|
Name |
Accession |
Description |
Interval |
E-value |
| Filament |
pfam00038 |
Intermediate filament protein; |
44-386 |
5.26e-40 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 147.76 E-value: 5.26e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506429 44 QEKDHLTSLNSRLATYIDKVRQLEQENNRLQVQIRDIEVVEKKEKSNLADRFEAEKARLRRALDSAQDELAKYRIEYDAA 123
Cdd:pfam00038 1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506429 124 KVEVKKLKpqvEKLERELagaeeqalhaqsiadqsqakqktlqarNDKLVVENDdlkkqnitlrdtVEGLKKAVEDETLL 203
Cdd:pfam00038 81 RLAAEDFR---QKYEDEL---------------------------NLRTSAEND------------LVGLRKDLDEATLA 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506429 204 RTAANNKIKALEEDLAFALQQHKGELEEVRhkRQVDMTTYAKQINDEYQSKLQDQIEEMRAQFKNNLHQNKTAFEDAYKN 283
Cdd:pfam00038 119 RVDLEAKIESLKEELAFLKKNHEEEVRELQ--AQVSDTQVNVEMDAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQS 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506429 284 K---LNAARERQEEAV----SEAIHLRARVRDLETSSSG----NASLIERLRSELDTLKR---SFQEKLDDKDARIAELN 349
Cdd:pfam00038 197 KleeLQQAAARNGDALrsakEEITELRRTIQSLEIELQSlkkqKASLERQLAETEERYELqlaDYQELISELEAELQETR 276
|
330 340 350
....*....|....*....|....*....|....*..
gi 17506429 350 QEIERMMSEFHDLLDVKIQLDAELKTYQALLEGEEER 386
Cdd:pfam00038 277 QEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
|
|
| LTD |
pfam00932 |
Lamin Tail Domain; The lamin-tail domain (LTD), which has an immunoglobulin (Ig) fold, is ... |
443-547 |
5.00e-12 |
|
Lamin Tail Domain; The lamin-tail domain (LTD), which has an immunoglobulin (Ig) fold, is found in Nuclear Lamins, Chlo1887 from Chloroflexus, and several bacterial proteins where it occurs with membrane associated hydrolases of the metallo-beta-lactamase,synaptojanin, and calcineurin-like phosphoesterase superfamilies.
Pssm-ID: 460003 [Multi-domain] Cd Length: 108 Bit Score: 62.44 E-value: 5.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506429 443 TVGPVGIDEVDEEG-----KWVRVANNSEEEQSIGGYKLVVKAGNkeaSFQFSSRMKLAPHASATVWSAD----AGAVHH 513
Cdd:pfam00932 3 ATGDVVISEVVYDGsggndEFIELYNTGSKAVDLSGWKLQDASGG---TYTFPNGTTLAPGQTVVVWTGSgtnsATAGYW 79
|
90 100 110
....*....|....*....|....*....|....
gi 17506429 514 PPEVYVMKkqqwpiGDNPSARLEDSEGDTVSSIT 547
Cdd:pfam00932 80 GPSNAVWN------NGGDAVALYDANGELVDSVG 107
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
43-342 |
1.62e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 64.19 E-value: 1.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506429 43 LQEKDHLTSLNSRLATYIDKVRQLEQENNRLQVQIRDIEVVEKKeksnlADRFEAEKARLRRALDSAQDELAKYRIEYDA 122
Cdd:COG1196 218 LKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAE-----LAELEAELEELRLELEELELELEEAQAEEYE 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506429 123 AKVEVKKLKPQVEKLERELAGAEEQALHAQSIADQSQAKQKTLQARNDKLVVENDDLKKQNITLRDTVEGLKKAVEDETL 202
Cdd:COG1196 293 LLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506429 203 LRTAANNKIKALEEDLAFALQQHKGELEEVRHKRQvdmttyAKQINDEYQSKLQDQIEEMRAQFKNNLHQnktafEDAYK 282
Cdd:COG1196 373 ELAEAEEELEELAEELLEALRAAAELAAQLEELEE------AEEALLERLERLEEELEELEEALAELEEE-----EEEEE 441
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506429 283 NKLNAARERQEEAVSEAIHLRARVRDLETSSSGNASLIERLRSELDTLKRSFQEKLDDKD 342
Cdd:COG1196 442 EALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEA 501
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
28-392 |
2.75e-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: 63.54 E-value: 2.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506429 28 GGDDSFGSTLLETSR----LQEK-----DHLTSLNSRLATYIDKVRQLEQENNRLQVQIRDIEVVEKKEKSNLAdRFEAE 98
Cdd:TIGR02168 663 GGSAKTNSSILERRReieeLEEKieeleEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLA-RLEAE 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506429 99 KARLRRALDSAQDELAKYRIEYDAAKVEVKKLKPQVEKLERELAGAEEQALHAQSIADQS-------------------- 158
Cdd:TIGR02168 742 VEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALrealdelraeltllneeaan 821
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506429 159 -QAKQKTLQARNDKLVVENDDLKKQNITLRDTVEGLKKAVEDETLLRTAANNKIKALEEDLA---FALQQHKGELEEVRH 234
Cdd:TIGR02168 822 lRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERAsleEALALLRSELEELSE 901
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506429 235 KRQvDMTTYAKQINDEYQsKLQDQIEEMR---AQFKNNLHQNKTAFEDAYKNKLNAARERQEEAVSEAIHLRARVRDLET 311
Cdd:TIGR02168 902 ELR-ELESKRSELRRELE-ELREKLAQLElrlEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLEN 979
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506429 312 S--SSGNASL-----IERLRSELDTLKRSFqEKLDDKDARIAELNQEIERMMSE-FHDLLDvkiQLDAEL-KTYQALLEG 382
Cdd:TIGR02168 980 KikELGPVNLaaieeYEELKERYDFLTAQK-EDLTEAKETLEEAIEEIDREARErFKDTFD---QVNENFqRVFPKLFGG 1055
|
410
....*....|
gi 17506429 383 EEERLNLTQE 392
Cdd:TIGR02168 1056 GEAELRLTDP 1065
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
62-387 |
6.58e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 62.26 E-value: 6.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506429 62 KVRQLEQENNRLQVQIRdieVVEKKEKSNLADRFEAEKARLRRALDSAQDELAKYRIEYDAAKVEVKKLKPQVEKLEREL 141
Cdd:COG1196 214 RYRELKEELKELEAELL---LLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEE 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506429 142 AGAEEQALHAQSIADQSQAKQKTLQARNDKLVVENDDLKKQNITLRDTVEGLKKAVEDETLLRTAANNKIKALEEDLAFA 221
Cdd:COG1196 291 YELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEA 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506429 222 LQQHKGELEEVRHKRQVDMTTYAKQINdeyqskLQDQIEEMRAQFKNNLHQnktafedayKNKLNAARERQEEAVSEAIH 301
Cdd:COG1196 371 EAELAEAEEELEELAEELLEALRAAAE------LAAQLEELEEAEEALLER---------LERLEEELEELEEALAELEE 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506429 302 LRARVRDLETSSSGNASLIERLRSELDTLKRSFQEKLDDKDARIAELNQEIERMMSEFHDLLDVKIQLDAELKTYQALLE 381
Cdd:COG1196 436 EEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALL 515
|
....*.
