|
Name |
Accession |
Description |
Interval |
E-value |
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
418-722 |
1.41e-145 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 427.25 E-value: 1.41e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 418 SLESAKQELVDYKQKATRILQSKEKLINSLKEGSSFEGLDSSTASSMELEELRHERELQKEEIQKLMGQIHQLRSELQDM 497
Cdd:pfam09787 1 NLESAKQELADYKQKAARILQSKEKLIASLKEGSGVEGLDSSTALTLELEELRQERDLLREEIQKLRGQIQQLRTELQEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 498 EAQQVSEAESAREQLQDLQDQIAKQRASKQELETELDRMKQEFHYVEEDLHRTKNTLQSRIKDREEEIQKLRNQLTNKTL 577
Cdd:pfam09787 81 EAQQQEEAESSREQLQELEEQLATERSARREAEAELERLQEELRYLEEELRRSKATLQSRIKDREAEIEKLRNQLTSKSQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 578 SNSSQSELESRLHQLTETLIQKQTLLESLSTEKNSLVFQLERLEQQLHSAATGPSSGSSINMSGVDSGEGTRLRNVPVLF 657
Cdd:pfam09787 161 SSSSQSELENRLHQLTETLIQKQTMLEALSTEKNSLVLQLERMEQQIKELQGEGSNGTSINMEGISDGEGTRLRNVPGLF 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1939872721 658 NDTETNLAGMYGKVRKAASSIDQFSIRLGIFLRRYPIARVFVIIYMALLHLWVMIVLLTYSPEMH 722
Cdd:pfam09787 241 SESDSDRAGMYGKVRKAASVIDKFSIRLGIFLRRYPIARLFVIIYMGLLHLWVMIVLLTYTPEMH 305
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
226-558 |
6.68e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 78.83 E-value: 6.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 226 RLENQLLRNEVQSLNQEMASLLQRSKETQEELNKARVRVEKWNVDnsksdriTRELRAQVDDLTEAVAAKDSQLAVLKVR 305
Cdd:COG1196 224 ELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAE-------LEELRLELEELELELEEAQAEEYELLAE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 306 LQEADQVLSSRTEALEALQSEKSRIMQDHNEgsslQNQALQTLQERLHEADATLKREQESYKQMQSEFATRLNKMEVERQ 385
Cdd:COG1196 297 LARLEQDIARLEERRRELEERLEELEEELAE----LEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 386 NLAEAVTLAERKYSEERkkvdDLQQQVKLHRSSLESAKQELVDYKQKATRILQSKEKLINSLKEgssfegldsstassme 465
Cdd:COG1196 373 ELAEAEEELEELAEELL----EALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAE---------------- 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 466 leeLRHERELQKEEIQKLMGQIHQLRSELQDMEAQQVSEAESAREQLQDLQDQIAKQRASKQELETELDRMKQEFHYVEE 545
Cdd:COG1196 433 ---LEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEG 509
|
330
....*....|...
gi 1939872721 546 DLHRTKNTLQSRI 558
Cdd:COG1196 510 VKAALLLAGLRGL 522
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
280-598 |
1.54e-14 |
|
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: 77.79 E-value: 1.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 280 ELRAQVDDLTEAVAAKDSQLAVLKVRLQEADQVLSSRTEALEALQSEKSRIMQDHNEGSSlQNQALQTLQERLHEADATL 359
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRK-DLARLEAEVEQLEERIAQL 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 360 KREQESYKQMQSEFATRLNKmevERQNLAEAvtlaERKYSEERKKVDDLQQQVKLHRSSLESAKQELVDYKQKATRILQS 439
Cdd:TIGR02168 753 SKELTELEAEIEELEERLEE---AEEELAEA----EAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRER 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 440 KEKLINSLKE-GSSFEGLDSSTAssmELEELRHERELQKEEIQKLMGQIHQLRSELQDMEAQQVSEAESAREQLQDLQDQ 518
Cdd:TIGR02168 826 LESLERRIAAtERRLEDLEEQIE---ELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEE 902
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 519 IAKQRASKQELETELDRMKQEFHYVEEDLHRTKNTLQsRIKDR--EEEIQKLRNQLTNKTLSNSSQSELESRLHQLTETL 596
Cdd:TIGR02168 903 LRELESKRSELRRELEELREKLAQLELRLEGLEVRID-NLQERlsEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKI 981
|
..
gi 1939872721 597 IQ 598
Cdd:TIGR02168 982 KE 983
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
232-540 |
6.46e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 72.40 E-value: 6.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 232 LRNEVQSLnQEMASLLQRSKETQEELNKARVR--VEKWNVDNSKSDRITRELRA---QVDDLTEAVAAKDSQLAVLKVRL 306
Cdd:TIGR02168 198 LERQLKSL-ERQAEKAERYKELKAELRELELAllVLRLEELREELEELQEELKEaeeELEELTAELQELEEKLEELRLEV 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 307 QEADQVLSSRTEALEALQSEKSRIMQD---HNEGSSLQNQALQTLQERLHEADATLKREQESYKQMQSEFAT-------- 375
Cdd:TIGR02168 277 SELEEEIEELQKELYALANEISRLEQQkqiLRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEElkeelesl 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 376 --RLNKMEVERQNLAEAVTLAERKYSEERKKVDDLQQQVKLHRSSLESAKQELVDYKQKATRILQSKEKLINSLKEgssf 453
Cdd:TIGR02168 357 eaELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEE---- 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 454 egldsstassmeleelrHERELQKEEIQKLMGQIHQLRSELQDMEaQQVSEAESAREQLQDLQDQIAKQRASKQELETEL 533
Cdd:TIGR02168 433 -----------------AELKELQAELEELEEELEELQEELERLE-EALEELREELEEAEQALDAAERELAQLQARLDSL 494
|
....*..
gi 1939872721 534 DRMKQEF 540
Cdd:TIGR02168 495 ERLQENL 501
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
346-628 |
8.47e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 71.89 E-value: 8.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 346 QTLQERLHEADATL--------KREQESYKQMQSEFATRLNKMEVERQNLAEAVTLAERKYSEERKKVDDLQQQVKLHRS 417
Cdd:COG1196 216 RELKEELKELEAELlllklrelEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 418 SLESAKQELVDYKQKATRILQSKEKLINSLKEgssfegldsstassmeleeLRHERELQKEEIQKLMGQIHQLRSELQDM 497
Cdd:COG1196 296 ELARLEQDIARLEERRRELEERLEELEEELAE-------------------LEEELEELEEELEELEEELEEAEEELEEA 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 498 EAQQVSEAESAREQLQDLQDQIAKQRASKQELETELDRMKQEFHYVEEDLHRTKNTLQSRIKDREEEIQKLRNQLTNKTL 577
Cdd:COG1196 357 EAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEE 436
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1939872721 578 SNSSQSELESRLHQLTETLIQKQTLLESLSTEKNSLVFQLERLEQQLHSAA 628
Cdd:COG1196 437 EEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELA 487
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
248-628 |
1.03e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 71.89 E-value: 1.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 248 QRSKETQEELNKAR---VRVEkwnvdnsksDrITRELRAQVDDL-TEAVAAKDSQlaVLKVRLQEADQVLSSRteALEAL 323
Cdd:COG1196 172 ERKEEAERKLEATEenlERLE---------D-ILGELERQLEPLeRQAEKAERYR--ELKEELKELEAELLLL--KLREL 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 324 QSEksrimqdhnegsslqnqaLQTLQERLHEADATLKREQESYKQMQSEfatrLNKMEVERQNLAEAVTLAERKYSEERK 403
Cdd:COG1196 238 EAE------------------LEELEAELEELEAELEELEAELAELEAE----LEELRLELEELELELEEAQAEEYELLA 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 404 KVDDLQQQVKLHRSSLESAKQELVDYKQKATRILQSKEKLINSLKEGSSfegldsstassmELEELRHERELQKEEIQKL 483
Cdd:COG1196 296 ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEE------------ELEEAEEELEEAEAELAEA 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 484 MGQIHQLRSELQDMEAQQVSEAESAREQLQDLQDQIAKQRASKQELETELDRMKQEFHYVEEDLHRTKNTLQSRIKDREE 563
Cdd:COG1196 364 EEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEA 443
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1939872721 564 EIQKLRNQLTNKTLSNSSQSELESRLHQLTETLIQKQTLLESLSTEKNSLVFQLERLEQQLHSAA 628
Cdd:COG1196 444 LEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLE 508
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
217-627 |
9.66e-12 |
|
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: 68.56 E-value: 9.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 217 SMSHELSNLRLENQLLRNEVQSLNQEMASLLQRSKETQEELNKARVRVEKWNVDNSKSDRITRELRAQVDDLTEAVAAKD 296
Cdd:TIGR02169 678 RLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVK 757
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 297 SQLAVLKVRLQEADQVLSSRTEALEALQSEKSR-IMQDHNEGSSLQNQALQTLQERLHEADATLKREQESYKQMQSEfat 375
Cdd:TIGR02169 758 SELKELEARIEELEEDLHKLEEALNDLEARLSHsRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKE--- 834
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 376 rlnkmeveRQNLAEAVTLAERKYSEERKKVDDLQQQvklhrssLESAKQELvdyKQKATRILQSKEKLINslkegssfeg 455
Cdd:TIGR02169 835 --------IQELQEQRIDLKEQIKSIEKEIENLNGK-------KEELEEEL---EELEAALRDLESRLGD---------- 886
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 456 ldsstassmeleelrherelQKEEIQKLMGQIHQLRSELQDMEAQqvseAESAREQLQDLQdqiAKQRASKQELETELDR 535
Cdd:TIGR02169 887 --------------------LKKERDELEAQLRELERKIEELEAQ----IEKKRKRLSELK---AKLEALEEELSEIEDP 939
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 536 MKQEFHYVEEDLHRTKntLQSRIKDREEEIQKLrnqltnKTLSNSSQSELESRLHQLTETLIQKQTLLEslstEKNSLVF 615
Cdd:TIGR02169 940 KGEDEEIPEEELSLED--VQAELQRVEEEIRAL------EPVNMLAIQEYEEVLKRLDELKEKRAKLEE----ERKAILE 1007
|
410
....*....|..
gi 1939872721 616 QLERLEQQLHSA 627
Cdd:TIGR02169 1008 RIEEYEKKKREV 1019
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
217-543 |
1.87e-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: 67.77 E-value: 1.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 217 SMSHELSNLRLENQLLRNEVQSLNQEMASLLQRSKETQEELNKARVRVEKWNVDNSKSDRITRELRAQVDDLTEAVAAKD 296
Cdd:TIGR02168 723 ELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALR 802
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 297 SQLAVLKVRLQEADQVLSSRTEALEALQSEKSRIMQdhnegsslQNQALQTLQERLHEADATLKREQESYKQMQSEFATR 376
Cdd:TIGR02168 803 EALDELRAELTLLNEEAANLRERLESLERRIAATER--------RLEDLEEQIEELSEDIESLAAEIEELEELIEELESE 874
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 377 LNKMEVERQNLAEAVTLAERKYSEERKKVDDLQQQVKLHRSSLESAKQELVDYKQKatriLQSKEKLINSLKEGSSFEGl 456
Cdd:TIGR02168 875 LEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELR----LEGLEVRIDNLQERLSEEY- 949
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 457 dsstasSMELEELRHERELQKEEIQKLMGQIHQLRSELQDM---------EAQQVSE-----------AESAREQLQDLQ 516
Cdd:TIGR02168 950 ------SLTLEEAEALENKIEDDEEEARRRLKRLENKIKELgpvnlaaieEYEELKErydfltaqkedLTEAKETLEEAI 1023
|
330 340
....*....|....*....|....*..
gi 1939872721 517 DQIakQRASKQELETELDRMKQEFHYV 543
Cdd:TIGR02168 1024 EEI--DREARERFKDTFDQVNENFQRV 1048
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
386-627 |
5.82e-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: 66.23 E-value: 5.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 386 NLAEAVTLAERKYSEE-RKKVDDLQQQVKLHRSSLESAKQELVDYKQ---KATRILQSKEKLINSLKEGSSFEGLDSSTA 461
Cdd:TIGR02168 666 AKTNSSILERRREIEElEEKIEELEEKIAELEKALAELRKELEELEEeleQLRKELEELSRQISALRKDLARLEAEVEQL 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 462 SSMELEELRHERELQkEEIQKLMGQIHQLRSELQDMEAqqvsEAESAREQLQDLQDQIAKQRASKQELETELDRMKQEFH 541
Cdd:TIGR02168 746 EERIAQLSKELTELE-AEIEELEERLEEAEEELAEAEA----EIEELEAQIEQLKEELKALREALDELRAELTLLNEEAA 820
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 542 YVEEDLHRtkntLQSRIKDREEEIQKLRNQLTNKTLS----NSSQSELESRLHQLTETLIQKQTLLESLSTEKNSLVFQL 617
Cdd:TIGR02168 821 NLRERLES----LERRIAATERRLEDLEEQIEELSEDieslAAEIEELEELIEELESELEALLNERASLEEALALLRSEL 896
|
250
....*....|
gi 1939872721 618 ERLEQQLHSA 627
Cdd:TIGR02168 897 EELSEELREL 906
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
246-631 |
1.40e-10 |
|
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: 64.97 E-value: 1.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 246 LLQRSKETQEELNKARvrvEKWNVDNSKSDRITRELRAQVD---DLTEAVAAKDSQLAVLK--VRLQEAdqvLSSRTEAL 320
Cdd:COG3096 283 LSERALELRRELFGAR---RQLAEEQYRLVEMARELEELSAresDLEQDYQAASDHLNLVQtaLRQQEK---IERYQEDL 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 321 EALqSEKSRImqdhnegsslQNQALQTLQERLHEADATLKREQESYKQMQSEFATRlnkmeveRQNLAEAVTLAeRKYSE 400
Cdd:COG3096 357 EEL-TERLEE----------QEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADY-------QQALDVQQTRA-IQYQQ 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 401 ERKKVDDLQQQVKLHRSSLESAKQELVDYKQKA----TRILQSKEKLINSLKEGSSFE-----------GLDSSTASSme 465
Cdd:COG3096 418 AVQALEKARALCGLPDLTPENAEDYLAAFRAKEqqatEEVLELEQKLSVADAARRQFEkayelvckiagEVERSQAWQ-- 495
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 466 leeLRHERELQKEEIQKLMGQIHQLRSELQDMEaQQVSEAESAREQLQDLQDQIAKQRASKQELETELDRMKQEFHYVEE 545
Cdd:COG3096 496 ---TARELLRRYRSQQALAQRLQQLRAQLAELE-QRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEE 571
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 546 DLhRTKNTLQSRIKDREEEIQKLRNQLTNK------------TLSNSSQSELESRlHQLTETLiqkQTLLE---SLSTEK 610
Cdd:COG3096 572 QA-AEAVEQRSELRQQLEQLRARIKELAARapawlaaqdaleRLREQSGEALADS-QEVTAAM---QQLLErerEATVER 646
|
410 420
....*....|....*....|...
gi 1939872721 611 NSLVFQLERLEQQLH--SAATGP 631
Cdd:COG3096 647 DELAARKQALESQIErlSQPGGA 669
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
279-629 |
1.99e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 64.55 E-value: 1.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 279 RELRAQVDDLTEAVAAKDSQLAVLKVRLQEA-DQVLSSRTEALEALQSEKSRIMQDHNEgsslQNQALQTLQERLHEADA 357
Cdd:COG4913 298 EELRAELARLEAELERLEARLDALREELDELeAQIRGNGGDRLEQLEREIERLERELEE----RERRRARLEALLAALGL 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 358 TLKREQESYKQMQSEFATRLNKMEVERQNLAEAVTLAERKYSEERKKVDDLQQQ---VKLHRSSLESAKQ---------- 424
Cdd:COG4913 374 PLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEiasLERRKSNIPARLLalrdalaeal 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 425 -----------ELVDYKQK---------------ATRILQSKEKL------INSLKEGS--SFEGLDSSTASSMELEELR 470
Cdd:COG4913 454 gldeaelpfvgELIEVRPEeerwrgaiervlggfALTLLVPPEHYaaalrwVNRLHLRGrlVYERVRTGLPDPERPRLDP 533
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 471 HERELQ------------KEEIQKLM---------------------GQIHQLRS--ELQDmeAQQVSEA----ESAREQ 511
Cdd:COG4913 534 DSLAGKldfkphpfrawlEAELGRRFdyvcvdspeelrrhpraitraGQVKGNGTrhEKDD--RRRIRSRyvlgFDNRAK 611
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 512 LQDLQDQIAKQRASKQELETELDRMKQEFHYVEE--DLHRTKNTLQSRIKD---REEEIQKLRNQLTNKTLSNSSQSELE 586
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAELDALQErrEALQRLAEYSWDEIDvasAEREIAELEAELERLDASSDDLAALE 691
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1939872721 587 SRLHQLTETLIQKQTLLESLSTEKNSLVFQLERLEQQLHSAAT 629
Cdd:COG4913 692 EQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQD 734
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
233-623 |
2.28e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 64.02 E-value: 2.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 233 RNEVQSLNQEMASLLQRSKETQEELNKARVRVEKWNvdnSKSDRITRELRAQvdDLTEAVAAKDSQLAVLKVRLQEADQV 312
Cdd:COG4717 80 LKEAEEKEEEYAELQEELEELEEELEELEAELEELR---EELEKLEKLLQLL--PLYQELEALEAELAELPERLEELEER 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 313 LSSRTEALEALQSEKSRIMQDHNEGSSLQNQALQTLQERLHEADATLKREQESYKQMQSEFATRLNKMEVERQNLAEAVT 392
Cdd:COG4717 155 LEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLEN 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 393 LAERKYSEERKKVDDLQQQVKLHRSSLESAKQELVDYKQKATRILQSKEKLInslkegSSFEGLDSSTASSMELEELRHE 472
Cdd:COG4717 235 ELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLL------ALLFLLLAREKASLGKEAEELQ 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 473 RELQKEEIQKLmgQIHQLRSELQDMEAQQVSEAESAREQLQDLQDQI-----AKQRASKQELETELDRMKQEFHYVEEDL 547
Cdd:COG4717 309 ALPALEELEEE--ELEELLAALGLPPDLSPEELLELLDRIEELQELLreaeeLEEELQLEELEQEIAALLAEAGVEDEEE 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 548 HRTKNTLQSRIKDREEEIQKLRNQLTNKT------LSNSSQSELESRLHQLTETLIQKQTLLESLSTEKNSLVFQLERLE 621
Cdd:COG4717 387 LRAALEQAEEYQELKEELEELEEQLEELLgeleelLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLE 466
|
..
