|
Name |
Accession |
Description |
Interval |
E-value |
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1066-1324 |
2.61e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 78.44 E-value: 2.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1066 LRKLIANGNRRLEALALVVQHIFSERESAIKQREELSVQINNLREQLSNSVSCCEQLEKEKEEVRVTLEALFQKLQEQHQ 1145
Cdd:COG1196 244 LEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEE 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1146 sELQQLEERLKDFYS--AEWDKTHEAYQREADKCRVLMQQQVEDVRYKQEALRKQQEAAHTEQIATLkhEHETSLTELKK 1223
Cdd:COG1196 324 -ELAELEEELEELEEelEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELL--EALRAAAELAA 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1224 AYENDMQELDKTLKESEAMLNEKIETLTAENEALKERLREEQEWRRAAADKSQKDAHTLYLEQELESLRAVLEIKTNQIH 1303
Cdd:COG1196 401 QLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALA 480
|
250 260
....*....|....*....|.
gi 528467808 1304 QKDKKLMQMDKLIDDNLKLEE 1324
Cdd:COG1196 481 ELLEELAEAAARLLLLLEAEA 501
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1084-1373 |
3.27e-12 |
|
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: 71.63 E-value: 3.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1084 VQHIFSERESAIKQREeLSVQINNLreQLSNSVSCCEQLEKEKEEVRVTLEALfQKLQEQHQSELQQLEERLKDF--YSA 1161
Cdd:TIGR02168 202 LKSLERQAEKAERYKE-LKAELREL--ELALLVLRLEELREELEELQEELKEA-EEELEELTAELQELEEKLEELrlEVS 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1162 EWDKTHEAYQRE-----ADKCRvlMQQQVEDVRYKQEALRKQQEAAhTEQIATLKHEHETSLTELkkayeNDMQELDKTL 1236
Cdd:TIGR02168 278 ELEEEIEELQKElyalaNEISR--LEQQKQILRERLANLERQLEEL-EAQLEELESKLDELAEEL-----AELEEKLEEL 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1237 KESEAMLNEKIETLTAENEALKERLRE-EQEWRRAAADKSQK-------DAHTLYLEQELESLRAVLEIKTNQI--HQKD 1306
Cdd:TIGR02168 350 KEELESLEAELEELEAELEELESRLEElEEQLETLRSKVAQLelqiaslNNEIERLEARLERLEDRRERLQQEIeeLLKK 429
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528467808 1307 KKLMQMDKLIDDNLKLEECLNKVQQENEDYKARMDKHAALSRQLSTEqamLQQTLQKESKVNKRLSM 1373
Cdd:TIGR02168 430 LEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQA---LDAAERELAQLQARLDS 493
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1057-1361 |
3.78e-12 |
|
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: 71.24 E-value: 3.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1057 EKKNQCILHLRKLIANGNRRLEALAlvvqhifSERESAIKQREELSVQINNLREQLSNSVSCCEQLEKEKEEVRVTLEAL 1136
Cdd:TIGR02168 666 AKTNSSILERRREIEELEEKIEELE-------EKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARL 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1137 FQKlQEQHQSELQQLEERLKDF------YSAEWDKTHEAYQREADKcRVLMQQQVEDVRYKQEALRKQQEAAHTEqiATL 1210
Cdd:TIGR02168 739 EAE-VEQLEERIAQLSKELTELeaeieeLEERLEEAEEELAEAEAE-IEELEAQIEQLKEELKALREALDELRAE--LTL 814
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1211 KHEHETSLTELKKAYENDMQELDKTLKESE---AMLNEKIETLTAENEALKERLREEQEWRRAAADKSQKdahtlyLEQE 1287
Cdd:TIGR02168 815 LNEEAANLRERLESLERRIAATERRLEDLEeqiEELSEDIESLAAEIEELEELIEELESELEALLNERAS------LEEA 888
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1288 LESLRAVLEIKTNQIHQKDKKLMQ--------MDKLIDDNLKLEECLNKVQQE----NEDYKARMDKHAALSRQLSTEQA 1355
Cdd:TIGR02168 889 LALLRSELEELSEELRELESKRSElrreleelREKLAQLELRLEGLEVRIDNLqerlSEEYSLTLEEAEALENKIEDDEE 968
|
....*.
gi 528467808 1356 MLQQTL 1361
Cdd:TIGR02168 969 EARRRL 974
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1076-1366 |
6.06e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 67.39 E-value: 6.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1076 RLEALALVVQHIFSERESAIKQREELSVQINNLREQLSNSVSCCEQLEKEKEEVRVTLEALFQKLQ------EQHQSELQ 1149
Cdd:TIGR02168 233 RLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISrleqqkQILRERLA 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1150 QLEERLK--DFYSAEWDKTHEAYQREADKcrvlMQQQVEDVRYKQEALRKQQEAAHTEQiatlkHEHETSLTELKKAYEN 1227
Cdd:TIGR02168 313 NLERQLEelEAQLEELESKLDELAEELAE----LEEKLEELKEELESLEAELEELEAEL-----EELESRLEELEEQLET 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1228 DMQELDKtLKESEAMLNEKIETLTAENEALK---ERLREEQEWRRAAADKSQKDAhtlyLEQELESLRAVLEIKTNQIHQ 1304
Cdd:TIGR02168 384 LRSKVAQ-LELQIASLNNEIERLEARLERLEdrrERLQQEIEELLKKLEEAELKE----LQAELEELEEELEELQEELER 458
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528467808 1305 KDKKLMQMDKLIDdnlKLEECLNKVQQENEDYKARMDKHAALSRQLSTEQAMLQQTLQKESK 1366
Cdd:TIGR02168 459 LEEALEELREELE---EAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSG 517
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1055-1296 |
8.80e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 67.00 E-value: 8.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1055 QNEKKNQCILHLRKLIANGNRRLEALALVVQHIFSERESAIKQREELSVQINNLREQLSNSVSCCEQLEKEKEEVRVTLE 1134
Cdd:TIGR02168 275 EVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELE 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1135 ALFQKLQEQHQsELQQLEERLKdfysaEWDKTHEAYQREadkcRVLMQQQVEDVRYKQEALRKQQEAAHteqiATLKHEH 1214
Cdd:TIGR02168 355 SLEAELEELEA-ELEELESRLE-----ELEEQLETLRSK----VAQLELQIASLNNEIERLEARLERLE----DRRERLQ 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1215 ETSLTELKKAYENDMQELDKTLKESEAMLNEKIETLTAENEALkERLREEQEWRRAAADKSQKDAHTlyLEQELESLRAV 1294
Cdd:TIGR02168 421 QEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEAL-EELREELEEAEQALDAAERELAQ--LQARLDSLERL 497
|
..
gi 528467808 1295 LE 1296
Cdd:TIGR02168 498 QE 499
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1089-1378 |
2.42e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 65.47 E-value: 2.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1089 SERESAIKQREELSVQINNLREQLSNSVSCCEQLEKEKEEVRVTLEALFQKLQEQHQSELQQLEERLKDFYS--AEWDKT 1166
Cdd:TIGR02169 230 KEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAeiASLERS 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1167 HEAYQRE---ADKCRVLMQQQVEDVRYKQEALRKQQE------AAHTEQIATLKHEHETSLTELkkayendmQELDKTLK 1237
Cdd:TIGR02169 310 IAEKEREledAEERLAKLEAEIDKLLAEIEELEREIEeerkrrDKLTEEYAELKEELEDLRAEL--------EEVDKEFA 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1238 ESEAMLN---EKIETLTAE-NEALKERLREEQEWRRAAADKSQKDAHTLYLEQELESLRAVLEIKTNQIHQKDKKLMQmd 1313
Cdd:TIGR02169 382 ETRDELKdyrEKLEKLKREiNELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQ-- 459
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528467808 1314 kliddnlkleeclnkvqqenedykarmdkhaaLSRQLSTEQAMLQQTLQKESKVNKRLSMENEEL 1378
Cdd:TIGR02169 460 --------------------------------LAADLSKYEQELYDLKEEYDRVEKELSKLQREL 492
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1063-1382 |
3.38e-10 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 64.99 E-value: 3.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1063 ILHLRKLIANGNRRLEALALVVQHIFSERESAIKQREELSVQI----------NNLREQLSNSVSCCEQLEKEKEE---- 1128
Cdd:TIGR00618 302 VTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRrllqtlhsqeIHIRDAHEVATSIREISCQQHTLtqhi 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1129 --VRVTLEALFQKLQ-----------EQHQSELQQLEERLKDFYSAEWDKTHEAYQREADKCRVLMQQQVEDVRYKQEAL 1195
Cdd:TIGR00618 382 htLQQQKTTLTQKLQslckeldilqrEQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHL 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1196 RKQQEA--AHTEQIATLK--HEHETSLTELKKAYENDMQELDKTLKESEAMLNEKIeTLTAENEALKERL-REEQEWRra 1270
Cdd:TIGR00618 462 QESAQSlkEREQQLQTKEqiHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPAR-QDIDNPGPLTRRMqRGEQTYA-- 538
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1271 aadksqkdahtlYLEQELESLRAVLEIKTNQIhQKDKKlmQMDKLIDDNLKLEECLNKvqqenedYKARMDKhaalsrqL 1350
Cdd:TIGR00618 539 ------------QLETSEEDVYHQLTSERKQR-ASLKE--QMQEIQQSFSILTQCDNR-------SKEDIPN-------L 589
|
330 340 350
....*....|....*....|....*....|..
gi 528467808 1351 STEQAMLQQTLQKESKVNKRLSMENEELLWKL 1382
Cdd:TIGR00618 590 QNITVRLQDLTEKLSEAEDMLACEQHALLRKL 621
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1091-1379 |
9.72e-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: 9.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1091 RESAIKQREELSVQINNLREQLSNSVSCCEQLEKEKEEVRVTLEAL---FQKLQEQHQSELQQLEERLKDFYSAEwdKTH 1167
Cdd:TIGR02168 665 SAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELeeeLEQLRKELEELSRQISALRKDLARLE--AEV 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1168 EAYQREADkcrvlmQQQVEDVRYKQEalrKQQEAAHTEQIATLKHEHETSLTELKKAYENDMQELD-------------K 1234
Cdd:TIGR02168 743 EQLEERIA------QLSKELTELEAE---IEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKalrealdelraelT 813
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1235 TLKESEAMLNEKIETLTAENEALKERLRE-EQEWRRAAADKSQKDAHTLYLEQELESLRAVLEIKTNQIHQKDKKLM--- 1310
Cdd:TIGR02168 814 LLNEEAANLRERLESLERRIAATERRLEDlEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALAllr 893
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1311 -QMDKLIDDNLKLEEclnKVQQENEDYKARMDKHAALSRQLSTEQAMLQQTLQkesKVNKRLSMENEELL 1379
Cdd:TIGR02168 894 sELEELSEELRELES---KRSELRRELEELREKLAQLELRLEGLEVRIDNLQE---RLSEEYSLTLEEAE 957
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1121-1379 |
9.80e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 63.42 E-value: 9.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1121 QLEKEKEEVRVTLEalFQKLQEQhqselqqLEERLKDFYSAEWDKTHEAYQREadkcrvlmQQQVEDVRYKQEALRKQQE 1200
Cdd:COG1196 201 QLEPLERQAEKAER--YRELKEE-------LKELEAELLLLKLRELEAELEEL--------EAELEELEAELEELEAELA 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1201 AAHTEqIATLKHEHEtsltELKKAYENDMQELDKTLKESEAMLNEKIETLTAENEALKERLREEQEWRRAAADKSQKDAH 1280
Cdd:COG1196 264 ELEAE-LEELRLELE----ELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEE 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1281 TLYLEQELESLRAVLEIKTNQIHQKDKKLMQMDKLIDDNLKLEEclnkvqQENEDYKARMDKHAALSRQLSTEQAMLQQT 1360
Cdd:COG1196 339 LEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELE------ELAEELLEALRAAAELAAQLEELEEAEEAL 412
|
250
....*....|....*....
gi 528467808 1361 LQKESKVNKRLSMENEELL 1379
Cdd:COG1196 413 LERLERLEEELEELEEALA 431
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1066-1260 |
1.33e-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: 58.62 E-value: 1.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1066 LRKLIANGNRRLEALALVVQHIFSERESAIKQREELSVQINNLREQLSNSVSCCEQLEKEKEEVRVTLEALFQKLQEQ-- 1143
Cdd:COG4942 32 LQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELlr 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1144 ---------------HQSELQQLEERLKDF-YSAEWDKTHEAYQREADKCRVLMQQQVEDVRYKQEALRKQQEAAHtEQI 1207
Cdd:COG4942 112 alyrlgrqpplalllSPEDFLDAVRRLQYLkYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEER-AAL 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 528467808 1208 ATLKHEHETSLTELKKAYENDMQELDKtLKESEAMLNEKIETLTAENEALKER 1260
Cdd:COG4942 191 EALKAERQKLLARLEKELAELAAELAE-LQQEAEELEALIARLEAEAAAAAER 242
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1093-1293 |
2.24e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 59.16 E-value: 2.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1093 SAIKQREELSVQINNLREQLSNSVSCCEQLEKEKEEVRVTLEALfQKLQEQHQSEL--QQLEERLkdfysAEWDKTHEAY 1170
Cdd:COG4913 607 DNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREAL-QRLAEYSWDEIdvASAEREI-----AELEAELERL 680
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1171 QREADKCRVLmQQQVEDVRYKQEALRKQQEAAhTEQIATLKHEHETSLTELKKAYENDMQELDKTLKESEAMLNEKIETL 1250
Cdd:COG4913 681 DASSDDLAAL-EEQLEELEAELEELEEELDEL-KGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAA 758
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 528467808 1251 TAEN--EALKERLREEQEwrRAAADKSQkdahtlyLEQELESLRA 1293
Cdd:COG4913 759 LGDAveRELRENLEERID--ALRARLNR-------AEEELERAMR 794
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1089-1346 |
5.40e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 57.74 E-value: 5.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1089 SERESAIkqrEELSVQINNLREQLSNSVSCCEQLEKEKEEVRVTLEALFQKLQEQhQSELQQLEERLKdfysaewdkthE 1168
Cdd:PRK02224 380 EDRREEI---EELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAEL-EATLRTARERVE-----------E 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1169 AYQ-READKCRVLMQ--------QQVEDVRYKQEALRKQQEAAHTEQiATLKHEHEtSLTELKKAyENDMQELDKTLKES 1239
Cdd:PRK02224 445 AEAlLEAGKCPECGQpvegsphvETIEEDRERVEELEAELEDLEEEV-EEVEERLE-RAEDLVEA-EDRIERLEERREDL 521
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1240 EAMLNEKIETLTAENEALkERLREEQEWRRAAADKSQKDAHTLYLEQElESLRAVLEIktnqihqkDKKLMQMDKLIDDN 1319
Cdd:PRK02224 522 EELIAERRETIEEKRERA-EELRERAAELEAEAEEKREAAAEAEEEAE-EAREEVAEL--------NSKLAELKERIESL 591
|
250 260
....*....|....*....|....*..
