|
Name |
Accession |
Description |
Interval |
E-value |
| Filament |
pfam00038 |
Intermediate filament protein; |
96-407 |
1.24e-151 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 434.73 E-value: 1.24e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145561 96 QEKEQIKSLNNKFASFIDKVRFLEQQNKMLETKWSLLQQQKTSR-SNMDNMFESYINNLRRQLEALGQEKLKLEAELGNM 174
Cdd:pfam00038 1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEpSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145561 175 QGLVEDFKNKYEDEINKRTEMENEFVLIKKDVDEAYMNKVELESRLEGLTDEINFLRQIHEEEIRELQSQISDTSVVLSM 254
Cdd:pfam00038 81 RLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145561 255 DNSRSLDMDGIIAEVRAQYEDIANRSRAEAETMYQIKYEELQTLAGKHGDDLRRTKTEISEMNRNINRLQAEIEALKGQR 334
Cdd:pfam00038 161 DAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQK 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 114145561 335 ASLEAAIADAEQRGEMAIKDAQTKLAELEAALQRAKQDMARQLREYQELMNVKLALDIEITTYRKLLEGEESR 407
Cdd:pfam00038 241 ASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
91-415 |
3.34e-13 |
|
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: 72.40 E-value: 3.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145561 91 QAVRTQEKEQIKSLNNKFASFIDKVRFLEQQNKMLETKWSLLQQQKTSRSNMDNMFESYINNLRRQLEALGQEKLKLEAE 170
Cdd:TIGR02168 669 NSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEER 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145561 171 LGNMQGLVEDFKNKYEDEINKRTEMENEFVlikkdvdEAYMNKVELESRLEGLTDEINFLRqiheEEIRELQSQISDTSV 250
Cdd:TIGR02168 749 IAQLSKELTELEAEIEELEERLEEAEEELA-------EAEAEIEELEAQIEQLKEELKALR----EALDELRAELTLLNE 817
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145561 251 VLSMDNSRSLDMDGIIAEVRAQYEDIANRSRAEAETMYQIK--YEELQTLAGKHGDDLRRTKTEISEMNRNINRLQAEIE 328
Cdd:TIGR02168 818 EAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAaeIEELEELIEELESELEALLNERASLEEALALLRSELE 897
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145561 329 ALKGQRASLEAAIADAEQrgemAIKDAQTKLAELEAALQRAKQDMARQLR----EYQELMNVKLALDIEITTYRKLLEGE 404
Cdd:TIGR02168 898 ELSEELRELESKRSELRR----ELEELREKLAQLELRLEGLEVRIDNLQErlseEYSLTLEEAEALENKIEDDEEEARRR 973
|
330
....*....|.
gi 114145561 405 ESRLESGMQNM 415
Cdd:TIGR02168 974 LKRLENKIKEL 984
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
235-379 |
4.44e-10 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 61.14 E-value: 4.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145561 235 EEEIRELQSQISDTSVVLSMDNSRSLDMDGIIAEVRAQYEDI-ANRSRAEA-ETMYQIKYEELQTLAGKHGDDLRRTKTE 312
Cdd:PRK09039 52 DSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSAAeAERSRLQAlLAELAGAGAAAEGRAGELAQELDSEKQV 131
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 114145561 313 ISEMNRNINRLQAEIEALKGQRASLEAAIADAEQRGemaiKDAQTKLA----ELEAALQRAKQDMAR-------QLRE 379
Cdd:PRK09039 132 SARALAQVELLNQQIAALRRQLAALEAALDASEKRD----RESQAKIAdlgrRLNVALAQRVQELNRyrseffgRLRE 205
|
|
| Keratin_2_head |
pfam16208 |
Keratin type II head; |
69-93 |
3.45e-09 |
|
Keratin type II head;
Pssm-ID: 465068 [Multi-domain] Cd Length: 156 Bit Score: 55.43 E-value: 3.45e-09
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
149-410 |
6.74e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.41 E-value: 6.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145561 149 YINNLRRQLEALGQEKLKLEAELgnmqglvEDFKNKYEDEINKRTEMENEFVLIKKDVDEAYMNKVELESRLEGLTDEIN 228
Cdd:COG1196 233 KLRELEAELEELEAELEELEAEL-------EELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIA 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145561 229 FLrqihEEEIRELQSQISDTSVVLSMDNSRSLDMDGIIAEVRAQYEDIANRSRAEAETMYQI--KYEELQTLAGKHGDDL 306
Cdd:COG1196 306 RL----EERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAeeALLEAEAELAEAEEEL 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145561 307 RRTKTEISEMNRNINRLQAEIEALKGQRASLEAAIADAEQRGEMAIKDAQTKLAELEAALQRAKQDMARQLREYQELMNV 386
Cdd:COG1196 382 EELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEAL 461
|
250 260
....*....|....*....|....
