVNERKYL 200
Cdd:TIGR02169 256 LTEEISELEKRLEEIEQLLEeLNKKIKdlGEEEQLRVKEKigELEAEIASLERSIAEKERELEDAeERLAKLEAEIDKLL 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 201 NEKEKENEKIikeLTQKLEQNKKMNRDHMRNASTFLERNDLRIEDGISSTLSSKESKRKGSLDYLKQVENE---TRDKSE 277
Cdd:TIGR02169 336 AEIEELEREI---EEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINElkrELDRLQ 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 278 NEKNRNQEdnKVKDLNQEIEKLKTQIKHFES-----------LEEELKKMRAKNNDLQDNYL---TELN----RNRSLAS 339
Cdd:TIGR02169 413 EELQRLSE--ELADLNAAIAGIEAKINELEEekedkaleikkQEWKLEQLAADLSKYEQELYdlkEEYDrvekELSKLQR 490
|
330
....*....|
gi 119433663 340 QLEEIKLQVR 349
Cdd:TIGR02169 491 ELAEAEAQAR 500
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
20-353 |
6.33e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 47.20 E-value: 6.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 20 LQSLSRRLDELEEATKNLQRAEDELLDLQDKVIQAEGSDSSTLAEIEVLRQRVLKIEGKDEEIKRAEDLCHTMKEKLEEE 99
Cdd:PRK01156 175 IDMLRAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRY 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 100 ENLTRELKSEIERLQKRMVDLEKLEEALSRSKNecSQLCLSLNEER---NLTKKISSELEMLRVKVKELESSEDRLDKTE 176
Cdd:PRK01156 255 ESEIKTAESDLSMELEKNNYYKELEERHMKIIN--DPVYKNRNYINdyfKYKNDIENKKQILSNIDAEINKYHAIIKKLS 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 177 --QSLVSELEKLKSLTLSFVNERKYLNEKEKENEKIIKELTQ---KLEQNKKMNRDHMRNASTFLERNDL------RIED 245
Cdd:PRK01156 333 vlQKDYNDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESlkkKIEEYSKNIERMSAFISEILKIQEIdpdaikKELN 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 246 GISSTL---SSKESKRKGSLDYLKQVENETRDKSE-------------------NEKNRNQEDNKVKDLNQEIEKLKTQI 303
Cdd:PRK01156 413 EINVKLqdiSSKVSSLNQRIRALRENLDELSRNMEmlngqsvcpvcgttlgeekSNHIINHYNEKKSRLEEKIREIEIEV 492
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 119433663 304 KHFESLEEELKKMRAKNNDLQDN-YLTELNRNRSLASQLEEIKLQVRKQKE 353
Cdd:PRK01156 493 KDIDEKIVDLKKRKEYLESEEINkSINEYNKIESARADLEDIKIKINELKD 543
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
103-363 |
8.43e-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: 8.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 103 TRELKSEIERLQKRMVDLEKLEEALSRSKNECSQLCLSLNEER------NLTKKISSELEMLRV--KVKELESSEDRLDK 174
Cdd:pfam02463 165 SRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKkaleyyQLKEKLELEEEYLLYldYLKLNEERIDLLQE 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 175 TEQSLVSELEKLKSL------TLSFVNERKYLNEKEKENEKIIKELTQKLEQNKKMNRDHMRNASTFLERNDLRIEDGIS 248
Cdd:pfam02463 245 LLRDEQEEIESSKQEiekeeeKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKK 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 249 STLSSKESKRKGSLDYLKQVENETRDKSENE-KNRNQEDNKVKDLNQEIEKLKTQIKHFESLEEELKKmRAKNNDLQDNY 327
Cdd:pfam02463 325 KAEKELKKEKEEIEELEKELKELEIKREAEEeEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKL-KEEELELKSEE 403
|
250 260 270
....*....|....*....|....*....|....*.
gi 119433663 328 LTELNRNRSLASQLEEIkLQVRKQKELGNGDIEGED 363
Cdd:pfam02463 404 EKEAQLLLELARQLEDL-LKEEKKEELEILEEEEES 438
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
15-238 |
1.04e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.45 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 15 HLRFKLQSLSRRLDELEEATKNLQRAEDELLDLQDkviqaegsdssTLAEIEVLRQRVLKIEGKDEEIkraedlchtmke 94
Cdd:COG4913 614 ALEAELAELEEELAEAEERLEALEAELDALQERRE-----------ALQRLAEYSWDEIDVASAEREI------------ 670
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 95 kleeeenltRELKSEIERLQKRMVDLEKLEEALSRSKNECSQlclsLNEERNLTKKISSELEmlrvkvKELESSEDRLDK 174
Cdd:COG4913 671 ---------AELEAELERLDASSDDLAALEEQLEELEAELEE----LEEELDELKGEIGRLE------KELEQAEEELDE 731
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119433663 175 TeQSLVSELEKLKSLTLSFVNERKYLNEKEKENEkiiKELTQKLEQNKKMNRDHMRNASTFLER 238
Cdd:COG4913 732 L-QDRLEAAEDLARLELRALLEERFAAALGDAVE---RELRENLEERIDALRARLNRAEEELER 791
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
27-332 |
1.29e-04 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 46.36 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 27 LDELEEATKNLQRAEDELLDLQDKVIQAEGSDSST--LAEIEVLRQRvlkIEGKDEEIKRAEDLCHTMkekleeeenltr 104
Cdd:PTZ00440 690 IKNLKKELQNLLSLKENIIKKQLNNIEQDISNSLNqyTIKYNDLKSS---IEEYKEEEEKLEVYKHQI------------ 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 105 elkseIERLQKRMVDLEKLEEALSRSKNECSQLCLSLNEERNLTKKISSELEMLRVKVK----ELESSEDRLDKTEQSLV 180
Cdd:PTZ00440 755 -----INRKNEFILHLYENDKDLPDGKNTYEEFLQYKDTILNKENKISNDINILKENKKnnqdLLNSYNILIQKLEAHTE 829
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 181 SELEKLKSLTLSFVNERKYLNEKEKENE-----KIIKELTQKLEQ-NKKMNRDHMRNASTFLERNDLRIedgISSTLSSK 254
Cdd:PTZ00440 830 KNDEELKQLLQKFPTEDENLNLKELEKEfnennQIVDNIIKDIENmNKNINIIKTLNIAINRSNSNKQL---VEHLLNNK 906
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 255 ESKRKGSLDYLKQVENET----RDKSENEKNRNQEDNKV-KDLNQE-IEKLKTQIkhfESLEEELKKMRAKNNDLQDNYL 328
Cdd:PTZ00440 907 IDLKNKLEQHMKIINTDNiiqkNEKLNLLNNLNKEKEKIeKQLSDTkINNLKMQI---EKTLEYYDKSKENINGNDGTHL 983
|
....
gi 119433663 329 TELN 332
Cdd:PTZ00440 984 EKLD 987
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
19-188 |
2.10e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.68 E-value: 2.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 19 KLQSLSRRLDELEEAtknLQRAEDELLDLQDKVIQAEgsdsstlAEIEVLRQRVLKIEGKDEEikraedlchtmkeklee 98
Cdd:COG4913 289 RLELLEAELEELRAE---LARLEAELERLEARLDALR-------EELDELEAQIRGNGGDRLE----------------- 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 99 eenltrELKSEIERLQKRmvdLEKLEEALSRSKNECSQLCLSLNEE-----------RNLTKKISSELEMLRVKVKELES 167
Cdd:COG4913 342 ------QLEREIERLERE---LEERERRRARLEALLAALGLPLPASaeefaalraeaAALLEALEEELEALEEALAEAEA 412
|
170 180
....*....|....*....|.