gi 17506429 382 GEEERL 387
Cdd:COG1196 516 LAGLRG 521
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
37-348 |
3.87e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.57 E-value: 3.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506429 37 LLETSRLQEKDHLTSLNSRLATYIDKVRQLEQENNRLQvQIRDIEVVEKKEKSNLADRFEAEKARLRRALDSAQDELAKY 116
Cdd:COG1196 264 ELEAELEELRLELEELELELEEAQAEEYELLAELARLE-QDIARLEERRRELEERLEELEEELAELEEELEELEEELEEL 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506429 117 RIEYDAAKVEVKKLKPQVEKLERELAGAEEQALHAQSIADQSQAKQKTLQARNDKLVVENDDLKKQNITLRDTVEGLKKA 196
Cdd:COG1196 343 EEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEE 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506429 197 VEDETLLRTAANNKIKALEEDLAFA---LQQHKGELEEVRHKRQVDMTTYAKQINDEYQSKLQDQIEEMRAQFKNNLHQN 273
Cdd:COG1196 423 LEELEEALAELEEEEEEEEEALEEAaeeEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEAD 502
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17506429 274 KTAFEDAYKN-KLNAARERQEEAVSEAIHLRARVRDLETSSSGnASLIERLRSELDTLKRSFQEKLDDKDARIAEL 348
Cdd:COG1196 503 YEGFLEGVKAaLLLAGLRGLAGAVAVLIGVEAAYEAALEAALA-AALQNIVVEDDEVAAAAIEYLKAAKAGRATFL 577
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
61-285 |
1.17e-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: 54.00 E-value: 1.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506429 61 DKVRQLEQENNRLQVQIRDIEVVEKKEKSNlADRFEAEKARLRRALDSAQDELAKYRIEYDAAKVEVKKLKPQVEKLERE 140
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKE-EKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506429 141 LAGAEEQalhaqsIADQSQAKQKTLQARNDKLVVENDD----------LKKQNITLRDTVEGLKKAVEDETLLRTAANNK 210
Cdd:COG4942 99 LEAQKEE------LAELLRALYRLGRQPPLALLLSPEDfldavrrlqyLKYLAPARREQAEELRADLAELAALRAELEAE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506429 211 IKALEEDLAfALQQHKGELEEVRHKRQV-------DMTTYAKQIND--EYQSKLQDQIEEMRAQFKNNLHQNKTAFEDAY 281
Cdd:COG4942 173 RAELEALLA-ELEEERAALEALKAERQKllarlekELAELAAELAElqQEAEELEALIARLEAEAAAAAERTPAAGFAAL 251
|
....
gi 17506429 282 KNKL 285
Cdd:COG4942 252 KGKL 255
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
49-294 |
1.57e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.54 E-value: 1.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506429 49 LTSLNSRLATYIDKVRQLEQENNRLQVQIRDIEVVEKKEKSNL----ADRFEAEKARLRRALDSAQDELAKYRIEYDAAK 124
Cdd:COG4913 619 LAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIdvasAEREIAELEAELERLDASSDDLAALEEQLEELE 698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506429 125 VEVKKLKPQVEKLERELAGAEEQALHAQSIADQSQAKQKTLQARNDKLVVENDDLKKQNITLRDTVEGLKKAVEDEtllR 204
Cdd:COG4913 699 AELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEER---I 775
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506429 205 TAANNKIKALEEDLAFALQQHKGELEEVRHKRQVDMTTYakqinDEYQSKLQ----DQIEEMRAQFKNNLHQNKTAFEDA 280
Cdd:COG4913 776 DALRARLNRAEEELERAMRAFNREWPAETADLDADLESL-----PEYLALLDrleeDGLPEYEERFKELLNENSIEFVAD 850
|
250
....*....|....
gi 17506429 281 YKNKLNAARERQEE 294
Cdd:COG4913 851 LLSKLRRAIREIKE 864
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
70-380 |
5.39e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 52.61 E-value: 5.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506429 70 NNRLQVQIRDIEVVEKKEKSNLADRFEAEKARLRRALDSAQDELAKYRiEYDAAKVEVKKLKPQVEKLERELAGAEEqal 149
Cdd:COG4913 607 DNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLA-EYSWDEIDVASAEREIAELEAELERLDA--- 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506429 150 hAQSIADQSQAKQKTLQARNDKLVVENDDLKKQNITLRDTVEGLKKAVED-ETLLRTAANNKIKALEEDLAFALQQHKGE 228
Cdd:COG4913 683 -SSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDElQDRLEAAEDLARLELRALLEERFAAALGD 761
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506429 229 --LEEVRHKRQVDMTTYAKQINdeyqsKLQDQIEEMRAQFKN---NLHQNKTAFEDAYknklNAARERQEEAVSEAIH-L 302
Cdd:COG4913 762 avERELRENLEERIDALRARLN-----RAEEELERAMRAFNRewpAETADLDADLESL----PEYLALLDRLEEDGLPeY 832
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506429 303 RARVRDLETSSSGN--ASLIERLRSELDTLKRsfqeklddkdaRIAELNQEIERMmsEFHD----LLDVKIQLDAELKTY 376
Cdd:COG4913 833 EERFKELLNENSIEfvADLLSKLRRAIREIKE-----------RIDPLNDSLKRI--PFGPgrylRLEARPRPDPEVREF 899
|
....