gi 1939872721 622 QQ 623
Cdd:COG4717 467 ED 468
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
232-572 |
5.29e-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: 63.16 E-value: 5.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 232 LRNEVQSLNQEMASLLqRSKETQEELNKAR--VRVEKWNvdnsKSDRITRELRAQVDDLTEAVAAKDSQLAVLKVRLQEA 309
Cdd:TIGR02169 196 KRQQLERLRREREKAE-RYQALLKEKREYEgyELLKEKE----ALERQKEAIERQLASLEEELEKLTEEISELEKRLEEI 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 310 DQVLSSRTEALEALQSEKSRimqdhnegsslqnqALQTLQERLHEADATLKREQESYKQMQSEFATRLNKMEVERQNLAE 389
Cdd:TIGR02169 271 EQLLEELNKKIKDLGEEEQL--------------RVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLA 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 390 AVTLAERKYSEERKKVDDLQQQVKLHRSSLESAKQEL--VDYKQKATRILQSKEKlinslkegssfEGLDSSTassmele 467
Cdd:TIGR02169 337 EIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELeeVDKEFAETRDELKDYR-----------EKLEKLK------- 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 468 elrHERELQKEEIQKLMGQIHQLRSELQDMEAqqvsEAESAREQLQDLQDQIAKQRASKQELETELDRMKQEFHYVEEDL 547
Cdd:TIGR02169 399 ---REINELKRELDRLQEELQRLSEELADLNA----AIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQEL 471
|
330 340
....*....|....*....|....*...
gi 1939872721 548 HRTKNT---LQSRIKDREEEIQKLRNQL 572
Cdd:TIGR02169 472 YDLKEEydrVEKELSKLQRELAEAEAQA 499
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
278-565 |
8.25e-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: 62.39 E-value: 8.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 278 TRELRAQVDDLTEAVAAKDSQLAVLKVRLQEADQVLSSRTEALEALQSEKSRIMqdhNEGSSLQNQAlQTLQERLHEADA 357
Cdd:TIGR02169 669 SRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIE---KEIEQLEQEE-EKLKERLEELEE 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 358 ---TLKREQESYKQMQSEFATRLNKMEVERQNLAEAVTLAERKYSEER-KKVDDLQQQVKLHRSSLESAKQELVDYKQKA 433
Cdd:TIGR02169 745 dlsSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRiPEIQAELSKLEEEVSRIEARLREIEQKLNRL 824
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 434 TRILQSKEKLINSLKEgssfegldsstassmELEELRHERELQKEEIQKLMGQIHQLRSELQDMEAQqVSEAESAREQLQ 513
Cdd:TIGR02169 825 TLEKEYLEKEIQELQE---------------QRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAA-LRDLESRLGDLK 888
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1939872721 514 ----DLQDQIAKQRASKQELETELDRMKQEFhyveEDLHRTKNTLQSRIKDREEEI 565
Cdd:TIGR02169 889 kerdELEAQLRELERKIEELEAQIEKKRKRL----SELKAKLEALEEELSEIEDPK 940
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
221-624 |
2.09e-09 |
|
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: 60.80 E-value: 2.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 221 ELSNLRLENQLLRNEVQSLNQEMASLLQRSKETQEELNKARVRVEKWNvdNSKSDRITRELRAQVDDlteavaaKDSQLA 300
Cdd:TIGR04523 254 QLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLN--NQKEQDWNKELKSELKN-------QEKKLE 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 301 VLKVRLQEADQVLSSRTEALEALQSEKsriMQDHNEGSSLQNQalqtLQERLHEADaTLKREQESYKQMQSEFATRLNKM 380
Cdd:TIGR04523 325 EIQNQISQNNKIISQLNEQISQLKKEL---TNSESENSEKQRE----LEEKQNEIE-KLKKENQSYKQEIKNLESQINDL 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 381 EVERQNLAEAVTLAERKYSEERKKVDDLQQQVKLHRSSLESAKQELVDYKQKATrilqSKEKLINSLKegssfegldsst 460
Cdd:TIGR04523 397 ESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDS----VKELIIKNLD------------ 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 461 assmeleelrHERELQKEEIQKLMGQIHQLRSELQDME---AQQVSEAESAREQLQDLQDQIakqraskQELETELDRMK 537
Cdd:TIGR04523 461 ----------NTRESLETQLKVLSRSINKIKQNLEQKQkelKSKEKELKKLNEEKKELEEKV-------KDLTKKISSLK 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 538 QEfhyvEEDLHRTKNTLQSRIKDREEEIQKLRNQLTNKTLS---NSSQSELEsRLHQLTETLI----QKQTLLESLSTEK 610
Cdd:TIGR04523 524 EK----IEKLESEKKEKESKISDLEDELNKDDFELKKENLEkeiDEKNKEIE-ELKQTQKSLKkkqeEKQELIDQKEKEK 598
|
410
....*....|....
gi 1939872721 611 NSLVFQLERLEQQL 624
Cdd:TIGR04523 599 KDLIKEIEEKEKKI 612
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
343-581 |
1.04e-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: 57.85 E-value: 1.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 343 QALQTLQERLHEADATLKREQESYKQMQSEfatrLNKMEVERQNLAEAVTLAERKYSEERKKVDDLQQQVKLHRSSLESA 422
Cdd:COG4942 27 AELEQLQQEIAELEKELAALKKEEKALLKQ----LAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 423 KQELVDYKQKATRILQskeklINSLKEGSSFEGLDSSTASSMELEELRHERELQKEEIQKLMGQIHQLRSELQDMEAQQV 502
Cdd:COG4942 103 KEELAELLRALYRLGR-----QPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1939872721 503 SEAESAREQLQDLQDQIAKQRASKQELETELDRMKQEfhyvEEDLHRTKNTLQSRIKDREEEIQKLRNQLTNKTLSNSS 581
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKLLARLEKELAELAAE----LAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
304-608 |
1.39e-08 |
|
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: 58.54 E-value: 1.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 304 VRLQEADQVLSSRtEALEALQSEKSRIMQDHNEGSSLQNQALQTLQErLHEADATLKREQESYKQMQSEFATRLNKMEVE 383
Cdd:TIGR02169 668 FSRSEPAELQRLR-ERLEGLKRELSSLQSELRRIENRLDELSQELSD-ASRKIGEIEKEIEQLEQEEEKLKERLEELEED 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 384 RQNLAEAVTLAERKYSEERKKVDDLQQQVKLHRSSLESAKQELvdykqkATRILQSKEKLINSLKEgssfegldsstass 463
Cdd:TIGR02169 746 LSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARL------SHSRIPEIQAELSKLEE-------------- 805
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 464 meleelrherelqkeEIQKLMGQIHQLRSELQDMEAQQVSeAESAREQLQDLQDQIAKQRASKQELETELDRMKQEFHYV 543
Cdd:TIGR02169 806 ---------------EVSRIEARLREIEQKLNRLTLEKEY-LEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEE 869
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1939872721 544 EEDLHRTKNTLQSRI----KDREEEIQKLRNQLTNKTLSNSSQSELESRLHQLTETLiqkQTLLESLST 608
Cdd:TIGR02169 870 LEELEAALRDLESRLgdlkKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKL---EALEEELSE 935
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
222-618 |
2.22e-08 |
|
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: 57.52 E-value: 2.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 222 LSNLRLENQLLRNEVQSLNQEMASLLQRSKETQEELNKARVRV-EKWNVDNSKSDRITR------ELRAQVDDLTEAVAA 294
Cdd:pfam10174 312 LETLTNQNSDCKQHIEVLKESLTAKEQRAAILQTEVDALRLRLeEKESFLNKKTKQLQDlteeksTLAGEIRDLKDMLDV 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 295 KDSQLAVLKVRLQEADQVLSSRTEALEALQseksRIMQDHNEGSSLQNQALQTLQERLHEADATLKREQESYKQMQSEFA 374
Cdd:pfam10174 392 KERKINVLQKKIENLQEQLRDKDKQLAGLK----ERVKSLQTDSSNTDTALTTLEEALSEKERIIERLKEQREREDRERL 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 375 TRLNKMEVERQNLAEAVTLAERKYSEERKKVDDLQQqvklHRSSL-ESAKQELVDYKQKATRILQSKE---KLINSLKEG 450
Cdd:pfam10174 468 EELESLKKENKDLKEKVSALQPELTEKESSLIDLKE----HASSLaSSGLKKDSKLKSLEIAVEQKKEecsKLENQLKKA 543
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 451 SSFEglDSSTAS---SMELEELRHERELQKEEIQKLMGQIHQLRSELQDMEA------QQVSEAES-AREQLQDLQDQIA 520
Cdd:pfam10174 544 HNAE--EAVRTNpeiNDRIRLLEQEVARYKEESGKAQAEVERLLGILREVENekndkdKKIAELESlTLRQMKEQNKKVA 621
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 521 KQRASKQELETELDRMKQEFHYVEEDLHRtkNTLQSRIKDREEEIQKLRNQL--TNKTLSNSSQSELESRLH-------- 590
Cdd:pfam10174 622 NIKHGQQEMKKKGAQLLEEARRREDNLAD--NSQQLQLEELMGALEKTRQELdaTKARLSSTQQSLAEKDGHltnlraer 699
|
410 420 430
....*....|....*....|....*....|
gi 1939872721 591 --QLTETLIQKQTLLESLSTEKNSLVFQLE 618
Cdd:pfam10174 700 rkQLEEILEMKQEALLAAISEKDANIALLE 729
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
221-622 |
2.37e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 57.74 E-value: 2.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 221 ELSNLRLENQLLRNEVQSLNQEMASLLQRSKETQEELNKARVRVEKWNvdnSKSDRitreLRAQVDDLTEAVAAKDSQLA 300
Cdd:PRK02224 294 ERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHN---EEAES----LREDADDLEERAEELREEAA 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 301 VLKVRLQEADQVLSSRTEALEALQSEksrimqdhnegsslqnqaLQTLQERLHEADATLKREQESYKQMQSEFA---TRL 377
Cdd:PRK02224 367 ELESELEEAREAVEDRREEIEELEEE------------------IEELRERFGDAPVDLGNAEDFLEELREERDelrERE 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 378 NKMEVERQNLAEAVTLAER--------------KYSEERKKVDDLQQQVKLHRSSLESAKQELVDYKQKATRI--LQSKE 441
Cdd:PRK02224 429 AELEATLRTARERVEEAEAlleagkcpecgqpvEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAedLVEAE 508
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 442 KLINSLKEgssfegldsstassmeleelrherelQKEEIQKLmgqIHQLRSELQDMEAQqvseAESAREQLQDLQDQIAK 521
Cdd:PRK02224 509 DRIERLEE--------------------------RREDLEEL---IAERRETIEEKRER----AEELRERAAELEAEAEE 555
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 522 QRASKQELETELDRMKQEFHYVEEDLHRTKNTLQS--RIKDREEEIQKLRNQLtnktlsnssqSELESRLHQLTETLIQK 599
Cdd:PRK02224 556 KREAAAEAEEEAEEAREEVAELNSKLAELKERIESleRIRTLLAAIADAEDEI----------ERLREKREALAELNDER 625
|
410 420
....*....|....*....|....*
gi 1939872721 600 QTLLESLSTEKNSLV--FQLERLEQ 622
Cdd:PRK02224 626 RERLAEKRERKRELEaeFDEARIEE 650
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
345-623 |
3.31e-08 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 56.95 E-value: 3.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 345 LQTLQERLHEADATLKREQESYKqmqsefaTRLNKMEVERQNLAEAVTLAERKYSEERKKVDDLQQQVKLHR-------- 416
Cdd:TIGR04523 150 KEKELEKLNNKYNDLKKQKEELE-------NELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKslesqise 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 417 -----SSLESAKQELVDYKQKATRILQSKEKLINSLKegssfeglDSSTASSMELEELRHERELQKEEIQKLMGQIHQLR 491
Cdd:TIGR04523 223 lkkqnNQLKDNIEKKQQEINEKTTEISNTQTQLNQLK--------DEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLK 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 492 SELQDMEAQQV--------SEAESAREQLQDLQDQIAKQRASKQELETELDRMKQEFhyveEDLHRTKNTLQSRIKDREE 563
Cdd:TIGR04523 295 SEISDLNNQKEqdwnkelkSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKEL----TNSESENSEKQRELEEKQN 370
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1939872721 564 EIQKLRNQ----LTNKTLSNSSQSELESRLHQLTETLIQKQTLLESLSTEKNSLVFQLERLEQQ 623
Cdd:TIGR04523 371 EIEKLKKEnqsyKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKET 434
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
226-613 |
3.66e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 56.97 E-value: 3.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 226 RLENQLLRNEVQSLNQEMASLLQRSKETQEEL-----NKARVRVEKWNVDnsksDRITR---------ELRAQVDDLTEA 291
Cdd:PRK02224 191 QLKAQIEEKEEKDLHERLNGLESELAELDEEIeryeeQREQARETRDEAD----EVLEEheerreeleTLEAEIEDLRET 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 292 VAAKDSQLAVLKVRLQEADQVLSSRTEALEALQSEKSRimqdhnegSSLQNQALQTLQERLHEADATLKREQESYKQMQS 371
Cdd:PRK02224 267 IAETEREREELAEEVRDLRERLEELEEERDDLLAEAGL--------DDADAEAVEARREELEDRDEELRDRLEECRVAAQ 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 372 EFATrlnkmevERQNLAEAVTLAERKYSEERKKVDDLQqqvklhrSSLESAKQELVDYKQKATRIlqskEKLINSLKEGS 451
Cdd:PRK02224 339 AHNE-------EAESLREDADDLEERAEELREEAAELE-------SELEEAREAVEDRREEIEEL----EEEIEELRERF 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 452 SFEGLDSSTASSMELEELrherelqkEEIQKLMGQIHQLRSELQDM-----EAQQVSEAESAREQLQDLQDQ-----IAK 521
Cdd:PRK02224 401 GDAPVDLGNAEDFLEELR--------EERDELREREAELEATLRTArerveEAEALLEAGKCPECGQPVEGSphvetIEE 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 522 QRASKQELETELDRMKQEFHYVEEDLHRTKNtlqsrIKDREEEIQKLRNQLTNktlsnssqseLESRLHQLTETLIQKQT 601
Cdd:PRK02224 473 DRERVEELEAELEDLEEEVEEVEERLERAED-----LVEAEDRIERLEERRED----------LEELIAERRETIEEKRE 537
|
410
....*....|..