gi 119433663 168 SEDRLDKTEQSLVSELEKLKS 188
Cdd:COG4913 413 ALRDLRRELRELEAEIASLER 433
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
79-345 |
2.34e-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: 2.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 79 DEEIKRAEDLCHTMKEKLEEEENLTRELKSEIERLQKRMVDLEKLEeALSRSKNECSQLCLSLNEERNLT--KKISSELE 156
Cdd:TIGR02169 169 DRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQ-ALLKEKREYEGYELLKEKEALERqkEAIERQLA 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 157 MLRvkvKELESSEDRLDKTEQSLVSELEKLKSLT--LSFVNERKYLNEKEKenekiIKELTQKLEQNKKMNRDHMRNAST 234
Cdd:TIGR02169 248 SLE---EELEKLTEEISELEKRLEEIEQLLEELNkkIKDLGEEEQLRVKEK-----IGELEAEIASLERSIAEKERELED 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 235 fLERNDLRIEDGISSTLSSKESKRKGSLDYLKQVENETrdkSENEKNRNQEDNKVKDLNQEIEKLKTQIKHFESLEEELK 314
Cdd:TIGR02169 320 -AEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLT---EEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLE 395
|
250 260 270
....*....|....*....|....*....|.
gi 119433663 315 KMRAKNNDLQDNYLTELNRNRSLASQLEEIK 345
Cdd:TIGR02169 396 KLKREINELKRELDRLQEELQRLSEELADLN 426
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
121-353 |
2.66e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 45.01 E-value: 2.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 121 EKLEEALSRSKNECSQLCLSL-NEERNLTKKISsELEMLRVKVKELESSEDRLDKTEQSLVSELEKLKSLTLSFVNERKY 199
Cdd:TIGR04523 36 KQLEKKLKTIKNELKNKEKELkNLDKNLNKDEE-KINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKN 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 200 LNEKEKENEKIIKELTQKLEQNKKmnrdhmrNASTFLerNDLRIEDGISSTLSSKES---KRKGSL-DYLKQVENETRDK 275
Cdd:TIGR04523 115 DKEQKNKLEVELNKLEKQKKENKK-------NIDKFL--TEIKKKEKELEKLNNKYNdlkKQKEELeNELNLLEKEKLNI 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119433663 276 SENEKNRNQEDNKvkdLNQEIEKLKTQIKHFESLEEELKKMRAKNNDLQDNYLTELNRNRSLASQLEEIKLQVRKQKE 353
Cdd:TIGR04523 186 QKNIDKIKNKLLK---LELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKD 260
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
16-366 |
3.21e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 44.71 E-value: 3.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 16 LRFKLQSLSRRLDELE-EATKNLQRAEDELLDLQDKVIQAEGSDSSTLAEIEVLRQRVLKIEGK----DEEIKRAEDLCH 90
Cdd:pfam05483 213 MHFKLKEDHEKIQHLEeEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKtklqDENLKELIEKKD 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 91 TMkekleeeenlTRELKSEIERLQKRMVDLEKLEEALSRSKNECSQLC-------LSLNEERNLTKKISSEL-------- 155
Cdd:pfam05483 293 HL----------TKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTeekeaqmEELNKAKAAHSFVVTEFeattcsle 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 156 EMLRVKVKELESSEDRLDKTEQSLVSELEKLKSLTlsfvnerKYLNEKEKENEKIIKELTQK---LEQNKKMNRdhmrna 232
Cdd:pfam05483 363 ELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMT-------KFKNNKEVELEELKKILAEDeklLDEKKQFEK------ 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 233 stflerndlriedgISSTLSSKESKRKGSLdylkqvenETRDKseneknrnqednKVKDLNQEIEKLKTQIKHF----ES 308
Cdd:pfam05483 430 --------------IAEELKGKEQELIFLL--------QAREK------------EIHDLEIQLTAIKTSEEHYlkevED 475
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 119433663 309 LEEELKKMRAKNNDLQDNYLTELNRNRSLASQLEEIKLQVRKQKELGNGDIEGEDAFL 366
Cdd:pfam05483 476 LKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERML 533
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
29-360 |
3.46e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 44.89 E-value: 3.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 29 ELEEATKNLQRAEDELLDLQDKVIQAEGSDSSTLAEIEVLR-QRVLKIEGKDEEIKRAEDLCHTMKEKLEEEENLTRELK 107
Cdd:PRK01156 410 ELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNgQSVCPVCGTTLGEEKSNHIINHYNEKKSRLEEKIREIE 489
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 108 SEIERLQKRMVDLEKLEEALSRSKNEcsqlclSLNEERNLTKKISSELEMLRVKVKELESSEDRLDKTEQSLVS-ELEKL 186
Cdd:PRK01156 490 IEVKDIDEKIVDLKKRKEYLESEEIN------KSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRYKSlKLEDL 563
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 187 KSLTLSFVNERKYLNEKEKENEKiikelTQKLEQNKKMNRdhmrnastfLERNDLRIEDGISSTLSSKESkrkgsldYLK 266
Cdd:PRK01156 564 DSKRTSWLNALAVISLIDIETNR-----SRSNEIKKQLND---------LESRLQEIEIGFPDDKSYIDK-------SIR 622
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 267 QVENETRDkSENEKNRNQEDNKVKD-LNQEIEKLKTQIKHFESLEEELKKMRAKNNDLQDNY------LTELNRNRSLAS 339
Cdd:PRK01156 623 EIENEANN-LNNKYNEIQENKILIEkLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLkksrkaLDDAKANRARLE 701
|
330 340
....*....|....*....|.