gi 114145561 387 KLALDIEITTYRKLLEGEESRLES 410
Cdd:COG1196 462 LELLAELLEEAALLEAALAELLEE 485
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
116-410 |
3.02e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 56.60 E-value: 3.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145561 116 RFLEQQNKMLETKWSLLQQQKTSrsnmdnmFESYINNLRRQLEALGQEKLKLEAELGNMQGLVEDFKNKyedeinkRTEM 195
Cdd:TIGR02168 214 RYKELKAELRELELALLVLRLEE-------LREELEELQEELKEAEEELEELTAELQELEEKLEELRLE-------VSEL 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145561 196 ENEFVLIKKDVDEAYMNKVELESRLegltdeinflrQIHEEEIRELQSQISDTSVVLSMDNSRSLDMDGIIAEVRAQYED 275
Cdd:TIGR02168 280 EEEIEELQKELYALANEISRLEQQK-----------QILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEE 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145561 276 IANRSRAEAETM--YQIKYEELQTLAGKHGDDLRRTKTEISEMNRNINRLQAEIEALKGQRASLEAAIADAEQRG----- 348
Cdd:TIGR02168 349 LKEELESLEAELeeLEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIeellk 428
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 114145561 349 ---EMAIKDAQTKLAELEAALQRAKQDMARQLREYQELMNVKLALDIEITTYRKLLEGEESRLES 410
Cdd:TIGR02168 429 kleEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDS 493
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
142-385 |
3.64e-08 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 55.79 E-value: 3.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145561 142 MDNMFESYINNLRRQLEALGQEKLKLEAELGNMQGLVEDFKNKyedeinkrtemeNEFVLIKKDVDEAYMNKVELESRLE 221
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQK------------NGLVDLSEEAKLLLQQLSELESQLA 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145561 222 GLTDEINFLRQiheeEIRELQSQISDTSVVLSmdnsrSLDMDGIIAEVRAQYEDiANRSRAEAETMYQIKYEELQTLAGK 301
Cdd:COG3206 230 EARAELAEAEA----RLAALRAQLGSGPDALP-----ELLQSPVIQQLRAQLAE-LEAELAELSARYTPNHPDVIALRAQ 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145561 302 hgddLRRTKTEI-SEMNRNINRLQAEIEALKGQRASLEAAIADAEQRgemaikdaQTKLAELEAALQRAKQDMARQLREY 380
Cdd:COG3206 300 ----IAALRAQLqQEAQRILASLEAELEALQAREASLQAQLAQLEAR--------LAELPELEAELRRLEREVEVARELY 367
|
....*
gi 114145561 381 QELMN 385
Cdd:COG3206 368 ESLLQ 372
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
215-410 |
4.29e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 55.71 E-value: 4.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145561 215 ELESRLEGLTDEINFLR-QIHEEEIRELQSQISDTSVVLSMDNSRSLDMDGIIAEVRAQYEDIANRSRAEAETMYQIKyE 293
Cdd:COG1196 217 ELKEELKELEAELLLLKlRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELL-A 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145561 294 ELQTLAGkhgdDLRRTKTEISEMNRNINRLQAEIEALKGQRASLEAAIADAEQRGEMA---IKDAQTKLAELEAALQRAK 370
Cdd:COG1196 296 ELARLEQ----DIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAeeeLEEAEAELAEAEEALLEAE 371
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 114145561 371 QDMARQLREYQELMNVKLALDIEITTYRKLLEGEESRLES 410
Cdd:COG1196 372 AELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEA 411
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
156-379 |
8.39e-08 |
|
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: 54.38 E-value: 8.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145561 156 QLEALGQEKLKLEAELGNMQGLVEDFKNKYEDEINKRTEMENEFVLIKKDVDEAYMNKVELESRLEGLTDEINFLRQihe 235
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA--- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145561 236 eEIRELQSQISDTSVVLSMDNSRSLDM------DGIIAEVRAQYEDIANRSRAEAETMYQIKYEELQTLAgkhgDDLRRT 309
Cdd:COG4942 98 -ELEAQKEELAELLRALYRLGRQPPLAlllspeDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALR----AELEAE 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145561 310 KTEISEMNRNINRLQAEIEALKGQRASLEAAIADAEQRGEMAIKDAQTKLAELEAALQRAKQDMARQLRE 379
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
215-413 |
1.66e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.15 E-value: 1.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145561 215 ELESRLEGLTDEINFLrqihEEEIRELQSQISDtsvvlsmdnsrsldmdgiIAEVRAQYEDIANRSRAEAETMYQIkyEE 294
Cdd:COG4913 614 ALEAELAELEEELAEA----EERLEALEAELDA------------------LQERREALQRLAEYSWDEIDVASAE--RE 669
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145561 295 LQTLAGKHgDDLRRTKTEISEMNRNINRLQAEIEALKGQRASLEAAIADAEQRgemaIKDAQTKLAELEAALQRAKQDMA 374
Cdd:COG4913 670 IAELEAEL-ERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKE----LEQAEEELDELQDRLEAAEDLAR 744
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 114145561 375 RQLREYQELM-----------NVKLALDIEITTYRKLLEGEESRLESGMQ 413
Cdd:COG4913 745 LELRALLEERfaaalgdaverELRENLEERIDALRARLNRAEEELERAMR 794
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
305-381 |
7.26e-07 |
|
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: 51.30 E-value: 7.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145561 305 DLRRTKTEISEMNRNINRLQAEIEALKGQRASLEAAIADAEQR----------GEMAIKDAQTKLAELEAALQRAKQDMA 374
Cdd:COG4942 28 ELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRiraleqelaaLEAELAELEKEIAELRAELEAQKEELA 107
|
....*..
gi 114145561 375 RQLREYQ 381
Cdd:COG4942 108 ELLRALY 114
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
98-402 |
9.86e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.60 E-value: 9.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145561 98 KEQIKSLNNKFASFIDKVRFLEQQNKMLETKWSLLQQQKtsrSNMDNMFESyINNLRRQLEALGQEKLKLEAELGNMQGL 177
Cdd:PRK03918 192 EELIKEKEKELEEVLREINEISSELPELREELEKLEKEV---KELEELKEE-IEELEKELESLEGSKRKLEEKIRELEER 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145561 178 VEDFKNKYED------EINKRTEMENEFVLIKKDVDEAYMNKVELESRLEGLTDEINFL-RQIHE--------EEIRELQ 242
Cdd:PRK03918 268 IEELKKEIEEleekvkELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIeERIKEleekeerlEELKKKL 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145561 243 SQISDTSVVLSMDNSRSLDMDGIIAEVRAQYEDIANRSRAEAETmyqiKYEELQTLAGKHGDDLRRTKTEISEMNRNINR 322
Cdd:PRK03918 348 KELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEK----ELEELEKAKEEIEEEISKITARIGELKKEIKE 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145561 323 LQAEIEALKGQRAS--LEAAIADAEQRGEMaIKDAQTKLAELEAALQRAKqDMARQLREYQELMNVKLALDIEITTYRKL 400
Cdd:PRK03918 424 LKKAIEELKKAKGKcpVCGRELTEEHRKEL-LEEYTAELKRIEKELKEIE-EKERKLRKELRELEKVLKKESELIKLKEL 501
|
..