gi 1939872721 602 LLESLSTEKNSL 613
Cdd:PRK02224 538 RAEELRERAAEL 549
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
232-574 |
5.87e-08 |
|
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: 56.34 E-value: 5.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 232 LRNEVQSLNQEMASLLQRSKETQEELNKARVRVEKWNVDNSKSDRITRELRAQVDDLTEAVAAKDSQ------------- 298
Cdd:pfam01576 220 LQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAArnkaekqrrdlge 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 299 -LAVLKVRLQE------ADQVLSSR-----TEALEALQSEKSRIMQDHNEGSSLQNQALQTLQERLHEAdatlKREQESY 366
Cdd:pfam01576 300 eLEALKTELEDtldttaAQQELRSKreqevTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQA----KRNKANL 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 367 KQMQSEFATRLNKMEVERQNLAEAVTLAERKyseeRKKVDDLQQQVKLHRSSLESAKQELVDYKQKATRILQSKEKLINS 446
Cdd:pfam01576 376 EKAKQALESENAELQAELRTLQQAKQDSEHK----RKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNE 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 447 LKEGSSFEGLDSSTASSmelEELRHERELQKEEIQKLM--GQIHQLRSELQDMEAQQVSEAESARE---QLQDLQDQIAK 521
Cdd:pfam01576 452 AEGKNIKLSKDVSSLES---QLQDTQELLQEETRQKLNlsTRLRQLEDERNSLQEQLEEEEEAKRNverQLSTLQAQLSD 528
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 522 QR--------------ASKQELETELDRMKQEFHYVE---EDLHRTKNTLQSRIKDREEEIQKLRNQLTN 574
Cdd:pfam01576 529 MKkkleedagtlealeEGKKRLQRELEALTQQLEEKAaayDKLEKTKNRLQQELDDLLVDLDHQRQLVSN 598
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
377-629 |
9.39e-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: 55.83 E-value: 9.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 377 LNKMEVERQNLAEAVTLAErkysEERKKVDDLQQQVK-----------LHRSSLESAKQELVDYKQKATRILQSKEKLIN 445
Cdd:TIGR02168 178 ERKLERTRENLDRLEDILN----ELERQLKSLERQAEkaerykelkaeLRELELALLVLRLEELREELEELQEELKEAEE 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 446 SLKEGSSfeGLDSSTASSMELEELRHERELQKEEIQKLMGQIHQLRSELQDMEAQQVSEAESAREQLQDLQDQIAKQRAS 525
Cdd:TIGR02168 254 ELEELTA--ELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESK 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 526 KQELETELDRMKQEFHYVEED----------LHRTKNTLQSRIKDREEEIQKLRN---QLTNKTLSNSSQ-SELESRLHQ 591
Cdd:TIGR02168 332 LDELAEELAELEEKLEELKEElesleaeleeLEAELEELESRLEELEEQLETLRSkvaQLELQIASLNNEiERLEARLER 411
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1939872721 592 LTETLIQKQTLLESL-----STEKNSLVFQLERLEQQLHSAAT 629
Cdd:TIGR02168 412 LEDRRERLQQEIEELlkkleEAELKELQAELEELEEELEELQE 454
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
217-619 |
1.38e-07 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 55.03 E-value: 1.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 217 SMSHELSNLRLENQLLRNEVQSLNQEMASLLQRSKETQEELNKARVR---VEKWNVDNSKSDRITRELRAQVDDLTEAVA 293
Cdd:TIGR04523 156 KLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLlsnLKKKIQKNKSLESQISELKKQNNQLKDNIE 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 294 AKDSQLAVLKVRLQEAD----QVLSSRTEALEALQSEKSRIMQDHNEGSSLQNQaLQTLQERLHEADAtlKREQESYKQM 369
Cdd:TIGR04523 236 KKQQEINEKTTEISNTQtqlnQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQ-LNQLKSEISDLNN--QKEQDWNKEL 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 370 QSEFATRLNKMEVerqnlaeavtlAERKYSEERKKVDDLQQQVklhrSSLESAKQELVDYKQKATRILQSKEKLINSLKE 449
Cdd:TIGR04523 313 KSELKNQEKKLEE-----------IQNQISQNNKIISQLNEQI----SQLKKELTNSESENSEKQRELEEKQNEIEKLKK 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 450 GSSfEGLDSSTASSMELEELRHERELQKEEIQKLMGQIHQLRSELQDMEAQQ---VSEAESAREQLQDLQDQIAKQRASK 526
Cdd:TIGR04523 378 ENQ-SYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIerlKETIIKNNSEIKDLTNQDSVKELII 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 527 QELETELDRMKQEFHYVEEDLHRTKNTL---QSRIKDREEEIQKLRNQltnKTLSNSSQSELESRLHQLTEtliqKQTLL 603
Cdd:TIGR04523 457 KNLDNTRESLETQLKVLSRSINKIKQNLeqkQKELKSKEKELKKLNEE---KKELEEKVKDLTKKISSLKE----KIEKL 529
|
410
....*....|....*.
gi 1939872721 604 ESLSTEKNSLVFQLER 619
Cdd:TIGR04523 530 ESEKKEKESKISDLED 545
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
221-433 |
1.79e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 54.00 E-value: 1.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 221 ELSNLRLENQLLRNEVQSLNQEMASLLQRSKETQEELNKARVRVEkwnvdnsKSDRITRELRAQVDDLTEAVAAkdsQLA 300
Cdd:COG4942 42 ELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELA-------ELEKEIAELRAELEAQKEELAE---LLR 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 301 VL-KVRLQEADQVLSSRTEALEALQSekSRIMQDHNEGSSLQNQALQTLQERLHEADATLKREQESYKQMQSEFATRLNK 379
Cdd:COG4942 112 ALyRLGRQPPLALLLSPEDFLDAVRR--LQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAA 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1939872721 380 MEVERQNLAEAVTLAERKYSEERKKVDDLQQQVKLHRSSLESAKQELVDYKQKA 433
Cdd:COG4942 190 LEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERT 243
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
226-624 |
2.75e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.15 E-value: 2.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 226 RLENQLLRNEVQSLNQEMASLLQRSKETQEELNKARVRVE--KWNVDNSKSDRITReLRAQVDDLTEAVAAKDSQLAVLK 303
Cdd:COG4913 287 QRRLELLEAELEELRAELARLEAELERLEARLDALREELDelEAQIRGNGGDRLEQ-LEREIERLERELEERERRRARLE 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 304 VRLQEADQVLSSRTEALEALQSEKSRIMQDHNEGSSLQNQALQTLQERLHEAD---ATLKREQESYKQMQS--------- 371
Cdd:COG4913 366 ALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRrelRELEAEIASLERRKSniparllal 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 372 --EFATRLNKMEVERQNLAEAVTLAE------------------------RKYSEERKKVDDLQ-------QQVKLHRSS 418
Cdd:COG4913 446 rdALAEALGLDEAELPFVGELIEVRPeeerwrgaiervlggfaltllvppEHYAAALRWVNRLHlrgrlvyERVRTGLPD 525
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 419 LESAK-------------------------------------QELVDYKQKATRILQSK------EKLINSLKEGSSFEG 455
Cdd:COG4913 526 PERPRldpdslagkldfkphpfrawleaelgrrfdyvcvdspEELRRHPRAITRAGQVKgngtrhEKDDRRRIRSRYVLG 605
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 456 LDSSTAssmeLEELRHERELQKEEIQKLMGQIHQLRSELQDMEAQQ---------------VSEAESAREQLQD------ 514
Cdd:COG4913 606 FDNRAK----LAALEAELAELEEELAEAEERLEALEAELDALQERRealqrlaeyswdeidVASAEREIAELEAelerld 681
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 515 --------LQDQIAKQRASKQELETELDRMKQEfhyveedlhrtKNTLQSRIKDREEEIQKLRNQLTNKTLSNSSQ--SE 584
Cdd:COG4913 682 assddlaaLEEQLEELEAELEELEEELDELKGE-----------IGRLEKELEQAEEELDELQDRLEAAEDLARLElrAL 750
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1939872721 585 LESRLHQLTETLIQKQtLLESLSTEKNSLVFQLERLEQQL 624
Cdd:COG4913 751 LEERFAAALGDAVERE-LRENLEERIDALRARLNRAEEEL 789
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
219-569 |
3.89e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 53.62 E-value: 3.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 219 SHELSNLRLENQLLRNEVQSLN---------QEMASLLQRSKETQEELNKARVRVEKWNVDNSKSDRITRELRAQVDDLT 289
Cdd:COG4717 101 EEELEELEAELEELREELEKLEkllqllplyQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELE 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 290 EAV----AAKDSQLAVLKVRLQEADQVLSSRTEALEALQSEKSRIMQDHNEGSSlqNQALQTLQERLHEADATLK----- 360
Cdd:COG4717 181 ELLeqlsLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLEN--ELEAAALEERLKEARLLLLiaaal 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 361 -------REQESYKQMQSEFA-----------TRLNKMEVERQNLAEAVTLAERKYSEERKKVDDLQQQVKLHRSSLESA 422
Cdd:COG4717 259 lallglgGSLLSLILTIAGVLflvlgllallfLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEE 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 423 KQELVDYKQKATRILQSKEKLINSLKEGSSFEGLDSS-TASSMELEELRHERELQKEEIQKLMGQIHQLRSELQDM---- 497
Cdd:COG4717 339 LLELLDRIEELQELLREAEELEEELQLEELEQEIAALlAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELlgel 418
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1939872721 498 -EAQQVSEAESAREQLQDLQDQIAKQRASKQELETELDRMKQEFHYVEED-----LHRTKNTLQSRIKDREEEIQKLR 569
Cdd:COG4717 419 eELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDgelaeLLQELEELKAELRELAEEWAALK 496
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
230-609 |
4.66e-07 |
|
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: 52.98 E-value: 4.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 230 QLLRNEVQSLNQEMASLLQRSKETQEELNKARvrvEKWNVDNSKSDRITRELRAQVDDLTEAVAAKDSQLAVLKVRLQEA 309
Cdd:pfam07888 30 ELLQNRLEECLQERAELLQAQEAANRQREKEK---ERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKEL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 310 DQVLSSRTEALEALQSEKS----RIMQDHNEGSSLQNQA------LQTLQERLHEADATLKREQESYKQMQSEfatrLNK 379
Cdd:pfam07888 107 SASSEELSEEKDALLAQRAaheaRIRELEEDIKTLTQRVlereteLERMKERAKKAGAQRKEEEAERKQLQAK----LQQ 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 380 MEVERQNLAEAVTLAERKYSEERKKVDDLQQQVKLHRSSLESAKQELVDYKQKATRILQSKEKLINSLKegsSFEGLDSS 459
Cdd:pfam07888 183 TEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASER---KVEGLGEE 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 460 TASSMELEELRHERELQ-KEEIQKLMGQIHQLRSELQDMEAQQVSEAESAREQLQDLQDQIAKQRASKQELETELDRMKQ 538
Cdd:pfam07888 260 LSSMAAQRDRTQAELHQaRLQAAQLTLQLADASLALREGRARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEERM 339
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1939872721 539 EFHYVEEDLHRTKNTLQSRIKDREEEIQKLRNQLtnktlsNSSQSELESRLHQLTETLIQKQTLLESLSTE 609
Cdd:pfam07888 340 EREKLEVELGREKDCNRVQLSESRRELQELKASL------RVAQKEKEQLQAEKQELLEYIRQLEQRLETV 404
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
395-600 |
5.05e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 53.10 E-value: 5.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 395 ERKYSEERKKVDDLQQQVKLHRSSLESAKQELVDYKQK-------------ATRILQSKEKLINSLKEGSSFEGLDSSTA 461
Cdd:COG3206 167 ELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKnglvdlseeakllLQQLSELESQLAEARAELAEAEARLAALR 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 462 SSMELEELRHERELQKEEIQKLMGQIHQLRSELQDMEAQ---QVSEAESAREQLQDLQDQIAKQ-RASKQELETELDRMK 537
Cdd:COG3206 247 AQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARytpNHPDVIALRAQIAALRAQLQQEaQRILASLEAELEALQ 326
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1939872721 538 QEfhyvEEDLHRTKNTLQSRIK---DREEEIQKLRNQLTNKtlsnssQSELESRLHQLTETLIQKQ 600
Cdd:COG3206 327 AR----EASLQAQLAQLEARLAelpELEAELRRLEREVEVA------RELYESLLQRLEEARLAEA 382
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
288-539 |
6.00e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.46 E-value: 6.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 288 LTEAVAAKDSQLAVLKVRLQEADQVLSSRTEALEALQSEKSRIMQDHNEgsslQNQALQTLQERLHEADATLKREQESYK 367
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAA----LERRIAALARRIRALEQELAALEAELA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 368 QMQSEFATRLNKMEVERQNLAEAVTLAERKYSEERKKV-------DDLQQQVKLHRSSLESAKQELVDYKQKATRILQSK 440
Cdd:COG4942 87 ELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALllspedfLDAVRRLQYLKYLAPARREQAEELRADLAELAALR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 441 EKLinslkegssfegldsstassmeleelrherELQKEEIQKLMGQIHQLRSELQDMEAQQVSEAESAREQLQDLQDQIA 520
Cdd:COG4942 167 AEL------------------------------EAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELA 216
|
250
....*....|....*....
gi 1939872721 521 KQRASKQELETELDRMKQE 539
Cdd:COG4942 217 ELQQEAEELEALIARLEAE 235
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
221-629 |
1.38e-06 |
|
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: 52.04 E-value: 1.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 221 ELSNLRLENQLLRNEVQSLNQEMASLLQRSKETQEELNKARVRVEK-WNVDNSKSDRITrELRAQVDDLTEAVAAKDSQL 299
Cdd:pfam15921 357 ELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRlWDRDTGNSITID-HLRRELDDRNMEVQRLEALL 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 300 AVLKV----RLQEADQVLSSRTEALEALQSEKSRIMQdhnegsslQNQALQTLQERLHEADATLkreqESYKQMQSEFAT 375
Cdd:pfam15921 436 KAMKSecqgQMERQMAAIQGKNESLEKVSSLTAQLES--------TKEMLRKVVEELTAKKMTL----ESSERTVSDLTA 503
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 376 RLNKMEverqnlaEAVTLAERKYSEERKKVD-DLQ--QQVKLHRSSLESAKQELVDYKQKATRILQSKEKLINSLKEGSS 452
Cdd:pfam15921 504 SLQEKE-------RAIEATNAEITKLRSRVDlKLQelQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQ 576
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 453 FEGLDSSTASSMELEELRHERE--LQKEEIQKLM-------GQIHQLRSELQDMEAQQVSEAESAREQLQDLQD------ 517
Cdd:pfam15921 577 LVGQHGRTAGAMQVEKAQLEKEinDRRLELQEFKilkdkkdAKIRELEARVSDLELEKVKLVNAGSERLRAVKDikqerd 656
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 518 ----QIAKQRASKQELETELDRMKQEFHYVEEDLHRTKNTLQSRIKDREEEIQKLRNQLTNKTLSNSS--------QSEL 585
Cdd:pfam15921 657 qllnEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHamkvamgmQKQI 736
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1939872721 586 ESRLHQLTETLIQKQTLLESLST---EKNSLVFQLERLEQQLHSAAT 629
Cdd:pfam15921 737 TAKRGQIDALQSKIQFLEEAMTNankEKHFLKEEKNKLSQELSTVAT 783
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
217-623 |
2.69e-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: 50.84 E-value: 2.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 217 SMSHELSNLRLENQLLRNEVQSLNQEMASLLQRSKETQEELNKARVRVEKWNVDNSKSDRITRELRAQVDDLTEAVAAKD 296
Cdd:TIGR02169 354 KLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIE 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 297 SQLAVLKVRLQEADQVLSSRTEALEALQ----SEKSRIMQDHNEGSSLQNQaLQTLQERLHEADATLK---REQESYK-- 367
Cdd:TIGR02169 434 AKINELEEEKEDKALEIKKQEWKLEQLAadlsKYEQELYDLKEEYDRVEKE-LSKLQRELAEAEAQARaseERVRGGRav 512
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 368 -------------------QMQSEFAT--------RLNKMEVERQNLAEAVT--LAERKYSEE-----RKKVDDLQQQVK 413
Cdd:TIGR02169 513 eevlkasiqgvhgtvaqlgSVGERYATaievaagnRLNNVVVEDDAVAKEAIelLKRRKAGRAtflplNKMRDERRDLSI 592
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 414 LHRSSLESAKQELVDYKQK----------ATRILQSKE---KLINSLK----EGSSFEGLDSSTASSMELEELRHERELQ 476
Cdd:TIGR02169 593 LSEDGVIGFAVDLVEFDPKyepafkyvfgDTLVVEDIEaarRLMGKYRmvtlEGELFEKSGAMTGGSRAPRGGILFSRSE 672
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 477 KEEIQKLM---------------------GQIHQLRSELQDMEAQQVS----------EAESAREQLQDLQDQIAKQRAS 525
Cdd:TIGR02169 673 PAELQRLRerleglkrelsslqselrrieNRLDELSQELSDASRKIGEiekeieqleqEEEKLKERLEELEEDLSSLEQE 752
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 526 KQELETELDRMKQEFHYVEEDLHRTKNTL--------QSRIKDREEEIQKLRNQLtnktlsnssqSELESRLHQLTETLI 597
Cdd:TIGR02169 753 IENVKSELKELEARIEELEEDLHKLEEALndlearlsHSRIPEIQAELSKLEEEV----------SRIEARLREIEQKLN 822
|
490 500
....*....|....*....|....*.
gi 1939872721 598 QKQTLLESLSTEKNSLVFQLERLEQQ 623
Cdd:TIGR02169 823 RLTLEKEYLEKEIQELQEQRIDLKEQ 848
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
233-625 |
3.22e-06 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 50.24 E-value: 3.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 233 RNEVQSLNQEMASLLQRSkeTQEELNKAR---------VRVEKWNvdnSKSDRITRELRAQVDD-LTEAVAAKDSqLAVL 302
Cdd:pfam06160 9 YKEIDELEERKNELMNLP--VQEELSKVKklnltgetqEKFEEWR---KKWDDIVTKSLPDIEElLFEAEELNDK-YRFK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 303 KVR--LQEADQVLSSRTEALEALQSEKSRIMQDHNEgsslQNQALQTLQERLHEADATLKREQESYKQMQSEFATRLNKM 380
Cdd:pfam06160 83 KAKkaLDEIEELLDDIEEDIKQILEELDELLESEEK----NREEVEELKDKYRELRKTLLANRFSYGPAIDELEKQLAEI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 381 EVErqnLAEAVTLAER-KYSEERKKVDDLQQQVKLHRSSLESAKQELVDYKQKATRILQSKEKLINSLKE-GSSFEGLDS 458
Cdd:pfam06160 159 EEE---FSQFEELTESgDYLEAREVLEKLEEETDALEELMEDIPPLYEELKTELPDQLEELKEGYREMEEeGYALEHLNV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 459 StassmeleelrherelqkEEIQKLMGQIHQLRSELQDMEAQQVSEA----ESAREQLQD------------------LQ 516
Cdd:pfam06160 236 D------------------KEIQQLEEQLEENLALLENLELDEAEEAleeiEERIDQLYDllekevdakkyveknlpeIE 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 517 DQIAKQRASKQELETELDRMKQEFHYVEEDLHRTKNtLQSRIKDREEEIQKLRNQLTNKTlsnSSQSELESRLHQLTETL 596
Cdd:pfam06160 298 DYLEHAEEQNKELKEELERVQQSYTLNENELERVRG-LEKQLEELEKRYDEIVERLEEKE---VAYSELQEELEEILEQL 373
|
410 420 430
....*....|....*....|....*....|....*.