gi 528467808 1320 LKLEECLNKVQQENEDYKARMDKHAAL 1346
Cdd:PRK02224 592 ERIRTLLAAIADAEDEIERLREKREAL 618
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1090-1374 |
6.34e-08 |
|
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: 56.83 E-value: 6.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1090 ERESAIKQREELSVQINNLREQLSNSVSCCE-QLEKEKEEVRVTLEALfQKLQEQHQsELQQLEERLKDFYSA--EWDKT 1166
Cdd:pfam07888 49 AQEAANRQREKEKERYKRDREQWERQRRELEsRVAELKEELRQSREKH-EELEEKYK-ELSASSEELSEEKDAllAQRAA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1167 HEAYQREADKCRVLMQQQVEDVRYKQEALRKQQEAAHTeQIATLKHEHETSLTELKKAYE------NDMQELDKTLKESE 1240
Cdd:pfam07888 127 HEARIRELEEDIKTLTQRVLERETELERMKERAKKAGA-QRKEEEAERKQLQAKLQQTEEelrslsKEFQELRNSLAQRD 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1241 A---MLNEKIETLT----------AENEALKERLREEQEwrRAAAdkSQKDAHTlyLEQELESLRAVLEIKTNQIHQKDK 1307
Cdd:pfam07888 206 TqvlQLQDTITTLTqklttahrkeAENEALLEELRSLQE--RLNA--SERKVEG--LGEELSSMAAQRDRTQAELHQARL 279
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528467808 1308 KLMQMD-KLIDDNLKLEECLNKVQQENEDYKARMDKHAALSRQLSTEQAMLQQTLQKESKVNKRLSME 1374
Cdd:pfam07888 280 QAAQLTlQLADASLALREGRARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEERMEREKLEVE 347
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1057-1296 |
7.51e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 57.37 E-value: 7.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1057 EKKNQCILHLRKLIANGNRRLEALALVVQHIFSERESAIKQREELSVQINNLREQLsnsvsccEQLEKEKEEVRVTLEAL 1136
Cdd:TIGR02168 743 EQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEEL-------KALREALDELRAELTLL 815
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1137 FQKLQEQhQSELQQLEERLkdfysAEWDKTHEAYQREADKCRVLMQQ---QVEDVRYKQEALRKQ------QEAAHTEQI 1207
Cdd:TIGR02168 816 NEEAANL-RERLESLERRI-----AATERRLEDLEEQIEELSEDIESlaaEIEELEELIEELESEleallnERASLEEAL 889
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1208 ATLKHEHETSLTELKKAyENDMQELDKTLKESEAMLNE---KIETLTAENEALKERLREEQ--EWRRAAADKSQKDAHTL 1282
Cdd:TIGR02168 890 ALLRSELEELSEELREL-ESKRSELRRELEELREKLAQlelRLEGLEVRIDNLQERLSEEYslTLEEAEALENKIEDDEE 968
|
250
....*....|....
gi 528467808 1283 YLEQELESLRAVLE 1296
Cdd:TIGR02168 969 EARRRLKRLENKIK 982
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1075-1293 |
8.05e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 57.23 E-value: 8.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1075 RRLEALALVVQHIFSERESAIKQREELSVQINNLREQLSNSVSCCEQLEKEK--EEVRVTLEALFQKLQ--EQHQSELQQ 1150
Cdd:COG4913 610 AKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIdvASAEREIAELEAELErlDASSDDLAA 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1151 LEERLKdfysaEWDKTHEAYQREADKCrvlmQQQVEDVRYKQEALRKQQEAAHTEQIATLKHEHETSLTELKKAYENDMQ 1230
Cdd:COG4913 690 LEEQLE-----ELEAELEELEEELDEL----KGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALG 760
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528467808 1231 elDKTLKESEAMLNEKIETLTAENEALKERLREE-----QEWRRAAADKSQKDAHTLYLEQELESLRA 1293
Cdd:COG4913 761 --DAVERELRENLEERIDALRARLNRAEEELERAmrafnREWPAETADLDADLESLPEYLALLDRLEE 826
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1055-1372 |
1.10e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 56.31 E-value: 1.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1055 QNEKKNQCILHLRKLIANGNRRLEALALVVQHIFSERESAIKQREELSVQINNLREQLSN--SVSCCEQLEKEKEEVRVT 1132
Cdd:COG4717 172 LAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQleNELEAAALEERLKEARLL 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1133 LEALF---------------------------------------QKLQEQHQSELQQLEERLKDFYSAEWDKTHEAYQRE 1173
Cdd:COG4717 252 LLIAAallallglggsllsliltiagvlflvlgllallflllarEKASLGKEAEELQALPALEELEEEELEELLAALGLP 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1174 ADKCRVLMQQQVEDVRYKQEALRKQQEAAHTEQIATLKHEHETSLTELKKAYENDMQELdktlkeseAMLNEKIETLTAE 1253
Cdd:COG4717 332 PDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAA--------LEQAEEYQELKEE 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1254 NEALKERLREEQEWRRAAADKSQKDAhtlyLEQELESLRAVLEIKTNQIHQKDKKL----MQMDKLIDDNLkleecLNKV 1329
Cdd:COG4717 404 LEELEEQLEELLGELEELLEALDEEE----LEEELEELEEELEELEEELEELREELaeleAELEQLEEDGE-----LAEL 474
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 528467808 1330 QQENEDYKARMDKHAALSRQLSTEQAMLQQTLQ-----KESKVNKRLS 1372
Cdd:COG4717 475 LQELEELKAELRELAEEWAALKLALELLEEAREeyreeRLPPVLERAS 522
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1075-1264 |
1.12e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.85 E-value: 1.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1075 RRLEALALVVQHIFSERESAIKQREelsvqINNLREQLSNSVSCCEQLEKEKEEVRVTLEALFQKLQEQHQSELQQLEER 1154
Cdd:COG4913 272 AELEYLRAALRLWFAQRRLELLEAE-----LEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLERE 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1155 LKDfysaeWDKTHEAYQREADKCRVLMQQQVEDVRYKQEALRKQQEAAHT--EQIATLKHEHETSLTELKKAYENDMQEL 1232
Cdd:COG4913 347 IER-----LERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAAllEALEEELEALEEALAEAEAALRDLRREL 421
|
170 180 190
....*....|....*....|....*....|..
gi 528467808 1233 DKTLKESEAmLNEKIETLTAENEALKERLREE 1264
Cdd:COG4913 422 RELEAEIAS-LERRKSNIPARLLALRDALAEA 452
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1080-1301 |
1.88e-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: 55.16 E-value: 1.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1080 LALVVQHIFSERESAIKQREELSVQINNLREQLSNSVSCCEQLEKEKEEVRVTLEALFQKLQEQhQSELQQLEERLKDF- 1158
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRAL-EQELAALEAELAELe 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1159 -----YSAEWDKTHEAYQR---------EADKCRVLMQQQVEDVRYKQEALRKQQEAAHTEQIATLKHEHETsLTELKKA 1224
Cdd:COG4942 90 keiaeLRAELEAQKEELAEllralyrlgRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAE-LAALRAE 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528467808 1225 YENDMQELDKTLKESEAmLNEKIETLTAENEALKERLREEQEWRRAAADKSQKDAHTlyLEQELESLRAVLEIKTNQ 1301
Cdd:COG4942 169 LEAERAELEALLAELEE-ERAALEALKAERQKLLARLEKELAELAAELAELQQEAEE--LEALIARLEAEAAAAAER 242
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1057-1382 |
2.57e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.16 E-value: 2.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1057 EKKNQCILHLRKLIANGNRRLEALALVVQH--IFSERESAIKQREELSVQINNLREQLSNSVSCCEQLEKEKEEVRVTLE 1134
Cdd:COG4717 98 EELEEELEELEAELEELREELEKLEKLLQLlpLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQE 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1135 ALFQKLQEQHQSELQQLEERLKDFysAEWDKTHEAYQREADKCrvlmQQQVEDVRYKQEALRKQQEAAHTEQ-------- 1206
Cdd:COG4717 178 ELEELLEQLSLATEEELQDLAEEL--EELQQRLAELEEELEEA----QEELEELEEELEQLENELEAAALEErlkearll 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1207 ------IATL-----------------------------------KHEHETSLTELKKAYENDM---QELDKTLKE---- 1238
Cdd:COG4717 252 lliaaaLLALlglggsllsliltiagvlflvlgllallflllareKASLGKEAEELQALPALEEleeEELEELLAAlglp 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1239 ---SEAMLNEKIETLTAENEALKERLREEQEWRRAAADKSQKDAHTLYLEQELESLRAVLEIKtNQIHQKDKKLmqmdKL 1315
Cdd:COG4717 332 pdlSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQA-EEYQELKEEL----EE 406
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528467808 1316 IDDNLKLEECLNKVQQENEDYKARMDKHAALSRQLSTEQAMLQQTLQKESKVNKRLS-MENEELLWKL 1382
Cdd:COG4717 407 LEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEqLEEDGELAEL 474
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1182-1378 |
2.86e-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: 54.38 E-value: 2.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1182 QQQVEDVRYKQEALRKQQEAAhTEQIATLKHEHETSLTELKKAyENDMQELDKTLKESE---AMLNEKIETLTAENEALK 1258
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAEL-EKELAALKKEEKALLKQLAAL-ERRIAALARRIRALEqelAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1259 ERLREEQEWR----RAAADKSQKDAHTLYLEQE--------LESLRAVLEIKTNQIHQKDKKLMQMDKLIDDNL----KL 1322
Cdd:COG4942 97 AELEAQKEELaellRALYRLGRQPPLALLLSPEdfldavrrLQYLKYLAPARREQAEELRADLAELAALRAELEaeraEL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 528467808 1323 EECLNKVQQENEDYKARMDKHAALSRQLSTEQAMLQQTLQKESKVNKRLSMENEEL 1378
Cdd:COG4942 177 EALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARL 232
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1120-1375 |
3.76e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 54.64 E-value: 3.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1120 EQLEKEKEEVRVTLEALFQKLQEQhQSELQQLEERLKDFysaewDKTHEAYQREADkcRVLMQQQVEDVRYKQEALRKQQ 1199
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPEL-RKELEEAEAALEEF-----RQKNGLVDLSEE--AKLLLQQLSELESQLAEARAEL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1200 EAAhTEQIATLKHEHETSLTELKKAYEND-MQELDKTLKESEAMLNEKIETLTAENEALKERLREEQEWRRAAADKSQKD 1278
Cdd:COG3206 236 AEA-EARLAALRAQLGSGPDALPELLQSPvIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRI 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1279 AHTLylEQELESLRAVLEIKTNQIHQKDKKLMQmdkliddnlkleecLNKVQQEnedykarmdkHAALSRQLSTEQAMLQ 1358
Cdd:COG3206 315 LASL--EAELEALQAREASLQAQLAQLEARLAE--------------LPELEAE----------LRRLEREVEVARELYE 368
|
250
....*....|....*....
gi 528467808 1359 QTLQK--ESKVNKRLSMEN 1375
Cdd:COG3206 369 SLLQRleEARLAEALTVGN 387
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1099-1372 |
6.11e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 54.30 E-value: 6.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1099 EELSVQINNLREQLSNSVSCCEQLEKEKEEVRVTLEALfQKLQEQHQ--SELQQLEERLKDFYSAEWDKTHEAYQREADK 1176
Cdd:PRK03918 455 EEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKE-SELIKLKElaEQLKELEEKLKKYNLEELEKKAEEYEKLKEK 533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1177 CRVLMQQQ--VEDVRYKQEALRKQQEAAHtEQIATLKHEHETSLTELKKAYENDMQELDKTLKESEAMLNEKIETLTAEN 1254
Cdd:PRK03918 534 LIKLKGEIksLKKELEKLEELKKKLAELE-KKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEK 612
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1255 EalKERLREEQEWRRAAADKSqkdahtlylEQELESLRAVLEIKTNQIHQKDKKLMQMD--KLIDDNLKLEECLNKVQQE 1332
Cdd:PRK03918 613 E--LEREEKELKKLEEELDKA---------FEELAETEKRLEELRKELEELEKKYSEEEyeELREEYLELSRELAGLRAE 681
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 528467808 1333 NEDYKARMDKHAALSRQLSTEQAMLQQTLQKESKVNKRLS 1372
Cdd:PRK03918 682 LEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALE 721
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1097-1331 |
6.33e-07 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 54.20 E-value: 6.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1097 QREELSVQINNLREQLSNSvSCCEQLEKEKEEVRVTLEALFQKLQEQH-----QSELQQLEERLKDFYSAEWDKTHEAYQ 1171
Cdd:TIGR00618 617 LLRKLQPEQDLQDVRLHLQ-QCSQELALKLTALHALQLTLTQERVREHalsirVLPKELLASRQLALQKMQSEKEQLTYW 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1172 REA-DKCRVLMQ-------------QQVEDVRYKQEALRKQQEAAHTEQIATLKHEHETSLTELKKAYENDMQEL----- 1232
Cdd:TIGR00618 696 KEMlAQCQTLLRelethieeydrefNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVtaalq 775
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1233 -DKTLKESEAMLNEKIETLTAENEALKERLREEQEWRRAaaDKSQKDAHTLYLEQELESLRAVLEIKTNQIHQKDKKLmq 1311
Cdd:TIGR00618 776 tGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPS--DEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQL-- 851
|
250 260
....*....|....*....|
gi 528467808 1312 mdkliddnLKLEECLNKVQQ 1331
Cdd:TIGR00618 852 --------LKYEECSKQLAQ 863
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1074-1350 |
1.56e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 53.15 E-value: 1.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1074 NRRLEALALVVQHIFSERESAIKQREELSVQINNLREQLSNSVSCCEQLEKEKEEVRV-TLEALFQKLQEQHQSelqqLE 1152
Cdd:TIGR02169 736 KERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIpEIQAELSKLEEEVSR----IE 811
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1153 ERLKDFYSAEWDKTHEAYQreADKCRVLMQQQVEDVRYKQEALRKQQEAAHT--EQIATLKHEHETSLTELKKAYEN--- 1227
Cdd:TIGR02169 812 ARLREIEQKLNRLTLEKEY--LEKEIQELQEQRIDLKEQIKSIEKEIENLNGkkEELEEELEELEAALRDLESRLGDlkk 889
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1228 DMQELDKTLKESEamlnEKIETLTAENEALKERLREEQEwrRAAADKSQKDAHTLYLEQELESLRAVLEIKTNQiHQKDK 1307
Cdd:TIGR02169 890 ERDELEAQLRELE----RKIEELEAQIEKKRKRLSELKA--KLEALEEELSEIEDPKGEDEEIPEEELSLEDVQ-AELQR 962
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 528467808 1308 KLMQMDKLIDDNLKLEECLNKVQQENEDYKARMDKHAALSRQL 1350
Cdd:TIGR02169 963 VEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAI 1005
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1077-1263 |
1.68e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 50.69 E-value: 1.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1077 LEALaLVVQHIFSERESAIKQREELSVQINNLREQLsnsvsccEQLEKEKEEVRVTLEALfQKLQEQHQSELQQLEERLK 1156
Cdd:COG1579 6 LRAL-LDLQELDSELDRLEHRLKELPAELAELEDEL-------AALEARLEAAKTELEDL-EKEIKRLELEIEEVEARIK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1157 DfYSAEWD-----KTHEAYQRE---ADKCRVLMQQQVEDVRYKQEALRKQQEAAhTEQIATLKHEhetsLTELKKAYEND 1228
Cdd:COG1579 77 K-YEEQLGnvrnnKEYEALQKEiesLKRRISDLEDEILELMERIEELEEELAEL-EAELAELEAE----LEEKKAELDEE 150
|
170 180 190
....*....|....*....|....*....|....*....