gi 119433663 340 QLEEIKLQVRKQKELGNGDIE 360
Cdd:PRK01156 702 STIEILRTRINELSDRINDIN 722
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
113-224 |
3.56e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 44.46 E-value: 3.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 113 LQKRMVDLEKLEEALSRSKNECSQLCLSLNEERNltKKISSELEMLRVKVKELESSEDRLDKTEQSLVSELEKLKSLTLS 192
Cdd:COG2433 382 LEELIEKELPEEEPEAEREKEHEERELTEEEEEI--RRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEERR 459
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 119433663 193 FVNERKYLNEKEKEN----------EKIIKELTQKLEQNKKM 224
Cdd:COG2433 460 EIRKDREISRLDREIerlereleeeRERIEELKRKLERLKEL 501
|
|
| DUF4686 |
pfam15742 |
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ... |
103-353 |
4.84e-04 |
|
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: 464838 [Multi-domain] Cd Length: 384 Bit Score: 43.90 E-value: 4.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 103 TRELKSEIER---LQKRMVDLEklEEALsRSKNECSQLCLSLNEERNLTKKISSELEMLRVKVKELE-----SSEDRldK 174
Cdd:pfam15742 33 EKELRYERGKnldLKQHNSLLQ--EENI-KIKAELKQAQQKLLDSTKMCSSLTAEWKHCQQKIRELElevlkQAQSI--K 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 175 TEQSLVSELEKLKS-----------------------LTLSFVNERKYLNEKEKENEKIIKELTQKL--EQNKKMNRDHM 229
Cdd:pfam15742 108 SQNSLQEKLAQEKSrvadaeekilelqqklehahkvcLTDTCILEKKQLEERIKEASENEAKLKQQYqeEQQKRKLLDQN 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 230 RNASTFLERNDLRIEDGISSTLSSKESKRKGSLDYLKQVENETRDKSENEKNRNQEDNKVKDLNQEIEKLKTQIKHF-ES 308
Cdd:pfam15742 188 VNELQQQVRSLQDKEAQLEMTNSQQQLRIQQQEAQLKQLENEKRKSDEHLKSNQELSEKLSSLQQEKEALQEELQQVlKQ 267
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 119433663 309 LEEELKK-------MRAKNNDLQDNYLTELN----RNRSLASQLEEIKLQVRKQKE 353
Cdd:pfam15742 268 LDVHVRKynekhhhHKAKLRRAKDRLVHEVEqrdeRIKQLENEIGILQQQSEKEKA 323
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
35-220 |
6.04e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.99 E-value: 6.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 35 KNLQRAEDELLDLQDKviqaegSDSSTLAEIEVLRQRVLKIEGKDEEIKRAEDlchtmkeKLEEEENLTRELKSEIERLQ 114
Cdd:COG4717 49 ERLEKEADELFKPQGR------KPELNLKELKELEEELKEAEEKEEEYAELQE-------ELEELEEELEELEAELEELR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 115 KRMVDLEKLEEALSRSKnECSQLCLSLNEERNLTKKISSELEMLRVKVKELESSEDRLDKTEQSLVSELEKLKSLTL--- 191
Cdd:COG4717 116 EELEKLEKLLQLLPLYQ-ELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEeel 194
|
170 180 190
....*....|....*....|....*....|
gi 119433663 192 -SFVNERKYLNEKEKENEKIIKELTQKLEQ 220
Cdd:COG4717 195 qDLAEELEELQQRLAELEEELEEAQEELEE 224
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
21-361 |
6.55e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 43.95 E-value: 6.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 21 QSLSRRLDELEEATKNLQRAEDELLDLQDKVIQAEGSDSSTLAEIEVLRQRV---------LKIEGkdEEIKRAEDLCHT 91
Cdd:pfam15921 475 EMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVdlklqelqhLKNEG--DHLRNVQTECEA 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 92 MKEKLEEEENLTRELKSEIERLQK------RMVDLEKLEEAlsRSKNECSQLCLSLNEERNLTKKISSELEMLRVKVKEL 165
Cdd:pfam15921 553 LKLQMAEKDKVIEILRQQIENMTQlvgqhgRTAGAMQVEKA--QLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDL 630
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 166 ESSEDRLDKTEQSLVSELEKLKSLTLSFVNE----RKYLNEKEKENEKIIKELTQKLEQNKKMN---RDHMRNASTFLE- 237
Cdd:pfam15921 631 ELEKVKLVNAGSERLRAVKDIKQERDQLLNEvktsRNELNSLSEDYEVLKRNFRNKSEEMETTTnklKMQLKSAQSELEq 710
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 238 -RNDLRIEDG-------ISSTLSSKESKRKGSLDYLKQ--------VENETRDKSENEKNRNQEDNKVKDLNQEIEKLKT 301
Cdd:pfam15921 711 tRNTLKSMEGsdghamkVAMGMQKQITAKRGQIDALQSkiqfleeaMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAG 790
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 302 QIKHFESLEEELKKMRAKNNDLQDNYLTELNRNRSLASQLEEIKLQVRKQKELGNGDIEG 361
Cdd:pfam15921 791 ELEVLRSQERRLKEKVANMEVALDKASLQFAECQDIIQRQEQESVRLKLQHTLDVKELQG 850
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
30-215 |
7.24e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 43.69 E-value: 7.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 30 LEEAtknLQRAEDELLDLQDKVIQAEGSDSStlAEIEVLRQRVLKiegKDEEIKRAEDLchtmkekleeeenlTRELKSE 109
Cdd:COG2433 378 IEEA---LEELIEKELPEEEPEAEREKEHEE--RELTEEEEEIRR---LEEQVERLEAE--------------VEELEAE 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 110 IERLQKRmvdLEKLEEALSRSKnecsqlclslnEERNLTKKISSELEMLRVKVKELESSEDRLDKTEQSLVSELEKLKSL 189
Cdd:COG2433 436 LEEKDER---IERLERELSEAR-----------SEERREIRKDREISRLDREIERLERELEEERERIEELKRKLERLKEL 501
|
170 180
....*....|....*....|....*.
gi 119433663 190 tlsfvneRKYLNEKEKENEKIIKELT 215
Cdd:COG2433 502 -------WKLEHSGELVPVKVVEKFT 520
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
73-374 |
8.39e-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: 43.89 E-value: 8.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 73 LKIEGKDEEIKRAEDLCHTMKEKLEEEENlTRELKSEIERLQKRMVDLEKLEEALSRSKNECSQL-CLSLNEERNLTKKI 151
Cdd:TIGR01612 1226 LFLEKIDEEKKKSEHMIKAMEAYIEDLDE-IKEKSPEIENEMGIEMDIKAEMETFNISHDDDKDHhIISKKHDENISDIR 1304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 152 SSELEMLRVKVKEleSSEDRLDKTEQSLVSELEKLKSLTLSFVNERKYLNEKEKEN--EKII---KELTQKLEQNKKMNR 226
Cdd:TIGR01612 1305 EKSLKIIEDFSEE--SDINDIKKELQKNLLDAQKHNSDINLYLNEIANIYNILKLNkiKKIIdevKEYTKEIEENNKNIK 1382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 227 DHMRNASTFLE--RNDLRIED---GISSTLSSKE-----SKRKGSLDYL--KQVENETRDKSENEKNRN----------- 283
Cdd:TIGR01612 1383 DELDKSEKLIKkiKDDINLEEcksKIESTLDDKDideciKKIKELKNHIlsEESNIDTYFKNADENNENvlllfkniema 1462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 284 ----------QEDNKVKDLNQEIEKLKTQIKHFESLEEEL---KKMRAKNNDLQDNYLTELNR--NRSLASQLEEIKLQV 348
Cdd:TIGR01612 1463 dnksqhilkiKKDNATNDHDFNINELKEHIDKSKGCKDEAdknAKAIEKNKELFEQYKKDVTEllNKYSALAIKNKFAKT 1542
|
330 340
....*....|....*....|....*..
gi 119433663 349 RKQKELGNGDI-EGEDAFLLGRGRHER 374
Cdd:TIGR01612 1543 KKDSEIIIKEIkDAHKKFILEAEKSEQ 1569
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
4-352 |
8.57e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.22 E-value: 8.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 4 LTNYKDAASNRHLRFKLQSLSRRLDELEEATKNLQRAEDELLDLQDKVIQAEGS-----DSSTLAEIEVLRQRVLKIEGK 78
Cdd:COG4717 125 LQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEEleellEQLSLATEEELQDLAEELEEL 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 79 DEEIKRAEDlchtmkeKLEEEENLTRELKSEIERLQKRMV---DLEKLEEALSRSKNECSQLCLSLNEERNL-------- 147
Cdd:COG4717 205 QQRLAELEE-------ELEEAQEELEELEEELEQLENELEaaaLEERLKEARLLLLIAAALLALLGLGGSLLsliltiag 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 148 ---------------TKKISSELEMLRVKVKELESSEDRLDKTEQSLVSELEKLKSLTLSFVNE--------RKYLNEKE 204
Cdd:COG4717 278 vlflvlgllallfllLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLElldrieelQELLREAE 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 205 KENEKI-----IKELTQKLEQNKKMNRDHMRNAST-FLERNDLRIE-DGISSTLSSKESKRKGSLDYLKQVENETRDkSE 277
Cdd:COG4717 358 ELEEELqleelEQEIAALLAEAGVEDEEELRAALEqAEEYQELKEElEELEEQLEELLGELEELLEALDEEELEEEL-EE 436
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 278 NEKNRNQEDNKVKDLNQEIEKLKTQIKHFES------LEEELKKMRAKNNDLQDNYLtelnRNRSLASQLEEIKLQVRKQ 351
Cdd:COG4717 437 LEEELEELEEELEELREELAELEAELEQLEEdgelaeLLQELEELKAELRELAEEWA----ALKLALELLEEAREEYREE 512
|
.