gi 1939872721 597 IQKQTLLESLSTEKNSLVF-------QLERLEQQLH 625
Cdd:pfam06160 374 EEIEEEQEEFKESLQSLRKdeleareKLDEFKLELR 409
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
220-541 |
3.65e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.15 E-value: 3.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 220 HELSNLRLENQLLRNEVQSLNQEMASLLQR-SKETQEELNKARVRVEKWNVDNSKSDRITRELRAQVDDLTEAVAAKDSQ 298
Cdd:COG4717 156 EELRELEEELEELEAELAELQEELEELLEQlSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENE 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 299 LAVLKV--RLQEADQVLSSRTEAL-------------------------------------EALQSEKSRIMQDHNEGSS 339
Cdd:COG4717 236 LEAAALeeRLKEARLLLLIAAALLallglggsllsliltiagvlflvlgllallflllareKASLGKEAEELQALPALEE 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 340 LQNQALQTLQERLHEADATLKREQESYKQMQSEFATRLNKMEVERQNLAEAVTLAERKYSEERKKVDDLQQqvklhrssL 419
Cdd:COG4717 316 LEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEE--------L 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 420 ESAKQELVDYKQKATRILQSKEKLINSLKEGSSFEGLDSSTASSMELEELRHERELQKEEIQKLMGQIHQLRSELQDMEA 499
Cdd:COG4717 388 RAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEE 467
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1939872721 500 QQ-VSEAESAREQLQDLQDQIAKQRASKQELETELDRMKQEFH 541
Cdd:COG4717 468 DGeLAELLQELEELKAELRELAEEWAALKLALELLEEAREEYR 510
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
277-527 |
4.31e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 50.02 E-value: 4.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 277 ITRELRAQVDDLTEAVAAKDSQLAVLKVRLQEADQvlssrteALEALQsEKSRIMqDHNEGSSLQNQALQTLQERLHEAD 356
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQLPELRKELEEAEA-------ALEEFR-QKNGLV-DLSEEAKLLLQQLSELESQLAEAR 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 357 ATLKREQESYKQMQSEFATRLNKM-----EVERQNLAEAVTLAERKYSEERKKVDDLQQQVKLHRSSLESAKQELvdyKQ 431
Cdd:COG3206 233 AELAEAEARLAALRAQLGSGPDALpellqSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQL---QQ 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 432 KATRILQSKEKLINSLKEgssfegldsstassmeleeLRHERELQKEEIQKLMGQIHQLRSELQDMEAqqvsEAESAREQ 511
Cdd:COG3206 310 EAQRILASLEAELEALQA-------------------REASLQAQLAQLEARLAELPELEAELRRLER----EVEVAREL 366
|
250
....*....|....*.
gi 1939872721 512 LQDLQDQIAKQRASKQ 527
Cdd:COG3206 367 YESLLQRLEEARLAEA 382
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
221-622 |
4.50e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.06 E-value: 4.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 221 ELSNLRLENQLLRNEVQSLNQEMASLLQRSKETQEELNKARVRVEKWNVDNSKSDRItRELRAQVDDLTEAvaakdsqLA 300
Cdd:PRK03918 239 EIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEY-IKLSEFYEEYLDE-------LR 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 301 VLKVRLQEADQVLSSRTEALEALQSEKSRIMQDHNEGSSLQNQ--ALQTLQERLHEADATLKREQESYKQMQSEFATRLN 378
Cdd:PRK03918 311 EIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRleELEERHELYEEAKAKKEELERLKKRLTGLTPEKLE 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 379 KMEVERQNLAEAVTLAERKYSEERKKVDDLQQQVKLHRSSLESAKQE------LVDYKQKATRILQSKEKLINSLKEGSS 452
Cdd:PRK03918 391 KELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKcpvcgrELTEEHRKELLEEYTAELKRIEKELKE 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 453 FEGLDSSTASSMELEELRHERELQKEEIQKLMGQIHQLRSELQDMEAQQVS----EAESAREQLQDLQDQI---AKQRAS 525
Cdd:PRK03918 471 IEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEkkaeEYEKLKEKLIKLKGEIkslKKELEK 550
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 526 KQELETELDRMKQEFHYVEEDLHRTKNTLQSR----IKDREEEIQKLRnQLTNKTLS-NSSQSELES---RLHQLTETLI 597
Cdd:PRK03918 551 LEELKKKLAELEKKLDELEEELAELLKELEELgfesVEELEERLKELE-PFYNEYLElKDAEKELEReekELKKLEEELD 629
|
410 420
....*....|....*....|....*
gi 1939872721 598 QKQTLLESLSTEKNSLVFQLERLEQ 622
Cdd:PRK03918 630 KAFEELAETEKRLEELRKELEELEK 654
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
229-447 |
6.44e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 49.63 E-value: 6.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 229 NQLLRNEVQSLNQEMASLLQRSKETQEELNKARVRVEKWNVDNSKSDritreLRAQVDDLTEAVAAKDSQLAVLKVRLQE 308
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVD-----LSEEAKLLLQQLSELESQLAEARAELAE 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 309 ADQVLSSRTEALEALQSEKSRIMQDhNEGSSLQNQaLQTLQERLHEADATLKREQESYKQMQSEFATRLNKMEVERQNLA 388
Cdd:COG3206 238 AEARLAALRAQLGSGPDALPELLQS-PVIQQLRAQ-LAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRIL 315
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1939872721 389 EAvtlAERKYSEERKKVDDLQQQVKLHRSSLESAKQELVDYKQkATRILQSKEKLINSL 447
Cdd:COG3206 316 AS---LEAELEALQAREASLQAQLAQLEARLAELPELEAELRR-LEREVEVARELYESL 370
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
476-623 |
7.17e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.99 E-value: 7.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 476 QKEEIQKLMGQIHQLRSELQDME---AQQVSEAESAREQLQDLQDQIAKQRASKQELETELDRMKQEFhyveEDLHRTKN 552
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEkelAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAEL----AELEKEIA 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1939872721 553 TLQSRIKDREEEIQKL--------RNQLTNKTLSNSSQSELESRLHQLTETLIQKQTLLESLSTEKNSLVFQLERLEQQ 623
Cdd:COG4942 94 ELRAELEAQKEELAELlralyrlgRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAE 172
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
170-464 |
9.86e-06 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 49.13 E-value: 9.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 170 ATEENSGSQSPEvsssdsmpEGHKKSTEESTVSNATSVEHSSAPSDgsmshELSNLRLENQLLRNEVQSLNQEMASLlqr 249
Cdd:PLN02939 189 AAQEKIHVEILE--------EQLEKLRNELLIRGATEGLCVHSLSK-----ELDVLKEENMLLKDDIQFLKAELIEV--- 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 250 sKETQEELnkarVRVEKwnvDNSKSDRITRELRAQVDDLTEAVaakdSQLAVLKVrlqeadQVLSSRTEALEALqseksr 329
Cdd:PLN02939 253 -AETEERV----FKLEK---ERSLLDASLRELESKFIVAQEDV----SKLSPLQY------DCWWEKVENLQDL------ 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 330 imqdhnegsslqnqaLQTLQERLHEADATLKREQEsykqmqseFATRLNKMEverQNLAEAVTlaerkYSEERKKVDDLQ 409
Cdd:PLN02939 309 ---------------LDRATNQVEKAALVLDQNQD--------LRDKVDKLE---ASLKEANV-----SKFSSYKVELLQ 357
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1939872721 410 QQVKLHRSSLESAKQELVDYKQKATRILQSKEKLINSLKEGSSFEGLDSStASSM 464
Cdd:PLN02939 358 QKLKLLEERLQASDHEIHSYIQLYQESIKEFQDTLSKLKEESKKRSLEHP-ADDM 411
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
221-594 |
1.03e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.16 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 221 ELSNLRLENQLLRNEVQSLNQEMASLLQRSKETQEELNKARVRVEKwnvDNSKSDRITRELRAQVDDLTEAVAAKDSQLA 300
Cdd:COG1196 387 ELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAE---LEEEEEEEEEALEEAAEEEAELEEEEEALLE 463
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 301 VLKVRLQEADQVLSSRTEALEALQSEKSRI-----MQDHNEG--SSLQNQALQTLQERLHEADATLKREQESYkqmQSEF 373
Cdd:COG1196 464 LLAELLEEAALLEAALAELLEELAEAAARLlllleAEADYEGflEGVKAALLLAGLRGLAGAVAVLIGVEAAY---EAAL 540
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 374 ATRLNKMEVERQNLAEAVTLAERKYSEERKK-------VDDLQQQVKLHRSSLESAKQELVDYKQKATRILQSKEKLINS 446
Cdd:COG1196 541 EAALAAALQNIVVEDDEVAAAAIEYLKAAKAgratflpLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGD 620
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 447 LKEGSSFEGLDSSTASSMELEELRHERELQKEEI------QKLMGQIHQLRSELQDMEAQQVSEAESAREQLQDLQDQIA 520
Cdd:COG1196 621 TLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEggsaggSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALL 700
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1939872721 521 KQRASKQELETELDRMKQEFHYVEEDLHRTKNTLQSRIKDREEEIQKLRNQLTNKTLSNSSQSELESRLHQLTE 594
Cdd:COG1196 701 AEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLER 774
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
221-411 |
1.11e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.86 E-value: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 221 ELSNLRLENQLLrnevqSLNQEMASLLQRSKETQEELNKARVRVEKwnvDNSKSDRITRELRAQVDDLTE-----AVAAK 295
Cdd:COG3206 197 ALEEFRQKNGLV-----DLSEEAKLLLQQLSELESQLAEARAELAE---AEARLAALRAQLGSGPDALPEllqspVIQQL 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 296 DSQLAVLKVRLQEADQVLSSRTEALEALQSEKSRIMQDHNEGSSLQNQALQTLQERLHEADATLKREQESYKQMqsefAT 375
Cdd:COG3206 269 RAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEAR----LA 344
|
170 180 190
....*....|....*....|....*....|....*.
gi 1939872721 376 RLNKMEVERQNLAEAVTLAERKYSEERKKVDDLQQQ 411
Cdd:COG3206 345 ELPELEAELRRLEREVEVARELYESLLQRLEEARLA 380
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
477-625 |
1.42e-05 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 48.29 E-value: 1.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 477 KEEIQKLMGQIHQLRSELQ-DMEAQQVSEAESAReqlqdLQDQIAKQRASKQELETELDRMKQEFHYVEEDLHRTKNtLQ 555
Cdd:PRK04778 281 EEKNEEIQERIDQLYDILErEVKARKYVEKNSDT-----LPDFLEHAKEQNKELKEEIDRVKQSYTLNESELESVRQ-LE 354
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1939872721 556 SRIKDREEEIQKLRNQLTNKTLSNSS-QSELESRLHQLTEtlIQKQ-----TLLESLSTEKNSLVFQLERLEQQLH 625
Cdd:PRK04778 355 KQLESLEKQYDEITERIAEQEIAYSElQEELEEILKQLEE--IEKEqeklsEMLQGLRKDELEAREKLERYRNKLH 428
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
245-627 |
2.63e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 47.73 E-value: 2.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 245 SLLQRSK--ETQEELNKARVRVEkwnvdnsksdRITRELRAQVDDLTEAVAAKDSqlAVLKVRLQEADQVLSSRTEALEA 322
Cdd:PRK02224 157 DLLQLGKleEYRERASDARLGVE----------RVLSDQRGSLDQLKAQIEEKEE--KDLHERLNGLESELAELDEEIER 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 323 LQSEKsrimqdhnegsslqnqalQTLQERLHEADATLkreqESYKQMQSEFATrlnkMEVERQNLAEAVTLAERKYSEER 402
Cdd:PRK02224 225 YEEQR------------------EQARETRDEADEVL----EEHEERREELET----LEAEIEDLRETIAETEREREELA 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 403 KKVDDLQQQvklhRSSLESAKQELVDykqkatrilqskeklinslkeGSSFEGLDSSTASsmeleelrherelqkeeiqk 482
Cdd:PRK02224 279 EEVRDLRER----LEELEEERDDLLA---------------------EAGLDDADAEAVE-------------------- 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 483 lmgqihQLRSELQDMEAQQVSEAESAREQLQDLQDQIAKQRASKQELETELDRMKQEFHYVEEDLHRTKNTlqsrIKDRE 562
Cdd:PRK02224 314 ------ARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREA----VEDRR 383
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1939872721 563 EEIQKLRNQLTnktlsnssqsELESRLHQLTETLIQKQTLLESLSTEKNSLVFQLERLEQQLHSA 627
Cdd:PRK02224 384 EEIEELEEEIE----------ELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTA 438
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
345-625 |
3.16e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 47.42 E-value: 3.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 345 LQTLQERLHEADATLKREQESYKQMQSEFATRLNKMEVERQNLAE-------------------------AVTLAERKYS 399
Cdd:pfam15921 87 VKDLQRRLNESNELHEKQKFYLRQSVIDLQTKLQEMQMERDAMADirrresqsqedlrnqlqntvheleaAKCLKEDMLE 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 400 EERKKVDDLQQQVKLHRSSLESAKQELVDYKQKATRILQSKEKLinslkEGSSFEGLDSSTASSMELEELrherelqkeE 479
Cdd:pfam15921 167 DSNTQIEQLRKMMLSHEGVLQEIRSILVDFEEASGKKIYEHDSM-----STMHFRSLGSAISKILRELDT---------E 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 480 IQKLMGQIHQLRSELQDMEAQQVSEAESAREQLQDLQDQIAkqraSKQELE------------TELDRMKQEFHYVEEDL 547
Cdd:pfam15921 233 ISYLKGRIFPVEDQLEALKSESQNKIELLLQQHQDRIEQLI----SEHEVEitgltekassarSQANSIQSQLEIIQEQA 308
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1939872721 548 HRTKNTLQSRIKDREEEIQKLRNQLTN-KTLSNSSQSELESRLHQLTETLIQKQTLLESLSTEKNSLVFQLERLEQQLH 625
Cdd:pfam15921 309 RNQNSMYMRQLSDLESTVSQLRSELREaKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLH 387
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
505-629 |
3.22e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 47.60 E-value: 3.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 505 AESAREQLQDLQDQ---IAKQRASKQELETEL------DRMKQEFhyveEDLHRTKNTLQSRIKDREEEIQKLRNQL--- 572
Cdd:PRK11281 38 EADVQAQLDALNKQkllEAEDKLVQQDLEQTLalldkiDRQKEET----EQLKQQLAQAPAKLRQAQAELEALKDDNdee 113
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 573 TNKTLSNSSQSELESRLhqlTETLIQKQTLLESLSTEKNSLV---FQLERLEQQLHSAAT 629
Cdd:PRK11281 114 TRETLSTLSLRQLESRL---AQTLDQLQNAQNDLAEYNSQLVslqTQPERAQAALYANSQ 170
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
221-568 |
3.37e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.37 E-value: 3.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 221 ELSNLRLENQLLRNEVQSLNQEMASLLQRSKETQ---EELNKARVR--VEKWNVDNSKSDRITRELRAQVDDLTEAVAAK 295
Cdd:PRK03918 392 ELEELEKAKEEIEEEISKITARIGELKKEIKELKkaiEELKKAKGKcpVCGRELTEEHRKELLEEYTAELKRIEKELKEI 471
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 296 DSQLAVLKVRLQEADQVLSSRTE------ALEALQSEKSRIMQDHNEGSSLQNQALQTLQERLHEADATLKREQESYKQM 369
Cdd:PRK03918 472 EEKERKLRKELRELEKVLKKESEliklkeLAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKL 551
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 370 QsEFATRLNKMEVERQNLAEAVTLAERKYSEER-KKVDDLQQQVKlhrsSLESAKQELVDYKqKATRILQSKEKLINSLK 448
Cdd:PRK03918 552 E-ELKKKLAELEKKLDELEEELAELLKELEELGfESVEELEERLK----ELEPFYNEYLELK-DAEKELEREEKELKKLE 625
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 449 EgssfegldsstassmeleelrhERELQKEEIQKLMGQIHQLRSELQDMEAQ-QVSEAESAREQLQDLQDQIAKQRASKQ 527
Cdd:PRK03918 626 E----------------------ELDKAFEELAETEKRLEELRKELEELEKKySEEEYEELREEYLELSRELAGLRAELE 683
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1939872721 528 ELETELDRMKQEFHYVEEDLhrtkntlqSRIKDREEEIQKL 568
Cdd:PRK03918 684 ELEKRREEIKKTLEKLKEEL--------EEREKAKKELEKL 716
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
221-463 |
3.93e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.75 E-value: 3.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 221 ELSNLRLENQLLRNEVQSLNQEMASLLQRSKETQEELNKARVRVEKwnvdnsksdritreLRAQVDDLTEAVAAKDSQLA 300
Cdd:COG3883 24 ELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDK--------------LQAEIAEAEAEIEERREELG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 301 VLKVRLQEADQVLSSrteaLEALQSEKSriMQDHNEgsslQNQALQTLQERLHEADATLKREQESYKQMQSEFATRLNKM 380
Cdd:COG3883 90 ERARALYRSGGSVSY----LDVLLGSES--FSDFLD----RLSALSKIADADADLLEELKADKAELEAKKAELEAKLAEL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 381 EVERQNLAEAVTLAERKYSEERKKVDDLQQQVKLHRSSLESAKQELVDYKQKATRILQSKEKLINSLKEGSSFEGLDSST 460
Cdd:COG3883 160 EALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 239
|
...