gi 17506429 377 QALL 380
Cdd:COG4913 900 RQEL 903
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
148-386 |
5.72e-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: 52.07 E-value: 5.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506429 148 ALHAQSIADQSQAKQKTLQARNDKLVVENDDLKKQNITLRDTVEGLKKAVEDETLLRTAANNKIKALEEDLAfALQQHKG 227
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELA-ELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506429 228 ELEEVRHKRQvdmTTYAKQINDEYQSKLQDQIEEMRAQfkNNLHQNKTAFEdaYKNKLNAARERQEEAVSEAihlRARVR 307
Cdd:COG4942 94 ELRAELEAQK---EELAELLRALYRLGRQPPLALLLSP--EDFLDAVRRLQ--YLKYLAPARREQAEELRAD---LAELA 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17506429 308 DLETSSSGNASLIERLRSELDTLKRSFQEKLDDKDARIAELNQEIERMMSEFHDLLDVKIQLDAELKTYQALLEGEEER 386
Cdd:COG4942 164 ALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
44-379 |
2.95e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.15 E-value: 2.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506429 44 QEKDHLTSLNSRLAT---YIDKVRQLEQENNRLQVQIRDIEVVEKKEKSNLADRFEAEKARLRRALDSAQDELAKYRIEY 120
Cdd:COG4717 136 ALEAELAELPERLEEleeRLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEEL 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506429 121 DAAKVEVKKLKPQVEKLERELAGAEEQ-------------------ALHAQSIADQSQAKQKTLQARNDKLVVENDDLKK 181
Cdd:COG4717 216 EEAQEELEELEEELEQLENELEAAALEerlkearlllliaaallalLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAR 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506429 182 QNITLRDTVEGLKKAVEDETLlrtaANNKIKALEEDLAFALQQHKGELEEVRHkrqvDMTTYAKQINDEYQSKLQDQIEE 261
Cdd:COG4717 296 EKASLGKEAEELQALPALEEL----EEEELEELLAALGLPPDLSPEELLELLD----RIEELQELLREAEELEEELQLEE 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506429 262 MRAQFKNNLHQNKTAFEDAYKNKLNAARERQEeAVSEAIHLRARVRDLETSSSGNASLI--ERLRSELDTLKR---SFQE 336
Cdd:COG4717 368 LEQEIAALLAEAGVEDEEELRAALEQAEEYQE-LKEELEELEEQLEELLGELEELLEALdeEELEEELEELEEeleELEE 446
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 17506429 337 KLDDKDARIAELNQEIERMMSE------FHDLLDVKIQLDAELKTYQAL 379
Cdd:COG4717 447 ELEELREELAELEAELEQLEEDgelaelLQELEELKAELRELAEEWAAL 495
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
62-353 |
3.48e-06 |
|
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: 50.02 E-value: 3.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506429 62 KVRQLEQENNRLQVQIRDIevveKKEKSNLadrfEAEKARLRRALDSAQDELAKYRIEYDAAKVEVKKLKPQVEKLEREL 141
Cdd:TIGR04523 329 QISQNNKIISQLNEQISQL----KKELTNS----ESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKI 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506429 142 AGAEEQalhaqsiADQSQAKQKTLQARNDKLVVENDDLKKQNITLRDTVEGL-------KKAVEDETLLRTAANNKIKAL 214
Cdd:TIGR04523 401 QNQEKL-------NQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLtnqdsvkELIIKNLDNTRESLETQLKVL 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506429 215 E---EDLAFALQQHKGELEEvrHKRQVDMTTYAKQINDEYQSKLQDQIEEMRAQFKnNLHQNKTAFEDAYKNKLNAARER 291
Cdd:TIGR04523 474 SrsiNKIKQNLEQKQKELKS--KEKELKKLNEEKKELEEKVKDLTKKISSLKEKIE-KLESEKKEKESKISDLEDELNKD 550
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17506429 292 QEEAVSEaihlrarvrDLETSSSGNASLIERLRSELDTLKRS---FQEKLDDKDARIAELNQEIE 353
Cdd:TIGR04523 551 DFELKKE---------NLEKEIDEKNKEIEELKQTQKSLKKKqeeKQELIDQKEKEKKDLIKEIE 606
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
93-237 |
4.22e-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: 48.38 E-value: 4.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506429 93 DRFEAEKARLRRALDSAQDELAKYRIEYDAAKVEVKKLKPQVEKLERELAGAEEQALHAQsiADQSQAK----QKTLQAR 168
Cdd:COG1579 20 DRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYE--EQLGNVRnnkeYEALQKE 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17506429 169 NDKLVVENDDLKKQNITLRDTVEGLKKAVEDETLLRTAANNKIKALEEDLAFALQQHKGELEEVRHKRQ 237
Cdd:COG1579 98 IESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAERE 166
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
163-398 |
1.12e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 48.51 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506429 163 KTLQARNDKLVVENDDLKKQNITLRDTVEGLKKAVEDETLLRTAANNKIKALEEDLAFALQQHKGELEEVRHkRQVDMTT 242
Cdd:TIGR02168 680 EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQ-LSKELTE 758
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506429 243 YAKQINdeyqsKLQDQIEEMRAQFKNNLHQNKTAFEDAykNKLNAARERQEEAVSEaihLRARVRDLETSSSGNASLIER 322
Cdd:TIGR02168 759 LEAEIE-----ELEERLEEAEEELAEAEAEIEELEAQI--EQLKEELKALREALDE---LRAELTLLNEEAANLRERLES 828
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17506429 323 LRSELDTLKRSFQekldDKDARIAELNQEIERMMSEFHDLLDVKIQLDAELKTYQALLEGEEERLNLTQEAPQNTS 398
Cdd:TIGR02168 829 LERRIAATERRLE----DLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELS 900
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
47-237 |
2.57e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.22 E-value: 2.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506429 47 DHLTSLNSRLATYIDKVRQLE---QENNRLQVQIRDIEVVEKkEKSNLADRFEAEK-ARLRRALDSAQDELAKYRIEYDA 122
Cdd:COG4913 235 DDLERAHEALEDAREQIELLEpirELAERYAAARERLAELEY-LRAALRLWFAQRRlELLEAELEELRAELARLEAELER 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506429 123 AKVEVKKLKPQVEKLERELAGAEEQALhaQSIADQSQAKQKTLQARNDKLVVENDDLKKQNITLRDTVEGLKKAVEDETL 202
Cdd:COG4913 314 LEARLDALREELDELEAQIRGNGGDRL--EQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAA 391
|
170 180 190
....*....|....*....|....*....|....*...
gi 17506429 203 LRTAANNKIKALEEDLA---FALQQHKGELEEVRHKRQ 237
Cdd:COG4913 392 LLEALEEELEALEEALAeaeAALRDLRRELRELEAEIA 429
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
93-388 |
2.75e-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: 2.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506429 93 DRFEAEKARLRRALDSAQDELAKYRIEydaakveVKKLKPQVEKLERElagaEEQALHAQSIADQSQAKQKTLQARNDKl 172
Cdd:TIGR02169 166 AEFDRKKEKALEELEEVEENIERLDLI-------IDEKRQQLERLRRE----REKAERYQALLKEKREYEGYELLKEKE- 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506429 173 vvendDLKKQNITLRDTVEGLKKAVEDETLLRTAANNKIKALEEDLAFALQQ--HKGELEEVRHKRQVDMTTYAkqinde 250
Cdd:TIGR02169 234 -----ALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKikDLGEEEQLRVKEKIGELEAE------ 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506429 251 yQSKLQDQIEEMRAQFKNNLHQNKTAFE--DAYKNKLNAARERQEEAVSEAIHLRARVRDLETSssgnaslIERLRSELD 328
Cdd:TIGR02169 303 -IASLERSIAEKERELEDAEERLAKLEAeiDKLLAEIEELEREIEEERKRRDKLTEEYAELKEE-------LEDLRAELE 374
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17506429 329 TLKRSFQE---KLDDKDARIAELNQEIERMMSEFHDLLDVKIQLDAELKTYQALLEGEEERLN 388
Cdd:TIGR02169 375 EVDKEFAEtrdELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKIN 437
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
38-406 |
3.61e-05 |
|
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: 46.71 E-value: 3.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506429 38 LETSRLQEKDHLTSLNSRLATYIDKVRQLEQENNRLQVQIRDIEVVEKKEKSNladRFEAEKArlRRALDSAQDELAKyr 117