gi 119433663 352 K 352
Cdd:COG4717 513 R 513
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
15-347 |
8.62e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 43.56 E-value: 8.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 15 HLRFKLQSLSRRLDELEEATKNLQRAEDELLDLQDKViqaeGSDSSTLAEIEVLRQRVLKIEGKDEEI--------KRAE 86
Cdd:pfam05483 378 QLKIITMELQKKSSELEEMTKFKNNKEVELEELKKIL----AEDEKLLDEKKQFEKIAEELKGKEQELifllqareKEIH 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 87 DL---CHTMKEKLEEEENLTRELKSEIERLQKRMVDLEKLEEALSRSK----NECSQLCLSL-NEERNLTKKISSELEML 158
Cdd:pfam05483 454 DLeiqLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENkeltQEASDMTLELkKHQEDIINCKKQEERML 533
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 159 rvkvKELESsedrLDKTEQSLVSELEKLKSLTLSFVNERKYLNEKEKENEKIIKELTQKLEQNKKMNRDHMRNASTFLER 238
Cdd:pfam05483 534 ----KQIEN----LEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIEN 605
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 239 NDLRIEDgisstlsskeskrkgsldyLKQVENETRDKSENE-KNRNQEDNKVKDLNQEIEKLKTQikhFESLEEELKKMR 317
Cdd:pfam05483 606 KNKNIEE-------------------LHQENKALKKKGSAEnKQLNAYEIKVNKLELELASAKQK---FEEIIDNYQKEI 663
|
330 340 350
....*....|....*....|....*....|
gi 119433663 318 AKNNDLQDNYLTELNRNRSLASqlEEIKLQ 347
Cdd:pfam05483 664 EDKKISEEKLLEEVEKAKAIAD--EAVKLQ 691
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
14-347 |
9.98e-04 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 43.53 E-value: 9.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 14 RHLRFKLQSLSRRLDELEEATKNL---QRAEDELLDLQDKVIQAEGSDSSTLAEievLRQRVLKIEGKDEEIKRAEDLCH 90
Cdd:COG5022 758 RYLRRRYLQALKRIKKIQVIQHGFrlrRLVDYELKWRLFIKLQPLLSLLGSRKE---YRSYLACIIKLQKTIKREKKLRE 834
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 91 TMKEKLEEEENLTRELKSEIERLQKRMVDLEKlEEALSRSKNEcsqlclSLNEERNLT--KKISSELEMLRVKVKELESS 168
Cdd:COG5022 835 TEEVEFSLKAEVLIQKFGRSLKAKKRFSLLKK-ETIYLQSAQR------VELAERQLQelKIDVKSISSLKLVNLELESE 907
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 169 EDRLDKTEQSlvSELEKLKSLTLSFVNERKYLNEKEKENEKIIKeltqkLEQNKKMNRDHMRNAS---TFLERNDLRIED 245
Cdd:COG5022 908 IIELKKSLSS--DLIENLEFKTELIARLKKLLNNIDLEEGPSIE-----YVKLPELNKLHEVESKlkeTSEEYEDLLKKS 980
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 246 GIS-STLSSKESKRKGSLDYLKQVENETRDKSENEKNRNQEDNKVKDLNQEIEKLKTQIKHFESLEEELKKMRA---KNN 321
Cdd:COG5022 981 TILvREGNKANSELKNFKKELAELSKQYGALQESTKQLKELPVEVAELQSASKIISSESTELSILKPLQKLKGLlllENN 1060
|
330 340
....*....|....*....|....*.
gi 119433663 322 DLQDNYLTELNRNRSLASQLEEIKLQ 347
Cdd:COG5022 1061 QLQARYKALKLRRENSLLDDKQLYQL 1086
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
81-413 |
1.02e-03 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 43.28 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 81 EIKRAEDLCHTMKE---KLEEEENLTRELKSEIERLQKRMVDLEKLEEALSRSKNECSQLCLSLNEERNLTKKISSELEM 157
Cdd:PTZ00440 496 YQEKVDELLQIINSikeKNNIVNNNFKNIEDYYITIEGLKNEIEGLIELIKYYLQSIETLIKDEKLKRSMKNDIKNKIKY 575
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 158 LR---VKVKELESSEDRLDKTEQslvsELEKLKSLTLSfvNERKYLNEKEKENEKIIKELTQKLEQNKKMNRDHMrnaST 234
Cdd:PTZ00440 576 IEenvDHIKDIISLNDEIDNIIQ----QIEELINEALF--NKEKFINEKNDLQEKVKYILNKFYKGDLQELLDEL---SH 646
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 235 FLERNdlriedgisstlsSKESKRKGSLDYLKQVENETRDKSENEKNRNQEDNkvkdlNQEIEKLKTQIKHFESLEEELK 314
Cdd:PTZ00440 647 FLDDH-------------KYLYHEAKSKEDLQTLLNTSKNEYEKLEFMKSDNI-----DNIIKNLKKELQNLLSLKENII 708
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 315 KMRAKN--NDLQDNYLTELNRNRSLASQLEEIKLQVRKQKELGNGDIEGEDAFLLGRGRHERTKLKGHGSEASVSKHtsr 392
Cdd:PTZ00440 709 KKQLNNieQDISNSLNQYTIKYNDLKSSIEEYKEEEEKLEVYKHQIINRKNEFILHLYENDKDLPDGKNTYEEFLQY--- 785
|
330 340
....*....|....*....|.
gi 119433663 393 elspqhkRERLRNREFALSNE 413
Cdd:PTZ00440 786 -------KDTILNKENKISND 799
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
28-349 |
1.45e-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: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 28 DELEEATKNLQRAEDELLDLQDKVIQAEGSDSSTLAEIEVLRQRVLKIEGKDEEIKRAEDLchtmkekleeeENLTRELK 107
Cdd:TIGR00606 577 DWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSQDE-----------ESDLERLK 645
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 108 SEIERLQKRMVDL-------EKLEEALSRSKNECSQLC----LSLNEERNLTKKISSELEMLRVKVKELESSEDRLDKTE 176
Cdd:TIGR00606 646 EEIEKSSKQRAMLagatavySQFITQLTDENQSCCPVCqrvfQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRR 725
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 177 QSLVSELEKLKSLTLSFVNERKYLNEKEKENEKIIKELTQKLEQNKKMNRDHM-RNASTFLERNDLRIEDGISSTLSSKE 255
Cdd:TIGR00606 726 DEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMpEEESAKVCLTDVTIMERFQMELKDVE 805
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 256 SKRKGSLDYLKQVENEtRDKSENEKNRNQEDNKVKDLNQEIEKLKtqiKHFESLEEELKKMRAKNNDLQDNYL---TELN 332
Cdd:TIGR00606 806 RKIAQQAAKLQGSDLD-RTVQQVNQEKQEKQHELDTVVSKIELNR---KLIQDQQEQIQHLKSKTNELKSEKLqigTNLQ 881
|
330
....*....|....*..