gi 1939872721 461 ASS 463
Cdd:COG3883 240 AAA 242
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
320-572 |
4.55e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.68 E-value: 4.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 320 LEALQSEKSRIMQDHNEGSSLQNQALQTLQERLHEAdatlKREQESYKQMQSEfatrlnkmeveRQNLAEAVTLAERKYS 399
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEA----EEKEEEYAELQEE-----------LEELEEELEELEAELE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 400 EERKKVDDLQQQVKLHR--SSLESAKQELVDYKQKATRILQSKEKLINslkegssfegldsstassmeleelrherelQK 477
Cdd:COG4717 113 ELREELEKLEKLLQLLPlyQELEALEAELAELPERLEELEERLEELRE------------------------------LE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 478 EEIQKLMGQIHQLRselQDMEAQQVSEAESAREQLQDLQDQIAKQRASKQELETELDRMKQEFHYVEEDLHRTKNTLQSr 557
Cdd:COG4717 163 EELEELEAELAELQ---EELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEA- 238
|
250
....*....|....*
gi 1939872721 558 iKDREEEIQKLRNQL 572
Cdd:COG4717 239 -AALEERLKEARLLL 252
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
387-623 |
4.73e-05 |
|
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: 46.30 E-value: 4.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 387 LAEAVTLAERKYSEERKKVDDLQQQVKLHRSSLESAKQElvdyKQKATRILQSKEKLINSLKEgssfegldsstassmel 466
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKE----EKALLKQLAALERRIAALAR----------------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 467 eelrherelqkeEIQKLMGQIHQLRSELQDMEAQQvseaESAREQLQDLQDQIAKQRASKQELE--------------TE 532
Cdd:COG4942 70 ------------RIRALEQELAALEAELAELEKEI----AELRAELEAQKEELAELLRALYRLGrqpplalllspedfLD 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 533 LDRMKQEFHYVEEDLHRTKNTLQSRIKDREEEIQKLRNQLTNKtlsNSSQSELESRLHQLTETLIQKQTLLESLSTEKNS 612
Cdd:COG4942 134 AVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAEL---EALLAELEEERAALEALKAERQKLLARLEKELAE 210
|
250
....*....|.
gi 1939872721 613 LVFQLERLEQQ 623
Cdd:COG4942 211 LAAELAELQQE 221
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
476-629 |
4.82e-05 |
|
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: 46.30 E-value: 4.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 476 QKEEIQKLMGQIHQLRSELQDMEaQQVSEAE----SAREQLQDLQDQIAKQRASKQELETELDRMKQEF----------- 540
Cdd:COG4942 39 LEKELAALKKEEKALLKQLAALE-RRIAALArrirALEQELAALEAELAELEKEIAELRAELEAQKEELaellralyrlg 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 541 --HYVE--------EDLHRTKNTLQSRIKDREEEIQKLRNQLTNKTLSNSSQSELESRLHQLTETLIQKQTLLESLSTEK 610
Cdd:COG4942 118 rqPPLAlllspedfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAER 197
|
170
....*....|....*....
gi 1939872721 611 NSLVFQLERLEQQLHSAAT 629
Cdd:COG4942 198 QKLLARLEKELAELAAELA 216
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
301-535 |
4.86e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 46.55 E-value: 4.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 301 VLKVRLQEADQVLSSRTEALEALQsEKSRIMQDH-NEGSSLQNQALQTLQERLHEadatLKREQESYKQMQSEFATRLNK 379
Cdd:PHA02562 171 LNKDKIRELNQQIQTLDMKIDHIQ-QQIKTYNKNiEEQRKKNGENIARKQNKYDE----LVEEAKTIKAEIEELTDELLN 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 380 MEVERQNLAEAVTLAERKYSEERKKVDDLQQQVKLHR---------SSLESAKQELVDYKQKATRILQSKEKLINSLKEG 450
Cdd:PHA02562 246 LVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKMYEkggvcptctQQISEGPDRITKIKDKLKELQHSLEKLDTAIDEL 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 451 SsfEGLDSSTASSMELEELRHERELQKEEIQKLMGQIHQLRSELQDMEAQQVSEAesarEQLQDLQDQIAKQRASKQELE 530
Cdd:PHA02562 326 E--EIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNA----EELAKLQDELDKIVKTKSELV 399
|
....*
gi 1939872721 531 TELDR 535
Cdd:PHA02562 400 KEKYH 404
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
354-641 |
5.44e-05 |
|
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: 46.30 E-value: 5.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 354 EADATLKREQESYKQMQSEFATRLNKMEVERQNLAEAVTLAERKYSEERKKVDDLQQQVKLHRSSLESAKQELvdykqka 433
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI------- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 434 trilqskEKLINSLKEgssfegldsstassmeleelrherelQKEEIQKLMGQIHQLRSELQDM---EAQQVSEAESARE 510
Cdd:COG4942 93 -------AELRAELEA--------------------------QKEELAELLRALYRLGRQPPLAlllSPEDFLDAVRRLQ 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 511 QLQDLQDQIAKQRASKQELETELDRMKQEfhyveedLHRTKNTLQSRIKDREEEIQKLRNQltnktlsnssQSELESRLH 590
Cdd:COG4942 140 YLKYLAPARREQAEELRADLAELAALRAE-------LEAERAELEALLAELEEERAALEAL----------KAERQKLLA 202
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1939872721 591 QLTETLIQKQTLLESLSTEKNSLVFQLERLEQQLHSAATGPSSGSSINMSG 641
Cdd:COG4942 203 RLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKG 253
|
|
| ATG16 |
pfam08614 |
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ... |
489-624 |
7.71e-05 |
|
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for eukaryotic cells. During autophagy, cytoplasmic components are enclosed in autophagosomes and delivered to lysosomes/vacuoles. ATG16 (also known as Apg16) has been shown to be bind to Apg5 and is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway.
Pssm-ID: 462536 [Multi-domain] Cd Length: 176 Bit Score: 43.77 E-value: 7.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 489 QLRSELQDMEAQQVSEAESAREQLQDLQDQIAKQRaskQELETeldrmkqefhyveedLHRTKNTLQSRIKDREEEIQKL 568
Cdd:pfam08614 29 EPESVLPSTSSSKLSKASPQSASIQSLEQLLAQLR---EELAE---------------LYRSRGELAQRLVDLNEELQEL 90
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 569 RNQLTNKTLSNSSQ----SELESRLHQLTETLIQKQTLLESLSTEKNSLVFQLERLEQQL 624
Cdd:pfam08614 91 EKKLREDERRLAALeaerAQLEEKLKDREEELREKRKLNQDLQDELVALQLQLNMAEEKL 150
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
486-628 |
1.19e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.15 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 486 QIHQLRSELQDMEAQQVSEAES-AREQLQDLQDQIAKQRaskQELETELDRMKQEFHYVEEDLHRTKNTL---QSRIKDR 561
Cdd:PRK12704 32 KIKEAEEEAKRILEEAKKEAEAiKKEALLEAKEEIHKLR---NEFEKELRERRNELQKLEKRLLQKEENLdrkLELLEKR 108
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1939872721 562 EEEIQKLRNQLTNKtlsnssQSELESRLHQLTETLIQKQTLLES---LSTE--KNSLvfqLERLEQQL-HSAA 628
Cdd:PRK12704 109 EEELEKKEKELEQK------QQELEKKEEELEELIEEQLQELERisgLTAEeaKEIL---LEKVEEEArHEAA 172
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
245-627 |
1.24e-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: 45.73 E-value: 1.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 245 SLLQRSKETQEELNKARvrvEKWNVDNSKSDRITRElRAQVDDLTEAVAAKDSQLAVLKVRLQ-EADQVLSSRTEALEAL 323
Cdd:TIGR00618 376 TLTQHIHTLQQQKTTLT---QKLQSLCKELDILQRE-QATIDTRTSAFRDLQGQLAHAKKQQElQQRYAELCAAAITCTA 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 324 QSEKSRI-----MQDHNEGSSLQNQALQTLQERLHEADATLKREQESYKQMQSEFATRLNKMEVERQNLAEAVTLAERKY 398
Cdd:TIGR00618 452 QCEKLEKihlqeSAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQ 531
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 399 SEErKKVDDLQQQVKLHRSSLESAKQELVDYKQKATRILQSKEKLinslkegssfegldsstassmeleelRHERELQKE 478
Cdd:TIGR00618 532 RGE-QTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSIL--------------------------TQCDNRSKE 584
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 479 EIQKLMGQIHQLRSELQDMEAQQVSEAESAREQLQDLQDQIAKQR--ASKQELETELDRMKQEFHYVEEDLHRTKNTLQS 556
Cdd:TIGR00618 585 DIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDvrLHLQQCSQELALKLTALHALQLTLTQERVREHA 664
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1939872721 557 RIKDREEEIQKLRNQLTNKtlsnssqsELESRLHQLT---ETLIQKQTLLESLSTEKNSLVFQLERLEQQLHSA 627
Cdd:TIGR00618 665 LSIRVLPKELLASRQLALQ--------KMQSEKEQLTywkEMLAQCQTLLRELETHIEEYDREFNEIENASSSL 730
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
478-614 |
1.62e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 45.01 E-value: 1.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 478 EEIQKLMGQIHQLRSELQDMEAQQVSEAESAREQLQDLQDQIAKqraskqeLETELDRMKQEFHYVEEdlHRTKNTLQSR 557
Cdd:PHA02562 223 DELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAK-------IKSKIEQFQKVIKMYEK--GGVCPTCTQQ 293
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1939872721 558 IKDREEEIQKLRNQLTNKTLS----NSSQSELESRLHQLTETLIQKQTLLESLSTEKNSLV 614
Cdd:PHA02562 294 ISEGPDRITKIKDKLKELQHSleklDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLI 354
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
171-574 |
1.66e-04 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 45.28 E-value: 1.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 171 TEENSgsqSPEVSSSDSMPEGHKKSTEESTVSNATSVEHSSApSDGSMSHELSNLRLENQLLRNEVQSLNQemasLLQRS 250
Cdd:PLN02939 69 TDENG---QLENTSLRTVMELPQKSTSSDDDHNRASMQRDEA-IAAIDNEQQTNSKDGEQLSDFQLEDLVG----MIQNA 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 251 KETQEELNKARVRVekwnvdnsksdritrelraqvddlteavaakdsqlavlkvrLQEADQVLSSRtealEALQSEksri 330
Cdd:PLN02939 141 EKNILLLNQARLQA-----------------------------------------LEDLEKILTEK----EALQGK---- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 331 mqdhnegsslqnqaLQTLQERLHEADATLKREQesykqmQSEFATRLNKMEVE--RQNLAEAVTLAERKYSEERKKVDDL 408
Cdd:PLN02939 172 --------------INILEMRLSETDARIKLAA------QEKIHVEILEEQLEklRNELLIRGATEGLCVHSLSKELDVL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 409 QQQVKLHRSSLESAKQELVDYKQKATRILQ-SKEKlinSLKEgSSFEGLDSSTASSMELEELRHERelqkeEIQKLMGQI 487
Cdd:PLN02939 232 KEENMLLKDDIQFLKAELIEVAETEERVFKlEKER---SLLD-ASLRELESKFIVAQEDVSKLSPL-----QYDCWWEKV 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 488 HQLRsELQDMEAQQVSEAESAREQLQDLQDQIAKQRASKQELET------ELDRMKQEFHYVEEDLHRTKNTLQSRIKDR 561
Cdd:PLN02939 303 ENLQ-DLLDRATNQVEKAALVLDQNQDLRDKVDKLEASLKEANVskfssyKVELLQQKLKLLEERLQASDHEIHSYIQLY 381
|
410
....*....|...
gi 1939872721 562 EEEIQKLRNQLTN 574
Cdd:PLN02939 382 QESIKEFQDTLSK 394
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
355-571 |
1.69e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.44 E-value: 1.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 355 ADATLKREQESYKQMQSEfatrLNKMEVERQNLAEAVTLAERKYSEERKKVDDLQQQVKLHRSSLESAKQELVDYKQKAT 434
Cdd:COG3883 14 ADPQIQAKQKELSELQAE----LEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 435 RILQSKEK------LINSLKEGSSFEG-LDSSTASSMELEELRHERELQKEEIQKLMGQIHQLRSELQDMEAQQvseaES 507
Cdd:COG3883 90 ERARALYRsggsvsYLDVLLGSESFSDfLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALK----AE 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1939872721 508 AREQLQDLQDQIAKQRASKQELETELDRMKQEFHYVEEDLHRTKNTLQSRIKDREEEIQKLRNQ 571
Cdd:COG3883 166 LEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAA 229
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
234-624 |
1.70e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.05 E-value: 1.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 234 NEVQSLNQEMASLLQRSKETQEELNKARVRVEKWNVDNSKSDRITRELRAQVDDLTEAVAAKDSQLAVLKVRLQEADQV- 312
Cdd:PRK03918 210 NEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELk 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 313 -LSSRTEALEALQSEKSRIMQDHNEGSSLQNQALQTLQERLHEADAT------LKREQESYKQMQSEFATRLNKMEVERQ 385
Cdd:PRK03918 290 eKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKeerleeLKKKLKELEKRLEELEERHELYEEAKA 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 386 NLAEAVTLAERKYSEERKKVDDLQQQVKLHRSSLESAKQELVDYKQKATRILQSKEKLINSLKEGSSF------EGLDSS 459
Cdd:PRK03918 370 KKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKcpvcgrELTEEH 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 460 TASSMELEELRHERElqKEEIQKLMGQIHQLRSELQDMEAQQVSEAESAR-----EQLQDLQDQIAKQRASK-------- 526
Cdd:PRK03918 450 RKELLEEYTAELKRI--EKELKEIEEKERKLRKELRELEKVLKKESELIKlkelaEQLKELEEKLKKYNLEElekkaeey 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 527 QELETELDRMKQEFHYVEEDLHR------TKNTLQSRIKDREEEIQKLRNQLTNktLSNSSQSELESRLHQLtETLIQKQ 600
Cdd:PRK03918 528 EKLKEKLIKLKGEIKSLKKELEKleelkkKLAELEKKLDELEEELAELLKELEE--LGFESVEELEERLKEL-EPFYNEY 604
|
410 420
....*....|....*....|....