gi 528467808 1229 MQELDKTLKEseamLNEKIETLTA--ENEALK--ERLRE 1263
Cdd:COG1579 151 LAELEAELEE----LEAEREELAAkiPPELLAlyERIRK 185
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1066-1356 |
2.33e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 52.35 E-value: 2.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1066 LRKLIANGNRRLEALALVVQHIFSERESAIKQREELSVQINNLR------EQLSNSVSC--CEQ-LE--------KEKEE 1128
Cdd:PRK02224 396 LRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARerveeaEALLEAGKCpeCGQpVEgsphvetiEEDRE 475
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1129 VRVTLEALFQKLQEQhQSELQQLEERLKDFYSAE------WDKTHEAYQREADKcrvlmQQQVEDVRYKQEALRKQQ--- 1199
Cdd:PRK02224 476 RVEELEAELEDLEEE-VEEVEERLERAEDLVEAEdrierlEERREDLEELIAER-----RETIEEKRERAEELRERAael 549
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1200 --EAAHTEQIATLKHEH-----------ETSLTELKKAYE--NDMQELDKTLKESEA---MLNEKIETLTAENEALKERL 1261
Cdd:PRK02224 550 eaEAEEKREAAAEAEEEaeeareevaelNSKLAELKERIEslERIRTLLAAIADAEDeieRLREKREALAELNDERRERL 629
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1262 REEQEWRRAAADKSQKDAhtlyleqeLESLRAVLEIKTNQIHQKDKKLMQMDKLIDDNLK--------LEEcLNKVQQEN 1333
Cdd:PRK02224 630 AEKRERKRELEAEFDEAR--------IEEAREDKERAEEYLEQVEEKLDELREERDDLQAeigaveneLEE-LEELRERR 700
|
330 340
....*....|....*....|...
gi 528467808 1334 EDYKARMDKHAALSRQLSTEQAM 1356
Cdd:PRK02224 701 EALENRVEALEALYDEAEELESM 723
|
|
| Macoilin |
pfam09726 |
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 ... |
993-1318 |
2.37e-06 |
|
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 trasnmembrane helices, followed by a C-terminal coiled-coil region. Macoilin is a highly conserved protein present in eukaryotes. Macoilin appears to be found in the ER and be involved in the function of neurons.
Pssm-ID: 462859 [Multi-domain] Cd Length: 670 Bit Score: 52.16 E-value: 2.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 993 NNQNALHRSGSTRPTRSLSVAVDKSSKGSKAAGPTAGRTPQHSPACQAGPVEEEDEREDLRLQNEKKNQCILHLRKL--- 1069
Cdd:pfam09726 305 SEEDLLVRESVSSKSSSSSSSSNKNYKNASGGSANSSNSSPRSHSHNSGSVTSSSSSKNSKKQKGPGGKSGARHKDPaen 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1070 -IANGN-------RRLEAlalVVQHIFSERESAIKQREELSVQINNLREQLSNSVSCCEQLEKEKEEVRVTLEALFQKLQ 1141
Cdd:pfam09726 385 cIPNNQlskpdalVRLEQ---DIKKLKAELQASRQTEQELRSQISSLTSLERSLKSELGQLRQENDLLQTKLHNAVSAKQ 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1142 EQHQSeLQQLEERLKDfysaewdktheayqrEADKCRVLMQQQVEDVRYKQEALRKQQEAAhtEQIATLKHEHETSLTEL 1221
Cdd:pfam09726 462 KDKQT-VQQLEKRLKA---------------EQEARASAEKQLAEEKKRKKEEEATAARAV--ALAAASRGECTESLKQR 523
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1222 KKAYENDMQELDKTLKESEAMLNEkIETLTAENEALKERLREEQEWRRAAADKSQKDAH-----------TLYLEQELES 1290
Cdd:pfam09726 524 KRELESEIKKLTHDIKLKEEQIRE-LEIKVQELRKYKESEKDTEVLMSALSAMQDKNQHlenslsaetriKLDLFSALGD 602
|
330 340
....*....|....*....|....*...
gi 528467808 1291 LRAVLEIKTNQIHQKDKKLMQMDKLIDD 1318
Cdd:pfam09726 603 AKRQLEIAQGQIYQKDQEIKDLKQKIAE 630
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1084-1296 |
3.30e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 51.96 E-value: 3.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1084 VQHIFSERESAIKQREE--LSVQINNLREQLSNSVSCCEQLEKEKEEVRVTLEALFQKLQ--EQHQSELQQLEERLKDFy 1159
Cdd:PRK02224 185 QRGSLDQLKAQIEEKEEkdLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEehEERREELETLEAEIEDL- 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1160 saewdkthEAYQREADKCRVLMQQQVEDVRYKQEALRKQQEAAHTEqiATLKHEHETSLTELKKAYENDMQELDKTLKE- 1238
Cdd:PRK02224 264 --------RETIAETEREREELAEEVRDLRERLEELEEERDDLLAE--AGLDDADAEAVEARREELEDRDEELRDRLEEc 333
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528467808 1239 --SEAMLNEKIETLTAENEALKERLREEQEWRRAAADKSQKDAHTL--------YLEQELESLRAVLE 1296
Cdd:PRK02224 334 rvAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVedrreeieELEEEIEELRERFG 401
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1189-1383 |
3.65e-06 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 51.89 E-value: 3.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1189 RYKQEAL--RKQQEAAHTE-QIATLKHEHETSLT-ELKKAYENDMQELDKTLKESEAMLNEKIET---LTAENEALKERL 1261
Cdd:TIGR00618 177 QYTQLALmeFAKKKSLHGKaELLTLRSQLLTLCTpCMPDTYHERKQVLEKELKHLREALQQTQQShayLTQKREAQEEQL 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1262 REEQEWRRAAADksqkdahtlylEQELESLRAVLEI---KTNQIHQKDKKLMQMDKLIDDNLKLEECLNKVQ-QENEDYK 1337
Cdd:TIGR00618 257 KKQQLLKQLRAR-----------IEELRAQEAVLEEtqeRINRARKAAPLAAHIKAVTQIEQQAQRIHTELQsKMRSRAK 325
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 528467808 1338 ARMDKHAALSRQLS-TEQAMLQQTLQKESKVNKRLSmeNEELLWKLH 1383
Cdd:TIGR00618 326 LLMKRAAHVKQQSSiEEQRRLLQTLHSQEIHIRDAH--EVATSIREI 370
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1120-1276 |
5.49e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.92 E-value: 5.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1120 EQLEKEKEEVRvTLEALFQKLQEQHQsELQQLEERLKDFYS--AEWDKTHEAYQREADKCRVLMQQQVEDVRYKQ----- 1192
Cdd:COG4717 78 EELKEAEEKEE-EYAELQEELEELEE-ELEELEAELEELREelEKLEKLLQLLPLYQELEALEAELAELPERLEEleerl 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1193 ---EALRKQQEAAhTEQIATLKHEHETSLTELKKAYENDMQELDKT---LKESEAMLNEKIETLTAENEALKERLREEQE 1266
Cdd:COG4717 156 eelRELEEELEEL-EAELAELQEELEELLEQLSLATEEELQDLAEEleeLQQRLAELEEELEEAQEELEELEEELEQLEN 234
|
170
....*....|
gi 528467808 1267 WRRAAADKSQ 1276
Cdd:COG4717 235 ELEAAALEER 244
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1076-1296 |
7.16e-06 |
|
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: 50.94 E-value: 7.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1076 RLEALALVVQHIFSERESAIKQREELSVQINNLREQLSNSVSCCEQLEKEKEEVR-------VTLEALFQKLQE------ 1142
Cdd:pfam01576 65 RLAARKQELEEILHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARqklqlekVTTEAKIKKLEEdillle 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1143 ----QHQSELQQLEERLKDFYS--AEWDKTHEAYQREADKCRVlMQQQVEDVRYKQEALRKQQEAAHTEQIATLKHEHEt 1216
Cdd:pfam01576 145 dqnsKLSKERKLLEERISEFTSnlAEEEEKAKSLSKLKNKHEA-MISDLEERLKKEEKGRQELEKAKRKLEGESTDLQE- 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1217 SLTELKKAYENDMQELDKTLKESEAMLNEKIETLTAENEALKE---------RLREEQEWRRAAADKSQKdaHTLYLEQE 1287
Cdd:pfam01576 223 QIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKireleaqisELQEDLESERAARNKAEK--QRRDLGEE 300
|
....*....
gi 528467808 1288 LESLRAVLE 1296
Cdd:pfam01576 301 LEALKTELE 309
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1095-1372 |
1.02e-05 |
|
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: 50.21 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1095 IKQREELSVQ--INNLREQLsnsvscceqleKEKEEVRVTLEALFQKLQEQH---QSELQQLEERLkdfysAEWDKTHEA 1169
Cdd:pfam10174 391 VKERKINVLQkkIENLQEQL-----------RDKDKQLAGLKERVKSLQTDSsntDTALTTLEEAL-----SEKERIIER 454
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1170 YQREADKCRVLMQQQVEDVRYKQEALRKQQEAAHTEqiatlKHEHETSLTELKKAYEN---DMQELDKTLKESEAMLNEK 1246
Cdd:pfam10174 455 LKEQREREDRERLEELESLKKENKDLKEKVSALQPE-----LTEKESSLIDLKEHASSlasSGLKKDSKLKSLEIAVEQK 529
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1247 IET--------LTAENEALKERLRE---------EQEWRRAAADKSQKDAhtlyleqELESLRAVLEIKTNQIHQKDKKL 1309
Cdd:pfam10174 530 KEEcsklenqlKKAHNAEEAVRTNPeindrirllEQEVARYKEESGKAQA-------EVERLLGILREVENEKNDKDKKI 602
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528467808 1310 MQMDKLID----------DNLKLEECLNKVQ--QENEDYKARMDKHAALSRQLSTEQAM--LQQTLQKESKVNKRLS 1372
Cdd:pfam10174 603 AELESLTLrqmkeqnkkvANIKHGQQEMKKKgaQLLEEARRREDNLADNSQQLQLEELMgaLEKTRQELDATKARLS 679
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1063-1363 |
1.08e-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: 50.17 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1063 ILHLRKLIANGNRRLEALALVVQHIFSERESAIKQREELSVQINNLREQLSNSVSCCEQLEKEKEEVRVTLEALF----- 1137
Cdd:pfam01576 231 IAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKteled 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1138 --------QKLQEQHQSELQQLEERLKdfysaEWDKTHEAYQREADK----CRVLMQQQVEDVRYKQEALRKQQEAAHTE 1205
Cdd:pfam01576 311 tldttaaqQELRSKREQEVTELKKALE-----EETRSHEAQLQEMRQkhtqALEELTEQLEQAKRNKANLEKAKQALESE 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1206 ------QIATLKHEHETSLTELKKAyENDMQELDKTLKESE---AMLNEKIETLTAENEALKERLREEQewrrAAADKSQ 1276
Cdd:pfam01576 386 naelqaELRTLQQAKQDSEHKRKKL-EGQLQELQARLSESErqrAELAEKLSKLQSELESVSSLLNEAE----GKNIKLS 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1277 KDAHTlyLEQELESLRAVLEIKTNQIHQKDKKLMQMDkliDDNLKLEEclnkvQQENEDYKARmdkhaALSRQLSTEQAM 1356
Cdd:pfam01576 461 KDVSS--LESQLQDTQELLQEETRQKLNLSTRLRQLE---DERNSLQE-----QLEEEEEAKR-----NVERQLSTLQAQ 525
|
....*..
gi 528467808 1357 LQQTLQK 1363
Cdd:pfam01576 526 LSDMKKK 532
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1089-1263 |
2.13e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 49.24 E-value: 2.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1089 SERESAIKQREELSVQINNLREQLSNSVSCCEQLEKEKEEVRVTLEALFQ-KLQEQHQSELQQLEERLKDfYSAEWDKTH 1167
Cdd:COG3206 212 EEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQsPVIQQLRAQLAELEAELAE-LSARYTPNH 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1168 EAYQReadkcrvlMQQQVEDVRYKQEALRKQQEAAHTEQIATLKHEhETSLTELKKAYENDMQELDKTLKESEAmLNEKI 1247
Cdd:COG3206 291 PDVIA--------LRAQIAALRAQLQQEAQRILASLEAELEALQAR-EASLQAQLAQLEARLAELPELEAELRR-LEREV 360
|
170
....*....|....*.