Cdd:pfam01576 150 LSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKG---RQELEKA--KRKLEGESTDLQE-- 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506429 118 ieydaakvEVKKLKPQVEKLERELAGAEEQALHAQSIADQSQAKQKTLQARNDKLVVENDDLKkqnitlrdtveglkkav 197
Cdd:pfam01576 223 --------QIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQ----------------- 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506429 198 EDETLLRtAANNKIKALEEDLAFALQQHKGELE----------EVRHKRQVDMTTYAKQINDEYQSKlQDQIEEMRAQFK 267
Cdd:pfam01576 278 EDLESER-AARNKAEKQRRDLGEELEALKTELEdtldttaaqqELRSKREQEVTELKKALEEETRSH-EAQLQEMRQKHT 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506429 268 NNLHQNKTAFEDAYKNKLNAARERQEEAvSEAIHLRARVRDLETSSSGnaslIERLRSELDTLKRSFQEKLDDKDARIAE 347
Cdd:pfam01576 356 QALEELTEQLEQAKRNKANLEKAKQALE-SENAELQAELRTLQQAKQD----SEHKRKKLEGQLQELQARLSESERQRAE 430
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 17506429 348 LNQEIERMMSEFHDLLDVKIQLDAELKTYQALLEGEEERLNLTQEAPQNTSVHHVSFSS 406
Cdd:pfam01576 431 LAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLST 489
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
40-328 |
4.29e-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: 46.60 E-value: 4.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506429 40 TSRLQEK-DHLTSLNSRLATYIDKVRQL-EQENNRLQVQIRDIEVVEKKEKSNLAD-------------RFEAEKARLRR 104
Cdd:TIGR02169 257 TEEISELeKRLEEIEQLLEELNKKIKDLgEEEQLRVKEKIGELEAEIASLERSIAEkereledaeerlaKLEAEIDKLLA 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506429 105 ALDSAQDELAKYRIEYDAAKVEVKKLKPQVEKLERELAGAEEQAlhaqsiaDQSQAKQKTLQARNDKLVVENDDLKKQNI 184
Cdd:TIGR02169 337 EIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEF-------AETRDELKDYREKLEKLKREINELKRELD 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506429 185 TLRDTVEGLKKAVEDetllrtaANNKIKALEEDLAfALQQHKGEL-EEVRHKRQVDMTTYAKqindeyQSKLQDQIEemr 263
Cdd:TIGR02169 410 RLQEELQRLSEELAD-------LNAAIAGIEAKIN-ELEEEKEDKaLEIKKQEWKLEQLAAD------LSKYEQELY--- 472
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17506429 264 aqfknnlhqnktafedAYKNKLNAARERQEEAVSEAIHLRARVRDLETSSSGNASLIERLRSELD 328
Cdd:TIGR02169 473 ----------------DLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQ 521
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
44-374 |
9.69e-05 |
|
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: 45.40 E-value: 9.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506429 44 QEKDHLTSLNSRLATYIDKVRQLEQENNRLQVQIRDIEVvEKKEKSNLADRFEAEKARLRRALDSAQDELAKYRIEYDAA 123
Cdd:TIGR04523 93 KNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEK-QKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEEL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506429 124 KVEVKKLKPQVEKLERELAGAEEQALhaqsIADQSQAKQKTLQARNDKLVVENDDLKKQNITLRDTVEGL---------- 193
Cdd:TIGR04523 172 ENELNLLEKEKLNIQKNIDKIKNKLL----KLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKqqeinektte 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506429 194 ------------------KKAVEDETLLRTAANNKIKALEEDlafaLQQHKGELEEVRHKRQVDMTtyaKQINDEYQSKl 255
Cdd:TIGR04523 248 isntqtqlnqlkdeqnkiKKQLSEKQKELEQNNKKIKELEKQ----LNQLKSEISDLNNQKEQDWN---KELKSELKNQ- 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506429 256 QDQIEEMRAQFKNN------LHQNKTAFEDAYKNKLNAARERQEEavseaihLRARVRDLETSSSGNASL---IERLRSE 326
Cdd:TIGR04523 320 EKKLEEIQNQISQNnkiisqLNEQISQLKKELTNSESENSEKQRE-------LEEKQNEIEKLKKENQSYkqeIKNLESQ 392
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 17506429 327 LDTLKRSFQEKLDD---KDARIAELNQEIERMMSEFHDLLDVKIQLDAELK 374
Cdd:TIGR04523 393 INDLESKIQNQEKLnqqKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIK 443
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
40-379 |
1.15e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 45.11 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506429 40 TSRLQEKD--------HLTSLNSRLATYIDKVRQLEQENN------------RLQVQIRD--IEVVEKK---------EK 88
Cdd:pfam15921 502 TASLQEKEraieatnaEITKLRSRVDLKLQELQHLKNEGDhlrnvqtecealKLQMAEKDkvIEILRQQienmtqlvgQH 581
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506429 89 SNLADRFEAEKARLRRALDSAQDELAKYRIEYDAAKVEVKKLKPQVEKLERE---LAGAEEQALHAQsiadqsqakqKTL 165
Cdd:pfam15921 582 GRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEkvkLVNAGSERLRAV----------KDI 651
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506429 166 QARNDKLVVENDDLKKQNITLRDTVEGLKKAVEDETLLRTAANNKIKaleedlaFALQQHKGELEEVRHkrqvdmTTYAK 245
Cdd:pfam15921 652 KQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLK-------MQLKSAQSELEQTRN------TLKSM 718
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506429 246 QINDEYQSK----LQDQIEEMRAQFknnlhqnktafeDAYKNKLNAARERQEEAVSEAIHLRARVRDLETSSSGNASLIE 321
Cdd:pfam15921 719 EGSDGHAMKvamgMQKQITAKRGQI------------DALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKN 786
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 17506429 322 RLRSELDTLkRSFQEKLDDKDARIAELNQEIERMMSEFHDLLDVKIQLDAELKTYQAL 379
Cdd:pfam15921 787 KMAGELEVL-RSQERRLKEKVANMEVALDKASLQFAECQDIIQRQEQESVRLKLQHTL 843
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
84-392 |
1.38e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.95 E-value: 1.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506429 84 EKKEKSNLADRFEAEKARLRRALDSAQDELAKYRIEYDAAKVEVKKLKP-----------------QVEKLER---ELAG 143
Cdd:PRK04863 280 ERRVHLEEALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQdyqaasdhlnlvqtalrQQEKIERyqaDLEE 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506429 144 AEEQALHAQSIADQSQAKQKTLQARNDKLVVENDDLKKQnitLRDTVEGLKkavedetllrtaannkikaLEEDLAFALQ 223
Cdd:PRK04863 360 LEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQ---LADYQQALD-------------------VQQTRAIQYQ 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506429 224 QHKGELEEVRHKRQVDMTTY--AKQINDEYQSKLQDQIEEMR-AQFKNNLHQN-KTAFEDAYK--NKLNAARERqEEAVS 297
Cdd:PRK04863 418 QAVQALERAKQLCGLPDLTAdnAEDWLEEFQAKEQEATEELLsLEQKLSVAQAaHSQFEQAYQlvRKIAGEVSR-SEAWD 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506429 298 EAihlRARVRDLETSSSGNASLiERLRSELDTLKRSFQEKlddkdariaelnQEIERMMSEFHDLLDVKIQLDAELKTYQ 377
Cdd:PRK04863 497 VA---RELLRRLREQRHLAEQL-QQLRMRLSELEQRLRQQ------------QRAERLLAEFCKRLGKNLDDEDELEQLQ 560
|
330
....*....|....*
gi 17506429 378 ALLEGEEERLNLTQE 392
Cdd:PRK04863 561 EELEARLESLSESVS 575
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
89-324 |
1.59e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 44.37 E-value: 1.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506429 89 SNLADRFEAEKARLRRALDSAQDELAKYRIEYDAAKVEVKKLKPQVEKLERELAGAEEQALHAQSIADQSQAKQKTLQAR 168
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506429 169 ndkLVVENDDLKKQNITL-----RDTVEGLKKAVEDETLLRTAAN-NKIKALEEDLAFALQQHKGELEEVRHKRQVDMTT 242
Cdd:COG4942 99 ---LEAQKEELAELLRALyrlgrQPPLALLLSPEDFLDAVRRLQYlKYLAPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506429 243 YAKQIND--EYQSKLQDQIEEmRAQFKNNLHQNKTAFEDAYKNKlnAARERQEEAVSEAIHLRARVRDLETSSSGNASLI 320
Cdd:COG4942 176 LEALLAEleEERAALEALKAE-RQKLLARLEKELAELAAELAEL--QQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
....