gi 119433663 333 RNRSLASQLEEIKLQVR 349
Cdd:TIGR00606 882 RRQQFEEQLVELSTEVQ 898
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
108-220 |
1.49e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.46 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 108 SEIERLQKRMVDLEKLE------EALSRSKNECSQLCLSLNEERNLTKKISSELEmLRVKVKE--LESSEDRLDKTEQSL 179
Cdd:PRK12704 34 KEAEEEAKRILEEAKKEaeaikkEALLEAKEEIHKLRNEFEKELRERRNELQKLE-KRLLQKEenLDRKLELLEKREEEL 112
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 119433663 180 VSELEKLKsltlsfvNERKYLNEKEKENEKIIKELTQKLEQ 220
Cdd:PRK12704 113 EKKEKELE-------QKQQELEKKEEELEELIEEQLQELER 146
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
25-364 |
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 119433663 25 RRLDELEEATKNLQRAEDELLDLQDKVIQAEGSDSSTLAE-----------IEVLRQRVLKiegKDEEIKRAEDLCHTMK 93
Cdd:PTZ00121 1134 RKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEdakkaeaarkaEEVRKAEELR---KAEDARKAEAARKAEE 1210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 94 EKLEEEENLTRELK--SEIERLQKRMVDLEKLEEALSRSKNECSQLCLSLNEERNLTKKISSELEMLRvKVKELESSEDR 171
Cdd:PTZ00121 1211 ERKAEEARKAEDAKkaEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEAR-KADELKKAEEK 1289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 172 LDKTEQSLVSELEKLKSLtlsfvnerkylnEKEKENEKIIKELTQKLEQNKKMNRDHMRNASTFLERNDLRIEDGISSTL 251
Cdd:PTZ00121 1290 KKADEAKKAEEKKKADEA------------KKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAAD 1357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 252 SSKESKRKGSLDYLKQveNETRDKSENEKNRNQEDNKVKDLNQEIEKLKTQIKHFESLEEELKKM-RAKNNDLQDNYLTE 330
Cdd:PTZ00121 1358 EAEAAEEKAEAAEKKK--EEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKAdEAKKKAEEKKKADE 1435
|
330 340 350
....*....|....*....|....*....|....
gi 119433663 331 LNRNRSLASQLEEIKLQVRKQKELGNGDIEGEDA 364
Cdd:PTZ00121 1436 AKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEA 1469
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
153-364 |
1.66e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.12 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 153 SELEMLRVKVKELESSEDRLDKTEQSLVSELEKLKSLTLSFVNERKYLNEKEKENEKIIKELTQKLEQNKKMNRDHMR-- 230
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARal 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 231 -----------------NASTFLERNDLRiedgisSTLSSKESKRkgsldyLKQVEnetRDKSENEKNRNQEDNKVKDLN 293
Cdd:COG3883 96 yrsggsvsyldvllgseSFSDFLDRLSAL------SKIADADADL------LEELK---ADKAELEAKKAELEAKLAELE 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119433663 294 QEIEKLKTQIKhfeSLEEELKKMRAKNNDLQDNYLTELNRNRSLASQLEEIKLQVRKQKELGNGDIEGEDA 364
Cdd:COG3883 161 ALKAELEAAKA---ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAA 228
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
27-345 |
1.81e-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. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 42.15 E-value: 1.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 27 LDELEEATK--NLQRAEDELLDLQDKVIQAEGSDSSTLAEIEVLrqrvLKIEGKD-EEIKRAEDLchtmkekleeeenlT 103
Cdd:pfam06160 69 LFEAEELNDkyRFKKAKKALDEIEELLDDIEEDIKQILEELDEL----LESEEKNrEEVEELKDK--------------Y 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 104 RELKSEIerLQKRM---VDLEKLEEALSRSKNECSQLcLSLNEE------RNLTKKISSELEMLRVKVKELEsseDRLDK 174
Cdd:pfam06160 131 RELRKTL--LANRFsygPAIDELEKQLAEIEEEFSQF-EELTESgdyleaREVLEKLEEETDALEELMEDIP---PLYEE 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 175 TEQSLVSELEKLKSLTLSFVNERKYLNEKEKENEkiIKELTQKLEQNKKM-NRDHMRNASTFLERNDLRIeDGISSTL-- 251
Cdd:pfam06160 205 LKTELPDQLEELKEGYREMEEEGYALEHLNVDKE--IQQLEEQLEENLALlENLELDEAEEALEEIEERI-DQLYDLLek 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 252 --SSK---ESKRKGSLDYLKQVENETRD-KSENE---KN---RNQEDNKVKDLNQEIEKLKTQikhFESLEEELKKMRAK 319
Cdd:pfam06160 282 evDAKkyvEKNLPEIEDYLEHAEEQNKElKEELErvqQSytlNENELERVRGLEKQLEELEKR---YDEIVERLEEKEVA 358
|
330 340
....*....|....*....|....*.
gi 119433663 320 NNDLQDNYLTELNRNRSLASQLEEIK 345
Cdd:pfam06160 359 YSELQEELEEILEQLEEIEEEQEEFK 384
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
16-353 |
1.95e-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: 1.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 16 LRFKLQSLSRRLDELEEATKNLQRAEDELLDLQDKVIQAEGSDSSTL-------AEIEVLRQRVLKIEGKDEEIKRAEDL 88
Cdd:TIGR00606 191 LRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSReivksyeNELDPLKNRLKEIEHNLSKIMKLDNE 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 89 CHTMKEKLEEEENLTRELKSEIERL----QKRMVDLEKLEEALSRSKNE----CSQLCLSLNEERNLTKKISSELEmlrV 160
Cdd:TIGR00606 271 IKALKSRKKQMEKDNSELELKMEKVfqgtDEQLNDLYHNHQRTVREKERelvdCQRELEKLNKERRLLNQEKTELL---V 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 161 KVKELESSEDRLDktEQSLVSELEKLKSLTLSFVNERKYLNEKEKENEKIIKELTQKLEQNKKMNRDHMrnastflernd 240
Cdd:TIGR00606 348 EQGRLQLQADRHQ--EHIRARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQLC----------- 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 241 lriedgisSTLSSKESKRKGSLDYLKQVENETRDKSENEKNR-NQEDNKVKDLNQEIEKLKTQIKHFESLEEELKKMRAK 319
Cdd:TIGR00606 415 --------ADLQSKERLKQEQADEIRDEKKGLGRTIELKKEIlEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERE 486
|
330 340 350
....*....|....*....|....*....|....