gi 528467808 1248 ETLTAENEALKERLRE 1263
Cdd:COG3206 361 EVARELYESLLQRLEE 376
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1066-1296 |
2.56e-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: 48.90 E-value: 2.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1066 LRKLIANGNRRLEALALVVQHIFSERESAIKQREELSVQINNLREQLSNSVSCCEQLEKEKEEVRVTLEALfQKLQEQHQ 1145
Cdd:TIGR02168 808 LRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEAL-LNERASLE 886
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1146 SELQQLEERLKDFYSA--EWDKTHEAYQREADKCRvlmqQQVEDVRYKQEALrKQQEAahtEQIATLKHEHETSLTELKK 1223
Cdd:TIGR02168 887 EALALLRSELEELSEElrELESKRSELRRELEELR----EKLAQLELRLEGL-EVRID---NLQERLSEEYSLTLEEAEA 958
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528467808 1224 AYENDMQELDKtLKESEAMLNEKIETLTAENEALKERLREEQEwRRAAADKSQKDahtlyLEQELESLRAVLE 1296
Cdd:TIGR02168 959 LENKIEDDEEE-ARRRLKRLENKIKELGPVNLAAIEEYEELKE-RYDFLTAQKED-----LTEAKETLEEAIE 1024
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1064-1378 |
2.67e-05 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 48.81 E-value: 2.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1064 LHLRKLIANGNRRLEALALVVQHIfsERESAIKQREELSVQINNLREQLSNSVSCCEQLEKEKEEVRVTLEALFQKLQEQ 1143
Cdd:pfam02463 675 LLEIQELQEKAESELAKEEILRRQ--LEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEE 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1144 HQSELQQLEErLKDFYSAEWDKTHEAYQREADKCRVLMQQQVEDVRYKQEALRKQQEAAHTEQIATLKHEHETSLTELKK 1223
Cdd:pfam02463 753 EKSRLKKEEK-EEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIK 831
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1224 AYENDMQELDKTLKESEAMLNEKIETLTAENEALKERLREEQEWRRaaadKSQKDAHTLYLEQELESLRavleiktNQIH 1303
Cdd:pfam02463 832 EEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEE----ELEEQKLKDELESKEEKEK-------EEKK 900
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528467808 1304 QKDKKLMQMDKLIDDNLKLEECLNKVQQENEDYKarmDKHAALSRQLSTEQAMLQQTLQKESKVNKRLSMENEEL 1378
Cdd:pfam02463 901 ELEEESQKLNLLEEKENEIEERIKEEAEILLKYE---EEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEEL 972
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1071-1377 |
3.06e-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: 48.58 E-value: 3.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1071 ANGNRRLEALALVVQHIFSERESAIKQREELSVQINNLREQLsnsVSCCEQLEKEKEEVRVTLEALFQklqeQHQSELQQ 1150
Cdd:pfam15921 199 ASGKKIYEHDSMSTMHFRSLGSAISKILRELDTEISYLKGRI---FPVEDQLEALKSESQNKIELLLQ----QHQDRIEQ 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1151 LEERLKDFYSAEWDKTHEAyQREADKcrvlMQQQVEDVrykQEALRKQQeAAHTEQIATLKH---EHETSLTELKKAYEN 1227
Cdd:pfam15921 272 LISEHEVEITGLTEKASSA-RSQANS----IQSQLEII---QEQARNQN-SMYMRQLSDLEStvsQLRSELREAKRMYED 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1228 DMQELDKTL-----------------KESEAMLNEKIETLTAENEALKERLREEQEWRRAAADKSQKDAHTlyleqeLES 1290
Cdd:pfam15921 343 KIEELEKQLvlanseltearterdqfSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSIT------IDH 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1291 LRAVLEIKTNQIHQKDKKLMQMDKliDDNLKLEECLNKVQQENEDykarMDKHAALSRQLSTEQAMLQQTLqkESKVNKR 1370
Cdd:pfam15921 417 LRRELDDRNMEVQRLEALLKAMKS--ECQGQMERQMAAIQGKNES----LEKVSSLTAQLESTKEMLRKVV--EELTAKK 488
|
....*..
gi 528467808 1371 LSMENEE 1377
Cdd:pfam15921 489 MTLESSE 495
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1121-1293 |
3.09e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 46.84 E-value: 3.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1121 QLEKEKEEVRVTLEALFQKLQEqHQSELQQLEERLKDFysaewDKTHEAYQREADKCrvlmQQQVEDVRYKQEALRKQQE 1200
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAE-LEDELAALEARLEAA-----KTELEDLEKEIKRL----ELEIEEVEARIKKYEEQLG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1201 AAHTE-QIATLKHEhetsLTELKKayenDMQELDKTLKEseamLNEKIETLTAENEALKERLREEQEwrRAAADKSQKDA 1279
Cdd:COG1579 84 NVRNNkEYEALQKE----IESLKR----RISDLEDEILE----LMERIEELEEELAELEAELAELEA--ELEEKKAELDE 149
|
170
....*....|....
gi 528467808 1280 HTLYLEQELESLRA 1293
Cdd:COG1579 150 ELAELEAELEELEA 163
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1168-1291 |
3.21e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 48.24 E-value: 3.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1168 EAYQREADkcRVLMQQQVEDVRYKQEALRKQQEAAHTeqiatLKHEHETSLTElkkaYENDMQELDKTLKESEAMLNEKI 1247
Cdd:PRK12704 34 KEAEEEAK--RILEEAKKEAEAIKKEALLEAKEEIHK-----LRNEFEKELRE----RRNELQKLEKRLLQKEENLDRKL 102
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 528467808 1248 ETLTAENEALkERLREEQEWRRAAADKSQKDAHTLYLEQ--ELESL 1291
Cdd:PRK12704 103 ELLEKREEEL-EKKEKELEQKQQELEKKEEELEELIEEQlqELERI 147
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1074-1377 |
4.33e-05 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 48.20 E-value: 4.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1074 NRRLEALALVVQH--IFSERESAIKQREELSVQINNLREQLSNSVSCCEQLEkEKEEVR-------VTLEALFQKLQEQH 1144
Cdd:pfam17380 268 NEFLNQLLHIVQHqkAVSERQQQEKFEKMEQERLRQEKEEKAREVERRRKLE-EAEKARqaemdrqAAIYAEQERMAMER 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1145 QSELQ--QLEERLKDFYSAEwdktHEAYQREADKCRVLMQQQVEDVRyKQEALRKQQEAAHTEQIATlkhehetslTELK 1222
Cdd:pfam17380 347 ERELEriRQEERKRELERIR----QEEIAMEISRMRELERLQMERQQ-KNERVRQELEAARKVKILE---------EERQ 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1223 KAYENDMQELDKTLKESEAMLNEKIETLTAENEALKERLREEQEWRraaadksqkdahtlylEQELESLRavleiktNQI 1302
Cdd:pfam17380 413 RKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQER----------------QQQVERLR-------QQE 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1303 HQKDKKLMQMDKLIDDNLKLEECLNKV-QQENEDYKARM----DKHAALSRQLSTEQ-AMLQQTLQKESKVNKRLSMENE 1376
Cdd:pfam17380 470 EERKRKKLELEKEKRDRKRAEEQRRKIlEKELEERKQAMieeeRKRKLLEKEMEERQkAIYEEERRREAEEERRKQQEME 549
|
.
gi 528467808 1377 E 1377
Cdd:pfam17380 550 E 550
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1066-1342 |
4.38e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.14 E-value: 4.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1066 LRKLIANGNRRLEALalvvqhifserESAIKQREELSVQINNLREQLSNSVSCCEQLEKEKEEVRVTLEALFQKLQ--EQ 1143
Cdd:PRK03918 167 LGEVIKEIKRRIERL-----------EKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKelEE 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1144 HQSELQQLEERLKdfySAEWD-KTHEAYQREADKCRVLMQQQVEDVRYKQEALRKQQEAAHT-EQIATLKHEHETSLTEL 1221
Cdd:PRK03918 236 LKEEIEELEKELE---SLEGSkRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEyIKLSEFYEEYLDELREI 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1222 KK---AYENDMQELDKTLKESEAMlNEKIETLTAENEALKERLREEQEWRRAAADKSQKdahtlylEQELESLRAVLEIK 1298
Cdd:PRK03918 313 EKrlsRLEEEINGIEERIKELEEK-EERLEELKKKLKELEKRLEELEERHELYEEAKAK-------KEELERLKKRLTGL 384
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 528467808 1299 TnqIHQKDKKLMQMDK----LIDDNLKLEECLNKVQQENEDYKARMDK 1342
Cdd:PRK03918 385 T--PEKLEKELEELEKakeeIEEEISKITARIGELKKEIKELKKAIEE 430
|
|
| FAM184 |
pfam15665 |
Family with sequence similarity 184, A and B; The function of FAM184 is not known. |
1084-1277 |
7.92e-05 |
|
Family with sequence similarity 184, A and B; The function of FAM184 is not known.
Pssm-ID: 464788 [Multi-domain] Cd Length: 211 Bit Score: 45.42 E-value: 7.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1084 VQHIFSERESAIKQREELSVQINNLREQLSNSVSCCEQLEKEKEEvrvtleALFQKLQEQHQSELQQLEerlkdfysaew 1163
Cdd:pfam15665 27 IQQILAETREKILQYKSKIGEELDLKRRIQTLEESLEQHERMKRQ------ALTEFEQYKRRVEERELK----------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1164 dktheayQREADKCRVL-MQQQVEDVRYKQEalrkQQEAAHTEQIATLKHEHETSLTELKKAYENDMQELDKTLKE-SEA 1241
Cdd:pfam15665 90 -------AEAEHRQRVVeLSREVEEAKRAFE----EKLESFEQLQAQFEQEKRKALEELRAKHRQEIQELLTTQRAqSAS 158
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 528467808 1242 MLNEKI---ETLTAENEALKERLRE-EQEWRRAAADKSQK 1277
Cdd:pfam15665 159 SLAEQEkleELHKAELESLRKEVEDlRKEKKKLAEEYEQK 198
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1120-1332 |
8.98e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.07 E-value: 8.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1120 EQLEKEKEEvrvtLEALFQKLQEQHQSELQQLEERLKdfysaEWDKTHEAYQREADKCRVL------MQQQVEDVRYKQE 1193
Cdd:COG4717 49 ERLEKEADE----LFKPQGRKPELNLKELKELEEELK-----EAEEKEEEYAELQEELEELeeeleeLEAELEELREELE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1194 ALRKQQEAAHTEQiatLKHEHETSLTELKKAYEndmqELDKTLKESEAMLNEkIETLTAENEALKERLREEQEWRRAAAD 1273
Cdd:COG4717 120 KLEKLLQLLPLYQ---ELEALEAELAELPERLE----ELEERLEELRELEEE-LEELEAELAELQEELEELLEQLSLATE 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 528467808 1274 KSQKDAHTLYleQELESLRAVLEIKTNQIHQKDKKLMQMDKLIDDNLKLEECLNKVQQE 1332
Cdd:COG4717 192 EELQDLAEEL--EELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEA 248
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1090-1271 |
9.56e-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: 46.98 E-value: 9.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1090 ERESAIKQREELSVQINNLREQLsnsvsccEQLEKEKEEVRVTLEALFQKLQEqHQSELQQLEERLKDFySAEWDKtHEA 1169
Cdd:TIGR02169 827 EKEYLEKEIQELQEQRIDLKEQI-------KSIEKEIENLNGKKEELEEELEE-LEAALRDLESRLGDL-KKERDE-LEA 896
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1170 YQREADKCRVLMQQQVEDVRYKQEALRKQQEAAhTEQIATLKH---------EHETSLTELKK---AYENDMQELD---- 1233
Cdd:TIGR02169 897 QLRELERKIEELEAQIEKKRKRLSELKAKLEAL-EEELSEIEDpkgedeeipEEELSLEDVQAelqRVEEEIRALEpvnm 975
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 528467808 1234 ---KTLKESEAMLNE---KIETLTAENEALKERLREEQEWRRAA 1271
Cdd:TIGR02169 976 laiQEYEEVLKRLDElkeKRAKLEEERKAILERIEEYEKKKREV 1019
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1089-1302 |
1.18e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.05 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1089 SERESAIKQREELSVQINNLREQLsnsvsccEQLEKEKEEVRVTLEALFQKLQEQhQSELQQLEERLKDfYSAEWDKTHE 1168
Cdd:COG4372 31 EQLRKALFELDKLQEELEQLREEL-------EQAREELEQLEEELEQARSELEQL-EEELEELNEQLQA-AQAELAQAQE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1169 AYQREADKCRVLmQQQVEDVRYKQEALRKQQEAAhTEQIATLKHEHETSLTELKKAyENDMQELDKTLKESE-------- 1240
Cdd:COG4372 102 ELESLQEEAEEL-QEELEELQKERQDLEQQRKQL-EAQIAELQSEIAEREEELKEL-EEQLESLQEELAALEqelqalse 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528467808 1241 AMLNEKIETL--TAENEALKERLREEQEWRRAAADKSQKDAHTLYLEQELESLRAVLEIKTNQI 1302
Cdd:COG4372 179 AEAEQALDELlkEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDAL 242
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1093-1385 |
1.67e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 46.12 E-value: 1.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1093 SAIKQREELSVQINNLREQLSNSVSCCEQLEKEKEEVRVTLEALFQKLQEQHQSELQQLEERlkdfysaewDKTHEAYQR 1172
Cdd:TIGR00618 553 SERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQ---------HALLRKLQP 623
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1173 EADKCRVLMQQQvedvrykQEALRKQQEAAHTEQIA-TLKHEHET----SLTELKKAY-------ENDMQELDKTLKESE 1240
Cdd:TIGR00618 624 EQDLQDVRLHLQ-------QCSQELALKLTALHALQlTLTQERVRehalSIRVLPKELlasrqlaLQKMQSEKEQLTYWK 696
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1241 AMLNEKIETLTAENEALKERLREEQEWRRAAADKSQK-----DAHT-------------------------------LYL 1284
Cdd:TIGR00618 697 EMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDlaareDALNqslkelmhqartvlkarteahfnnneevtaaLQT 776
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1285 EQELESLRAVLEIKTNQIHQKDKKLMQMDKLI-----DDNLKLEECLNKVQQENEDYKARMDKHAALSRQLSTEQAMLQQ 1359
Cdd:TIGR00618 777 GAELSHLAAEIQFFNRLREEDTHLLKTLEAEIgqeipSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEE 856
|
330 340
....*....|....*....|....*..
gi 528467808 1360 TL-QKESKVNKRLSMENEELLWKLHNG 1385
Cdd:TIGR00618 857 CSkQLAQLTQEQAKIIQLSDKLNGINQ 883
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1243-1387 |
1.89e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 46.00 E-value: 1.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1243 LNEKIETLTAEnEALKERLREEQEWRRAAADKSQKDAHTLYLEQELESLRAVLEIKTNQIHQKDKKLMqmdkliddnlKL 1322
Cdd:COG2433 378 IEEALEELIEK-ELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIE----------RL 446
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528467808 1323 EECLNKVQQEnedYKARMDKHAALSRqLSTEQAMLQQTLQKESKVNKRLSMENEEL--LWKL-HNGDL 1387
Cdd:COG2433 447 ERELSEARSE---ERREIRKDREISR-LDREIERLERELEEERERIEELKRKLERLkeLWKLeHSGEL 510
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1090-1359 |
1.92e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.21 E-value: 1.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1090 ERESAIKQREELSVQINNLREQLSnsvscceQLEKEKEEVRVTLEAL----------FQKLQEQHQSELqqLEErlkdfY 1159
Cdd:PRK03918 392 ELEELEKAKEEIEEEISKITARIG-------ELKKEIKELKKAIEELkkakgkcpvcGRELTEEHRKEL--LEE-----Y 457
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1160 SAEWDKTHEAYQREADKCRVLMQQ--QVEDVRYKQEALRKQQEAAhtEQIATLKHE-HETSLTELKKA---YENDMQELD 1233
Cdd:PRK03918 458 TAELKRIEKELKEIEEKERKLRKElrELEKVLKKESELIKLKELA--EQLKELEEKlKKYNLEELEKKaeeYEKLKEKLI 535
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1234 K----------------TLKESEAMLNEKIETLTAENEALKERLR-------EEQEWRRaaadKSQKDAHTLYLE----- 1285
Cdd:PRK03918 536 KlkgeikslkkelekleELKKKLAELEKKLDELEEELAELLKELEelgfesvEELEERL----KELEPFYNEYLElkdae 611
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528467808 1286 QELESLRAVLEIKTNQIHQKDKKLMQMDKLIDdnlKLEECLNKVQQE--NEDYKARMDKHAALSRQLSTEQAMLQQ 1359
Cdd:PRK03918 612 KELEREEKELKKLEEELDKAFEELAETEKRLE---ELRKELEELEKKysEEEYEELREEYLELSRELAGLRAELEE 684
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1094-1376 |
2.13e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 46.12 E-value: 2.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1094 AIKQREELSVQINNLREQLSNSVSCCEQLEKEKEEVRVTLEALFQKLQEQhQSELQQLEERLKDfysaewdktheayQRE 1173
Cdd:TIGR00618 185 EFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREA-LQQTQQSHAYLTQ-------------KRE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1174 ADKCRVLMQQQVEDVRYKQEALRKQQEAAHTEQIATLKHEHETSLTELKKAYENDMQELDKTLKESEAMLNEKIETLTAE 1253
Cdd:TIGR00618 251 AQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKR 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1254 NEALKERLREEQEWRRAAADKSQKDAHTLYLEQELeSLRAVLEIKTNQIHQKDKKLMQMDKLIDDNLKLEECLNKVQQEN 1333
Cdd:TIGR00618 331 AAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVAT-SIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQ 409
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 528467808 1334 EDYKARMDKHAALSRQLSTEQAmlQQTLQKESKVNKRLSMENE 1376
Cdd:TIGR00618 410 ATIDTRTSAFRDLQGQLAHAKK--QQELQQRYAELCAAAITCT 450
|
|
| CEP63 |
pfam17045 |
Centrosomal protein of 63 kDa; CEP63 is a family of eukaryotic proteins involved in centriole ... |
1092-1298 |
2.22e-04 |
|
Centrosomal protein of 63 kDa; CEP63 is a family of eukaryotic proteins involved in centriole activity.