gi 17506429 321 ERLR 324
Cdd:COG4942 253 GKLP 256
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
96-327 |
2.75e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.14 E-value: 2.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506429 96 EAEKARLRRA----LDSAQDELAKYRIEYDAAKVEVKKLKPQVEKLERELAGAEEQALHAQsiADQSQAKQKTLQARNDK 171
Cdd:COG4913 243 ALEDAREQIEllepIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAE--LARLEAELERLEARLDA 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506429 172 LVVENDDLKKQnitlrdtveglkkavedetlLRTAANNKIKALEEDLAfalqQHKGELEEVRHKRQvdmtTYAKQINDey 251
Cdd:COG4913 321 LREELDELEAQ--------------------IRGNGGDRLEQLEREIE----RLERELEERERRRA----RLEALLAA-- 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506429 252 qskLQDQIEEMRAQFKNNLHQ------NKTAFEDAYKNKLNAARERQEEAVSEAIHLRARVRDLETSSSGNASLIERLRS 325
Cdd:COG4913 371 ---LGLPLPASAEEFAALRAEaaalleALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRD 447
|
..
gi 17506429 326 EL 327
Cdd:COG4913 448 AL 449
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
126-387 |
3.37e-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: 43.52 E-value: 3.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506429 126 EVKKLKPQVEKLERELAGAEEQALHAQSIADQSQAKQKTLQARNDKLVVENDDLKKQNITLRDTVEGLKKAVEDETLLRT 205
Cdd:TIGR02169 675 ELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIE 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506429 206 AANNKIKALEEDLAfalqqhkgELEEVRHKrqvdmttYAKQINDEYQSKLQDQIEEMRAQfknnlhqnktafedayKNKL 285
Cdd:TIGR02169 755 NVKSELKELEARIE--------ELEEDLHK-------LEEALNDLEARLSHSRIPEIQAE----------------LSKL 803
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506429 286 NAARERQEeavseaihlrARVRDLETSSSGNASLIERLRSELDTLkrsfQEKLDDKDARIAELNQEIErmmsefhDLLDV 365
Cdd:TIGR02169 804 EEEVSRIE----------ARLREIEQKLNRLTLEKEYLEKEIQEL----QEQRIDLKEQIKSIEKEIE-------NLNGK 862
|
250 260
....*....|....*....|..
gi 17506429 366 KIQLDAELKTYQALLEGEEERL 387
Cdd:TIGR02169 863 KEELEEELEELEAALRDLESRL 884
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
124-362 |
3.41e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 43.46 E-value: 3.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506429 124 KVEVKKLKPQVEKLERELAGAEEQALHAQSIADQSQAKQKT----LQARNDKLVVENDDLKKQNITLRDTVEGLKKAVED 199
Cdd:PHA02562 173 KDKIRELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGEniarKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIED 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506429 200 etllRTAANNKIKALEEDLAFALQQHKGEleEVRHKRQVDMTTYAKQINDEyqsklqdqiEEMRAQFKNNLHQNKTAFEd 279
Cdd:PHA02562 253 ----PSAALNKLNTAAAKIKSKIEQFQKV--IKMYEKGGVCPTCTQQISEG---------PDRITKIKDKLKELQHSLE- 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506429 280 ayknKLNAARERQEEAVSEAIHLRARVRDLETSSSGNASLIERLRSELDTLKRSFQEKLD---DKDARIAELNQEIERMM 356
Cdd:PHA02562 317 ----KLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAefvDNAEELAKLQDELDKIV 392
|
....*.
gi 17506429 357 SEFHDL 362
Cdd:PHA02562 393 KTKSEL 398
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
38-256 |
4.79e-04 |
|
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: 43.12 E-value: 4.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506429 38 LETSRLQEKDHLTSLNSRLATYIDKVRQLEQENNRLQVQIRDIE------VVEKKEKSNLADRFEAEKARLRRALDSAQD 111
Cdd:TIGR02168 265 LEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRerlanlERQLEELEAQLEELESKLDELAEELAELEE 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506429 112 ELAKYRIEYDAAKVEVKKLKPQVEKLERELAGAEEQALHAQSIADQSQAKQKTLQARNDKLVVENDDLKKQNITLRDTVE 191
Cdd:TIGR02168 345 KLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIE 424
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17506429 192 GLKKAVEDETLLRTAAN-NKIKALEEDLAFALQQHKGELEEVRHKRQVdmttyAKQINDEYQSKLQ 256
Cdd:TIGR02168 425 ELLKKLEEAELKELQAElEELEEELEELQEELERLEEALEELREELEE-----AEQALDAAERELA 485
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
44-231 |
5.26e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.44 E-value: 5.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506429 44 QEKDHLTSLNSRLATYIDKVRQLEQENNRLQVQIRDIEVVEKKEKSNLAdRFEAEKARLRRALDSAQDELAK-----YRI 118
Cdd:COG4942 38 ELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELA-ELEKEIAELRAELEAQKEELAEllralYRL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506429 119 -EYDAAKVevkKLKPQ-VEKLERELAGAEEQALHAQSIADQSQAKQKTLQARNDKLVVENDDLKKQNITLRDTVEGLKKA 196
Cdd:COG4942 117 gRQPPLAL---LLSPEdFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEAL 193
|
170 180 190
....*....|....*....|....*....|....*
gi 17506429 197 VEDETLLRTAANNKIKALEEDLAfALQQHKGELEE 231
Cdd:COG4942 194 KAERQKLLARLEKELAELAAELA-ELQQEAEELEA 227
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
54-303 |
6.94e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.82 E-value: 6.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506429 54 SRLATYIDKVRQLEQENNRLQVQIRDIEVVEKKEKSNLADRFEAEKARLRRALDSAQDELAKYRIEYDAAKVEVKKLKPQ 133
Cdd:PTZ00121 1260 ARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAE 1339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506429 134 VEKLERELAGAEEQAlhAQSIADQSQAKQKTLQARNDKLVVENDDLKKQNITLRDTVEGLKKAVEDEtllRTAANNKIKA 213
Cdd:PTZ00121 1340 EAKKAAEAAKAEAEA--AADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDK---KKADELKKAA 1414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506429 214 LEEDLAfalQQHKGELEEVRHKRQVDMTTYAKQINDEYQSKLQD--QIEEMRAQFKNNLHQNKTAFEDAYKNKLNAARER 291
Cdd:PTZ00121 1415 AAKKKA---DEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEakKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKK 1491
|
250
....*....|..