gi 119433663 320 NNDLQDNYLTELNRNRSLASQLEEIKLQVRKQKE 353
Cdd:TIGR00606 487 LSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKL 520
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
25-315 |
2.13e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.44 E-value: 2.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 25 RRLDELEEATKNLQRAEDELLDLQDKVIQAEGSDSSTLAEIEVLRQRVLKIE--GKDEEIKRAEDLCHTMKEKLEEEENL 102
Cdd:PTZ00121 1230 KKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADelKKAEEKKKADEAKKAEEKKKADEAKK 1309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 103 TRELKSEIERLQKRMVDLEKLEEALSRSKNEcsqlclslNEERNLTKKISSELEMLRVKVKELESSEDRLDKTEQSLVSE 182
Cdd:PTZ00121 1310 KAEEAKKADEAKKKAEEAKKKADAAKKKAEE--------AKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKAD 1381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 183 LEKLKSLTLSFVNERKylnEKEKENEKIIKELTQKLEQNKKMnrDHMRNASTFLERND---LRIEDGISSTLSSKESKRK 259
Cdd:PTZ00121 1382 AAKKKAEEKKKADEAK---KKAEEDKKKADELKKAAAAKKKA--DEAKKKAEEKKKADeakKKAEEAKKADEAKKKAEEA 1456
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 119433663 260 GSLDYLKQVENETRdKSENEKNRNQEDNKVKDLNQEIEKLKTQIKHFESLEEELKK 315
Cdd:PTZ00121 1457 KKAEEAKKKAEEAK-KADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKK 1511
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
10-192 |
2.14e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 41.67 E-value: 2.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 10 AASNRHLRFKLQSLSRRLDELEEATKNLQRAEDELLDLQDKVIQAEGSDSSTLAEIEVLRQRvlkIEGKDEEIKR----- 84
Cdd:COG4942 37 AELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE---LEAQKEELAEllral 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 85 --------------AEDLcHTMKEKLEEEENLTRELKSEIERLQKRMVDLEKLEEALSRSKNECSQLCLSLNEERN---- 146
Cdd:COG4942 114 yrlgrqpplalllsPEDF-LDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAalea 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 119433663 147 -------LTKKISSELEMLRVKVKELESSEDRLDKTEQSLVSELEKLKSLTLS 192
Cdd:COG4942 193 lkaerqkLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
19-354 |
2.51e-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: 2.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 19 KLQSLSRRLDELEEATKNLQRAEDELLDlqdkviQAEGSDSSTLAEIEVLRQRVLKIEGKDEEIKRAEDLCHTMKEKLEE 98
Cdd:TIGR00606 406 EAKTAAQLCADLQSKERLKQEQADEIRD------EKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQE 479
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 99 EENLTREL-----KSEIERLQKRMVDLEKLEEALSRSKNECSQLclslNEERNLTKKISSELEML-RVKVKELESSEDRL 172
Cdd:TIGR00606 480 LRKAERELskaekNSLTETLKKEVKSLQNEKADLDRKLRKLDQE----MEQLNHHTTTRTQMEMLtKDKMDKDEQIRKIK 555
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 173 DKTEQSLVSELEKL---KSLTLSFVNERKYLNEKEKENEKIIKELtQKLEQNKkmnrDHMRNASTFLERNDLRIEDGISS 249
Cdd:TIGR00606 556 SRHSDELTSLLGYFpnkKQLEDWLHSKSKEINQTRDRLAKLNKEL-ASLEQNK----NHINNELESKEEQLSSYEDKLFD 630
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 250 TLSSKESKRK-------------------GSLDYLKQVENETRDKSENEKNRNQEDNKVK-DLNQEIEKLKTQIKHF--- 306
Cdd:TIGR00606 631 VCGSQDEESDlerlkeeieksskqramlaGATAVYSQFITQLTDENQSCCPVCQRVFQTEaELQEFISDLQSKLRLApdk 710
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119433663 307 -ESLEEELKK-------------MRAKNNDLQDNYLTEL-NRNRSLASQLEEIKLQVRKQKEL 354
Cdd:TIGR00606 711 lKSTESELKKkekrrdemlglapGRQSIIDLKEKEIPELrNKLQKVNRDIQRLKNDIEEQETL 773
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
103-380 |
2.92e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.43 E-value: 2.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 103 TRELKSEIERLQKRMVDLEKLEEALSRSKNECSQLCLSLNEERNLTKKISSELEMLRVKVKELESSEDRLDKTEQSLVSE 182
Cdd:COG4372 58 REELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQ 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 183 LEKLKSltlSFVNERKYLNEKEKENEKIIKELTQKLEQNKKMNRDHMRNASTFLERNDLRIEDGISSTLSSKESKRKGSL 262
Cdd:COG4372 138 IAELQS---EIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPR 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 263 DYLKQVENETRDKSENEKnRNQEDNKVKDLNQEIEKLKTQIKHFESLEEELKKMRAKNNDLQDNYLTELNrnrslaSQLE 342
Cdd:COG4372 215 ELAEELLEAKDSLEAKLG-LALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAAL------ELEA 287
|
250 260 270
....*....|....*....|....*....|....*...
gi 119433663 343 EIKLQVRKQKELGNGDIEGEDAFLLGRGRHERTKLKGH 380
Cdd:COG4372 288 LEEAALELKLLALLLNLAALSLIGALEDALLAALLELA 325
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
28-423 |
2.96e-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: 2.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 28 DELEEATKNLQRAEDELLDLQDKVIQAEGSDSSTLAEIEVLRQRVLKIEGKDEEIKR----------------------- 84
Cdd:pfam12128 471 ERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELqlfpqagtllhflrkeapdweqs 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 85 ------AEDLCHTMKEKLEEEENLTRELKSEIERLQKRMVDLEK---LEEALsrsKNECSQLCLSLNEERNLTKKISSEL 155
Cdd:pfam12128 551 igkvisPELLHRTDLDPEVWDGSVGGELNLYGVKLDLKRIDVPEwaaSEEEL---RERLDKAEEALQSAREKQAAAEEQL 627
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 156 EMLRVKVKELESSEDRldkTEQSLVSELEKLKSLTLSFVNERKYLNEKEKENEKIIKELTQKLEQNKKMNRDHMRNASTF 235
Cdd:pfam12128 628 VQANGELEKASREETF---ARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEE 704
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 236 LERNDLRIEDGISSTLSSKESKRKGSLDYLKQVENETRDKSENEKNRNQEDNKvKDLN------QEIEKLKTQIKHFESL 309
Cdd:pfam12128 705 QKEQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRSGAKAELKALETWYK-RDLAslgvdpDVIAKLKREIRTLERK 783
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 310 EEELKKMRAKNNDLQDNYL-TELNRNRSLASQLEEIKLQVRkqkelgngDIEGEdaflLGRGRHE-RTKLKGHGSEASVS 387
Cdd:pfam12128 784 IERIAVRRQEVLRYFDWYQeTWLQRRPRLATQLSNIERAIS--------ELQQQ----LARLIADtKLRRAKLEMERKAS 851
|
410 420 430
....*....|....*....|....*....|....*.
gi 119433663 388 KHTSRELSPQHKRERLRNREFALSNEHYSLSSKQAS 423
Cdd:pfam12128 852 EKQQVRLSENLRGLRCEMSKLATLKEDANSEQAQGS 887
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
23-325 |
4.65e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 40.93 E-value: 4.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 23 LSRRLDELEEATKNLQRAEDELLDLQDKVIQAEG----------SDSSTLAEIEVLRQRvlkIEGKDEEIkraEDLCHTM 92
Cdd:pfam01576 7 MQAKEEELQKVKERQQKAESELKELEKKHQQLCEeknalqeqlqAETELCAEAEEMRAR---LAARKQEL---EEILHEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 93 KEKLEEEENLTRELKSEIERLQKRMVDLE-KLEE------ALSRSKNECSQLCLSLNEERNLTKKISSELEmlrvkvKEL 165
Cdd:pfam01576 81 ESRLEEEEERSQQLQNEKKKMQQHIQDLEeQLDEeeaarqKLQLEKVTTEAKIKKLEEDILLLEDQNSKLS------KER 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 166 ESSEDRLDKTEQSLVSELEKLKSLT-LSFVNERKY--LNEKEKENEKiikeLTQKLEQNKKMNRDHMRNASTFLERNDLR 242
Cdd:pfam01576 155 KLLEERISEFTSNLAEEEEKAKSLSkLKNKHEAMIsdLEERLKKEEK----GRQELEKAKRKLEGESTDLQEQIAELQAQ 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 243 IEDgISSTLSSKESKRKGSLDylkQVENETRDKSENEKNRNQEDNKVKDLNQEIEKLKTQ----IKHFESLEEELKKMRA 318
Cdd:pfam01576 231 IAE-LRAQLAKKEEELQAALA---RLEEETAQKNNALKKIRELEAQISELQEDLESERAArnkaEKQRRDLGEELEALKT 306
|
....*..