gi 1939872721 601 TLLESLSTEKNSLVFQLERLEQQL 624
Cdd:PRK03918 605 LELKDAEKELEREEKELKKLEEEL 628
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
357-626 |
1.77e-04 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 44.73 E-value: 1.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 357 ATLKREQESYKQMQSEFATRLNKMEVERQNLAEAVTLAERKYSEERKKVDDLQQQVKLHRSSLESAKQELVDYKQKATRI 436
Cdd:pfam05557 2 AELIESKARLSQLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAELNRLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 437 LQSKEKLINSLKEGSSFEGLDSSTASSMELEELRHERELQKEEIQkLMGQIHQLR--SELQDMEAQQVSEAESAREQLQD 514
Cdd:pfam05557 82 KKYLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELE-LQSTNSELEelQERLDLLKAKASEAEQLRQNLEK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 515 LQDQIAKQRASKQELETELDRM---KQEFHYVEEDLHRTKnTLQSRIKDREEEIQKLRNQLTNKTLSNSSQSELESRLHQ 591
Cdd:pfam05557 161 QQSSLAEAEQRIKELEFEIQSQeqdSEIVKNSKSELARIP-ELEKELERLREHNKHLNENIENKLLLKEEVEDLKRKLER 239
|
250 260 270
....*....|....*....|....*....|....*
gi 1939872721 592 ltetliqkqtlLESLSTEKNSLVFQLERLEQQLHS 626
Cdd:pfam05557 240 -----------EEKYREEAATLELEKEKLEQELQS 263
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
381-602 |
1.97e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 44.62 E-value: 1.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 381 EVERQNLAEAVTLAERKYSEERKK----VDDLQQQVKLHRSSLESAKQELVDYKQKATRILQSKEKLINSLKEGSSFEGL 456
Cdd:PHA02562 187 DMKIDHIQQQIKTYNKNIEEQRKKngenIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAK 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 457 DSSTASSMELEELRHER-------ELQKEEIQKLMGQIHQLRSELQdmeaQQVSEAESAREQLQDLQDQIAKQRASKQEL 529
Cdd:PHA02562 267 IKSKIEQFQKVIKMYEKggvcptcTQQISEGPDRITKIKDKLKELQ----HSLEKLDTAIDELEEIMDEFNEQSKKLLEL 342
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1939872721 530 ETELdrmkqefhyveEDLHRTKNTLQSRIKDREEEIQKLRNQLTNKTlsnssqSELESRLHQLTETLIQKQTL 602
Cdd:PHA02562 343 KNKI-----------STNKQSLITLVDKAKKVKAAIEELQAEFVDNA------EELAKLQDELDKIVKTKSEL 398
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
226-513 |
2.05e-04 |
|
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: 44.73 E-value: 2.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 226 RLENQLLRNEVQSLNQEMA---SLLQRSKETQEELNK-ARVRVEKWNV---DNSKSDRITRELRAQVDDLT--EAVAAKD 296
Cdd:pfam17380 295 KMEQERLRQEKEEKAREVErrrKLEEAEKARQAEMDRqAAIYAEQERMameRERELERIRQEERKRELERIrqEEIAMEI 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 297 SQLAVLKvRLQEADQVLSSRT-EALEA------LQSEKSR-IMQDHNEGSSLQNQALQTLQERLHEADATLKREQESYKQ 368
Cdd:pfam17380 375 SRMRELE-RLQMERQQKNERVrQELEAarkvkiLEEERQRkIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRL 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 369 MQSEfatRLNKMEVERQNLAEAVTLAERKYSEERKKVDDLQQQVKLHRSSLESAKQELVDYKQKATRILQSKEKLINSLK 448
Cdd:pfam17380 454 EEQE---RQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIY 530
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 449 EgssfegldSSTASSMELEELRHERELQKEEIQKLMGQIHQLRSELQDMEAQ-----QVSEAESAREQLQ 513
Cdd:pfam17380 531 E--------EERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLEAMEREremmrQIVESEKARAEYE 592
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
221-421 |
3.37e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.26 E-value: 3.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 221 ELSNLRLENQLLRNEVQSLNQ--EMASLLQRSKETQEELNKarVRVEKWNVDNSKSDRITrELRAQVDDL-TEAVAAKDS 297
Cdd:PRK02224 483 ELEDLEEEVEEVEERLERAEDlvEAEDRIERLEERREDLEE--LIAERRETIEEKRERAE-ELRERAAELeAEAEEKREA 559
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 298 -------------QLAVLKVRLQEadqvLSSRTEALEALQSEKSRIMQDHNEGSSLqNQALQTLQERLHEADATLKREQE 364
Cdd:PRK02224 560 aaeaeeeaeeareEVAELNSKLAE----LKERIESLERIRTLLAAIADAEDEIERL-REKREALAELNDERRERLAEKRE 634
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1939872721 365 SYKQMQSEF-ATRLNKMEVERQNLAEAVTLAERKYSEERKKVDDLQQQVKLHRSSLES 421
Cdd:PRK02224 635 RKRELEAEFdEARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEE 692
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
375-547 |
3.79e-04 |
|
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: 42.60 E-value: 3.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 375 TRLNKMEVERQNLAEAVTLAERKYSEERKKVDDLQQQVKLHRSSLESAKQELvdyKQKATRILQSKEKL--INSLKEgss 452
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEI---EEVEARIKKYEEQLgnVRNNKE--- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 453 FEGLDSSTASsmeleeLRHERELQKEEIQKLMGQIHQLRSELQDMEAQQVSEAESAREQLQDLQDQIAKQRASKQELETE 532
Cdd:COG1579 91 YEALQKEIES------LKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAE 164
|
170
....*....|....*
gi 1939872721 533 LDRMKQEfhyVEEDL 547
Cdd:COG1579 165 REELAAK---IPPEL 176
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
275-626 |
3.88e-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: 43.88 E-value: 3.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 275 DRITRElRAQVDDLTEAVAAKDSQLAVLKVRLQEADQVLSSRTE---ALEALQSEKSRIMQDHNEGSSLQNQALQTLQER 351
Cdd:TIGR00606 224 DQITSK-EAQLESSREIVKSYENELDPLKNRLKEIEHNLSKIMKldnEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQ 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 352 LHEADATLKREQESYKQMQSEFATRLNKMEVERQNLAEAVTLAERKYSEERKKVDDLQQQVKLHRSSLES---------- 421
Cdd:TIGR00606 303 LNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSlatrleldgf 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 422 -----AKQELVDYKQKATRILQSKEKLINSL-KEGSSFEGLDSSTASSMELEELRHERELQ--KEEIQKLMGQIHQLRSE 493
Cdd:TIGR00606 383 ergpfSERQIKNFHTLVIERQEDEAKTAAQLcADLQSKERLKQEQADEIRDEKKGLGRTIElkKEILEKKQEELKFVIKE 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 494 LQDMEAQ-----------QVSEAESAREQLQDLQDQIAKQRASKQELETELDRMKQEFHYVEEDLHRTKNTLQSRIK--- 559
Cdd:TIGR00606 463 LQQLEGSsdrileldqelRKAERELSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMltk 542
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 560 ---DREEEIQKLRNQLTNKTLSNS----SQSELESRLH-------QLTETLIQKQTLLESLSTEKNSLVFQLERLEQQLH 625
Cdd:TIGR00606 543 dkmDKDEQIRKIKSRHSDELTSLLgyfpNKKQLEDWLHskskeinQTRDRLAKLNKELASLEQNKNHINNELESKEEQLS 622
|
.
gi 1939872721 626 S 626
Cdd:TIGR00606 623 S 623
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
279-427 |
3.96e-04 |
|
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: 42.60 E-value: 3.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 279 RELRAQVDDLTEAVAAKDSQLAVLKVRLQEADQVLSSRTEALEALQSEKSRIMQDHNEGSSlqNQALQTLQERLheadAT 358
Cdd:COG1579 27 KELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRN--NKEYEALQKEI----ES 100
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1939872721 359 LKREQESYKQMQSEFATRLNKMEVERQNLAEAVTLAERKYSEERKKVDDLQQQVKLHRSSLESAKQELV 427
Cdd:COG1579 101 LKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELA 169
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
193-624 |
4.72e-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: 43.80 E-value: 4.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 193 KKSTEESTVSNATSVEHSSAPSDGSMSH--ELSNLRLENQLLRNEVQSLNQEMASLLQRSKETQEELNKAR------VRV 264
Cdd:TIGR00618 220 RKQVLEKELKHLREALQQTQQSHAYLTQkrEAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARkaaplaAHI 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 265 EKWNVDNSKSDRITRELRAQVDDLTEAVaAKDSQLAVLKVRLQEADQVLSS--RTEALEALQSEKSRIMQDHNEGSSLQN 342
Cdd:TIGR00618 300 KAVTQIEQQAQRIHTELQSKMRSRAKLL-MKRAAHVKQQSSIEEQRRLLQTlhSQEIHIRDAHEVATSIREISCQQHTLT 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 343 QALQTLQER---LHEADATLKREQESYKQMQSEFATRLNKMEVERQNLAEAVT--LAERKYSEER-----KKVDDLQQQV 412
Cdd:TIGR00618 379 QHIHTLQQQkttLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKqqELQQRYAELCaaaitCTAQCEKLEK 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 413 KLHRSSLESAKQELVDYKQKATRILQSKEKLINSLKEGSSFEGLDSSTASSMELEELRHERELQKEEIQKLMGQIHQLRS 492
Cdd:TIGR00618 459 IHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYA 538
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 493 ELQDMEAQQVSEAESAREQLQDLQDQIAKQRASKQELETELDRMKQEFHYV------------EEDLHRTKNTLQSRIKD 560
Cdd:TIGR00618 539 QLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLqnitvrlqdlteKLSEAEDMLACEQHALL 618
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1939872721 561 REEEIQkLRNQLTNKTLSNSSQSE--LESRLHQLTETLIQKQTLLESLSTEknslVFQLERLEQQL 624
Cdd:TIGR00618 619 RKLQPE-QDLQDVRLHLQQCSQELalKLTALHALQLTLTQERVREHALSIR----VLPKELLASRQ 679
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
242-571 |
4.74e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.98 E-value: 4.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 242 EMASLLQRSKETQEELNKARVRVEKWNVDNSKSDRITR-ELRAQVDDLTEAVAAKDSQLAVLKVRLQEADQVlssrTEAL 320
Cdd:PTZ00121 1480 EEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKaEEAKKADEAKKAEEAKKADEAKKAEEKKKADEL----KKAE 1555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 321 EALQSEKSRIMQDHNEGSSLQNQALQTLQERLHEADATLKREQESYKQMQSEFATRLNKMEVERQNlAEAVtlaeRKYSE 400
Cdd:PTZ00121 1556 ELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIK-AEEL----KKAEE 1630
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 401 ERKKVDDLQQQVKLHRSSLESAKQELVDYKQKATRILQSKEKLINSLKEGSSFEGLDSSTASSMELeelrherelQKEEI 480
Cdd:PTZ00121 1631 EKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKK---------EAEEA 1701
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 481 QKLmgqihqlrSELQDMEAQQVSEAESAREqlqdlQDQIAKQRASKQELETELDRMKQEFHYVEEDlhrTKNTLQSRIKD 560
Cdd:PTZ00121 1702 KKA--------EELKKKEAEEKKKAEELKK-----AEEENKIKAEEAKKEAEEDKKKAEEAKKDEE---EKKKIAHLKKE 1765
|
330
....*....|.
gi 1939872721 561 REEEIQKLRNQ 571
Cdd:PTZ00121 1766 EEKKAEEIRKE 1776
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
478-603 |
4.97e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 43.53 E-value: 4.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 478 EEIQKLMGQIHQLRSELQDMEAQQvseAESAREQLQDLQDQIAkqraskqELETELDRMKQEFHyvEEdlhrtkntlqsr 557
Cdd:COG0542 411 EELDELERRLEQLEIEKEALKKEQ---DEASFERLAELRDELA-------ELEEELEALKARWE--AE------------ 466
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1939872721 558 iKDREEEIQKLRNQLTNKtlsNSSQSELESRLHQLTETLIQKQTLL 603
Cdd:COG0542 467 -KELIEEIQELKEELEQR---YGKIPELEKELAELEEELAELAPLL 508
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
221-568 |
5.00e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.77 E-value: 5.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 221 ELSNLRLENQLLRNEVQSLNQEMASLLQRSKETQEELNKARVRVEKW--NVDNSKSDRITRELRAQVDDLTEAVAAKDSQ 298
Cdd:COG1196 464 LLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVkaALLLAGLRGLAGAVAVLIGVEAAYEAALEAA 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 299 L-AVLKVRLQEADQVLSSRTEALEA----------LQSEKSRIMQDHNEGSSLQNQALQTLQERLHEADATLKREQES-- 365
Cdd:COG1196 544 LaAALQNIVVEDDEVAAAAIEYLKAakagratflpLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTll 623
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 366 -------YKQMQSEFATRLNKMEVERQNLAEAVTLAERKYSEERKKVDDLQQQVKLHRSSLESAKQELVDYKQKATRILQ 438
Cdd:COG1196 624 grtlvaaRLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEE 703
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 439 SKEKLINSLKEgssfegldsstassmELEELRHERELQKEEIQKLMGQIHQLRSELQDMEAQQVSEAESAREQLQDLQDQ 518
Cdd:COG1196 704 EEERELAEAEE---------------ERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERE 768
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 519 IAKQRASKQELET-------ELDRMKQEFHYVEE---DLHRTKNTLQSRIKDREEEIQKL 568
Cdd:COG1196 769 LERLEREIEALGPvnllaieEYEELEERYDFLSEqreDLEEARETLEEAIEEIDRETRER 828
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
318-442 |
5.09e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.23 E-value: 5.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 318 EALEALQSEKSRIMQDHNEgsslQNQALQTLQERLHEADATLKREQESYKQMQSEFATRLNKMEVERQNLAEAVTLAERK 397
Cdd:PRK12704 61 EAKEEIHKLRNEFEKELRE----RRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEEL 136
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1939872721 398 YSEERKKvddLQQQVKLhrsSLESAKQELVD-----YKQKATRILQSKEK 442
Cdd:PRK12704 137 IEEQLQE---LERISGL---TAEEAKEILLEkveeeARHEAAVLIKEIEE 180
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
220-606 |
5.59e-04 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 43.30 E-value: 5.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 220 HELSNLRLENQLLRNEVQSLNQEMASLLQRSKETQEELNKARVRVEKwnvdnsksdrITRELRAQVDDLTEAVAAKDSQL 299
Cdd:pfam06160 86 KALDEIEELLDDIEEDIKQILEELDELLESEEKNREEVEELKDKYRE----------LRKTLLANRFSYGPAIDELEKQL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 300 AVLKVRLQEADQVLSS-----RTEALEALQSEKSRIMQDHNEGSSLQNQALQTLQERLHEADATLKR-EQESYKQMQSEF 373
Cdd:pfam06160 156 AEIEEEFSQFEELTESgdyleAREVLEKLEEETDALEELMEDIPPLYEELKTELPDQLEELKEGYREmEEEGYALEHLNV 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 374 ATRLNKMEVERQNLAEAvtLAERKYSEERKKVDDLQQQVKLHRSSLE---SAKQ-------ELVDYKQKATRILQSKEKL 443
Cdd:pfam06160 236 DKEIQQLEEQLEENLAL--LENLELDEAEEALEEIEERIDQLYDLLEkevDAKKyveknlpEIEDYLEHAEEQNKELKEE 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 444 INSLKEgsSFEGLDSSTASSMELEELRHERELQKEEIQKLMGQIHQLRSELQDMEAQQVSEAESAREQLQDLQDQIAKQR 523
Cdd:pfam06160 314 LERVQQ--SYTLNENELERVRGLEKQLEELEKRYDEIVERLEEKEVAYSELQEELEEILEQLEEIEEEQEEFKESLQSLR 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 524 ASKQELETELDRMKQEFHYVEEDLHRTK-----NTLQSRIKDREEEIQKLRNQLTNKTL--------SNSSQSELEsRLH 590
Cdd:pfam06160 392 KDELEAREKLDEFKLELREIKRLVEKSNlpglpESYLDYFFDVSDEIEDLADELNEVPLnmdevnrlLDEAQDDVD-TLY 470
|
410
....*....|....*.
gi 1939872721 591 QLTETLIQKQTLLESL 606
Cdd:pfam06160 471 EKTEELIDNATLAEQL 486
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
197-420 |
5.64e-04 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 43.14 E-value: 5.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 197 EESTVSNATSVEHSSAPSDGSMSHELSNLRLENQLLR----NEVQSLNQEmASLLQRSKETQEELNKARVRVEKWNVDNS 272
Cdd:pfam05622 250 QQAELSQADALLSPSSDPGDNLAAEIMPAEIREKLIRlqheNKMLRLGQE-GSYRERLTELQQLLEDANRRKNELETQNR 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 273 KSDRITRELRAQVDDLTEAVAAKDSQLAVLKVRLQEADQVLSSRTEALEALQSEKSRIMQDHNEGSSLQNQALQTLQERL 352
Cdd:pfam05622 329 LANQRILELQQQVEELQKALQEQGSKAEDSSLLKQKLEEHLEKLHEAQSELQKKKEQIEELEPKQDSNLAQKIDELQEAL 408
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1939872721 353 HEADATLKREQESYKQMQSEFATRLNKMEVERQNLAEAVTLAERK-YSEERKKVDDLQQQVKLHRSSLE 420
Cdd:pfam05622 409 RKKDEDMKAMEERYKKYVEKAKSVIKTLDPKQNPASPPEIQALKNqLLEKDKKIEHLERDFEKSKLQRE 477
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
241-607 |
5.68e-04 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 43.20 E-value: 5.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 241 QEMASLLQRSKETQEELNKARVRVEKWNVDNSKSDRITRELRAQVDDLTEAVAAKDsqlaVLKVRLQEADQVLSSRTEAL 320
Cdd:pfam07111 73 QELRRLEEEVRLLRETSLQQKMRLEAQAMELDALAVAEKAGQAEAEGLRAALAGAE----MVRKNLEEGSQRELEEIQRL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 321 EalQSEKSRIMQDHNEGSSLQNQALQTLQERLHEADATLKREQESYKQMQSEFATRLNKMEVERQNLAEAVTLAE--RKY 398
Cdd:pfam07111 149 H--QEQLSSLTQAHEEALSSLTSKAEGLEKSLNSLETKRAGEAKQLAEAQKEAELLRKQLSKTQEELEAQVTLVEslRKY 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 399 --------------SEERKKVDDLQQQVKLHRSSLESAKQELVDYKQKATRILQ-SKEKLINSLKEGSSFEGLDSSTASS 463
Cdd:pfam07111 227 vgeqvppevhsqtwELERQELLDTMQHLQEDRADLQATVELLQVRVQSLTHMLAlQEEELTRKIQPSDSLEPEFPKKCRS 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 464 MELEELRH------ERELQKEEIQKLMGQIHQLRSELQDMEAQQVSEAESAREQLQDLQDQIAKQRASKQELETELDRMK 537
Cdd:pfam07111 307 LLNRWREKvfalmvQLKAQDLEHRDSVKQLRGQVAELQEQVTSQSQEQAILQRALQDKAAEVEVERMSAKGLQMELSRAQ 386
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 538 QefhyveedlhrTKNTLQSRIKDREEEIQKLRNQLtnktlsNSSQSELESRLHQLTETLIQKQTLLESLS 607
Cdd:pfam07111 387 E-----------ARRRQQQQTASAEEQLKFVVNAM------SSTQIWLETTMTRVEQAVARIPSLSNRLS 439
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
493-624 |
5.69e-04 |
|
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: 42.22 E-value: 5.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 493 ELQDMEaqqvSEAESAREQLQDLQDQIAKQRASKQELETELDRMKQEFhyveEDLHRTKNTLQSRIKDREEEIQKLRNQL 572
Cdd:COG1579 11 DLQELD----SELDRLEHRLKELPAELAELEDELAALEARLEAAKTEL----EDLEKEIKRLELEIEEVEARIKKYEEQL 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1939872721 573 ----TNKTLSN---------SSQSELESRLHQLTETLIQKQTLLESLSTEKNSLVFQLERLEQQL 624
Cdd:COG1579 83 gnvrNNKEYEAlqkeieslkRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAEL 147
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
235-391 |
6.23e-04 |
|
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: 41.83 E-value: 6.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 235 EVQSLNQEMASLLQRSKETQEELNKARVRVEKWNVDNSKSDRITRELRAQVDDLTEAVAAKDSQLAVLKVRLQEAD---- 310
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRnnke 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 311 -QVLSSRTEALEALQSEKSRIMQDHNEGSSLQNQALQTLQERLHEADATLKREQESYKQMQSEFATRLNKMEVERQNLAE 389
Cdd:COG1579 91 yEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAA 170
|
..