gi 114145561 401 LE 402
Cdd:PRK03918 502 AE 503
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
216-413 |
3.24e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 49.63 E-value: 3.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145561 216 LESRLEGLTDEinfLRQIhEEEIRELQSQ--ISDTSVVLSMDNSRSLDMDGIIAEVRAQYEDIANRsRAEAETMYQIKYE 293
Cdd:COG3206 180 LEEQLPELRKE---LEEA-EAALEEFRQKngLVDLSEEAKLLLQQLSELESQLAEARAELAEAEAR-LAALRAQLGSGPD 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145561 294 ELQTLAGkhGDDLRRTKTEISEMNRNINRLQA-------EIEALKGQRASLEAAIADAEQRG----EMAIKDAQTKLAEL 362
Cdd:COG3206 255 ALPELLQ--SPVIQQLRAQLAELEAELAELSArytpnhpDVIALRAQIAALRAQLQQEAQRIlaslEAELEALQAREASL 332
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 114145561 363 EAALQRAKQDMARQLREYQELMNVKLALDIEITTYRKLLEG-EESRLESGMQ 413
Cdd:COG3206 333 QAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRlEEARLAEALT 384
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
78-338 |
9.50e-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: 48.53 E-value: 9.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145561 78 LLSPLKLEVDPNIQAVRTQEKEQIKSLNNKFASFIDKVRFLEQQNKMLETKwslLQQQKTSRSNMDnmfeSYINNLRRQL 157
Cdd:TIGR02169 273 LLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEER---LAKLEAEIDKLL----AEIEELEREI 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145561 158 EALGQEKLKLEAElgnmqglVEDFKNKYEDEINKRTEMENEFvlikkdvDEAYMNKVELESRLEGLTDEINflrqiheeE 237
Cdd:TIGR02169 346 EEERKRRDKLTEE-------YAELKEELEDLRAELEEVDKEF-------AETRDELKDYREKLEKLKREIN--------E 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145561 238 IRELQSQISDTSVVLSMDNSR-SLDMDGIIAEVrAQYEDIANRSRAEAETMYQiKYEELQTLAGKHGDDLRRTKTEISEM 316
Cdd:TIGR02169 404 LKRELDRLQEELQRLSEELADlNAAIAGIEAKI-NELEEEKEDKALEIKKQEW-KLEQLAADLSKYEQELYDLKEEYDRV 481
|
250 260
....*....|....*....|..
gi 114145561 317 NRNINRLQAEIEALKGQRASLE 338
Cdd:TIGR02169 482 EKELSKLQRELAEAEAQARASE 503
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
99-374 |
9.83e-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: 48.53 E-value: 9.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145561 99 EQIKSLNNKFASFIDKVRFLEQQNKMLETKWSLLQQQKTSRSNMDNMFESYINNLRRQLEALGQEKLKLEAELGNmqglV 178
Cdd:TIGR02169 681 ERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIEN----V 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145561 179 EDFKNKYEDEINkrtEMENEFVLIKKDVDEAYMNkvELESRLEGLTDEINFLrqihEEEIRELQSQISDTSVVLSMDNSR 258
Cdd:TIGR02169 757 KSELKELEARIE---ELEEDLHKLEEALNDLEAR--LSHSRIPEIQAELSKL----EEEVSRIEARLREIEQKLNRLTLE 827
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145561 259 SLDMDGIIAEVRAQYEDIANRSRAEAETMyqikyEELQTLAGKHGDDLRRTKTEISEMNRNINRLQAEIEALKGQRASLE 338
Cdd:TIGR02169 828 KEYLEKEIQELQEQRIDLKEQIKSIEKEI-----ENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELE 902
|
250 260 270
....*....|....*....|....*....|....*.
gi 114145561 339 AAIADAeqrgEMAIKDAQTKLAELEAALQRAKQDMA 374
Cdd:TIGR02169 903 RKIEEL----EAQIEKKRKRLSELKAKLEALEEELS 934
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
154-382 |
3.27e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.83 E-value: 3.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145561 154 RRQLEALGQEKLKLEAELGNMQGLVEDFKNKYEDEINKRtemenefvlikkdvdeaymnkvELESRLEGLTDEINFLRQi 233
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERR----------------------EALQRLAEYSWDEIDVAS- 665
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145561 234 HEEEIRELQSQISDtsvvlsMDNSrsldmDGIIAEVRAQYEDiANRSRAEAETmyqiKYEELQTLAGKHGDDLRRTKTEI 313
Cdd:COG4913 666 AEREIAELEAELER------LDAS-----SDDLAALEEQLEE-LEAELEELEE----ELDELKGEIGRLEKELEQAEEEL 729
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 114145561 314 SEMNRNINRLQAEIEAlkGQRASLE---AAIADAEQRGEMAiKDAQTKLAELEAALQRAKQDMARQLREYQE 382
Cdd:COG4913 730 DELQDRLEAAEDLARL--ELRALLEerfAAALGDAVERELR-ENLEERIDALRARLNRAEEELERAMRAFNR 798
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
71-375 |
8.27e-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: 45.49 E-value: 8.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145561 71 AVTVNQSLLSPLKLEVDPNIQAVR--TQEKEQIKSLNNKFASF----IDKVRFLEQQNKMLETKWSLLQQQKTSRSNM-- 142
Cdd:pfam15921 511 AIEATNAEITKLRSRVDLKLQELQhlKNEGDHLRNVQTECEALklqmAEKDKVIEILRQQIENMTQLVGQHGRTAGAMqv 590
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145561 143 -DNMFESYINNLRRQLEALGQEKLKLEAELGNMQGLVEDFKNKYEDEINKRTEMENEFVLIKKDVDEAYMNKVELESRLE 221
Cdd:pfam15921 591 eKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELN 670
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145561 222 GLTDEINFL----RQIHEE----------EIRELQSQISDTSVVL-SMDNSrslDMDGIIAEVRAQYEDIANRSRAEAET 286
Cdd:pfam15921 671 SLSEDYEVLkrnfRNKSEEmetttnklkmQLKSAQSELEQTRNTLkSMEGS---DGHAMKVAMGMQKQITAKRGQIDALQ 747
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145561 287 MYQIKYEELQTLAGKHGDDLRRTKT----EISEMNRNINRLQAEIEALKGQRASLEAAIADAeqrgEMAIKDAQTKLAEL 362
Cdd:pfam15921 748 SKIQFLEEAMTNANKEKHFLKEEKNklsqELSTVATEKNKMAGELEVLRSQERRLKEKVANM----EVALDKASLQFAEC 823
|
330
....*....|...