gi 119433663 319 KNNDLQD 325
Cdd:pfam01576 307 ELEDTLD 313
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
35-347 |
4.72e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.77 E-value: 4.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 35 KNLQRAEDELlDLQDKVIQAEGSDSSTLAE----IEVLRQR---VLKIEGKDEEIKRAEDLC---------HTMKEKLEE 98
Cdd:COG3206 94 PVLERVVDKL-NLDEDPLGEEASREAAIERlrknLTVEPVKgsnVIEISYTSPDPELAAAVAnalaeayleQNLELRREE 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 99 EENLTRELKSEIERLQKRmvdLEKLEEALSRSKNEcSQLcLSLNEERNLTKKISSELEMLRVKVK-ELESSEDRLDKTEQ 177
Cdd:COG3206 173 ARKALEFLEEQLPELRKE---LEEAEAALEEFRQK-NGL-VDLSEEAKLLLQQLSELESQLAEARaELAEAEARLAALRA 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 178 SLVSELEKLKSLTlsfvnerkylnekekeNEKIIKELTQKLEQnkkMNRDHMRNASTFLERNDLRIEdgisstlssKESK 257
Cdd:COG3206 248 QLGSGPDALPELL----------------QSPVIQQLRAQLAE---LEAELAELSARYTPNHPDVIA---------LRAQ 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 258 RKGSLDYLKQVENETRDKSENEKNRNQEdnKVKDLNQEIEKLKTQIKHFESLEEELkkmraknNDLQDNYltELNRN--R 335
Cdd:COG3206 300 IAALRAQLQQEAQRILASLEAELEALQA--REASLQAQLAQLEARLAELPELEAEL-------RRLEREV--EVARElyE 368
|
330
....*....|..
gi 119433663 336 SLASQLEEIKLQ 347
Cdd:COG3206 369 SLLQRLEEARLA 380
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
262-346 |
4.90e-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: 4.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 262 LDYLKQVENETRDKSENEKNRNQEdnKVKDLNQEIEKLKTQIKHFESLEEELKKMRAKNNDLQDNYLTELNrnrSLASQL 341
Cdd:smart00787 188 LRQLKQLEDELEDCDPTELDRAKE--KLKKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIA---EAEKKL 262
|
....*
gi 119433663 342 EEIKL 346
Cdd:smart00787 263 EQCRG 267
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
104-341 |
5.04e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 40.65 E-value: 5.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 104 RELKSEIERLQKRMVDLEKLEEALSRSKNECSQLCLSLNEERNLtkkISSELEMLRVKVKELESSEDRLDKTEQSLVSEL 183
Cdd:pfam07888 76 RELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDA---LLAQRAAHEARIRELEEDIKTLTQRVLERETEL 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 184 EKLKSLTLSFVNERKylnEKEKENEKIIKELTQKLEQNKKMNRDHMRnastflERNDLRIEDGISSTLSSKESKRKGSLD 263
Cdd:pfam07888 153 ERMKERAKKAGAQRK---EEEAERKQLQAKLQQTEEELRSLSKEFQE------LRNSLAQRDTQVLQLQDTITTLTQKLT 223
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119433663 264 YLKQVEnetrdkSENEKNRnqednkvKDLNQEIEKLKTQIKHFESLEEELKKMRAknndLQDNYLTELNRNRSLASQL 341
Cdd:pfam07888 224 TAHRKE------AENEALL-------EELRSLQERLNASERKVEGLGEELSSMAA----QRDRTQAELHQARLQAAQL 284
|
|
| PilN |
COG3166 |
Type IV pilus assembly protein PilN [Cell motility, Extracellular structures]; |
277-347 |
5.07e-03 |
|
Type IV pilus assembly protein PilN [Cell motility, Extracellular structures];
Pssm-ID: 442399 [Multi-domain] Cd Length: 185 Bit Score: 39.18 E-value: 5.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 277 ENEKNRNQEdnkvkdLNQEIEKLKTQIKHFESLEEELKKMRAKNN---DLQDN------YLTELNRNRSLASQLEEIKLQ 347
Cdd:COG3166 48 AQQQARNAA------LQQEIAKLDKQIAEIKELKKQKAELLARLQvieQLQQSrppwvhLLDELARLLPEGVWLTSLSQQ 121
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
197-353 |
6.18e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.53 E-value: 6.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 197 RKYLNEKEKENEKIIKELTQKLEQNKKmnrDHMRNASTflERNDLRIEdgisstlSSKESKRKgsLDYLKQVENETRDKS 276
Cdd:PRK12704 30 EAKIKEAEEEAKRILEEAKKEAEAIKK---EALLEAKE--EIHKLRNE-------FEKELRER--RNELQKLEKRLLQKE 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119433663 277 ENEKNRNQednkvkDLNQEIEKLKTQIKHFESLEEELKKMRAKNNDLQDNYLTELNRNRSLASqlEEIKLQVRKQKE 353
Cdd:PRK12704 96 ENLDRKLE------LLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTA--EEAKEILLEKVE 164
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
15-354 |
6.73e-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: 40.72 E-value: 6.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 15 HLRFKLQSLSRRLDELEEATKNLQRAEDELLDLQDKVIQAEGSD-------------SSTLAEIEVLRQRVL-----KIE 76
Cdd:TIGR00618 390 TLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQelqqryaelcaaaITCTAQCEKLEKIHLqesaqSLK 469
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 77 GKDEEIKRAEDLCHTMKEKLEEEENLTRELKSEIERLQKRMVDLEKLEEALSRSKNECSQLCLSLNEERNLTK---KISS 153
Cdd:TIGR00618 470 EREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETseeDVYH 549
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 154 ELEMLRVKVKELESSEDRLDKTEQSLVSELEKLKSL---TLSFVNERKYLNEKEKENEKIIKELTQKL------EQNKKM 224
Cdd:TIGR00618 550 QLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDipnLQNITVRLQDLTEKLSEAEDMLACEQHALlrklqpEQDLQD 629
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 225 NRDHMRNAS-------TFLERNDL-----RIEDGISSTLSSKESKRKGSLDYLKQVENETRDKSENEKNRNQEDNKVKDL 292
Cdd:TIGR00618 630 VRLHLQQCSqelalklTALHALQLtltqeRVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLREL 709
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 119433663 293 NQEIEKLKTQIKHFESLEEELKKMRAKNNDLQDNYLTELNRNRSLASQLEEIKLQVRKQKEL 354
Cdd:TIGR00618 710 ETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVT 771
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
28-245 |
6.84e-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 organization 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: 459736 [Multi-domain] Cd Length: 235 Bit Score: 39.24 E-value: 6.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 28 DELEEATKNLQRAEDELLDLQDKVIQAEgsdsstlAEIEVLRQRVLKIEgkdEEIKRAEDLCHTMKEKLEEEENLTrelk 107
Cdd:pfam00261 8 EELDEAEERLKEAMKKLEEAEKRAEKAE-------AEVAALNRRIQLLE---EELERTEERLAEALEKLEEAEKAA---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 108 SEIERLQKrmvdleKLEEALSRSKNECSQLCLSLNEERNLTKKISSELEMLRVKVK----ELESSEDRLDKTEqSLVSEL 183
Cdd:pfam00261 74 DESERGRK------VLENRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVvvegDLERAEERAELAE-SKIVEL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 184 EK--------LKSLTLSfvnERKYlNEKEKENEKIIKELTQKLEQNKKMNRDHMRNASTfLERNDLRIED 245