Pssm-ID: 465338 [Multi-domain] Cd Length: 264 Bit Score: 44.81 E-value: 2.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1092 ESAIKQREELSV----QINNLREQLSNSVSCCEQLEKEK-EEVRVTlealfQKLQEQHQSELQQLEERLKDFY--SAEWD 1164
Cdd:pfam17045 66 EELEKGKQELVAkyeqQLQKLQEELSKLKRSYEKLQRKQlKEAREE-----AKSREEDRSELSRLNGKLEEFRqkSLEWE 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1165 KTHEAYqreadkcrvlmQQQVEDVRYKQEALRKQ----QEAAHTEQIATLKHEHETSLTE-------LKKAYE-NDMQEL 1232
Cdd:pfam17045 141 QQRLQY-----------QQQVASLEAQRKALAEQssliQSAAYQVQLEGRKQCLEASQSEiqrlrskLERAQDsLCAQEL 209
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528467808 1233 D-KTLKESEAMLNEKIETLTAENEALKERLREEQEWRRAaadksqkdahtlyLEQELESLRAVLEIK 1298
Cdd:pfam17045 210 ElERLRMRVSELGDSNRKLLEEQQRLLEELRMSQRQLQV-------------LQNELMELKATLQSQ 263
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1057-1278 |
2.25e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.90 E-value: 2.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1057 EKKNQCILHLRKLIANGNRRLEALALVVQHIFSERESAIKQREELSVQINNLREQLSNSVSCCEQLEKEKEEVRVTLEal 1136
Cdd:PTZ00121 1574 EDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEE-- 1651
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1137 FQKLQEQHQSELQQLEERLKDfysaEWDKTHEAYQREADKCRVLMQ-QQVEDVRYKQEALRKQ--QEAAHTEQIATLKHE 1213
Cdd:PTZ00121 1652 LKKAEEENKIKAAEEAKKAEE----DKKKAEEAKKAEEDEKKAAEAlKKEAEEAKKAEELKKKeaEEKKKAEELKKAEEE 1727
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528467808 1214 HETSLTELKKAYENDMQELDKTLKESE---------AMLNEKIETLTAENEA-LKERLREEQEWRRAAADKSQKD 1278
Cdd:PTZ00121 1728 NKIKAEEAKKEAEEDKKKAEEAKKDEEekkkiahlkKEEEKKAEEIRKEKEAvIEEELDEEDEKRRMEVDKKIKD 1802
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1146-1368 |
2.33e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 45.81 E-value: 2.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1146 SELQQLEERLKDFYSAEwdktheAYQREADKCRVLMQQQVEDVRYKQEALR----KQQEAAHTEQIATLKHEHETSLTEL 1221
Cdd:TIGR00606 166 SEGKALKQKFDEIFSAT------RYIKALETLRQVRQTQGQKVQEHQMELKylkqYKEKACEIRDQITSKEAQLESSREI 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1222 KKAYENDMQELDKTLKESEAMLNeKIETLTAENEALKERLREEQEWRRAAADKSQKdahtLYLEQElESLRAVLEIKTNQ 1301
Cdd:TIGR00606 240 VKSYENELDPLKNRLKEIEHNLS-KIMKLDNEIKALKSRKKQMEKDNSELELKMEK----VFQGTD-EQLNDLYHNHQRT 313
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528467808 1302 IHQKDKKLMQMDKLIDDNLKLEECLNKVQQENEDYKARMDKHAALSRQLSTEQAMLQQTLQKESKVN 1368
Cdd:TIGR00606 314 VREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELD 380
|
|
| DUF4515 |
pfam14988 |
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and ... |
1090-1270 |
2.65e-04 |
|
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and eukaryotes. Proteins in this family are typically between 198 and 469 amino acids in length. There are two completely conserved L residues that may be functionally important.
Pssm-ID: 405647 [Multi-domain] Cd Length: 206 Bit Score: 43.99 E-value: 2.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1090 ERESAIKQREELSV----QINNLREQLsnsvsccEQLEKEKEEVRVTLEAL--FQKLQEQHQSELQQLEERLKDFYSAEW 1163
Cdd:pfam14988 30 ECEEIERRRQELASrytqQTAELQTQL-------LQKEKEQASLKKELQALrpFAKLKESQEREIQDLEEEKEKVRAETA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1164 DKTHEAYQREAdKCRVLMQQQVEDVRykqeaLRKQQEAAHTEQIATLKHEHETSLTELKKAYENDMQElDKTLKESEAML 1243
Cdd:pfam14988 103 EKDREAHLQFL-KEKALLEKQLQELR-----ILELGERATRELKRKAQALKLAAKQALSEFCRSIKRE-NRQLQKELLQL 175
|
170 180 190
....*....|....*....|....*....|
gi 528467808 1244 NEKIETLTAENEAL---KERLREEQEWRRA 1270
Cdd:pfam14988 176 IQETQALEAIKSKLenrKQRLKEEQWYLEA 205
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1077-1291 |
2.77e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 45.71 E-value: 2.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1077 LEALALVVQHIfsERESA-------IKQREELSVQINNLrEQLSNSVSCCEQLEKEKEEVRVTLEALFQKLQEQHQS--- 1146
Cdd:COG3096 478 YELVCKIAGEV--ERSQAwqtarelLRRYRSQQALAQRL-QQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAaee 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1147 ---ELQQLEERLKDfysaewdktHEAYQREADKCRVLMQQQVEDVRYKQEALRKQQEAAHTEQiatlkheheTSLTELKk 1223
Cdd:COG3096 555 leeLLAELEAQLEE---------LEEQAAEAVEQRSELRQQLEQLRARIKELAARAPAWLAAQ---------DALERLR- 615
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528467808 1224 ayendmQELDKTLKESEAmlnekietLTAENEALKERLRE-EQEWRRAAADKSQkdahtlyLEQELESL 1291
Cdd:COG3096 616 ------EQSGEALADSQE--------VTAAMQQLLEREREaTVERDELAARKQA-------LESQIERL 663
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
1140-1335 |
3.23e-04 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 43.36 E-value: 3.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1140 LQEQHQSELQQLeerlKDFYSaewDKTHE--AYQREadkcrvlMQQQVEDVRyKQEALRKQQEAAHTEQIATLK---HEH 1214
Cdd:pfam13851 2 LMKNHEKAFNEI----KNYYN---DITRNnlELIKS-------LKEEIAELK-KKEERNEKLMSEIQQENKRLTeplQKA 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1215 ETSLTELKKA---YENDMQELdKTLKESEAMLNEKIETLTAENEALKERLREEQEWRRAAADKSQKDAHT---------L 1282
Cdd:pfam13851 67 QEEVEELRKQlenYEKDKQSL-KNLKARLKVLEKELKDLKWEHEVLEQRFEKVERERDELYDKFEAAIQDvqqktglknL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1283 YLEQELESLRAVLEIKTNQIHQ-------KDKKLMQMDKliddnlKLEECLNKVQQENED 1335
Cdd:pfam13851 146 LLEKKLQALGETLEKKEAQLNEvlaaanlDPDALQAVTE------KLEDVLESKNQLIKD 199
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1066-1368 |
3.90e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 44.13 E-value: 3.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1066 LRKLIANGNRRLEALALVVQHIFSERESAIKQREELSVQINNLREQLSNSVSCCEQLEKEKEEVRVTLEALFQKLqEQHQ 1145
Cdd:COG1340 20 LREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELREEL-DELR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1146 SELQQLEERLKDfysaewdktheayqreadkcRVLMQQQVEDVRYKQE--ALRKQQEAAHTEQIATLkhehETSLTELKK 1223
Cdd:COG1340 99 KELAELNKAGGS--------------------IDKLRKEIERLEWRQQteVLSPEEEKELVEKIKEL----EKELEKAKK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1224 AYE--NDMQELD---KTLKESEAMLNEKIETLTAENEALKERLreeQEWRRaAADKSQKDAHTLYleQELESLRAVLEIK 1298
Cdd:COG1340 155 ALEknEKLKELRaelKELRKEAEEIHKKIKELAEEAQELHEEM---IELYK-EADELRKEADELH--KEIVEAQEKADEL 228
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528467808 1299 TNQIHQKDKKLMQMDKLIDdnlKLEECLNKVQQENEDYKARMDKHAALSR-----QLSTEQAMLqqtLQKESKVN 1368
Cdd:COG1340 229 HEEIIELQKELRELRKELK---KLRKKQRALKREKEKEELEEKAEEIFEKlkkgeKLTTEELKL---LQKSGLLE 297
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1092-1377 |
4.03e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.13 E-value: 4.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1092 ESAIKQREELSVQINNLREQlsnsvsccEQLEKEKEEVRVTLEAlfQKLQEQHQSELQQLEERLK---DFYSAEWDKTHE 1168
Cdd:PTZ00121 1486 DEAKKKAEEAKKKADEAKKA--------AEAKKKADEAKKAEEA--KKADEAKKAEEAKKADEAKkaeEKKKADELKKAE 1555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1169 AYQREADKCRVLMQQQVEDVRY----KQEALRKQQEAAHTEQIATLKHEHETSLTELKKAYENDMQELDKTLKESEAMLN 1244
Cdd:PTZ00121 1556 ELKKAEEKKKAEEAKKAEEDKNmalrKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKV 1635
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1245 EKIETLTAENEALKERLREEQEWRRAAADKSQKDAHTlyLEQELESLRAVLEIKTNQIHQKDKKLMQMDKLIDDNLKLEE 1324
Cdd:PTZ00121 1636 EQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEE--DKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAE 1713
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 528467808 1325 CLNKVQQENEDYKARMDKHAALSRQLSTEQAMLQQTLQKESKVNKRLSMENEE 1377
Cdd:PTZ00121 1714 EKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEE 1766
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1193-1378 |
4.97e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.37 E-value: 4.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1193 EALRKQQEAAHTEQIATlkheHETSLTELKKAyENDMQELDKTLKESEAmLNEKIETLTAENEALKERLRE-EQEWRRAA 1271
Cdd:COG4717 49 ERLEKEADELFKPQGRK----PELNLKELKEL-EEELKEAEEKEEEYAE-LQEELEELEEELEELEAELEElREELEKLE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1272 AdksQKDAHTLYleQELESLRAVLEIKTNQIHQKDKKLMQMDKLIDDNLKLEECLNKVQQENEDYKARMDKHAALS-RQL 1350
Cdd:COG4717 123 K---LLQLLPLY--QELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEElQDL 197
|
170 180
....*....|....*....|....*...
gi 528467808 1351 STEQAMLQQTLQKESKVNKRLSMENEEL 1378
Cdd:COG4717 198 AEELEELQQRLAELEEELEEAQEELEEL 225
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1120-1350 |
5.17e-04 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 44.14 E-value: 5.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1120 EQLEKEKEEVRVTLEALFQKLQEQHQSELQQLEERLKDFYSAEwdkthEAYQREADK-CRVLMQQQVEDVRYKQEALRKQ 1198
Cdd:pfam13868 51 EERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEY-----EEKLQEREQmDEIVERIQEEDQAEAEEKLEKQ 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1199 QEaahteqiatLKHEHETSLTELKKA----YENDMQELDKTLK------ESEAMLNEKIETLTAENEALKERLREEQEwr 1268
Cdd:pfam13868 126 RQ---------LREEIDEFNEEQAEWkeleKEEEREEDERILEylkekaEREEEREAEREEIEEEKEREIARLRAQQE-- 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1269 RAAADKSQKDAHTLYLEQE--------------------LESLRAVLEIKTNQIHQKDKKLMQMDKLIDDNL--KLEECL 1326
Cdd:pfam13868 195 KAQDEKAERDELRAKLYQEeqerkerqkereeaekkarqRQELQQAREEQIELKERRLAEEAEREEEEFERMlrKQAEDE 274
|
250 260
....*....|....*....|....