gi 114145561 363 EAALQRAKQDMAR 375
Cdd:pfam15921 824 QDIIQRQEQESVR 836
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
89-343 |
9.59e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 45.05 E-value: 9.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145561 89 NIQAVRTQEKEQIKSLNNKFASFIDKVRFLEQQNKMLETKWSLLQQQKTSRSNMDNMFESYINNLRRQLEALGQEKLKLE 168
Cdd:TIGR02168 744 QLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLR 823
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145561 169 AELGNMQGLVEDFKNKYEDEINKRTEMENEFVLIKKDVDEAYMNKVELESRLEGLTDEinflRQIHEEEIRELQSQISDT 248
Cdd:TIGR02168 824 ERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNE----RASLEEALALLRSELEEL 899
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145561 249 SVVLSMDNSRSLDMDGIIAEVRAQYEDIANR-SRAEAETM---------YQIKYEELQTLAGKHGDDLRRTKTEISEMNR 318
Cdd:TIGR02168 900 SEELRELESKRSELRRELEELREKLAQLELRlEGLEVRIDnlqerlseeYSLTLEEAEALENKIEDDEEEARRRLKRLEN 979
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 114145561 319 NINR---------------------LQAEIEALKGQRASLEAAIAD 343
Cdd:TIGR02168 980 KIKElgpvnlaaieeyeelkerydfLTAQKEDLTEAKETLEEAIEE 1025
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
144-379 |
1.05e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.03 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145561 144 NMFESYINNLRRQLEALGQEKLKLEAELGNMQGLVEDfknkYEDeinKRTEMENefvlIKKDVDEAYMNKVELESRLEGL 223
Cdd:PRK02224 209 NGLESELAELDEEIERYEEQREQARETRDEADEVLEE----HEE---RREELET----LEAEIEDLRETIAETEREREEL 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145561 224 TDEINFLRQIhEEEIRELQSQISDTSVVLSMDNS----RSLDMDGIIAEVRAQYEDI----------ANRSRAEAETMyQ 289
Cdd:PRK02224 278 AEEVRDLRER-LEELEEERDDLLAEAGLDDADAEaveaRREELEDRDEELRDRLEECrvaaqahneeAESLREDADDL-E 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145561 290 IKYEELQTLAGKHGDDLRRTKTEISEMNRNINRLQAEIEALKGQRASLEAAIADAEQRGEMAIK---DAQTKLAELEAAL 366
Cdd:PRK02224 356 ERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREerdELREREAELEATL 435
|
250
....*....|....*
gi 114145561 367 QRAKQDM--ARQLRE 379
Cdd:PRK02224 436 RTARERVeeAEALLE 450
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
91-321 |
1.56e-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: 44.66 E-value: 1.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145561 91 QAVRTQEKEQIKSLNNKFASFIDKVRFLEQQNKMLETKWSLLQQQKTSRSNMDNMFESYINNLRRQ-LEALGQEKLKLEA 169
Cdd:TIGR01612 1161 KAISNDDPEEIEKKIENIVTKIDKKKNIYDEIKKLLNEIAEIEKDKTSLEEVKGINLSYGKNLGKLfLEKIDEEKKKSEH 1240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145561 170 ELGNMQGLVEDFknkyeDEINKRTEMENEFVLIKKDVDeAYMNKVELESRLEgltDEINFLRQIHEEEIrelqSQISDTS 249
Cdd:TIGR01612 1241 MIKAMEAYIEDL-----DEIKEKSPEIENEMGIEMDIK-AEMETFNISHDDD---KDHHIISKKHDENI----SDIREKS 1307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145561 250 VVLSMDNSRSLDMDGI-------IAEVRAQYEDIaNRSRAEAETMYQI-KYEELQTLAgkhgDDLRRTKTEISEMNRNIN 321
Cdd:TIGR01612 1308 LKIIEDFSEESDINDIkkelqknLLDAQKHNSDI-NLYLNEIANIYNIlKLNKIKKII----DEVKEYTKEIEENNKNIK 1382
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
98-410 |
1.77e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 44.24 E-value: 1.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145561 98 KEQIKSLNNKFASFIDKVRFLEQQNKMLETKWSLLQQQKTSRSNMDNMFESYINNLRRQLEALGQEKLKLEAELGNMQGL 177
Cdd:TIGR04523 130 EKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKK 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145561 178 VEDFKnKYEDEINkrtEMENEFVLIKKDVDEAYMNKVELESRLEGLTDEINFLRQIHEEEIRELQSQISDtsvvLSMDNS 257
Cdd:TIGR04523 210 IQKNK-SLESQIS---ELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKE----LEQNNK 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145561 258 RSLDMDGIIAEVRAQYEDIANRsrAEAETMYQIKyEELQtlagKHGDDLRRTKTEISEMNRNINRLQA------------ 325
Cdd:TIGR04523 282 KIKELEKQLNQLKSEISDLNNQ--KEQDWNKELK-SELK----NQEKKLEEIQNQISQNNKIISQLNEqisqlkkeltns 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145561 326 ------------------------------EIEALKGQRASLEAAIADAE---QRGEMAIKDAQTKLAELEAALQRAKQD 372
Cdd:TIGR04523 355 esensekqreleekqneieklkkenqsykqEIKNLESQINDLESKIQNQEklnQQKDEQIKKLQQEKELLEKEIERLKET 434
|
330 340 350
....*....|....*....|....*....|....*...
gi 114145561 373 MARQLREYQELMNVKLALDIEITTYRKLLEGEESRLES 410
Cdd:TIGR04523 435 IIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKV 472
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
215-384 |
1.81e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.99 E-value: 1.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145561 215 ELESRLEGLTDEINFLRQIHEE-EIRELQSQISDtsvVLSMDNSRSLDMDGIIAEVRAQYEDIANRsRAEAETMYQIKYE 293
Cdd:COG4717 341 ELLDRIEELQELLREAEELEEElQLEELEQEIAA---LLAEAGVEDEEELRAALEQAEEYQELKEE-LEELEEQLEELLG 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145561 294 ELQTLAGKHgdDLRRTKTEISEMNRNINRLQAEIEALKGQRASLEAAIADAEQRGEmaikdaqtkLAELEAALQRAKQDM 373
Cdd:COG4717 417 ELEELLEAL--DEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGE---------LAELLQELEELKAEL 485
|
170
....*....|.