gi 17506429 292 QEEAVSEAIHLR 303
Cdd:PTZ00121 1492 AEEAKKKADEAK 1503
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
94-392 |
7.04e-04 |
|
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: 42.74 E-value: 7.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506429 94 RFEAEKARLRRALDSAQDELAkyRIEyDAAKvEVKKlkpQVEKLERElagaEEQALHAQSIADQSQAKQKTLqarndkLV 173
Cdd:TIGR02168 169 KYKERRKETERKLERTRENLD--RLE-DILN-ELER---QLKSLERQ----AEKAERYKELKAELRELELAL------LV 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506429 174 VENDDLKKQnitlRDTVEGLKKAVEDEtllRTAANNKIKALEEDLAFaLQQHKGELEEVRHKRQVDMTTYAKQINDeyqs 253
Cdd:TIGR02168 232 LRLEELREE----LEELQEELKEAEEE---LEELTAELQELEEKLEE-LRLEVSELEEEIEELQKELYALANEISR---- 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506429 254 kLQDQIEEMRAQFKNnlhqnktafedaYKNKLNAARERQEEAVSEAIHLRARVRDLETSSSGNASLIERLRSELDTLKRS 333
Cdd:TIGR02168 300 -LEQQKQILRERLAN------------LERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAE 366
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 17506429 334 FQEKLDdkdaRIAELNQEIERMMSEFHDLLDVKIQLDAELKTYQALLEGEEERLNLTQE 392
Cdd:TIGR02168 367 LEELES----RLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQ 421
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
84-395 |
7.55e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.36 E-value: 7.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506429 84 EKKEKSNLADRFEAEKARLRRALDSAQDELAkyriEYDAAKVEVKKLKPQVEKLERELAGAEEQALHAQSIADQSQAKQK 163
Cdd:PRK03918 201 ELEEVLREINEISSELPELREELEKLEKEVK----ELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIE 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506429 164 TLQaRNDKLVVENDDLKKQNITLRDTVEGLKKAVEDETLLRTAANNKIKALEEDLAFA------LQQHKGELEEVRhKRQ 237
Cdd:PRK03918 277 ELE-EKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELeekeerLEELKKKLKELE-KRL 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506429 238 VDMTTYAKQINDEYQskLQDQIEEMRAQFKNNLhqnktafEDAYKNKLNAARERQEEAVSEAIHLRARVRDLETSSSGNA 317
Cdd:PRK03918 355 EELEERHELYEEAKA--KKEELERLKKRLTGLT-------PEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELK 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506429 318 SLIERLRS---ELDTLKRSFQEklDDKDARIAELNQEIERMMSEFHDLLDVKIQLDAELKTYQALLEGEEERLNLTQEAP 394
Cdd:PRK03918 426 KAIEELKKakgKCPVCGRELTE--EHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAE 503
|
.
gi 17506429 395 Q 395
Cdd:PRK03918 504 Q 504
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
84-299 |
9.33e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.74 E-value: 9.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506429 84 EKKEKSNLADRFEAEKARLRRALDSAQDELAKYRIEYDAAKVEVKKLKPQVEKLERELAGAEEQALHAQS-IADQSQAKQ 162
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREeLGERARALY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506429 163 KTLQARNDKLVVEN-----------DDLKKQNITLRDTVEGLKKAVEDETLLRTAANNKIKALEEDLAfALQQHKGELEE 231
Cdd:COG3883 97 RSGGSVSYLDVLLGsesfsdfldrlSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKA-ELEAAKAELEA 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17506429 232 VRHKRQVDMTTYAKQINDEYQSKLQDQIEEMRAQFKNNLHQNKTAFEDAYKNKLNAARERQEEAVSEA 299
Cdd:COG3883 176 QQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 243
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
2-340 |
9.46e-04 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 42.20 E-value: 9.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506429 2 SSRKGTRSSRIVTLERSANSSLSNNGGGDDSFGSTLLETS-RLQEK-----DHLTSLNSRLATYIDKVRQLEQENNRLQV 75
Cdd:PLN02939 44 SQQKKKRGKNIAPKQRSSNSKLQSNTDENGQLENTSLRTVmELPQKstssdDDHNRASMQRDEAIAAIDNEQQTNSKDGE 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506429 76 QIRD------IEVVEKKEKSNLadrfeaekaRLRRALDSAQDELAKYRIEYDAAKVEVKKLKPQVEKLERELAGAEEQAL 149
Cdd:PLN02939 124 QLSDfqledlVGMIQNAEKNIL---------LLNQARLQALEDLEKILTEKEALQGKINILEMRLSETDARIKLAAQEKI 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506429 150 HAQSIADQSQAKQKTLQARND-------KLVVENDDLKKQNITLRDTVEGLKKAVE-----DETLL-----RTAANNKIK 212
Cdd:PLN02939 195 HVEILEEQLEKLRNELLIRGAteglcvhSLSKELDVLKEENMLLKDDIQFLKAELIevaetEERVFklekeRSLLDASLR 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506429 213 ALEEDLAFALQ--------QHKGELEEV--------RHKRQVDMTTYAKQINDEyqskLQDQIEEMRAQFKN-NLHQNKT 275
Cdd:PLN02939 275 ELESKFIVAQEdvsklsplQYDCWWEKVenlqdlldRATNQVEKAALVLDQNQD----LRDKVDKLEASLKEaNVSKFSS 350
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17506429 276 AFEDAYKNKLNAARERQeEAVSEAIHlrARVRDLETSSSGNASLIERLRSEldTLKRSFQEKLDD 340
Cdd:PLN02939 351 YKVELLQQKLKLLEERL-QASDHEIH--SYIQLYQESIKEFQDTLSKLKEE--SKKRSLEHPADD 410
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
197-392 |
1.74e-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: 41.26 E-value: 1.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506429 197 VEDE-TLLRTAANNKIKALeedlafaLQQHKGELEEVRHKRQVDMTTYAKQIND--EYQSKLQDQIEEMRAQFKNnlhQN 273
Cdd:pfam15921 243 VEDQlEALKSESQNKIELL-------LQQHQDRIEQLISEHEVEITGLTEKASSarSQANSIQSQLEIIQEQARN---QN 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506429 274 ktafedayknklnaarerqeeavseAIHLRaRVRDLEtsssgnaSLIERLRSELDTLKRSFQEKLDDKDARIAELNQEIE 353
Cdd:pfam15921 313 -------------------------SMYMR-QLSDLE-------STVSQLRSELREAKRMYEDKIEELEKQLVLANSELT 359
|
170 180 190
....*....|....*....|....*....|....*....
gi 17506429 354 RMMSEFHDLLDVKIQLDAELKTYQALLEGEEERLNLTQE 392
Cdd:pfam15921 360 EARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKE 398
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
216-387 |
1.76e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.44 E-value: 1.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506429 216 EDLAFALQQHKGELEEVRH-----KRQVDMTTYAKQINDEYQSKLQ--DQIEEMR-------AQFKNNLHQNKTAFEDAY 281
Cdd:COG4913 224 FEAADALVEHFDDLERAHEaledaREQIELLEPIRELAERYAAARErlAELEYLRaalrlwfAQRRLELLEAELEELRAE 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506429 282 KNKLNAARERQEEAVSEAihlRARVRDLETSSSGN-ASLIERLRSELDTLKRSFQE---KLDDKDARIAELNQEIERMMS 357
Cdd:COG4913 304 LARLEAELERLEARLDAL---REELDELEAQIRGNgGDRLEQLEREIERLERELEErerRRARLEALLAALGLPLPASAE 380
|
170 180 190
....*....|....*....|....*....|
gi 17506429 358 EFHDLLDvkiQLDAELKTYQALLEGEEERL 387
Cdd:COG4913 381 EFAALRA---EAAALLEALEEELEALEEAL 407
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
56-291 |
2.04e-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: 41.36 E-value: 2.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506429 56 LATYIDKVRQLEQENNRLQVQIRDIEVVEkkekSNLADRFEAEKARLRRALDSAQDELAKYRIEYD----AAKVEVKKLK 131
Cdd:pfam12128 246 LQQEFNTLESAELRLSHLHFGYKSDETLI----ASRQEERQETSAELNQLLRTLDDQWKEKRDELNgelsAADAAVAKDR 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506429 132 PQVEKLEREL-----AGAEEQALHaQSIADQSQAKQKTLQARNDKL------VVENDDLKKQNITLR--DTVEGLKKAV- 197
Cdd:pfam12128 322 SELEALEDQHgafldADIETAAAD-QEQLPSWQSELENLEERLKALtgkhqdVTAKYNRRRSKIKEQnnRDIAGIKDKLa 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506429 198 ---EDETLLRTAANNKIKALEEDLAFALQQHKGELEEVRHKRQVDMTTYAKQIND-EYQSKLQDQIEemraQFKNNLHQN 273
Cdd:pfam12128 401 kirEARDRQLAVAEDDLQALESELREQLEAGKLEFNEEEYRLKSRLGELKLRLNQaTATPELLLQLE----NFDERIERA 476
|
250
....*....|....*...