gi 528467808 1327 NKVQQENEDYKARMDKHAALSRQL 1350
Cdd:pfam13868 275 EIEQEEAEKRRMKRLEHRRELEKQ 298
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1084-1378 |
5.48e-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: 44.78 E-value: 5.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1084 VQHIFSERESAIKQREELSVQINNLREQLSNSVSCCEQLEKEKEEVRVTLEALFQKLQEQhqseLQQLEERLKdfysaEW 1163
Cdd:pfam01576 17 VKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEI----LHELESRLE-----EE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1164 DKTHEAYQREADKcrvlMQQQVEDVRYKQEALRKQQEAAHTEQIAT----LKHEHET--------SLTELKKAYENDMQE 1231
Cdd:pfam01576 88 EERSQQLQNEKKK----MQQHIQDLEEQLDEEEAARQKLQLEKVTTeakiKKLEEDIllledqnsKLSKERKLLEERISE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1232 LDKTLKESEamlnEKIETLTA---ENEA----LKERLR-EEQEWRRAAADKSQKDAHTLYLEQELESLRAVLEIKTNQIH 1303
Cdd:pfam01576 164 FTSNLAEEE----EKAKSLSKlknKHEAmisdLEERLKkEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLA 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528467808 1304 QKDKklmqmdkliddnlKLEECLNKVQQENEDYKARMDKHAALSRQLSTEQAMLQQTLQKESKVNKRLSMENEEL 1378
Cdd:pfam01576 240 KKEE-------------ELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEEL 301
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1120-1377 |
6.49e-04 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 43.75 E-value: 6.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1120 EQLEkEKEEVRVTL----EALFQKLQEQHQSELQQLEERLKdfysaewdkthEAYQREADKCRVLmQQQVED--VRYKQE 1193
Cdd:pfam13868 26 AQIA-EKKRIKAEEkeeeRRLDEMMEEERERALEEEEEKEE-----------ERKEERKRYRQEL-EEQIEEreQKRQEE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1194 ALRKQQEAAHTEQIatlkhehetslteLKKAYENDMQELDKTLKESEAMLNEKIETLTAENEA-LKERLREEQEWRRAAA 1272
Cdd:pfam13868 93 YEEKLQEREQMDEI-------------VERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWkELEKEEEREEDERILE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1273 DKSQKDAHtlylEQELESLRAVLEIKTNQIHQKDKKLMQmdKLIDDNLKLEECLNKVQQENEDYKARMDKHAALSRQLST 1352
Cdd:pfam13868 160 YLKEKAER----EEEREAEREEIEEEKEREIARLRAQQE--KAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQ 233
|
250 260
....*....|....*....|....*
gi 528467808 1353 EQAMLQQTLQKESKVNKRLSMENEE 1377
Cdd:pfam13868 234 RQELQQAREEQIELKERRLAEEAER 258
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1067-1378 |
6.60e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 44.56 E-value: 6.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1067 RKLIANGNRRLEALALVVQHIfSERESAIKQ-----REELSVQINNLREQlsnsvsccEQLEKEKEEvrvtLEALFQKLQ 1141
Cdd:COG3096 298 RRQLAEEQYRLVEMARELEEL-SARESDLEQdyqaaSDHLNLVQTALRQQ--------EKIERYQED----LEELTERLE 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1142 EQH------QSELQQLEERLKdfySAEWD----KTHEA-YQREAD--KCRVLMQQQV------------------EDVRY 1190
Cdd:COG3096 365 EQEevveeaAEQLAEAEARLE---AAEEEvdslKSQLAdYQQALDvqQTRAIQYQQAvqalekaralcglpdltpENAED 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1191 KQEALRKQQEAAhTEQIATLKH----------EHETSLTELKK-AYENDMQELDKTLKE------SEAMLNEKIETLTAE 1253
Cdd:COG3096 442 YLAAFRAKEQQA-TEEVLELEQklsvadaarrQFEKAYELVCKiAGEVERSQAWQTAREllrryrSQQALAQRLQQLRAQ 520
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1254 NEALKERLREEQEWRRAAADKSQKDAHTLYLEQELESLRAVLEIktnqihQKDKKLMQMDKLIDDNLKLEECLNKVQQEN 1333
Cdd:COG3096 521 LAELEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEA------QLEELEEQAAEAVEQRSELRQQLEQLRARI 594
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 528467808 1334 EDYKAR----MDKHAALSR-------QLSTEQAM---LQQTLQKEskvnKRLSMENEEL 1378
Cdd:COG3096 595 KELAARapawLAAQDALERlreqsgeALADSQEVtaaMQQLLERE----REATVERDEL 649
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1056-1382 |
6.68e-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: 6.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1056 NEKKNQCILHLRKLIANGNRRLEalalVVQHIFSERESAIKQREElsvQINNLREQLSNSVSCCEQLEKEKEEVRVTLEA 1135
Cdd:TIGR04523 302 NQKEQDWNKELKSELKNQEKKLE----EIQNQISQNNKIISQLNE---QISQLKKELTNSESENSEKQRELEEKQNEIEK 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1136 LfQKLQEQHQSELQQLEERLKDFysaewdkthEAYQREADKCRVLMQQQVEDVRYKQEALRKQQE---AAHTEQIATLKh 1212
Cdd:TIGR04523 375 L-KKENQSYKQEIKNLESQINDL---------ESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIErlkETIIKNNSEIK- 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1213 ehetSLTELKKAYENDMQELDKTLKEseamLNEKIETLTAENEALKERL--------REEQEWRRAAADKSQKDAHTLYL 1284
Cdd:TIGR04523 444 ----DLTNQDSVKELIIKNLDNTRES----LETQLKVLSRSINKIKQNLeqkqkelkSKEKELKKLNEEKKELEEKVKDL 515
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1285 EQELESLRAVLEIKTNQIHQKDKKLMQMDKLI---DDNLK---LEECLNKVQQENEDYKARMDKHAALSRQLsteQAMLQ 1358
Cdd:TIGR04523 516 TKKISSLKEKIEKLESEKKEKESKISDLEDELnkdDFELKkenLEKEIDEKNKEIEELKQTQKSLKKKQEEK---QELID 592
|
330 340
....*....|....*....|....
gi 528467808 1359 QTLQKESKVNKRLSmENEELLWKL 1382
Cdd:TIGR04523 593 QKEKEKKDLIKEIE-EKEKKISSL 615
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1075-1345 |
6.83e-04 |
|
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: 44.44 E-value: 6.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1075 RRLEALALVVQhifSERESAIKQREEL---SVQINNLREQLSNSVSCCEQLEKEKEEVRVTLEALFQKLQEQHQSELQQL 1151
Cdd:pfam12128 604 ERLDKAEEALQ---SAREKQAAAEEQLvqaNGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSA 680
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1152 EERLKDFySAE---WDKTH----EAYQREADKCRVLMQQQVEDVrykqEALRKQQEAAHTEQIATLKHEHETSLTELKKA 1224
Cdd:pfam12128 681 NERLNSL-EAQlkqLDKKHqawlEEQKEQKREARTEKQAYWQVV----EGALDAQLALLKAAIAARRSGAKAELKALETW 755
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1225 YENDMQELD------KTLKESEAMLNEKIE------------------TLTAENEALKERLRE-EQEWRRAAADKSQKDA 1279
Cdd:pfam12128 756 YKRDLASLGvdpdviAKLKREIRTLERKIEriavrrqevlryfdwyqeTWLQRRPRLATQLSNiERAISELQQQLARLIA 835
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1280 HTLYLEQELESLRAVLE---IKTNQIHQKDKKLMQ---------------------MDKLIDDNLKLEECLNKVQQENED 1335
Cdd:pfam12128 836 DTKLRRAKLEMERKASEkqqVRLSENLRGLRCEMSklatlkedanseqaqgsigerLAQLEDLKLKRDYLSESVKKYVEH 915
|
330
....*....|
gi 528467808 1336 YKARMDKHAA 1345
Cdd:pfam12128 916 FKNVIADHSG 925
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1070-1279 |
7.27e-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: 7.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1070 IANGNRRLEALALVVQHIFSERESAIKQREELSVQINNLREQLsnsvsccEQLEKEKEEVRVTLEALFQKLQEQHqselQ 1149
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAEL-------EALQAEIDKLQAEIAEAEAEIEERR----E 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1150 QLEERLKDFYSAEWDKTHEAyqreadkcRVLMQQQVEDVRYKQEALRKQQEaAHTEQIATLKHEHEtSLTELKKAYENDM 1229
Cdd:COG3883 87 ELGERARALYRSGGSVSYLD--------VLLGSESFSDFLDRLSALSKIAD-ADADLLEELKADKA-ELEAKKAELEAKL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 528467808 1230 QELDKTLKESEAMLNEkIETLTAENEALKERLREEQEWRRAAADKSQKDA 1279
Cdd:COG3883 157 AELEALKAELEAAKAE-LEAQQAEQEALLAQLSAEEAAAEAQLAELEAEL 205
|
|
| SHE3 |
pfam17078 |
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an ... |
1192-1375 |
7.71e-04 |
|
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an RNA-binding protein that binds specific mRNAs, including the mRNA of Ash1, which is invalid in cell-fate determination. She3 acts as an adapter protein that docks the myosin motor Myo4p onto an Ash1-She2p ribonucleoprotein complex. She3 seems to bind to Myo4p and Shep2p via different domains.
Pssm-ID: 293683 [Multi-domain] Cd Length: 228 Bit Score: 42.81 E-value: 7.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1192 QEALRK-----QQEAAHTEQIATLKHEHEtSLTELKKAYENDMQELDKTLKEseamLNEKIETLTAENEALKERLR---- 1262
Cdd:pfam17078 27 QNLLSKleiaqQKESKFLENLASLKHEND-NLSSMLNRKERRLKDLEDQLSE----LKNSYEELTESNKQLKKRLEnssa 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1263 -----EEQEWRRAAADKSQKDAHTLYLE---QELESLRAVLEIKTNQIHQKDKKLMQM----DKLIDdnLKLEECLNKVQ 1330
Cdd:pfam17078 102 settlEAELERLQIQYDALVDSQNEYKDhyqQEINTLQESLEDLKLENEKQLENYQQRissnDKDID--TKLDSYNNKFK 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 528467808 1331 QENEDYKARMDKhaalsrqLSTEQAMLQQTLQKESKVNKRLSMEN 1375
Cdd:pfam17078 180 NLDNIYVNKNNK-------LLTKLDSLAQLLDLPSWLNLYPESRN 217
|
|
| DUF4455 |
pfam14643 |
Domain of unknown function (DUF4455); This domain family is found in bacteria and eukaryotes, ... |
1122-1376 |
8.04e-04 |
|
Domain of unknown function (DUF4455); This domain family is found in bacteria and eukaryotes, and is approximately 480 amino acids in length. There are two completely conserved residues (W and P) that may be functionally important.
Pssm-ID: 464231 [Multi-domain] Cd Length: 469 Bit Score: 43.81 E-value: 8.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1122 LEKEKEEVRVTL-------EALFQKLQEQH-QSEL------QQLEERLKDFysaewdKTHEAYQreadKCRVLMQ----Q 1183
Cdd:pfam14643 131 IDKEAMEINQALlenrrayAKLFANLMEAElKQELsfrlrwQDRVDRWKAL------KTEHLIQ----EFKEFIAseeiQ 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1184 QVEDVRYKQEALRKQQEAAHTEQIATLK--------HEHETSLTELKKAYENDMQELDKTLKESEAMLNEKIETLTAENE 1255
Cdd:pfam14643 201 NPPERKKELEEMLKEQKKLQQKRLELLQkisdllppAYSKSKVEEWWASLEALNEQLDQYHDQCMTKLRAEYEEVWQECL 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1256 ALKERLREE-QEWR---------------RAAADKSQKDAHTLY--LEQELESLRAVLEIKTNQIHQKDKKLMQ------ 1311
Cdd:pfam14643 281 ARVQKLKQElLDYKvcseeeaealvneefLPLVGKLQRDAEDELekLDKFLEELAKQTEAQSEDLFKFFREAAQlwdvhq 360
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528467808 1312 --MDKLIDDN-LKLEECLNKVQQENEDYKARMDKHAALSRQLSTEQAmLQQTLQkesKVNKRLS-MENE 1376
Cdd:pfam14643 361 teLAKQELELeKKLEQCRQKHDQENQAKEAALDKKLDQLRQASTEEK-LKECLD---KALKFLDdIEKE 425
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1182-1301 |
9.17e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 43.66 E-value: 9.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1182 QQQVEDVRYKQEALRKQQEAAHTEqIATLKHEHETSLTELKKAYENDMQELDKTLKESEAMLNEKIETLTAENEALKERL 1261
Cdd:PRK00409 515 KEKLNELIASLEELERELEQKAEE-AEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKEAKKEADEIIKEL 593
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 528467808 1262 RE-EQEWRRAAADKSQKDAHTLYLEQELESLRAVLEIKTNQ 1301
Cdd:PRK00409 594 RQlQKGGYASVKAHELIEARKRLNKANEKKEKKKKKQKEKQ 634
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1055-1384 |
9.74e-04 |
|
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: 43.67 E-value: 9.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1055 QNEKKNQCILHLR-KLIANGNRRLEALALVVQHIFSERESAIKQ------------REELSVQINNLREQLSNSVSCCEQ 1121
Cdd:pfam12128 247 QQEFNTLESAELRlSHLHFGYKSDETLIASRQEERQETSAELNQllrtlddqwkekRDELNGELSAADAAVAKDRSELEA 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1122 LEKEK---EEVRVTLEALFQKLQEQHQSELQQLEERLKDFYSAEWDKThEAYQREADKCRVLMQQQVEDVRYKQEALRKQ 1198
Cdd:pfam12128 327 LEDQHgafLDADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVT-AKYNRRRSKIKEQNNRDIAGIKDKLAKIREA 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1199 QEAAHTE-------QIATLKHEHETSLTELKKAYEndmqELDKTLKESEAMLNEKI---ETLT--AENEALKERLREEQE 1266
Cdd:pfam12128 406 RDRQLAVaeddlqaLESELREQLEAGKLEFNEEEY----RLKSRLGELKLRLNQATatpELLLqlENFDERIERAREEQE 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1267 WRRAAADKSQKD---AHTLYlEQELESLRAVlEIKTNQIHQKDKKLMQM-----------------------DKLID--- 1317
Cdd:pfam12128 482 AANAEVERLQSElrqARKRR-DQASEALRQA-SRRLEERQSALDELELQlfpqagtllhflrkeapdweqsiGKVISpel 559
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1318 ----------------------------------DNLKLEECLN-KVQQENEDYKARMDKHAALSRQLSTEQAMLQQtLQ 1362
Cdd:pfam12128 560 lhrtdldpevwdgsvggelnlygvkldlkridvpEWAASEEELReRLDKAEEALQSAREKQAAAEEQLVQANGELEK-AS 638
|
410 420
....*....|....*....|..
gi 528467808 1363 KESKVNKRLSMENEELLWKLHN 1384
Cdd:pfam12128 639 REETFARTALKNARLDLRRLFD 660
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1094-1362 |
1.04e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 43.64 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1094 AIKQREELSVQINNLR-EQLSNSVsccEQLEKEKEEVRVTLEALFQKLQEQhQSELQQL--EERLkdfYSAEWDKTHEA- 1169
Cdd:PRK10246 516 AVEAYQALEPGVNQSRlDALEKEV---KKLGEEGAALRGQLDALTKQLQRD-ESEAQSLrqEEQA---LTQQWQAVCASl 588
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1170 ---YQREADKCRVLMQQQvedvRYKQE--ALRKQQE-----AAHTEQIATLKHEHETSltelKKAYENDMQELDKTLKES 1239
Cdd:PRK10246 589 nitLQPQDDIQPWLDAQE----EHERQlrLLSQRHElqgqiAAHNQQIIQYQQQIEQR----QQQLLTALAGYALTLPQE 660
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1240 EamlnekietltAENEALKERLREEQEWRraaadksQKDAHTLYLEQELESLRAVLEIktnqIHQKDKKLMQMDKLIDDN 1319
Cdd:PRK10246 661 D-----------EEASWLATRQQEAQSWQ-------QRQNELTALQNRIQQLTPLLET----LPQSDDLPHSEETVALDN 718
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 528467808 1320 LKL--EECLNKVQQEnedykarmdkhAALSRQLSTEQAMLQQTLQ 1362
Cdd:PRK10246 719 WRQvhEQCLSLHSQL-----------QTLQQQDVLEAQRLQKAQA 752
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1068-1311 |
1.09e-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: 43.57 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1068 KLIANGNRRLEALALVVQhifseresaikQREELSVQINNLREQLSNSVSCCEQLEK----EKEEVRVTLEALFQKLQEQ 1143
Cdd:pfam15921 636 KLVNAGSERLRAVKDIKQ-----------ERDQLLNEVKTSRNELNSLSEDYEVLKRnfrnKSEEMETTTNKLKMQLKSA 704
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1144 hQSELQQLEERLkdfysaewdKTHEAYQREADKCRVLMQQQVEDVRYKQEALrkQQEAAHTEQIATLKHEHETSLTELKK 1223
Cdd:pfam15921 705 -QSELEQTRNTL---------KSMEGSDGHAMKVAMGMQKQITAKRGQIDAL--QSKIQFLEEAMTNANKEKHFLKEEKN 772
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1224 AYEndmQELDKTLKESEAMLNEkIETLTAENEALKERLREEQewrrAAADKSQ---KDAHTLYLEQELESLRAVLEiktn 1300
Cdd:pfam15921 773 KLS---QELSTVATEKNKMAGE-LEVLRSQERRLKEKVANME----VALDKASlqfAECQDIIQRQEQESVRLKLQ---- 840
|
250
....*....|.
gi 528467808 1301 qiHQKDKKLMQ 1311
Cdd:pfam15921 841 --HTLDVKELQ 849
|
|
| DUF2046 |
pfam09755 |
Uncharacterized conserved protein H4 (DUF2046); This is the conserved N-terminal 350 residues ... |
1108-1358 |
1.17e-03 |
|
Uncharacterized conserved protein H4 (DUF2046); This is the conserved N-terminal 350 residues of a family of proteins of unknown function possibly containing a coiled-coil domain.