gi 114145561 374 ARQLREYQELM 384
Cdd:COG4717 486 RELAEEWAALK 496
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
147-371 |
1.97e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.67 E-value: 1.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145561 147 ESYINNLRRQLEALGQEKLKLEAELGNMQGLVEDFKNKYEDEINKRTEMENEFVLIKKDVDEAymnkvelESRLEGLTDE 226
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEA-------EAEIEERREE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145561 227 InflrqihEEEIRELQSQISDTSVVLSMDNSRSLD-----MDGIIAEVRAQYEDIANRSRAEAEtmyqikYEELQTLAGK 301
Cdd:COG3883 88 L-------GERARALYRSGGSVSYLDVLLGSESFSdfldrLSALSKIADADADLLEELKADKAE------LEAKKAELEA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145561 302 HGDDLRRTKTEISEMNRNINRLQAEIEALKGQRASLEAAIADAEQRGEMAIKDAQTKLAELEAALQRAKQ 371
Cdd:COG3883 155 KLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAA 224
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
113-379 |
2.16e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 43.85 E-value: 2.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145561 113 DKVRFLEQQNKMLETKWSLLQQQKtsrsnmdNMFESYINNLRRQLEALGQEKlkleaelgnmqglvedfKNKYEDEINkr 192
Cdd:PHA02562 174 DKIRELNQQIQTLDMKIDHIQQQI-------KTYNKNIEEQRKKNGENIARK-----------------QNKYDELVE-- 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145561 193 tEMENefvlIKKDVDEAYMNKVELESRLEGLTDEINFLRQiheeEIRELQSQISDTSVVLSMdnsrsLDMDGIIAEVRAQ 272
Cdd:PHA02562 228 -EAKT----IKAEIEELTDELLNLVMDIEDPSAALNKLNT----AAAKIKSKIEQFQKVIKM-----YEKGGVCPTCTQQ 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145561 273 YEDIANRSRAEAETM--YQIKYEELQTlagkHGDDLRRTKTEISEMNRNINRLQAEIEALKGQRASLEAAIADAE---QR 347
Cdd:PHA02562 294 ISEGPDRITKIKDKLkeLQHSLEKLDT----AIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKaaiEE 369
|
250 260 270
....*....|....*....|....*....|..
gi 114145561 348 GEMAIKDAQTKLAELEAALQRAKQDMARQLRE 379
Cdd:PHA02562 370 LQAEFVDNAEELAKLQDELDKIVKTKSELVKE 401
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
94-384 |
2.67e-04 |
|
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: 43.35 E-value: 2.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145561 94 RTQEKEQIKSLNNKFASFIDKVRFLEQQNKMLETKWSLLQQQKTSRSNMDNMFESYINNLRRQLEALGQEKLKLEAELGN 173
Cdd:pfam07888 75 RRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELER 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145561 174 MQGLVEDFKNKYEDEINKRTEMEN-------EFVLIKKDVDEAYMNKVELESRLEGLTDEINFLRQI------HEEEIRE 240
Cdd:pfam07888 155 MKERAKKAGAQRKEEEAERKQLQAklqqteeELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKlttahrKEAENEA 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145561 241 LQSQISDTSVVLSMDNSRSLDMDGIIAEVRAQyedianRSRAEAEtMYQIKYEELQ--------TLAGKHG--------D 304
Cdd:pfam07888 235 LLEELRSLQERLNASERKVEGLGEELSSMAAQ------RDRTQAE-LHQARLQAAQltlqladaSLALREGrarwaqerE 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145561 305 DLRRT----KTEISEMNRNINRLQAEIEALKGQRASLEAAIADAEQRGEMAIKDAQTKLAELEAALQRAKQDMARQLREY 380
Cdd:pfam07888 308 TLQQSaeadKDRIEKLSAELQRLEERLQEERMEREKLEVELGREKDCNRVQLSESRRELQELKASLRVAQKEKEQLQAEK 387
|
....
gi 114145561 381 QELM 384
Cdd:pfam07888 388 QELL 391
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
118-376 |
4.45e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 42.85 E-value: 4.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145561 118 LEQQNKMLETKWSLLQQQKTSRSNMDNMFESyinnLRRQLEALGQEklkLEAELGNMQGLVEDFKNKYEDEINKRTEMEN 197
Cdd:pfam01576 31 LEKKHQQLCEEKNALQEQLQAETELCAEAEE----MRARLAARKQE---LEEILHELESRLEEEEERSQQLQNEKKKMQQ 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145561 198 EFVLIKKDVDEA-------YMNKVELESRLEGLTDEINFLRQIHEEEIRE---LQSQISDTSVVLSMDNSRSLDMDGIIA 267
Cdd:pfam01576 104 HIQDLEEQLDEEeaarqklQLEKVTTEAKIKKLEEDILLLEDQNSKLSKErklLEERISEFTSNLAEEEEKAKSLSKLKN 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145561 268 EVRAQYEDIANRSRAEAETmyqikYEELQTLAgkhgddlRRTKTEISEMNRNINRLQAEIEALKGQRASLEAAIADAEQR 347
Cdd:pfam01576 184 KHEAMISDLEERLKKEEKG-----RQELEKAK-------RKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALAR 251
|
250 260 270
....*....|....*....|....*....|..
gi 114145561 348 GE---MAIKDAQTKLAELEAALQRAKQDMARQ 376
Cdd:pfam01576 252 LEeetAQKNNALKKIRELEAQISELQEDLESE 283
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
150-410 |
4.70e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 42.72 E-value: 4.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145561 150 INNLRRQLEALGQEKLKLEAELGnmqglVEDFKNkyEDEINKRTEMENEFVLIKKDVDEAYMNKVELESRLEGLTDEINF 229
Cdd:PRK02224 281 VRDLRERLEELEEERDDLLAEAG-----LDDADA--EAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADD 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145561 230 LRQIHE---EEIRELQSQISDTSVVLSMDNSRSLDMDGIIAEVRAQYEDIANRsRAEAETMYQIKYEELQTLAGKHGDdl 306
Cdd:PRK02224 354 LEERAEelrEEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVD-LGNAEDFLEELREERDELREREAE-- 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145561 307 rrTKTEISEMNRNINRLQAEIEALK----GQ---RASLEAAIADAEQRG---EMAIKDAQTKLAELEAALQRAKqDMARQ 376
Cdd:PRK02224 431 --LEATLRTARERVEEAEALLEAGKcpecGQpveGSPHVETIEEDRERVeelEAELEDLEEEVEEVEERLERAE-DLVEA 507
|
250 260 270
....*....|....*....|....*....|....