gi 17506429 274 KTAFEDAYKNKLNAARER 291
Cdd:pfam12128 477 REEQEAANAEVERLQSEL 494
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
35-359 |
2.06e-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: 41.26 E-value: 2.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506429 35 STLLETSRLQE------KDHLTSLNSRLATYIDKVRQLEQENNRLQVQIRDIEV-VEKKEKsnladRFEAEKARLRRALD 107
Cdd:pfam15921 331 SELREAKRMYEdkieelEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLAdLHKREK-----ELSLEKEQNKRLWD 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506429 108 SAQDE---LAKYRIEYDAAKVEVKKLKPQVEKLERELAGAEEQALHAQSIADQSQAKQKTLQARND------KLVVENDD 178
Cdd:pfam15921 406 RDTGNsitIDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLEstkemlRKVVEELT 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506429 179 LKKQNITLRD-TVEGLKKAVEDETLLRTAANNKIKALEEDLAFALQQHKGELEEVRHKRQVDMTTYAKQIN----DEYQS 253
Cdd:pfam15921 486 AKKMTLESSErTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQmaekDKVIE 565
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506429 254 KLQDQIEEM-----------------RAQFKNNLHQNKTAFED--AYKNKLNAARERQEEAVSE------------AIHL 302
Cdd:pfam15921 566 ILRQQIENMtqlvgqhgrtagamqveKAQLEKEINDRRLELQEfkILKDKKDAKIRELEARVSDlelekvklvnagSERL 645
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17506429 303 RArVRDLETSSSGNASLIERLRSELDT-------LKRSFQEKLDDKDARIAELNQEIERMMSEF 359
Cdd:pfam15921 646 RA-VKDIKQERDQLLNEVKTSRNELNSlsedyevLKRNFRNKSEEMETTTNKLKMQLKSAQSEL 708
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
106-355 |
2.25e-03 |
|
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
Pssm-ID: 310534 [Multi-domain] Cd Length: 258 Bit Score: 40.09 E-value: 2.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506429 106 LDSAQDELAKYRIEYDAAKVevkklkpQVEKLERELAGAEEQALHAQSIADQSQAKQKTLQARNDKLVVENDDLKKQNIT 185
Cdd:pfam06008 21 LENLTKQLQEYLSPENAHKI-------QIEILEKELSSLAQETEELQKKATQTLAKAQQVNAESERTLGHAKELAEAIKN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506429 186 LRDTVEGLKKAVEdetllrTAANNKIKALEEDLAFALQQHKGELEEVRHKRqvdmTTYAKQINDEYQSKLQDQIEEMRAQ 265
Cdd:pfam06008 94 LIDNIKEINEKVA------TLGENDFALPSSDLSRMLAEAQRMLGEIRSRD----FGTQLQNAEAELKAAQDLLSRIQTW 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506429 266 FKNNLHQNKTAFEDA------YKNKLNAARERQEEAVSEAihlrARVRDLETSSSGNASLIERLRSELDTLKRSFQEKLD 339
Cdd:pfam06008 164 FQSPQEENKALANALrdslaeYEAKLSDLRELLREAAAKT----RDANRLNLANQANLREFQRKKEEVSEQKNQLEETLK 239
|
250
....*....|....*.
gi 17506429 340 DKDARIAELNQEIERM 355
Cdd:pfam06008 240 TARDSLDAANLLLQEI 255
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
30-170 |
3.06e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 40.44 E-value: 3.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506429 30 DDSFGSTLLETSRLQEK-----DHLTSLNSRLATYIDKVRQLEQENNRLQVQIRDIEvvekKEKSNLADRFEAEKARLRR 104
Cdd:TIGR02169 377 DKEFAETRDELKDYREKleklkREINELKRELDRLQEELQRLSEELADLNAAIAGIE----AKINELEEEKEDKALEIKK 452
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17506429 105 A---LDSAQDELAKYRIEYDAAKVEVKKLKPQVEKLERELAGAEEQALHAQSIADQSQAKQKTLQARND 170
Cdd:TIGR02169 453 QewkLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQ 521
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
46-364 |
3.85e-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: 40.16 E-value: 3.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506429 46 KDHLTSLNSRLATYIDKVRQLEQENNRLQVQIRdIEVVEKKEKSNLADRFEAEKARLRRALDSAQDELAKYRIEYDAAKV 125
Cdd:pfam01576 18 KERQQKAESELKELEKKHQQLCEEKNALQEQLQ-AETELCAEAEEMRARLAARKQELEEILHELESRLEEEEERSQQLQN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506429 126 EVKKLKPQVEKLERELAGAE--EQALHAQSIADQSQAKQK-----TLQARNDKLVVENDDLKKQNITLRDTVEGLKKAVE 198
Cdd:pfam01576 97 EKKKMQQHIQDLEEQLDEEEaaRQKLQLEKVTTEAKIKKLeedilLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKAK 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506429 199 DETLLRTAANNKIKALEEDLAfalQQHKGELEEVRHKRQVDMTTyakqindeyqSKLQDQIEEMRAQFKNNLHQNKTAFE 278
Cdd:pfam01576 177 SLSKLKNKHEAMISDLEERLK---KEEKGRQELEKAKRKLEGES----------TDLQEQIAELQAQIAELRAQLAKKEE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506429 279 DayknkLNAARERQEEAVSEAIHLRARVRDLEtssSGNASLIERLRSELDTLKRSFQEKLDdkdariaeLNQEIERMMSE 358
Cdd:pfam01576 244 E-----LQAALARLEEETAQKNNALKKIRELE---AQISELQEDLESERAARNKAEKQRRD--------LGEELEALKTE 307
|
....*.