Pssm-ID: 401633 [Multi-domain] Cd Length: 304 Bit Score: 42.51 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1108 LREQLSNSVSCCEQ----LEKEKEEVRVTLEALFQKLQEQHQSE--LQQLEERLKDFYSAEWDKTHEAYQREADKCRVLM 1181
Cdd:pfam09755 22 TREQLQKRIESLQQenrvLKMELETYKLRCKALQEENRALRQASvnIQAKAEQEEEFISNTLLKKIQALKKEKETLAMNY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1182 QQQVE----DVRYKQEALRkqQEAAHTEQiaTLKHEHETSLTELKKAYEN-----------------DMQELDKTL-KES 1239
Cdd:pfam09755 102 EQEEEfltnDLSRKLTQLR--QEKVELEQ--TLEQEQEYQVNKLMRKIEKleaetlnkqtnleqlrrEKVELENTLeQEQ 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1240 EAMLN---EKIETLTAENEALKERL----------REEQEWRRAAADKSqkdAHTLYLEQELESLRAVLEIKTNQIHQKD 1306
Cdd:pfam09755 178 EALVNrlwKRMDKLEAEKRLLQEKLdqpvsappspRDSTSEGDTAQNLT---AHIQYLRKEVERLRRQLATAQQEHTEKM 254
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 528467808 1307 KKLMQMDKLI-DDNLKLEEclnKVQQEnedykarMDKHAALSRQLSTEQAMLQ 1358
Cdd:pfam09755 255 AQYAQEERHIrEENLRLQR---KLQLE-------MERREALCRHLSESESSLE 297
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1094-1355 |
1.21e-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: 43.67 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1094 AIKQREELSVQINNLREQLSnsVSCCEQLEKEK---EEVRVTLEALFQKLQEQHQSELQQLEERLkdfysaewdktheay 1170
Cdd:pfam12128 647 ALKNARLDLRRLFDEKQSEK--DKKNKALAERKdsaNERLNSLEAQLKQLDKKHQAWLEEQKEQK--------------- 709
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1171 qREAdkcRVLMQQQVEDVrykqEALRKQQEAAHTEQIATLKHEHETSLTELKKAYENDMQELDKTlKESEAMLNEKIETL 1250
Cdd:pfam12128 710 -REA---RTEKQAYWQVV----EGALDAQLALLKAAIAARRSGAKAELKALETWYKRDLASLGVD-PDVIAKLKREIRTL 780
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1251 TAENEALKERLREEQEWRRAAADK--SQKDAHTLYL---EQELESLRAVLEIKTNQIHQKDKKLMQMDKLIDDNL-KLEE 1324
Cdd:pfam12128 781 ERKIERIAVRRQEVLRYFDWYQETwlQRRPRLATQLsniERAISELQQQLARLIADTKLRRAKLEMERKASEKQQvRLSE 860
|
250 260 270
....*....|....*....|....*....|.
gi 528467808 1325 CLNKVqqenedyKARMDKHAALSRQLSTEQA 1355
Cdd:pfam12128 861 NLRGL-------RCEMSKLATLKEDANSEQA 884
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1090-1382 |
1.50e-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: 43.24 E-value: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1090 ERESAIKQREELSVQINNLREQLSNSVSC-------CEQLEKEK-------EEVRVTLEALFQKLQEQHQSELQqLEERL 1155
Cdd:pfam01576 644 ALEEALEAKEELERTNKQLRAEMEDLVSSkddvgknVHELERSKraleqqvEEMKTQLEELEDELQATEDAKLR-LEVNM 722
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1156 KDFySAEWDKTHEAYQREADKCRVLMQQQVEDVRYKQEALRKQQEAAHT-------------EQIATLKHEHETSLTELK 1222
Cdd:pfam01576 723 QAL-KAQFERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAakkkleldlkeleAQIDAANKGREEAVKQLK 801
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1223 KAyENDMQELDKTLKESEAMLNE----------KIETLTAENEALKERLreeqewrrAAADKSQKDAhtlylEQELESLR 1292
Cdd:pfam01576 802 KL-QAQMKDLQRELEEARASRDEilaqskesekKLKNLEAELLQLQEDL--------AASERARRQA-----QQERDELA 867
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1293 AvlEIKTNQihqKDKKLMQMDK--LIDDNLKLEECLNKVQQENEDYKARMDKHAALSRQLSTEQAMLQQTLQKESKVNKR 1370
Cdd:pfam01576 868 D--EIASGA---SGKSALQDEKrrLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQ 942
|
330
....*....|..
gi 528467808 1371 LSMENEELLWKL 1382
Cdd:pfam01576 943 LERQNKELKAKL 954
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1055-1297 |
1.68e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 43.04 E-value: 1.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1055 QNEKKNQCILHLRKLiangnrRLEALALVVQHIFSERESAIKQREELSVQINNLREQLSNsvsccEQLEKEKEEVRVTLE 1134
Cdd:pfam02463 284 QEEELKLLAKEEEEL------KSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEI-----EELEKELKELEIKRE 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1135 ALfqKLQEQHQSELQQLEERLKDFYSAEWDKTHEAYQREADKCRVLMQQQVEDVRYKQEALRKQQEAAHTEQ----IATL 1210
Cdd:pfam02463 353 AE--EEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKeekkEELE 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1211 KHEHETSLTELKKAYENDMQELDKTLKESEAMLNEKIETLTAENEALKERLREEQewrRAAADKSQKDAHTLYLEQELES 1290
Cdd:pfam02463 431 ILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQ---LELLLSRQKLEERSQKESKARS 507
|
....*..
gi 528467808 1291 LRAVLEI 1297
Cdd:pfam02463 508 GLKVLLA 514
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1092-1377 |
1.83e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.21 E-value: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1092 ESAIKQREELSVQINNLREQLSNSVSCCEQLEKEKEEVRVTLEALFQKLQEQHQS-ELQQLEERLKDfySAEWDKTHEAY 1170
Cdd:PTZ00121 1339 EEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKAdEAKKKAEEDKK--KADELKKAAAA 1416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1171 QREADKcrvlMQQQVEDVRyKQEALRKQQEAAHTEQIATLKHEHETSLTELKKAYENDMQELDKTLKESEAMLNEKIETL 1250
Cdd:PTZ00121 1417 KKKADE----AKKKAEEKK-KADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKK 1491
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1251 TAENEALKERLREEQEWRRAAADKSQKDAhtlylEQELESLRAVLEIKTNQIHQKDKKLMQMDKLID-DNLKLEECLNKV 1329
Cdd:PTZ00121 1492 AEEAKKKADEAKKAAEAKKKADEAKKAEE-----AKKADEAKKAEEAKKADEAKKAEEKKKADELKKaEELKKAEEKKKA 1566
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 528467808 1330 QQEN--EDYKARMDKHAALSRQLSTEQAMLQQTLQKESKVNKRLSMENEE 1377
Cdd:PTZ00121 1567 EEAKkaEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAE 1616
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
1084-1272 |
1.94e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 42.37 E-value: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1084 VQHIFSERESAIK----QREELSVQ-------INNLREQLSNSVSCCEQLEKEKEEVRVTLEALFQKLQEQHQSELQQLE 1152
Cdd:PRK11637 52 IQQDIAAKEKSVRqqqqQRASLLAQlkkqeeaISQASRKLRETQNTLNQLNKQIDELNASIAKLEQQQAAQERLLAAQLD 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1153 -----------------------ERLKDFYS----------AEWDKTHE--AYQREA--DKcrvlmQQQVEDVRYKQEAL 1195
Cdd:PRK11637 132 aafrqgehtglqlilsgeesqrgERILAYFGylnqarqetiAELKQTREelAAQKAEleEK-----QSQQKTLLYEQQAQ 206
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528467808 1196 RKQQEAAHTEQIATlkhehetsLTELKKAYENDMQELdKTLKESEAMLNEKIEtlTAENEAlkeRLREEQEWRRAAA 1272
Cdd:PRK11637 207 QQKLEQARNERKKT--------LTGLESSLQKDQQQL-SELRANESRLRDSIA--RAEREA---KARAEREAREAAR 269
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1220-1378 |
2.15e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 42.65 E-value: 2.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1220 ELKKAYENDMQELD-KTLKESEAMLNEKIETLTAENEALKERLREEQEWRRAAADKSQKDAHTLYLEQELESLRAVLEIK 1298
Cdd:pfam02463 170 KKKEALKKLIEETEnLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDE 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1299 TNQIHQKDKKLMQMDKLIDDNLK-LEECLNKVQQENEDYKARMDKHAALSRQLSTEQAMLQQTLQKESKVNKRLSMENEE 1377
Cdd:pfam02463 250 QEEIESSKQEIEKEEEKLAQVLKeNKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKE 329
|
.
gi 528467808 1378 L 1378
Cdd:pfam02463 330 L 330
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1178-1383 |
2.49e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 41.83 E-value: 2.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1178 RVLMQQQVEDVRYKQEALRKQQEAAHTEQIATLKHEHETSLTELKKAYENDMQELDKTLKESEAMLNEKIETLTAENEAL 1257
Cdd:pfam13868 13 SKLLAAKCNKERDAQIAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1258 KERLREEQEWRRAAADKSQKDAHTLYLEQE---LESLRAVLEIKTNQIHQKDKKLMQMDKlidDNLKLEECLNKVQQENE 1334
Cdd:pfam13868 93 YEEKLQEREQMDEIVERIQEEDQAEAEEKLekqRQLREEIDEFNEEQAEWKELEKEEERE---EDERILEYLKEKAEREE 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 528467808 1335 DYKARMdKHAALSRQLstEQAMLQQTLQKEskvnKRLSMENEELLWKLH 1383
Cdd:pfam13868 170 EREAER-EEIEEEKER--EIARLRAQQEKA----QDEKAERDELRAKLY 211
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1123-1279 |
2.54e-03 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 41.75 E-value: 2.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1123 EKEKEEVRVTLEALFQKLQEQHQseLQQLEERLKDfysAEWDKTHEayqrEADKCRVLMQQQVEDVRYKQEALRKQQEAA 1202
Cdd:TIGR02794 68 ERQKKLEQQAEEAEKQRAAEQAR--QKELEQRAAA---EKAAKQAE----QAAKQAEEKQKQAEEAKAKQAAEAKAKAEA 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1203 HTEQIATLKHEHETSLTELKKAYENDMQELDKTLKESEAMLNEK--------IETLTAENEALKERLREEQEwRRAAADK 1274
Cdd:TIGR02794 139 EAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKaeaeakakAEEAKAKAEAAKAKAAAEAA-AKAEAEA 217
|
....*
gi 528467808 1275 SQKDA 1279
Cdd:TIGR02794 218 AAAAA 222
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1099-1311 |
2.61e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 42.63 E-value: 2.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1099 EELSVQINNLREQLSNSVSCCEQLEKEKEEVRVTLEALFQKLQEQHQSELQQLEERLKDFySAEWDKTHEA---YQREAD 1175
Cdd:COG3096 839 AALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLLNKLLPQANLLADETLADRLEEL-REELDAAQEAqafIQQHGK 917
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1176 KCRVL----------------MQQQVEDVRYKQEALRKQQEAAhTEQIATLKHehetsltelkKAYEndmqeldktlkES 1239
Cdd:COG3096 918 ALAQLeplvavlqsdpeqfeqLQADYLQAKEQQRRLKQQIFAL-SEVVQRRPH----------FSYE-----------DA 975
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528467808 1240 EAMLNEKietlTAENEALKERLREEQEWRRAA--ADKSQKDAHTLYLeQELESLRAVLEIKtNQIHQKDKKLMQ 1311
Cdd:COG3096 976 VGLLGEN----SDLNEKLRARLEQAEEARREAreQLRQAQAQYSQYN-QVLASLKSSRDAK-QQTLQELEQELE 1043
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1221-1379 |
2.64e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.06 E-value: 2.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1221 LKKAYENDMQELDKTLKESEAMLNEKIETLtaeNEALKERLREEQEWRRAAADKSQkdahtlyLEQELESLRAVLEIKTN 1300
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLKELKEL---EEELKEAEEKEEEYAELQEELEE-------LEEELEELEAELEELRE 116
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528467808 1301 QIHQKDKKLmQMDKLIDDNLKLEECLNKVQQENEDYKARMDKHAALSRQLSTEQAMLQQTLQKESKVNKRLSMENEELL 1379
Cdd:COG4717 117 ELEKLEKLL-QLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEEL 194
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
1148-1305 |
3.63e-03 |
|
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.