gi 114145561 377 LREYQELMNVKLALDIEITTYRKLLEGEESRLES 410
Cdd:PRK02224 508 EDRIERLEERREDLEELIAERRETIEEKRERAEE 541
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
150-347 |
7.32e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.06 E-value: 7.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145561 150 INNLRRQLEALGQEKLKLEAELGNMQGLVEDFKNKYEDEINKRTEMENefVLIKKDVDEAYMNKVELESRLEGLTDEINF 229
Cdd:COG4717 73 LKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEK--LEKLLQLLPLYQELEALEAELAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145561 230 LRQiHEEEIRELQSQIsdtsvvlsmdnsrsldmdgiiAEVRAQYEDIANRSRAEAETMYQIKYEELQTLAgkhgDDLRRT 309
Cdd:COG4717 151 LEE-RLEELRELEEEL---------------------EELEAELAELQEELEELLEQLSLATEEELQDLA----EELEEL 204
|
170 180 190
....*....|....*....|....*....|....*...
gi 114145561 310 KTEISEMNRNINRLQAEIEALKGQRASLEAAIADAEQR 347
Cdd:COG4717 205 QQRLAELEEELEEAQEELEELEEELEQLENELEAAALE 242
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
90-320 |
1.11e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 41.96 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145561 90 IQAVRTQEKEQIKSLNNK---FASFIDKVRFLEQQNKMLE--TKWSLLQQQK----------TSRSNMDNMFESYINNLR 154
Cdd:TIGR01612 598 INKLKLELKEKIKNISDKneyIKKAIDLKKIIENNNAYIDelAKISPYQVPEhlknkdkiysTIKSELSKIYEDDIDALY 677
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145561 155 RQLEALGQEKLKLEAElgnMQGLVEDFKNKYEDEINKRTEMENEFVLIKKDVDEAYMNK-----VELESRLEG-LTDEIN 228
Cdd:TIGR01612 678 NELSSIVKENAIDNTE---DKAKLDDLKSKIDKEYDKIQNMETATVELHLSNIENKKNElldiiVEIKKHIHGeINKDLN 754
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145561 229 FLRQIHEEEIRELQSQISDtsvvLSMDNSRSLDMDGIIAEVRAQYED---IANRSRAEAETMYQIKYEELQTLAGKHgDD 305
Cdd:TIGR01612 755 KILEDFKNKEKELSNKIND----YAKEKDELNKYKSKISEIKNHYNDqinIDNIKDEDAKQNYDKSKEYIKTISIKE-DE 829
|
250
....*....|....*
gi 114145561 306 LRRTKTEISEMNRNI 320
Cdd:TIGR01612 830 IFKIINEMKFMKDDF 844
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
126-347 |
1.12e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 41.64 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145561 126 ETKWSLLQQQKTSRSNMDNMFESYINNLRRQLEALGQEKLKLEAELGNM----QGLVE------DFKNKYEDEINKRT-E 194
Cdd:pfam15921 390 EKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMksecQGQMErqmaaiQGKNESLEKVSSLTaQ 469
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145561 195 MENEFVLIKKDVDEAYMNKVELESRLEGLTDEINFLRQiHEEEIRELQSQISD--TSVVLSMDNSRSLDMDG-----IIA 267
Cdd:pfam15921 470 LESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQE-KERAIEATNAEITKlrSRVDLKLQELQHLKNEGdhlrnVQT 548
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145561 268 EVRAQYEDIANRSRAEAETMYQIkyEELQTLAGKHGDDLRRTKTEISEMNRNINRLQAEIEALKGQRASLEAAIADAEQR 347
Cdd:pfam15921 549 ECEALKLQMAEKDKVIEILRQQI--ENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEAR 626
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
305-408 |
1.15e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 40.68 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145561 305 DLRRTKTEISEMNRNINRLQAEIEALKGQRASLEAAIADAEQR---GEMAIKDAQTKLAELEAALQR--AKQDMARQLRE 379
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTEledLEKEIKRLELEIEEVEARIKKyeEQLGNVRNNKE 90
|
90 100
....*....|....*....|....*....
gi 114145561 380 YQelmnvklALDIEITTYRKLLEGEESRL 408
Cdd:COG1579 91 YE-------ALQKEIESLKRRISDLEDEI 112
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
198-399 |
1.16e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.82 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145561 198 EFVLIKKDVDEA-------YMNKVELESRLEGLTDEINFLRQI--HEEEIRELQSQISDTSVVLSM-----DNSRSLDMD 263
Cdd:COG4913 215 EYMLEEPDTFEAadalvehFDDLERAHEALEDAREQIELLEPIreLAERYAAARERLAELEYLRAAlrlwfAQRRLELLE 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145561 264 GIIAEVRAQYEDIANRsRAEAETMYQIKYEELQTLAGKH----GDDLRRTKTEISEMNRNINRLQAEIEALKGQRASLEA 339
Cdd:COG4913 295 AELEELRAELARLEAE-LERLEARLDALREELDELEAQIrgngGDRLEQLEREIERLERELEERERRRARLEALLAALGL 373
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145561 340 AIADAEQRGEMAIKDAQTKLAELEAALQRAKQDMARQLREYQELMNVKLALDIEITTYRK 399
Cdd:COG4913 374 PLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLER 433
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
276-373 |
1.26e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.97 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145561 276 IANRSRAEAETMYQIKYEELQTLAGKHGD---DLRRTKTEISEMNRNINRLQAEIEALKGQRASLEAAIADAEQRgemaI 352
Cdd:COG3883 6 LAAPTPAFADPQIQAKQKELSELQAELEAaqaELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAE----I 81
|
90 100
....*....|....*....|.