gi 1939872721 390 AV 391
Cdd:COG1579 171 KI 172
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
242-620 |
7.21e-04 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 43.12 E-value: 7.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 242 EMASLLQRSKETQEELNKARVRVEKWNVDNSKSDRITRELRAQVDDLTEAVAAKDSQLAVLKVRlQEADQVLSSRTEALE 321
Cdd:PRK10929 45 EIVEALQSALNWLEERKGSLERAKQYQQVIDNFPKLSAELRQQLNNERDEPRSVPPNMSTDALE-QEILQVSSQLLEKSR 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 322 ALQSEKSRIMQDHNEGSSLQNQ------ALQTLQERLHEADATLK-REQESYKQMQSEFATR---LNKMEVE------RQ 385
Cdd:PRK10929 124 QAQQEQDRAREISDSLSQLPQQqtearrQLNEIERRLQTLGTPNTpLAQAQLTALQAESAALkalVDELELAqlsannRQ 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 386 NLAEA-VTLAERKYseerkkvDDLQQQVKLHRSSLESAKQelvdykQKATRILQSKEKlinsLKEGSsfEGLDSSTASSM 464
Cdd:PRK10929 204 ELARLrSELAKKRS-------QQLDAYLQALRNQLNSQRQ------REAERALESTEL----LAEQS--GDLPKSIVAQF 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 465 ELEEL-RHERELQKEEIQKLMGQIHQLRSELqdmeaQQVSEAESA-REQLQ----------DLQDQIAK--QRASKQELE 530
Cdd:PRK10929 265 KINRElSQALNQQAQRMDLIASQQRQAASQT-----LQVRQALNTlREQSQwlgvsnalgeALRAQVARlpEMPKPQQLD 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 531 TELDRMK-QEFHYveedlhrtkntlqsrikdrEEEIQKLRNQLTNKTLSNSSQSELESRLhqLTETLIQKQTLLESLSTE 609
Cdd:PRK10929 340 TEMAQLRvQRLRY-------------------EDLLNKQPQLRQIRQADGQPLTAEQNRI--LDAQLRTQRELLNSLLSG 398
|
410
....*....|.
gi 1939872721 610 KNSLVFQLERL 620
Cdd:PRK10929 399 GDTLILELTKL 409
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
343-572 |
8.12e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.98 E-value: 8.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 343 QALQTLQERLhEADATLKREQESYKQMQSEFAT-RLNKMEVERQNLAEAVTLAERKYSEERKKVDDLQQQVKLHRSSLES 421
Cdd:COG4913 242 EALEDAREQI-ELLEPIRELAERYAAARERLAElEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDA 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 422 AKQELVDYKQkatRILQSKEKLINSLKEgssfegldsstassmELEELRHERELQKEEIQKLMGQIHQL-------RSEL 494
Cdd:COG4913 321 LREELDELEA---QIRGNGGDRLEQLER---------------EIERLERELEERERRRARLEALLAALglplpasAEEF 382
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1939872721 495 QDMEAQQVSEAESAREQLQDLQDQIAKQRASKQELETELDRMKQEFhyveedlhrtkNTLQSRIKDREEEIQKLRNQL 572
Cdd:COG4913 383 AALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEI-----------ASLERRKSNIPARLLALRDAL 449
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
234-611 |
9.07e-04 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 42.73 E-value: 9.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 234 NEVQSLNQEMASLLQRS----KETQEELNkarVRVEKWNVDNSKSDRITRELRAQVDDLTEAVAAKDSQLAVLKVRLQEA 309
Cdd:TIGR01612 1372 KEIEENNKNIKDELDKSekliKKIKDDIN---LEECKSKIESTLDDKDIDECIKKIKELKNHILSEESNIDTYFKNADEN 1448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 310 DQVLSSRTEALEALQSEKSRIMQDH-NEGSSLQNQALQTLQERLH-------EADATLK---REQESYKQMQSEFATRLN 378
Cdd:TIGR01612 1449 NENVLLLFKNIEMADNKSQHILKIKkDNATNDHDFNINELKEHIDkskgckdEADKNAKaieKNKELFEQYKKDVTELLN 1528
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 379 KM-EVERQNlaeavTLAERKYSEER--KKVDDLQQQVKLHRsslESAKQELVDYKQKATRILQSKEKLINSLKEG----S 451
Cdd:TIGR01612 1529 KYsALAIKN-----KFAKTKKDSEIiiKEIKDAHKKFILEA---EKSEQKIKEIKKEKFRIEDDAAKNDKSNKAAidiqL 1600
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 452 SFEGLDSSTASSMELEELRHERELQKEEIQKlmgQIHQLRSELQDMEaqqVSEAESAREQLQDLQDQIAKQRASKQELET 531
Cdd:TIGR01612 1601 SLENFENKFLKISDIKKKINDCLKETESIEK---KISSFSIDSQDTE---LKENGDNLNSLQEFLESLKDQKKNIEDKKK 1674
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 532 ELDRMKQEFHYVEEDLHRTKNTLQSRIKDREEEIQKlrnqlTNKTLSNSSQSELESRLHQLTETL-------IQKQTLLE 604
Cdd:TIGR01612 1675 ELDELDSEIEKIEIDVDQHKKNYEIGIIEKIKEIAI-----ANKEEIESIKELIEPTIENLISSFntndlegIDPNEKLE 1749
|
....*..
gi 1939872721 605 SLSTEKN 611
Cdd:TIGR01612 1750 EYNTEIG 1756
|
|
| ADIP |
pfam11559 |
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ... |
477-573 |
9.23e-04 |
|
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at cell-cell adherens junctions, and in Sch. pombe and other fungi where it anchors spindle-pole bodies to spindle microtubules. It is a coiled-coil structure, and in pombe, it is required for anchoring the minus end of spindle microtubules to the centrosome equivalent, the spindle-pole body. The name ADIP derives from the family being composed of Afadin- and alpha -Actinin-Binding Proteins localized at Cell-Cell Adherens Junctions.
Pssm-ID: 463295 [Multi-domain] Cd Length: 151 Bit Score: 40.38 E-value: 9.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 477 KEEIQKLMGQIHQLRSELQdmeaQQVSEAESAREQLQDLQDQIAKQRASKQELETELDRMKQEFHYVEEDLHRTKNTLQS 556
Cdd:pfam11559 51 LEFRESLNETIRTLEAEIE----RLQSKIERLKTQLEDLERELALLQAKERQLEKKLKTLEQKLKNEKEELQRLKNALQQ 126
|
90 100
....*....|....*....|....
gi 1939872721 557 R-------IKDREEEIQKLRNQLT 573
Cdd:pfam11559 127 IktqfaheVKKRDREIEKLKERLA 150
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
478-624 |
9.48e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.20 E-value: 9.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 478 EEIQKLMGQIHQLRSELQDMEAqqvsEAESAREQLQDLQDQIAKQRASKQELETELDRMKQEFHYVEEDLhrtkNTLQSR 557
Cdd:COG4372 38 FELDKLQEELEQLREELEQARE----ELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEEL----ESLQEE 109
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1939872721 558 IKDREEEIQKLRNQLTNKtlsNSSQSELESRLHQLTETLIQKQTLLESLSTEKNSLVFQLERLEQQL 624
Cdd:COG4372 110 AEELQEELEELQKERQDL---EQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQEL 173
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
280-428 |
1.04e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.59 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 280 ELRAQVDDLTEAVAAKDSQLAVLKVRLQEADQVLS----------------SRTEALEALQSEKSRIMQDHNEGSSLQ-- 341
Cdd:COG4913 614 ALEAELAELEEELAEAEERLEALEAELDALQERREalqrlaeyswdeidvaSAEREIAELEAELERLDASSDDLAALEeq 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 342 ----NQALQTLQERLHEAD---ATLKREQESYKQMQSEFATRLNkmEVERQNLAEAVTLAERKYSE------ERKKVDDL 408
Cdd:COG4913 694 leelEAELEELEEELDELKgeiGRLEKELEQAEEELDELQDRLE--AAEDLARLELRALLEERFAAalgdavERELRENL 771
|
170 180
....*....|....*....|
gi 1939872721 409 QQQVKLHRSSLESAKQELVD 428
Cdd:COG4913 772 EERIDALRARLNRAEEELER 791
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
478-626 |
1.04e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.59 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 478 EEIQKLMGQIHQLRSELQDMEA-QQVSEAESAREQLQDLQDQIAKQRASKQELETELDRMKQEFHYVEEDL--------- 547
Cdd:COG4913 255 EPIRELAERYAAARERLAELEYlRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELdeleaqirg 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 548 --HRTKNTLQSRIKDREEEIQKLRNQLTN-----KTL---SNSSQSELESRLHQLTETLIQKQTLLESLSTEKNSLVFQL 617
Cdd:COG4913 335 ngGDRLEQLEREIERLERELEERERRRARleallAALglpLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAAL 414
|
....*....
gi 1939872721 618 ERLEQQLHS 626
Cdd:COG4913 415 RDLRRELRE 423
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
251-575 |
1.14e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.44 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 251 KETQEELNKARVRVEKWNVDNSKSDRITR--ELRAQVDDLTEAvAAKDSQLAVLKVRLQEADQVLSSRTEALEALQSEK- 327
Cdd:PTZ00121 1384 KKKAEEKKKADEAKKKAEEDKKKADELKKaaAAKKKADEAKKK-AEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEa 1462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 328 SRIMQDHNEGSSLQNQAlqtlqERLHEADATLKREQESYKQmqsefATRLNKMEVERQNLAEAVTLAERKYSEERKKVDD 407
Cdd:PTZ00121 1463 KKKAEEAKKADEAKKKA-----EEAKKADEAKKKAEEAKKK-----ADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEE 1532
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 408 LQQQVKLHRSSLESAKQELvdykQKATRILQSKE-KLINSLKEGSSFEGLDSSTASSMELEELRHERELQKEEIQKLMGQ 486
Cdd:PTZ00121 1533 AKKADEAKKAEEKKKADEL----KKAEELKKAEEkKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMK 1608
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 487 IHQLRSELQD-MEAQQVSEAESAREQLQDLQDQIAKQRASKQELETELD----RMKQEFHYVEEDLHRTKntlqsRIKDR 561
Cdd:PTZ00121 1609 AEEAKKAEEAkIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEenkiKAAEEAKKAEEDKKKAE-----EAKKA 1683
|
330
....*....|....
gi 1939872721 562 EEEIQKLRNQLTNK 575
Cdd:PTZ00121 1684 EEDEKKAAEALKKE 1697
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
478-606 |
1.16e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 42.15 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 478 EEIQKLMGQIHQLRSELQDMeaqqvseaesaREQLQDLQDQIAKQRASKQELETELDRMKQEfhyVEEDLHRTKntlqsR 557
Cdd:COG2433 406 RELTEEEEEIRRLEEQVERL-----------EAEVEELEAELEEKDERIERLERELSEARSE---ERREIRKDR-----E 466
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1939872721 558 IKDREEEIQKLRNQLtnktlsnssqSELESRLHQLTETLIQKQTLLESL 606
Cdd:COG2433 467 ISRLDREIERLEREL----------EEERERIEELKRKLERLKELWKLE 505
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
478-628 |
1.36e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.74 E-value: 1.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 478 EEIQKLMGQIHQLRSELQDMEAQQVS---EAESAREQLQDLQDQIAKQRASKQE----------------LETELDRMkq 538
Cdd:COG3883 44 AELEELNEEYNELQAELEALQAEIDKlqaEIAEAEAEIEERREELGERARALYRsggsvsyldvllgsesFSDFLDRL-- 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 539 efHYVEEDLHRTKNTLQSRIKDREEEIQKLRNQLTNKTLSNSSQSELESRLHQLTETLIQKQTLLESLSTEKNSLVFQLE 618
Cdd:COG3883 122 --SALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLA 199
|
170
....*....|
gi 1939872721 619 RLEQQLHSAA 628
Cdd:COG3883 200 ELEAELAAAE 209
|
|
| HlpA |
COG2825 |
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ... |
478-575 |
1.36e-03 |
|
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 442073 [Multi-domain] Cd Length: 171 Bit Score: 40.20 E-value: 1.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 478 EEIQKLMGQIHQLRSELQDMEAQQVSEAESAREQLQDLQDQIAKQRAS-----KQELETELDRMKQEFhyveedlhrtkn 552
Cdd:COG2825 32 QRILQESPEGKAAQKKLEKEFKKRQAELQKLEKELQALQEKLQKEAATlseeeRQKKERELQKKQQEL------------ 99
|
90 100
....*....|....*....|...
gi 1939872721 553 tlQSRIKDREEEIQKLRNQLTNK 575
Cdd:COG2825 100 --QRKQQEAQQDLQKRQQELLQP 120
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
477-572 |
1.83e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 40.68 E-value: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 477 KEEIQKLMGQIHQLRSELQDMEA------QQVSEAESAREqLQDLQDQIAKQRASKQELETE-------LDRMKQEFHYV 543
Cdd:COG1579 51 KTELEDLEKEIKRLELEIEEVEArikkyeEQLGNVRNNKE-YEALQKEIESLKRRISDLEDEilelmerIEELEEELAEL 129
|
90 100
....*....|....*....|....*....
gi 1939872721 544 EEDLHRTKNTLQSRIKDREEEIQKLRNQL 572
Cdd:COG1579 130 EAELAELEAELEEKKAELDEELAELEAEL 158
|
|
| OmpH |
pfam03938 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
500-616 |
1.93e-03 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 461098 [Multi-domain] Cd Length: 140 Bit Score: 39.10 E-value: 1.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 500 QQVSEAESAREQLQDLQdqiakqraskQELETELDRMKQEFHYVEEDLHRTKNTLQSRIKDREEEIQKLRNQLtnKTLSN 579
Cdd:pfam03938 12 EESPEGKAAQAQLEKKF----------KKRQAELEAKQKELQKLYEELQKDGALLEEEREEKEQELQKKEQEL--QQLQQ 79
|
90 100 110
....*....|....*....|....*....|....*....
gi 1939872721 580 SSQSELESRLHQLTETLIQK-QTLLESLSTEKN-SLVFQ 616
Cdd:pfam03938 80 KAQQELQKKQQELLQPIQDKiNKAIKEVAKEKGyDLVLD 118
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
221-401 |
2.48e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.44 E-value: 2.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 221 ELSNLRLENQLLRNEVQSLNQEMASLLQRS----------------KETQEELnkARVRVEKWNVDNSKSDriTRELRAQ 284
Cdd:COG4913 618 ELAELEEELAEAEERLEALEAELDALQERRealqrlaeyswdeidvASAEREI--AELEAELERLDASSDD--LAALEEQ 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 285 VDDLTEAVAAKDSQLAVLKVRLQEADQVLSSRTEALEALQSEKSRImqdhneGSSLQNQALQTLQERLHEADAtlkreQE 364
Cdd:COG4913 694 LEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAA------EDLARLELRALLEERFAAALG-----DA 762
|
170 180 190
....*....|....*....|....*....|....*..
gi 1939872721 365 SYKQMQSEFATRLNKMEVERQNLAEAVTLAERKYSEE 401
Cdd:COG4913 763 VERELRENLEERIDALRARLNRAEEELERAMRAFNRE 799
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
220-539 |
2.76e-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: 41.03 E-value: 2.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 220 HELSNLRLENQLLRNEVQSLNQEMASLLQRSKETQ---EELNKARVRVEKWNVDNSKsdRItRELRAQVDDLTEAVAAKD 296
Cdd:pfam07888 73 RQRRELESRVAELKEELRQSREKHEELEEKYKELSassEELSEEKDALLAQRAAHEA--RI-RELEEDIKTLTQRVLERE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 297 SQLAVLKvrlQEADQVLSSRTEALEALQSEKSRIMQDHNEGSSLqNQALQTLQERLHEADATLKREQESYKQMQSEFATR 376
Cdd:pfam07888 150 TELERMK---ERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSL-SKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTA 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 377 LNKMEVERQNLAEAVTLAERKYSEERKKV---DDL--------QQQVKLHRSSLESAKQELvdykQKATRILQSKEKLIN 445
Cdd:pfam07888 226 HRKEAENEALLEELRSLQERLNASERKVEglgEELssmaaqrdRTQAELHQARLQAAQLTL----QLADASLALREGRAR 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 446 SLKEGssfEGLDSSTassmelEELRHERELQKEEIQKLMGQIHQLRSELQDMEAQQVSEAESAREQLQDLQDQIAKQRAS 525
Cdd:pfam07888 302 WAQER---ETLQQSA------EADKDRIEKLSAELQRLEERLQEERMEREKLEVELGREKDCNRVQLSESRRELQELKAS 372
|
330
....*....|....
gi 1939872721 526 KQELETELDRMKQE 539
Cdd:pfam07888 373 LRVAQKEKEQLQAE 386
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
457-627 |
2.96e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 40.28 E-value: 2.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 457 DSSTASSMELEELRHERELQKEEIQKLMGQIHQLRSELQDMEAQQvseaESAREQLQDLQDQIAKQRASKQELETELDRM 536
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKR----DELNAQVKELREEAQELREKRDELNEKVKEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 537 KQEfhyveedlhrtKNTLQSRIKDREEEIQKLRNQLTNKTLSNSSQSELESRLHQLTETLiqkQTllESLSTEK-NSLVF 615
Cdd:COG1340 77 KEE-----------RDELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQ---QT--EVLSPEEeKELVE 140
|
170
....*....|..