Pssm-ID: 460211 [Multi-domain] Cd Length: 175 Bit Score: 39.94 E-value: 3.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1148 LQQLEERLKDFYSAEWDKtheaYQREADKCRVLMQQQVEDVRYKQEALRKQQEAAHTEQIATLKHEHETSLTELKKAYEN 1227
Cdd:pfam01442 13 AEELQEQLGPVAQELVDR----LEKETEALRERLQKDLEEVRAKLEPYLEELQAKLGQNVEELRQRLEPYTEELRKRLNA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1228 DMQELDKTLKESEAMLNEKIE--------TLTAENEALKERLREE-QEWRRAAADKSQKdAHTLyLEQELESLRAVLEIK 1298
Cdd:pfam01442 89 DAEELQEKLAPYGEELRERLEqnvdalraRLAPYAEELRQKLAERlEELKESLAPYAEE-VQAQ-LSQRLQELREKLEPQ 166
|
....*..
gi 528467808 1299 TNQIHQK 1305
Cdd:pfam01442 167 AEDLREK 173
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1120-1278 |
3.68e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 41.44 E-value: 3.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1120 EQLEKEKEEVRvtlEALFQKL---QEQHQSELQQLEERLKDFYSAEWDKTHEAYQREADKCRVLMQQQVEDVRYKQEALR 1196
Cdd:pfam13868 172 EAEREEIEEEK---EREIARLraqQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIELK 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1197 KQQEAahtEQIATLKHEHETSLTELKKAYENDMQELDKTLKESEAmLNEKIETLTAENEALKERLREEQEWRRAAADKSQ 1276
Cdd:pfam13868 249 ERRLA---EEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLE-HRRELEKQIEEREEQRAAEREEELEEGERLREEE 324
|
..
gi 528467808 1277 KD 1278
Cdd:pfam13868 325 AE 326
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1090-1342 |
4.01e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.43 E-value: 4.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1090 ERESAIKQREELSVQINNLREQLSNSVSCCEQLEKEKEEVRVTLEALFQKLQ------EQHQSELQQLEERLKdfysaew 1163
Cdd:COG4372 11 ARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEqleeelEQARSELEQLEEELE------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1164 dKTHEAYQrEADKCRVLMQQQVEDVRYKQEALRKQQEAAHTEQiATLKHEHEtSLTELKKAYENDMQELDKTLKESE--- 1240
Cdd:COG4372 84 -ELNEQLQ-AAQAELAQAQEELESLQEEAEELQEELEELQKER-QDLEQQRK-QLEAQIAELQSEIAEREEELKELEeql 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1241 AMLNEKIETLTAENEALKERLREEQEWRRAAADKSQKDAHTLYLEQELESLRAVLEIKTNQIHQKDKKLMQMDKLIDDNL 1320
Cdd:COG4372 160 ESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALL 239
|
250 260
....*....|....*....|..
gi 528467808 1321 KLEECLNKVQQENEDYKARMDK 1342
Cdd:COG4372 240 DALELEEDKEELLEEVILKEIE 261
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
1098-1261 |
4.18e-03 |
|
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.
Pssm-ID: 460211 [Multi-domain] Cd Length: 175 Bit Score: 39.94 E-value: 4.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1098 REELSVQINNLREQLSNSVS-CCEQLEKEKEEVRVTLEALFQKLQEQHQSELQQLEERLkdfysaewdkthEAYQREadk 1176
Cdd:pfam01442 39 RERLQKDLEEVRAKLEPYLEeLQAKLGQNVEELRQRLEPYTEELRKRLNADAEELQEKL------------APYGEE--- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1177 crvlMQQQVEDvryKQEALRkQQEAAHTEQIATLKHEHetsLTELKkayendmQELDKTLKESEAMLNEKI----ETLTA 1252
Cdd:pfam01442 104 ----LRERLEQ---NVDALR-ARLAPYAEELRQKLAER---LEELK-------ESLAPYAEEVQAQLSQRLqelrEKLEP 165
|
....*....
gi 528467808 1253 ENEALKERL 1261
Cdd:pfam01442 166 QAEDLREKL 174
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1110-1370 |
4.22e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.67 E-value: 4.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1110 EQLSNSVSCCEQLEKEKEEVRvtlealfQKLQEQHQSELQQLEERLKDFYSAEWDKTHEAYQREADKCRvlmqqQVEDVR 1189
Cdd:PTZ00121 1223 AKKAEAVKKAEEAKKDAEEAK-------KAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELK-----KAEEKK 1290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1190 yKQEALRKQQEAAHTEQiATLKHEHETSLTELKKAYENDMQELDKTLKESEAMlNEKIETLTAENEALKERLREEQEWRR 1269
Cdd:PTZ00121 1291 -KADEAKKAEEKKKADE-AKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEA-KKAAEAAKAEAEAAADEAEAAEEKAE 1367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1270 AAADK-SQKDAHTLYLEQELESLRAVLEIKtNQIHQKDKKLMQMDKLIDDNLKLEECLNK---VQQENEDYKARMDKHAA 1345
Cdd:PTZ00121 1368 AAEKKkEEAKKKADAAKKKAEEKKKADEAK-KKAEEDKKKADELKKAAAAKKKADEAKKKaeeKKKADEAKKKAEEAKKA 1446
|
250 260
....*....|....*....|....*
gi 528467808 1346 LSRQLSTEQAMLQQTLQKESKVNKR 1370
Cdd:PTZ00121 1447 DEAKKKAEEAKKAEEAKKKAEEAKK 1471
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
1094-1378 |
4.36e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 41.60 E-value: 4.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1094 AIKQREELSVQINnlREQLSNSVSCCEQLEKEKEEVRVTLEALFQKLQEQHQSELQQLEERLKDFYSAEWDKTHEAYQRE 1173
Cdd:COG5022 796 FIKLQPLLSLLGS--RKEYRSYLACIIKLQKTIKREKKLRETEEVEFSLKAEVLIQKFGRSLKAKKRFSLLKKETIYLQS 873
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1174 ADKCRVLMQQQVEdvrykqealrKQQEAAHTEQIATLKHEHETSLTELKKAYENDMQELDKTLKESEAMLNEKIETLTAE 1253
Cdd:COG5022 874 AQRVELAERQLQE----------LKIDVKSISSLKLVNLELESEIIELKKSLSSDLIENLEFKTELIARLKKLLNNIDLE 943
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1254 NEALKERLREEQEWRRAAADKSQKDAhtlylEQELESLRAVLEIKTNQIHQKDKKLMQMDKLIDDNLKLEECLNKVQQEN 1333
Cdd:COG5022 944 EGPSIEYVKLPELNKLHEVESKLKET-----SEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQYGALQESTKQL 1018
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 528467808 1334 EDYKARMDKHAALSRQLSTEQAMLQQtLQKESKVNKRLSMENEEL 1378
Cdd:COG5022 1019 KELPVEVAELQSASKIISSESTELSI-LKPLQKLKGLLLLENNQL 1062
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
1138-1292 |
4.47e-03 |
|
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.
Pssm-ID: 460721 [Multi-domain] Cd Length: 297 Bit Score: 40.73 E-value: 4.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1138 QKLQEQHQSELQ---QLEERLKDFYSAEwdKTHEAYQREADKCRVLMQQQVEDVRYKQEALRKQQEAahteqiatlkheh 1214
Cdd:pfam02841 158 DKLEAKYNQVPRkgvKAEEVLQEFLQSK--EAVEEAILQTDQALTAKEKAIEAERAKAEAAEAEQEL------------- 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1215 etsLTELKKAYENDMQELDKTLKESEAMLNEKIET----LTAENEALKERLREEQEWRRAAADKSQKDAhtlyLEQELES 1290
Cdd:pfam02841 223 ---LREKQKEEEQMMEAQERSYQEHVKQLIEKMEAereqLLAEQERMLEHKLQEQEELLKEGFKTEAES----LQKEIQD 295
|
..
gi 528467808 1291 LR 1292
Cdd:pfam02841 296 LK 297
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1120-1272 |
5.14e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.30 E-value: 5.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1120 EQLEKEKEevrvtLEA--LFQKLQEQHQ-------SELQQLEERLKdfysaewdktheayQREadkcrvlmqqqvEDVRY 1190
Cdd:PRK12704 52 EAIKKEAL-----LEAkeEIHKLRNEFEkelrerrNELQKLEKRLL--------------QKE------------ENLDR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1191 KQEALRKQQEAAhteqiatlkHEHETSLTELKKAYENDMQELDKTLKESEAMLnEKIETLTAEnEAlKERLRE--EQEWR 1268
Cdd:PRK12704 101 KLELLEKREEEL---------EKKEKELEQKQQELEKKEEELEELIEEQLQEL-ERISGLTAE-EA-KEILLEkvEEEAR 168
|
....
gi 528467808 1269 RAAA 1272
Cdd:PRK12704 169 HEAA 172
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1082-1268 |
5.15e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 40.72 E-value: 5.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1082 LVVQHIFSE----RESAIkqrEELSVQINNLREQLSnsvscceqLEKE-KEEVRVTLEALFQKLqeqhqSELQQLEERLK 1156
Cdd:PRK09039 38 VVAQFFLSReisgKDSAL---DRLNSQIAELADLLS--------LERQgNQDLQDSVANLRASL-----SAAEAERSRLQ 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1157 DFYSAEWDKTHEAYQREADKCRVL-MQQQVEDVRYKQEALRKQQEAAHTEQIATLkhehetsltelkkayENDMQELDKT 1235
Cdd:PRK09039 102 ALLAELAGAGAAAEGRAGELAQELdSEKQVSARALAQVELLNQQIAALRRQLAAL---------------EAALDASEKR 166
|
170 180 190
....*....|....*....|....*....|....
gi 528467808 1236 LKESEAmlneKIETLTAE-NEALKERLREEQEWR 1268
Cdd:PRK09039 167 DRESQA----KIADLGRRlNVALAQRVQELNRYR 196
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1055-1270 |
5.72e-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: 41.20 E-value: 5.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1055 QNEKKNQCilhLRKLIANGNRRLEALALVVQHIFSERESAIKQREELSVQINNLREQLSNSVSCCEQLEKEKEEVR---V 1131
Cdd:TIGR02168 327 ELESKLDE---LAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNneiE 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1132 TLEALFQKLQEQHQSELQQLEERLKDFYSAEWDKTHEAYQrEADKCRVLMQQQVEDVRYKQEALRKQQEAAHTEQIATLK 1211
Cdd:TIGR02168 404 RLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELE-ELEEELEELQEELERLEEALEELREELEEAEQALDAAER 482
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 528467808 1212 HEHEtsLTELKKAYENDMQELDKTLKESEAMLNEKiETLTAENEALKERLREEQEWRRA 1270
Cdd:TIGR02168 483 ELAQ--LQARLDSLERLQENLEGFSEGVKALLKNQ-SGLSGILGVLSELISVDEGYEAA 538
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
1118-1332 |
6.55e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 40.39 E-value: 6.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1118 CCEQLEKEKEEVRvtleALFQKLQEQHQSELQQLeerLKDFYSAewdktheayqreADKCRVLMQQQVEDVR--YKQEA- 1194
Cdd:smart00787 71 SCKELKKYISEGR----DLFKEIEEETLINNPPL---FKEYFSA------------SPDVKLLMDKQFQLVKtfARLEAk 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1195 -----LRKQQeaahteqIATLKHEHETSLTELKKAYENDMQELDK------TLKESEAMLNEKIETLT-----------A 1252
Cdd:smart00787 132 kmwyeWRMKL-------LEGLKEGLDENLEGLKEDYKLLMKELELlnsikpKLRDRKDALEEELRQLKqledeledcdpT 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1253 ENEALKERLREEQewrRAAADKSQKDAHtlyLEQELESLRAVLEIKTNQIHQKDKKLMQMDKLIDDN--------LKLEE 1324
Cdd:smart00787 205 ELDRAKEKLKKLL---QEIMIKVKKLEE---LEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCrgftfkeiEKLKE 278
|
....*...
gi 528467808 1325 CLNKVQQE 1332
Cdd:smart00787 279 QLKLLQSL 286
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1055-1329 |
7.43e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 40.65 E-value: 7.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1055 QNEKKNQCILHLRKLIANGNRRLEALALVVQHIFSERESAIKQREELSVQINNLREQLSNSVSCCEQLEKEKEEVRvtle 1134
Cdd:pfam07888 123 QRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELR---- 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1135 alfqKLQEQHQSELQQLEERLkdfySAEWDKTHEAYQREADkcrvlMQQQVEDVRYKQEALRKQQEAAHT--EQIATLKH 1212
Cdd:pfam07888 199 ----NSLAQRDTQVLQLQDTI----TTLTQKLTTAHRKEAE-----NEALLEELRSLQERLNASERKVEGlgEELSSMAA 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1213 EHETSLTELKK----AYENDMQELDKTL----------KESEAMLN------EKIETLTAENEALKERLREEQEWRRAAA 1272
Cdd:pfam07888 266 QRDRTQAELHQarlqAAQLTLQLADASLalregrarwaQERETLQQsaeadkDRIEKLSAELQRLEERLQEERMEREKLE 345
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528467808 1273 DK--SQKDAHtlyLEQELESLRAVLEIKTN-QIHQKDKKLMQMDK--LIDDNLKLEECLNKV 1329
Cdd:pfam07888 346 VElgREKDCN---RVQLSESRRELQELKASlRVAQKEKEQLQAEKqeLLEYIRQLEQRLETV 404
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1067-1378 |
9.72e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 40.71 E-value: 9.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1067 RKLIANGNRRLEALAlvvqhifsERESAIKQRE-ELSVQINNLREQLsNSVSCCEQLEKEKEEVRVTLEALFQKLQEQHQ 1145
Cdd:PRK04863 299 RRQLAAEQYRLVEMA--------RELAELNEAEsDLEQDYQAASDHL-NLVQTALRQQEKIERYQADLEELEERLEEQNE 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1146 -SELQ--QLEERLKDFYSAEWD----KTHEA-YQR--------------------EADKCRVLMQQQVEDVRYKQEALRK 1197
Cdd:PRK04863 370 vVEEAdeQQEENEARAEAAEEEvdelKSQLAdYQQaldvqqtraiqyqqavqaleRAKQLCGLPDLTADNAEDWLEEFQA 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1198 QQEAAhTEQIATLKHE---HETSLTELKKAYE---------------NDMQELDKTLkESEAMLNEKIETLTAENEALKE 1259
Cdd:PRK04863 450 KEQEA-TEELLSLEQKlsvAQAAHSQFEQAYQlvrkiagevsrseawDVARELLRRL-REQRHLAEQLQQLRMRLSELEQ 527
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467808 1260 RLREEQEWRRAAADKSQKDAHTLYLEQELESLRAVLEIKTNQIHQkdkklmQMDKLIDDNLKLEECLNKVQQENEDYKAR 1339
Cdd:PRK04863 528 RLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSE------SVSEARERRMALRQQLEQLQARIQRLAAR 601
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 528467808 1340 ----MDKHAALSR-------QLSTEQAM---LQQTLQKEskvnKRLSMENEEL 1378
Cdd:PRK04863 602 apawLAAQDALARlreqsgeEFEDSQDVteyMQQLLERE----RELTVERDEL 650
|
|
| |