gi 17506429 359 FHDLLD 364
Cdd:pfam01576 308 LEDTLD 313
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
209-355 |
3.97e-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: 39.14 E-value: 3.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506429 209 NKIKALEEDLAFALQQHKGELEEVRhKRQVDMTTYAKQINDEyQSKLQDQIEEMRAQ---FKNNLHQNKTAFE-DAYKNK 284
Cdd:COG1579 20 DRLEHRLKELPAELAELEDELAALE-ARLEAAKTELEDLEKE-IKRLELEIEEVEARikkYEEQLGNVRNNKEyEALQKE 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17506429 285 LNAARERQEEAVSEAIHLRARVRDLETSSSGNASLIERLRSELDTLKRSFQEKLDDKDARIAELNQEIERM 355
Cdd:COG1579 98 IESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREEL 168
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
37-233 |
4.06e-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: 4.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506429 37 LLETSRLQEKDHLTSLNSRLATYIDKVRQLEQENNRLQVQIRDIEVVEKKEKSNLADRFEAEKARLRRALDSAQDELAKY 116
Cdd:COG4913 292 LLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAAL 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506429 117 RIEYDAAKVEVKKLKPQVEKLERELAGAEEQalhAQSIADQSQAKQKTLQARNDKLVVENDDLKKQNITLRDTVEGLKKA 196
Cdd:COG4913 372 GLPLPASAEEFAALRAEAAALLEALEEELEA---LEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDA 448
|
170 180 190
....*....|....*....|....*....|....*..
gi 17506429 197 VEDETLLRtaannkikalEEDLAFAlqqhkGELEEVR 233
Cdd:COG4913 449 LAEALGLD----------EAELPFV-----GELIEVR 470
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
61-377 |
4.56e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.02 E-value: 4.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506429 61 DKVRQLEQENNRLQVQIRDIEvvEKKEKSNLADRFEAEKARLRRALDSAQDELAKYRIEYDAAKVEVKKLKPQVEKLERE 140
Cdd:PRK02224 475 ERVEELEAELEDLEEEVEEVE--ERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAE 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506429 141 LAGAEEQALHAQSIADQSQAKQKTLQARNDKLVVENDDLKKQNiTLRDTVEGLKKAVEDETLLRTAANNKIKALEEDLAf 220
Cdd:PRK02224 553 AEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIR-TLLAAIADAEDEIERLREKREALAELNDERRERLA- 630
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506429 221 ALQQHKGELEEVRHKRQVDMTTYAKQINDEYQSKLQDQIEEMRAQfKNNLHQNKTAFEDAYKNkLNAARERQEeavseai 300
Cdd:PRK02224 631 EKRERKRELEAEFDEARIEEAREDKERAEEYLEQVEEKLDELREE-RDDLQAEIGAVENELEE-LEELRERRE------- 701
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506429 301 HLRARVRDLETsssgnaslierLRSELDTLKRSFQEKLDDKDARIAElnqEIERMMSEFHDLL-----DVKIQLDAE--L 373
Cdd:PRK02224 702 ALENRVEALEA-----------LYDEAEELESMYGDLRAELRQRNVE---TLERMLNETFDLVyqndaYSHIELDGEyeL 767
|
....
gi 17506429 374 KTYQ 377
Cdd:PRK02224 768 TVYQ 771
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
49-392 |
4.80e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.05 E-value: 4.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506429 49 LTSLNSRLATYIDKVRQLEQENNRLQVQIRDIEVVEK-----KEKSNLADRFEAEKARLRRALDSAQDELAKYR------ 117
Cdd:PRK03918 247 LESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKelkelKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEeeingi 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506429 118 ----IEYDAAKVEVKKLKPQVEKLERELAGAEEQALHAQsiadqsQAKQKTLQARNDKLVVENDDLKKQNITLrDTVEGL 193
Cdd:PRK03918 327 eeriKELEEKEERLEELKKKLKELEKRLEELEERHELYE------EAKAKKEELERLKKRLTGLTPEKLEKEL-EELEKA 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506429 194 KKAVEDETLLRTAANNKIKALEEDLAFALQQHKG----------ELEEvrHKRQVDMTTYAKQIND--EYQSKLQDQIEE 261
Cdd:PRK03918 400 KEEIEEEISKITARIGELKKEIKELKKAIEELKKakgkcpvcgrELTE--EHRKELLEEYTAELKRieKELKEIEEKERK 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506429 262 MRAQFKN---------NLHQNKTAFED--AYKNKLNA-ARERQEEAVSEAIHLRARVRDLETSSSGNASLIERLRsELDT 329
Cdd:PRK03918 478 LRKELRElekvlkkesELIKLKELAEQlkELEEKLKKyNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLE-ELKK 556
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506429 330 LKRSFQEKLDDKDARIAELNQEIERMMSEFHDLLDVKIQ-LDA------ELKTYQALLEGEEERLNLTQE 392
Cdd:PRK03918 557 KLAELEKKLDELEEELAELLKELEELGFESVEELEERLKeLEPfyneylELKDAEKELEREEKELKKLEE 626
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
46-365 |
5.95e-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: 39.65 E-value: 5.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506429 46 KDHLTSLNSRLATYIDKVRQ-----------LEQENNRLQVQIR----------DIEVVEKKEKSNLADRFEAEKARLRR 104
Cdd:TIGR01612 1428 KNHILSEESNIDTYFKNADEnnenvlllfknIEMADNKSQHILKikkdnatndhDFNINELKEHIDKSKGCKDEADKNAK 1507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506429 105 ALDSAQDELAKYRIEYDA-----AKVEVKKLKPQVEKlERELAGAEEQALHAQSIADQSQAKQKTLQARNDKLVVE---- 175
Cdd:TIGR01612 1508 AIEKNKELFEQYKKDVTEllnkySALAIKNKFAKTKK-DSEIIIKEIKDAHKKFILEAEKSEQKIKEIKKEKFRIEddaa 1586
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506429 176 -NDDLKKQNITLRDTVEGLKKAVEDETLLRTAANNKIK---ALEEDLA-FALQQHKGELEEvrhkrqvdmttyakqiNDE 250
Cdd:TIGR01612 1587 kNDKSNKAAIDIQLSLENFENKFLKISDIKKKINDCLKeteSIEKKISsFSIDSQDTELKE----------------NGD 1650
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506429 251 YQSKLQDQIEEMRAQfKNNLHQNKTAFED------AYKNKLNAARERQEEAVSEAIHLRARV--RDLETSSSGNASLIER 322
Cdd:TIGR01612 1651 NLNSLQEFLESLKDQ-KKNIEDKKKELDEldseieKIEIDVDQHKKNYEIGIIEKIKEIAIAnkEEIESIKELIEPTIEN 1729
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 17506429 323 LRSELDTlkrsfqEKLD--DKDARIAELNQEIERMMSEFHDLLDV 365
Cdd:TIGR01612 1730 LISSFNT------NDLEgiDPNEKLEEYNTEIGDIYEEFIELYNI 1768
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
45-181 |
7.78e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 38.79 E-value: 7.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506429 45 EKDHLTSLNSRLATYIDKVRQLEQENNRLQVQIrdievvekKEKSNLADRFEAEKARLRRALDSAQDELAKyrieyDAAK 124
Cdd:PRK09039 72 ERQGNQDLQDSVANLRASLSAAEAERSRLQALL--------AELAGAGAAAEGRAGELAQELDSEKQVSAR-----ALAQ 138
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 17506429 125 VEVkkLKPQVEKLERELAgAEEQALHAQSIADQ-SQAKQKTLQAR-NDKLVVENDDLKK 181
Cdd:PRK09039 139 VEL--LNQQIAALRRQLA-ALEAALDASEKRDReSQAKIADLGRRlNVALAQRVQELNR 194
|
|
| |