gi 114145561 353 KDAQTKLAELEAALQRAKQDM 373
Cdd:COG3883 82 EERREELGERARALYRSGGSV 102
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
95-387 |
1.80e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 40.77 E-value: 1.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145561 95 TQEKEQIKSLNNKFASFIDKVRFLEQQNKMLETKwslLQQQKTSRSNMDNmfesyinnlrrQLEALGQEKLKLEAELGNM 174
Cdd:TIGR04523 366 EEKQNEIEKLKKENQSYKQEIKNLESQINDLESK---IQNQEKLNQQKDE-----------QIKKLQQEKELLEKEIERL 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145561 175 QGLVEDFKNKYEDEINKRTEMENEFVLIKKDVDeaymnkvELESRLEGLTDEINFLRQIHEEEIRELQSQISDtsvvLSM 254
Cdd:TIGR04523 432 KETIIKNNSEIKDLTNQDSVKELIIKNLDNTRE-------SLETQLKVLSRSINKIKQNLEQKQKELKSKEKE----LKK 500
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145561 255 DNSRSLDMDGIIAEVRAQYEDIANRSRAEAETMYQIKYE--ELQTLAGKHGDDLRRT--KTEISEMNRNINRLQAEIEAL 330
Cdd:TIGR04523 501 LNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKisDLEDELNKDDFELKKEnlEKEIDEKNKEIEELKQTQKSL 580
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 114145561 331 KGQRASLEAAIADAEQRgemaIKDAQTKLAELEAALQRAKQDMARQLREYQELMNVK 387
Cdd:TIGR04523 581 KKKQEEKQELIDQKEKE----KKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSII 633
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
301-403 |
1.85e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.05 E-value: 1.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145561 301 KHGDDLRRTKTEISEMNRNINRLQaEIEALKGQRASLEAAIADAEQRGEMA-IKDAQTKLAELEAALQRAKQDMARQLRE 379
Cdd:COG4913 232 EHFDDLERAHEALEDAREQIELLE-PIRELAERYAAARERLAELEYLRAALrLWFAQRRLELLEAELEELRAELARLEAE 310
|
90 100
....*....|....*....|....
gi 114145561 380 YQELMNVKLALDIEITTYRKLLEG 403
Cdd:COG4913 311 LERLEARLDALREELDELEAQIRG 334
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
215-382 |
2.25e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 39.52 E-value: 2.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145561 215 ELESRLegltDEINFLRQIHEEEIRELQSQISDtsvvlsmdnsrsldMDGIIAEVRAQYEDIaNRSRAEAETmyqiKYEE 294
Cdd:COG1579 14 ELDSEL----DRLEHRLKELPAELAELEDELAA--------------LEARLEAAKTELEDL-EKEIKRLEL----EIEE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145561 295 LQTLAGKHGDDLRRTKTeisemNRNINRLQAEIEALKGQRASLEAAIADAEQRgemaIKDAQTKLAELEAALQRAKQDMA 374
Cdd:COG1579 71 VEARIKKYEEQLGNVRN-----NKEYEALQKEIESLKRRISDLEDEILELMER----IEELEEELAELEAELAELEAELE 141
|
....*...
gi 114145561 375 RQLREYQE 382
Cdd:COG1579 142 EKKAELDE 149
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
91-351 |
2.70e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.28 E-value: 2.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145561 91 QAVRTQEK----EQIKSLNNKFASFIDKVRFLEQQNKML-----ETKWSLLQQQktsrsnmdnmfesyINNLRRQLEALG 161
Cdd:COG4913 243 ALEDAREQiellEPIRELAERYAAARERLAELEYLRAALrlwfaQRRLELLEAE--------------LEELRAELARLE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145561 162 QEKLKLEAELGNMQGLVEDFKNKYEDEINKRTEmenefvlikkdvdeaymnkvELESRLEGLTDEinflRQIHEEEIREL 241
Cdd:COG4913 309 AELERLEARLDALREELDELEAQIRGNGGDRLE--------------------QLEREIERLERE----LEERERRRARL 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145561 242 QSQIsdtsvvlsmdnsRSLDMDgiIAEVRAQYEDIANRSRAEAetmyqikyEELQTLAGKHGDDLRRTKTEISEMNRNIN 321
Cdd:COG4913 365 EALL------------AALGLP--LPASAEEFAALRAEAAALL--------EALEEELEALEEALAEAEAALRDLRRELR 422
|
250 260 270
....*....|....*....|....*....|
gi 114145561 322 RLQAEIEALKGQRASLEAAIADAeqRGEMA 351
Cdd:COG4913 423 ELEAEIASLERRKSNIPARLLAL--RDALA 450
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
90-414 |
3.50e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 39.92 E-value: 3.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145561 90 IQAVRTQEKEQIKSLNNKFASFIDKVRFLEQQNKMLETKWSLLQQQKTSRSNMDNMFESYINNLRRQLEALGQEKLKLEA 169
Cdd:COG1196 258 LEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEE 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145561 170 ELGNMQGLVEDFKNKYEDEINKRTEMENEfvlikkdvdeaymnKVELESRLEGLTDEINFLRQIHEEEIRELQSQISDts 249
Cdd:COG1196 338 ELEELEEELEEAEEELEEAEAELAEAEEA--------------LLEAEAELAEAEEELEELAEELLEALRAAAELAAQ-- 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145561 250 vvlsmdnsrsldmdgiIAEVRAQYEDIANRsRAEAETMYQIKYEELQTLAgkhgDDLRRTKTEISEMNRNINRLQAEIEA 329
Cdd:COG1196 402 ----------------LEELEEAEEALLER-LERLEEELEELEEALAELE----EEEEEEEEALEEAAEEEAELEEEEEA 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145561 330 LKGQRASLEAAIADAEQRGEMAIKDAQTKLAELEAALQRAKQDM-----ARQLREYQELMNVKLALDIEITTYRKLLEGE 404
Cdd:COG1196 461 LLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEgflegVKAALLLAGLRGLAGAVAVLIGVEAAYEAAL 540
|
330
....*....|
gi 114145561 405 ESRLESGMQN 414
Cdd:COG1196 541 EAALAAALQN 550
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
253-372 |
3.79e-03 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 40.20 E-value: 3.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145561 253 SMDNSRSLDMDGIiAEVRAQYEDIANR---SRAEAETMyQIKYEELQTLAGKHGDDlRRTKTEISEMNRNINRLQAEIEA 329
Cdd:NF012221 1661 QLDDAKKISGKQL-ADAKQRHVDNQQKvkdAVAKSEAG-VAQGEQNQANAEQDIDD-AKADAEKRKDDALAKQNEAQQAE 1737