Cdd:pfam00261 147 EEelkvvgnnLKSLEAS---EEKA-SEREDKYEEQIRFLTEKLKEAETRAEFAERSVQK-LEKEVDRLED 211
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
147-354 |
7.61e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.14 E-value: 7.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 147 LTKKISSELEML-RVKVKELESSEDRLDKTEQSLVSELEKLKSLTlSFVNERKYLNEKEKENEKIIKELTQKLEQNKKMN 225
Cdd:COG4717 47 LLERLEKEADELfKPQGRKPELNLKELKELEEELKEAEEKEEEYA-ELQEELEELEEELEELEAELEELREELEKLEKLL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 226 RdhmrNASTFLERNDLRIEdgisstLSSKESKrkgsLDYLKQVENETRDKSENEKNRNQEdnkVKDLNQEIEKLKTQI-- 303
Cdd:COG4717 126 Q----LLPLYQELEALEAE------LAELPER----LEELEERLEELRELEEELEELEAE---LAELQEELEELLEQLsl 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 119433663 304 ---KHFESLEEELKKMRAKNNDLQDNYLTELNRNRSLASQLEEIKLQVRKQKEL 354
Cdd:COG4717 189 ateEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE 242
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
37-380 |
8.09e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 40.11 E-value: 8.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 37 LQRAEDELLDLQDKVIQAEGSDSSTLAEIEvlRQRVLKIEGKDEEIKRAEDLCHTMKEKLEEEENLTRELKSEIERLQKR 116
Cdd:pfam05557 4 LIESKARLSQLQNEKKQMELEHKRARIELE--KKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAELNRLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 117 MvdleKLEEALSRSKNECSQLCLSLNE-ERNLTKKIS--------SELEmLRVKVKELESSEDRLDKTEQSLvSELEKLK 187
Cdd:pfam05557 82 K----KYLEALNKKLNEKESQLADAREvISCLKNELSelrrqiqrAELE-LQSTNSELEELQERLDLLKAKA-SEAEQLR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 188 SLTLSFVNERKYLNEKEKENEKIIKELTQKLEQNKKMNRDHMRNAStfLERNDLRIEDGISSTLSSKESKrkgslDYLKQ 267
Cdd:pfam05557 156 QNLEKQQSSLAEAEQRIKELEFEIQSQEQDSEIVKNSKSELARIPE--LEKELERLREHNKHLNENIENK-----LLLKE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 268 VENETRDKSENEKNRNQEdnkVKDLNQEIEKLKTQIKHFESLEEELKKMRAKNNDLQDNYLTELNRNRSLASQLEEIKLQ 347
Cdd:pfam05557 229 EVEDLKRKLEREEKYREE---AATLELEKEKLEQELQSWVKLAQDTGLNLRSPEDLSRRIEQLQQREIVLKEENSSLTSS 305
|
330 340 350
....*....|....*....|....*....|...
gi 119433663 348 VRkQKELGNGDIEGEDAFLLGRGRHERTKLKGH 380
Cdd:pfam05557 306 AR-QLEKARRELEQELAQYLKKIEDLNKKLKRH 337
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
28-220 |
8.37e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.81 E-value: 8.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 28 DELEEATKNLQRAEDELLDLQDKVIQAEGSDSSTLAEIEVLRQrvlKIEGKDEEIKRAEdlchtmkekleeeenltrelk 107
Cdd:COG3883 23 KELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQA---EIDKLQAEIAEAE--------------------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 108 seiERLQKRMVDLEKLEEALSRSKNECSQLCLSLNEE---------RNLTKKISSELEMLrvkvKELESSEDRLDKTEQS 178
Cdd:COG3883 79 ---AEIEERREELGERARALYRSGGSVSYLDVLLGSEsfsdfldrlSALSKIADADADLL----EELKADKAELEAKKAE 151
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 119433663 179 LVSELEKLKSLTLSFVNERKYLNEKEKENEKIIKELTQKLEQ 220
Cdd:COG3883 152 LEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAA 193
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
11-223 |
8.86e-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: 40.05 E-value: 8.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 11 ASNRHLRFKLQSLSRRLDELEEATKNLQRAEDElLDLQDKVIQAEGSDS-----STLAEIEVLRQRVLKIEGKDEEIKRA 85
Cdd:TIGR02169 812 ARLREIEQKLNRLTLEKEYLEKEIQELQEQRID-LKEQIKSIEKEIENLngkkeELEEELEELEAALRDLESRLGDLKKE 890
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 86 EDlchTMKEKLEEEENLTRELKSEIERLQKRMVDL-EKLEEALSRSKnecsqlclSLNEERNLTKKISSELEMLRVKVKE 164
Cdd:TIGR02169 891 RD---ELEAQLRELERKIEELEAQIEKKRKRLSELkAKLEALEEELS--------EIEDPKGEDEEIPEEELSLEDVQAE 959
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 119433663 165 LESSEDRLDKTEQSLVSELEKLKSlTLSFVNERKYLNEKEKENEKIIKELTQKLEQNKK 223
Cdd:TIGR02169 960 LQRVEEEIRALEPVNMLAIQEYEE-VLKRLDELKEKRAKLEEERKAILERIEEYEKKKR 1017
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
21-326 |
9.40e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 39.50 E-value: 9.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 21 QSLSRRLDELEEATKNLQRAEDELLDLQDKVIQAEGSDSSTLAEIEVLRQRVLKIEGKDEEIKRA-EDLCHTMKEKLEEE 99
Cdd:COG4372 59 EELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKErQDLEQQRKQLEAQI 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 100 ENLTRELKSEIERLQKRMVDLEKLEEALSRsknecsqlcLSLNEERNLTKKISSELEMLRVKVKELESSEDRLDKTEQSL 179
Cdd:COG4372 139 AELQSEIAEREEELKELEEQLESLQEELAA---------LEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLI 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 180 VSELEKLKSLTLSFVNERKY---LNEKEKENEKIIKELTQKLEQNKKMNRDHMRNASTFLERNDLRIEDGISSTLSSKES 256
Cdd:COG4372 210 ESLPRELAEELLEAKDSLEAklgLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALE 289
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 257 KRKGSLDYLKQVENETRDKSENEKNRNQEDNKVKDLNQEIEKLKTQIKHFESLEEELKKMRAKNNDLQDN 326
Cdd:COG4372 290 EAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELL 359
|
|
| PKK |
pfam12474 |
Polo kinase kinase; This domain family is found in eukaryotes, and is approximately 140 amino ... |
110-224 |
9.60e-03 |
|
Polo kinase kinase; This domain family is found in eukaryotes, and is approximately 140 amino acids in length. The family is found in association with pfam00069. Polo-like kinase 1 (Plx1) is essential during mitosis for the activation of Cdc25C, for spindle assembly, and for cyclin B degradation. This family is Polo kinase kinase (PKK) which phosphorylates Polo kinase and Polo-like kinase to activate them. PKK is a serine/threonine kinase.
Pssm-ID: 463600 [Multi-domain] Cd Length: 139 Bit Score: 37.54 E-value: 9.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119433663 110 IERLQKRMVdlEKLEEALSrsknecsqlclslNEERNLTKKISSE--------LEMLRVKVKELESSEDRLDKTEQSlvs 181
Cdd:pfam12474 30 LERQQKQQI--EKLEQRQT-------------QELRRLPKRIRAEqkkrlkmfRESLKQEKKELKQEVEKLPKFQRK--- 91
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 119433663 182 ELEKLKSLTLSFVNERKYLNEKEKENEKIIKELTQKLEQNKKM 224
Cdd:pfam12474 92 EAKRQRKEELELEQKHEELEFLQAQSEALERELQQLQNEKRKE 134
|
|
| |