gi 1939872721 616 QLERLEQQLHSA 627
Cdd:COG1340 141 KIKELEKELEKA 152
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
290-591 |
3.84e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 40.54 E-value: 3.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 290 EAVAAKDSQLAVLKVRLQEADQVLSSRTEALEALQSEKSRIMQDHNEGSSLQNQA----------LQTLQERLHEADATL 359
Cdd:pfam01576 5 EEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAeemrarlaarKQELEEILHELESRL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 360 KREQESYKQMQSEfatrlnkmeveRQNLAEAVTLAERKYSEERKKVDDLQQQVKLHRSSLESAKQELVDYKQKATRILQS 439
Cdd:pfam01576 85 EEEEERSQQLQNE-----------KKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 440 KEKLINSLKEGSSFEGLDSSTASSMELEELRHERELQkeEIQKLMGQIHQLRSELQDMEAQQVSEAESAREQLQDLQDQI 519
Cdd:pfam01576 154 RKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMIS--DLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQI 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 520 AKQRAS----KQELETELDRMKQE-----------------FHYVEEDLHRTK---NTLQSRIKDREEEIQKLRNQLTNK 575
Cdd:pfam01576 232 AELRAQlakkEEELQAALARLEEEtaqknnalkkireleaqISELQEDLESERaarNKAEKQRRDLGEELEALKTELEDT 311
|
330
....*....|....*.
gi 1939872721 576 TLSNSSQSELESRLHQ 591
Cdd:pfam01576 312 LDTTAAQQELRSKREQ 327
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
229-449 |
4.31e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 40.38 E-value: 4.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 229 NQLLRNEVQSLNQEMASLlqrskETQEELNKARVRVEKWNVDNS--KSDRITRELRAQVDDLTEAVAAKDSQLAVLKVRL 306
Cdd:PHA02562 169 DKLNKDKIRELNQQIQTL-----DMKIDHIQQQIKTYNKNIEEQrkKNGENIARKQNKYDELVEEAKTIKAEIEELTDEL 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 307 QEADQVLSSRTEALEALQSEKSRIMQDHNEGSSL-----QNQALQTLQERLHEADATLKREQESYKQMQsefaTRLNKME 381
Cdd:PHA02562 244 LNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVikmyeKGGVCPTCTQQISEGPDRITKIKDKLKELQ----HSLEKLD 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 382 VERQNLAEAVTlaerKYSEERKKVDDLQQQVKLHRSSL--------------ESAKQELVDYKQKATRILQSKEKLINSL 447
Cdd:PHA02562 320 TAIDELEEIMD----EFNEQSKKLLELKNKISTNKQSLitlvdkakkvkaaiEELQAEFVDNAEELAKLQDELDKIVKTK 395
|
..
gi 1939872721 448 KE 449
Cdd:PHA02562 396 SE 397
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
479-623 |
4.31e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 39.52 E-value: 4.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 479 EIQKLMGQIHQLRSELQDMEAQQV---SEAESAREQLQDLQDQIAKQRASKQELETELDRMKQEFHYVE-----EDLHRT 550
Cdd:COG1579 18 ELDRLEHRLKELPAELAELEDELAaleARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRnnkeyEALQKE 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1939872721 551 KNTLQSRIKDREEEIQKLRNQLTNKTlsnSSQSELESRLHQLTETLIQKQTLLESLSTEKNSlvfQLERLEQQ 623
Cdd:COG1579 98 IESLKRRISDLEDEILELMERIEELE---EELAELEAELAELEAELEEKKAELDEELAELEA---ELEELEAE 164
|
|
| FtsB |
COG2919 |
Cell division protein FtsB [Cell cycle control, cell division, chromosome partitioning]; |
499-545 |
4.44e-03 |
|
Cell division protein FtsB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442163 [Multi-domain] Cd Length: 96 Bit Score: 37.17 E-value: 4.44e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1939872721 499 AQQVSEAESAREQLQDLQDQIAKQRASKQELETELDRMKQEFHYVEE 545
Cdd:COG2919 25 DGGLLAYRELRQEIAELEAENAKLKARNAELEAEVADLKDGPDYIEE 71
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
219-630 |
4.70e-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: 40.59 E-value: 4.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 219 SHELSNLRLENQLLRNEVQSLNQEMASLLQRSKETQEELN-------------KARVRVE------KWNVDNSKSDRITR 279
Cdd:pfam12128 250 FNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNqllrtlddqwkekRDELNGElsaadaAVAKDRSELEALED 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 280 ELRAQVDDLTEAVAAKDSQLAVLKVRLQEADQVLSSRTEAL----EALQSEKSRIMQDHN--------------EGSSLQ 341
Cdd:pfam12128 330 QHGAFLDADIETAAADQEQLPSWQSELENLEERLKALTGKHqdvtAKYNRRRSKIKEQNNrdiagikdklakirEARDRQ 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 342 N-------QAL-QTLQERLHEADATLKREQESYKQMQSEFATRLNKMEVE------RQNLAEAVTLAERKYSEERKKVDD 407
Cdd:pfam12128 410 LavaeddlQALeSELREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATpelllqLENFDERIERAREEQEAANAEVER 489
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 408 LQQQVKLHRSSLESAKQELVDYKQKATRILQSKEKLINSL--KEGSSFEGLDS-------------STASSMELEELRHE 472
Cdd:pfam12128 490 LQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLfpQAGTLLHFLRKeapdweqsigkviSPELLHRTDLDPEV 569
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 473 RELQKEEIQKLMG-----------QIHQLRSELQDMEAQQVSEAESAREQLQDLQDQIAKQRASKQELETELDRMKQEFH 541
Cdd:pfam12128 570 WDGSVGGELNLYGvkldlkridvpEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALK 649
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 542 YVEEDLHRTKNTLQS-----------RIKDREEEIQKLRNQLtnKTLSNSSQSELESRLHQLTETLIQKQTLLESLSTEK 610
Cdd:pfam12128 650 NARLDLRRLFDEKQSekdkknkalaeRKDSANERLNSLEAQL--KQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGAL 727
|
490 500
....*....|....*....|
gi 1939872721 611 NSlvfQLERLEQQLHSAATG 630
Cdd:pfam12128 728 DA---QLALLKAAIAARRSG 744
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
260-391 |
5.02e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 40.45 E-value: 5.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 260 ARVRVEKwnvdNSKSDRItRELRAQVDDL-TEAVAAKDSQLAVLKVRLQEADQVLSSRTEALEAL----QSEKSRImqdh 334
Cdd:COG0542 400 ARVRMEI----DSKPEEL-DELERRLEQLeIEKEALKKEQDEASFERLAELRDELAELEEELEALkarwEAEKELI---- 470
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1939872721 335 negsslqnQALQTLQERLHEADATLKREQESYKQMQSEFA--TRLNKMEVERQNLAEAV 391
Cdd:COG0542 471 --------EEIQELKEELEQRYGKIPELEKELAELEEELAelAPLLREEVTEEDIAEVV 521
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
221-375 |
5.55e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 39.75 E-value: 5.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 221 ELSNLRLENQLLRNEVQSLNQEMASLLQRSKETQEELNK------ARVRVEKWNVDNSKSD------------RITRELR 282
Cdd:COG4942 70 RIRALEQELAALEAELAELEKEIAELRAELEAQKEELAEllralyRLGRQPPLALLLSPEDfldavrrlqylkYLAPARR 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 283 AQVDDL---TEAVAAKDSQLAVLKVRLQEADQVLSSRTEALEALQSEKSRIMQDHNEGSSLQNQALQTLQERLHEADATL 359
Cdd:COG4942 150 EQAEELradLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALI 229
|
170
....*....|....*.
gi 1939872721 360 KREQESYKQMQSEFAT 375
Cdd:COG4942 230 ARLEAEAAAAAERTPA 245
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
421-584 |
5.56e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 39.76 E-value: 5.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 421 SAKQELVDYKQKATRILQSKEKLINSLKEGSSFEgldsstassmeleelrherelQKEEIqklmgqiHQLRSELQDmeaq 500
Cdd:PRK12704 28 IAEAKIKEAEEEAKRILEEAKKEAEAIKKEALLE---------------------AKEEI-------HKLRNEFEK---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 501 qvsEAESAREQLQDLQDQIA-KQRASKQELEtELDRMKQEFHYVEEDLHRTKNTLQSRIKDREEEIQKLRNQLTNktLSN 579
Cdd:PRK12704 76 ---ELRERRNELQKLEKRLLqKEENLDRKLE-LLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELER--ISG 149
|
....*
gi 1939872721 580 SSQSE 584
Cdd:PRK12704 150 LTAEE 154
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
239-622 |
6.06e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 40.17 E-value: 6.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 239 LNQEMASLLQRSKETQEELNKARVRVEKWNVdnSKSDRITRELRAQVDDLTEAVAAKDSQLAVLKVRLQEAdqvlssrte 318
Cdd:PRK10246 255 LQQEASRRQQALQQALAAEEKAQPQLAALSL--AQPARQLRPHWERIQEQSAALAHTRQQIEEVNTRLQST--------- 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 319 alealQSEKSRIMQDHNEGSSLQNQALQTLQERLHEADA------------TLKREQESYKQMQSEFATRLNKMEVERQN 386
Cdd:PRK10246 324 -----MALRARIRHHAAKQSAELQAQQQSLNTWLAEHDRfrqwnnelagwrAQFSQQTSDREQLRQWQQQLTHAEQKLNA 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 387 L--------AEAVTLAERKYSEER-----------------KKVDDLQQQVKLHRSSLESAKQELV----DYKQKATRIL 437
Cdd:PRK10246 399 LpaitltltADEVAAALAQHAEQRplrqrlvalhgqivpqqKRLAQLQVAIQNVTQEQTQRNAALNemrqRYKEKTQQLA 478
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 438 QSK-----EKLINSLKE--------------GSS-------FEGLDSsTASSMELEELRHERELQKEEIQKLMGQIHQLR 491
Cdd:PRK10246 479 DVKticeqEARIKDLEAqraqlqagqpcplcGSTshpaveaYQALEP-GVNQSRLDALEKEVKKLGEEGAALRGQLDALT 557
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 492 SELQ--DMEAQQVSEAESA-REQLQDLQDQIAKQRASKQELETELDrmKQEFHYVEEDLHRTKNTLQSRIKDREEEI--- 565
Cdd:PRK10246 558 KQLQrdESEAQSLRQEEQAlTQQWQAVCASLNITLQPQDDIQPWLD--AQEEHERQLRLLSQRHELQGQIAAHNQQIiqy 635
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1939872721 566 --------QKLRNQLTNKTLSNSSQSELESRLH---QLTETLIQKQTLLESLSTEKNSLVFQLERLEQ 622
Cdd:PRK10246 636 qqqieqrqQQLLTALAGYALTLPQEDEEASWLAtrqQEAQSWQQRQNELTALQNRIQQLTPLLETLPQ 703
|
|
| PRK06975 |
PRK06975 |
bifunctional uroporphyrinogen-III synthetase/uroporphyrin-III C-methyltransferase; Reviewed |
273-381 |
7.18e-03 |
|
bifunctional uroporphyrinogen-III synthetase/uroporphyrin-III C-methyltransferase; Reviewed
Pssm-ID: 235899 [Multi-domain] Cd Length: 656 Bit Score: 39.70 E-value: 7.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 273 KSDRITRELRAQVDDLTEAVAAKDSQLAVLKVRLQEADqvlsSRTEALEALQSEKSRIMQD--HNEGSSLQNQALQTLQ- 349
Cdd:PRK06975 361 ANDAQTAELRVKTEQAQASVHQLDSQFAQLDGKLADAQ----SAQQALEQQYQDLSRNRDDwmIAEVEQMLSSASQQLQl 436
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1939872721 350 --------ERLHEADATLKREQES-YKQMQSEFATRLNKME 381
Cdd:PRK06975 437 tgnvqlalIALQNADARLATSDSPqAVAVRKAIAQDIERLK 477
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
291-449 |
7.41e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.43 E-value: 7.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 291 AVAAKDSQLAVLKVRLQEADQVLSSRTEALEALQSEKSRIMQDHNEgsslQNQALQTLQERLHEADATLKREQESYKQMQ 370
Cdd:COG3883 10 TPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNE----LQAELEALQAEIDKLQAEIAEAEAEIEERR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 371 SEFATRLNKME---------------------VERQNLAEAVTLAERK----YSEERKKVDDLQQQVKLHRSSLESAKQE 425
Cdd:COG3883 86 EELGERARALYrsggsvsyldvllgsesfsdfLDRLSALSKIADADADlleeLKADKAELEAKKAELEAKLAELEALKAE 165
|
170 180
....*....|....*....|....
gi 1939872721 426 LVDYKQKATRILQSKEKLINSLKE 449
Cdd:COG3883 166 LEAAKAELEAQQAEQEALLAQLSA 189
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
221-556 |
7.57e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 39.64 E-value: 7.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 221 ELSNLRLENQLLRNEVQSLNQEMASLLQRSKETQEELNKARVRVEKWN-------VDNSKSDRITRELRAQVDDLTEAVA 293
Cdd:PRK02224 406 DLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKcpecgqpVEGSPHVETIEEDRERVEELEAELE 485
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 294 akdsqlavlKVRLQEADqvLSSRTEALEALQSEKSRImqdhnegSSLQNQAlQTLQERLHEADATLKREQESYKQMQSEF 373
Cdd:PRK02224 486 ---------DLEEEVEE--VEERLERAEDLVEAEDRI-------ERLEERR-EDLEELIAERRETIEEKRERAEELRERA 546
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 374 ATRLNKMEVERQNLAEAVTLAERKySEERKKVDDLQQQVKLHRSSLESAKQELVDYKQKATRILQSKEKLIN-SLKEGSS 452
Cdd:PRK02224 547 AELEAEAEEKREAAAEAEEEAEEA-REEVAELNSKLAELKERIESLERIRTLLAAIADAEDEIERLREKREAlAELNDER 625
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 453 FEGLDSstassmeleelrherelQKEEIQKLMGQ-----IHQLRSELQDMEA--QQVSEA-ESAREQLQDLQDQIAKQRA 524
Cdd:PRK02224 626 RERLAE-----------------KRERKRELEAEfdearIEEAREDKERAEEylEQVEEKlDELREERDDLQAEIGAVEN 688
|
330 340 350
....*....|....*....|....*....|....
gi 1939872721 525 SKQELETELDRMKQEFHYVE--EDLHRTKNTLQS 556
Cdd:PRK02224 689 ELEELEELRERREALENRVEalEALYDEAEELES 722
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
280-624 |
8.38e-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: 39.82 E-value: 8.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 280 ELRAQVDDLTeAVAAKDSQLAVLKVRLQEADQVLSSRTEALEALQSEK----------SRIMQDHNEGSSLQNQALQTLQ 349
Cdd:pfam12128 448 ELKLRLNQAT-ATPELLLQLENFDERIERAREEQEAANAEVERLQSELrqarkrrdqaSEALRQASRRLEERQSALDELE 526
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 350 ERLHEADATL-------------------KREQ------------ESYKQMQSEFATRLNKMEVE-------RQNLAEAV 391
Cdd:pfam12128 527 LQLFPQAGTLlhflrkeapdweqsigkviSPELlhrtdldpevwdGSVGGELNLYGVKLDLKRIDvpewaasEEELRERL 606
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 392 TLAERKYSEERKKVDDLQQQVKLHRSSLESAKQELVDYKQKatrILQSKEKLINSLKEGSSFE-GLDSSTASsmeleelr 470
Cdd:pfam12128 607 DKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTA---LKNARLDLRRLFDEKQSEKdKKNKALAE-------- 675
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 471 hERELQKEEIQKLMGQIHQLRSELQDMEAQQVSEAESAREQLQ--------DLQDQIAKQRASKQELETELDRmkqEFHY 542
Cdd:pfam12128 676 -RKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQaywqvvegALDAQLALLKAAIAARRSGAKA---ELKA 751
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 543 VEEDLHRTKNTL---QSRIKDREEEIQKLRNQLTNktLSNSSQSELESRLHQLTETLIQKQTLLESLSTEKNSlvfqLER 619
Cdd:pfam12128 752 LETWYKRDLASLgvdPDVIAKLKREIRTLERKIER--IAVRRQEVLRYFDWYQETWLQRRPRLATQLSNIERA----ISE 825
|
....*
gi 1939872721 620 LEQQL 624
Cdd:pfam12128 826 LQQQL 830
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
230-507 |
8.90e-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: 39.72 E-value: 8.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 230 QLLRNEVQSLNQ-------EMASLLQRSKETQEELNKARVRVEKWNVDNSKSDRITRELRAQVDDL----TEAVAAKDSQ 298
Cdd:pfam15921 565 EILRQQIENMTQlvgqhgrTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLelekVKLVNAGSER 644
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 299 LAVLKVRLQEADQVLS------------------------SRTEALEA--------LQSEKSRIMQDHN-----EGSS-- 339
Cdd:pfam15921 645 LRAVKDIKQERDQLLNevktsrnelnslsedyevlkrnfrNKSEEMETttnklkmqLKSAQSELEQTRNtlksmEGSDgh 724
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 340 -------LQNQ---------ALQTLQERLHEADATLKREQESYKQMQSEFATRLNKMEVERQNLAEAVTLAERKYSEERK 403
Cdd:pfam15921 725 amkvamgMQKQitakrgqidALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKE 804
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939872721 404 KVDDLqqQVKLHRSSLESA-------KQELVDYKQKATRILQSKE--------------KLINSLKEGSSFEGLDSSTAS 462
Cdd:pfam15921 805 KVANM--EVALDKASLQFAecqdiiqRQEQESVRLKLQHTLDVKElqgpgytsnssmkpRLLQPASFTRTHSNVPSSQST 882
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1939872721 463 SMELEELRHERELQKEEIQKLMGQIHQ-LRSELQDMEAQQVSEAES 507
Cdd:pfam15921 883 ASFLSHHSRKTNALKEDPTRDLKQLLQeLRSVINEEPTVQLSKAED 928
|
|
| |