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 114145561 330 LKGqraslEAAIADAEQRGEMAIKDAQTKLAELEAALQRAKQD 372
Cdd:NF012221 1738 SDA-----NAAANDAQSRGEQDASAAENKANQAQADAKGAKQD 1775
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
98-383 |
4.14e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 39.66 E-value: 4.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145561 98 KEQIKSLNNKFASFIDKVRFLEQQNKMLETKwsLLQQQKTSRsnMDNMFESyINNLRRQLEALGQEKLKLEAEL-----G 172
Cdd:PRK03918 458 TAELKRIEKELKEIEEKERKLRKELRELEKV--LKKESELIK--LKELAEQ-LKELEEKLKKYNLEELEKKAEEyeklkE 532
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145561 173 NMQGLVEDFKNkYEDEINKRTEMENEFVLIKKDVDEAYMNKVELESRL--------EGLTDEINFLRQIHEE-------- 236
Cdd:PRK03918 533 KLIKLKGEIKS-LKKELEKLEELKKKLAELEKKLDELEEELAELLKELeelgfesvEELEERLKELEPFYNEylelkdae 611
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145561 237 -EIRELQSQISDTSVVLSMDNSRSLDMDGIIAEVRAQYEDIanrsraeaetmyQIKYEElqtlagkhgDDLRRTKTEISE 315
Cdd:PRK03918 612 kELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEEL------------EKKYSE---------EEYEELREEYLE 670
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 114145561 316 MNRNINRLQAEIEALKGQRASLEAAIADAEQRGEmAIKDAQTKLAELEAALQRAkQDMARQLREYQEL 383
Cdd:PRK03918 671 LSRELAGLRAELEELEKRREEIKKTLEKLKEELE-EREKAKKELEKLEKALERV-EELREKVKKYKAL 736
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
111-384 |
5.27e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 39.42 E-value: 5.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145561 111 FIDKVRFLEQQNKMLETKWSLLQQQKTSRsnmdnmfESYINNLRRQLEALGQEKLKLEAELGNMQGLVEDFK---NKYED 187
Cdd:pfam10174 466 RLEELESLKKENKDLKEKVSALQPELTEK-------ESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKeecSKLEN 538
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145561 188 EINKRTEMEN------EFVL--------IKKDVDEAYMNKVELEsRLEGLTDEINFLRQIHEEEIRELQSQISDTSVVLS 253
Cdd:pfam10174 539 QLKKAHNAEEavrtnpEINDrirlleqeVARYKEESGKAQAEVE-RLLGILREVENEKNDKDKKIAELESLTLRQMKEQN 617
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145561 254 MDNSRSLDMDGIIAEVRAQ-YEDIANRSRAEAETMYQIKYEELQTLAGKHGDDLRRTKTEISEMNRNINRLQAEIEALKG 332
Cdd:pfam10174 618 KKVANIKHGQQEMKKKGAQlLEEARRREDNLADNSQQLQLEELMGALEKTRQELDATKARLSSTQQSLAEKDGHLTNLRA 697
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 114145561 333 QRASLEAAIADAEQRGEMAI---KDAQTKLAELEAALQRAKQDMARQL-REYQELM 384
Cdd:pfam10174 698 ERRKQLEEILEMKQEALLAAiseKDANIALLELSSSKKKKTQEEVMALkREKDRLV 753
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
144-358 |
5.30e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 39.53 E-value: 5.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145561 144 NMFEsyINNLRRQLEAL-GQEKLKLEAELGNMQGLVEDFKNKYEdeINKRTEMENEFVLIKKDVDEAYMNKVELESRLEG 222
Cdd:PRK05771 29 GVVH--IEDLKEELSNErLRKLRSLLTKLSEALDKLRSYLPKLN--PLREEKKKVSVKSLEELIKDVEEELEKIEKEIKE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145561 223 LTDEINFLrqihEEEIRELQSQISD-------------------TSVVLSMDNSRSLDMDGIIAEVRAQYED-------- 275
Cdd:PRK05771 105 LEEEISEL----ENEIKELEQEIERlepwgnfdldlslllgfkyVSVFVGTVPEDKLEELKLESDVENVEYIstdkgyvy 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145561 276 --IANRSRAEAETMYQIK---YEELQTLAGKHGDD-LRRTKTEISEMNRNINRLQAEIEALKGQRASLEAAIADA----E 345
Cdd:PRK05771 181 vvVVVLKELSDEVEEELKklgFERLELEEEGTPSElIREIKEELEEIEKERESLLEELKELAKKYLEELLALYEYleieL 260
|
250
....*....|...
gi 114145561 346 QRGEMAIKDAQTK 358
Cdd:PRK05771 261 ERAEALSKFLKTD 273
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
147-240 |
5.80e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 39.07 E-value: 5.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145561 147 ESYINNLRRQLEALGQEKLKLEAELgnmqglvEDFKNKYEDEINKRTE---MENEFVLIKKDVDeaymnkvELESRLEGL 223
Cdd:COG2433 426 EAEVEELEAELEEKDERIERLEREL-------SEARSEERREIRKDREisrLDREIERLERELE-------EERERIEEL 491
|
90
....*....|....*..
gi 114145561 224 TDEINFLRQIHEEEIRE 240
Cdd:COG2433 492 KRKLERLKELWKLEHSG 508
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
307-409 |
6.81e-03 |
|
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: 39.27 E-value: 6.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145561 307 RRTKTEISEMNRNINRLQAEIEALKGQRASLEAAIADAE---QRGEMAIKDAQTKLAELEAALQRAKQDMARQLREYQEL 383
Cdd:TIGR02168 666 AKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRkelEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQL 745
|
90 100
....*....|....*....|....*.
gi 114145561 384 MNVKLALDIEITTYRKLLEGEESRLE 409
Cdd:TIGR02168 746 EERIAQLSKELTELEAEIEELEERLE 771
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
266-409 |
9.06e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 37.98 E-value: 9.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114145561 266 IAEVRAQYEDIANRsRAEAETmyqiKYEELQTLAGKHGDDLRRTKTEISEMNRNINRLQAEIEALKGQR--ASLEAAIAD 343
Cdd:COG1579 26 LKELPAELAELEDE-LAALEA----RLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKeyEALQKEIES 100
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 114145561 344 AEQR---GEMAIKDAQTKLAELEAALQRAKQDMARQLREYQELmnvKLALDIEITTYRKLLEGEESRLE 409
Cdd:COG1579 101 LKRRisdLEDEILELMERIEELEEELAELEAELAELEAELEEK---KAELDEELAELEAELEELEAERE 166
|
|
| |
