|
Name |
Accession |
Description |
Interval |
E-value |
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
6-628 |
0e+00 |
|
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in eukaryotes. CCCAP is also known as SDCCAG8, serologically defined colon cancer antigen 8. It is associated with the centrosome.
Pssm-ID: 435040 [Multi-domain] Cd Length: 703 Bit Score: 769.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672617 6 GNSTLEDSLGQYQRSLRERANRSIHQLKCALREVDATIEEDALDPSTSINVENVDTGVAWHELQHSHAVNQLKALLRQQT 85
Cdd:pfam15964 1 GNSTLEESLGQYQRSLRERANRSIHQLKCALHESDSTISEDEQEESLSSVVQNEDSGSPWSELQHSHAVNQLKALLQQQT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672617 86 STENETSPRRRKLSPSRPSDCEDGSLPTMHNLVPIINDQSQYIHHLEAEVKFCKDELSSMKNRVQVVVLENERLQQELKS 165
Cdd:pfam15964 81 KKENELSPRRRKLSPSRTSEDESSSLPTVHDLVPIINDQSQYIHHLEAEVKFCKEELSEMKQRVQVVVLENEKLQQELKS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672617 166 QRQEETLREQTLLDMSGNVQNSWMkTREDSRVIETTKRPFSHGDAETGKAASTGDADKWRLELERLKLTYEAKTDLLESQ 245
Cdd:pfam15964 161 QTQEETLREQTLLDSSGNMQNSWC-TPEDSRVHQTSKRPASHNLAERLKSATTGEDEKWRLELEKLKLLYEAKTEVLESQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672617 246 LKLLRKDLVEYQKTCEDLKERLKHKESLVTASASSRVGGLCLKCAQHEAVLSQTHNNVHIQTIETLTKERDDLMSVLVSV 325
Cdd:pfam15964 240 VKSLRKDLAESQKTCEDLKERLKHKESLVAASTSSRVGGLCLKCAQHEAVLAQTHTNVHMQTIERLTKERDDLMSALVSV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672617 326 RSSLAEAQERETSAYKQVKHAVQMTEEANFEKTKALIQCEQLRSELERQTDRLEKELASQQEKRALEKEMIKKEVTRERE 405
Cdd:pfam15964 320 RSSLAEAQQRESSAYEQVKQAVQMTEEANFEKTKALIQCEQLKSELERQKERLEKELASQQEKRAQEKEALRKEMKKERE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672617 406 EAEAKMLILSQNIAKLEAEIEKITREKTSAVSQLEEVQNQLASQEMDVTKVCGEMRFQLNKTKMEKDEAEKEHKEYKAKS 485
Cdd:pfam15964 400 ELGATMLALSQNVAQLEAQVEKVTREKNSLVSQLEEAQKQLASQEMDVTKVCGEMRYQLNQTKMKKDEAEKEHREYRTKT 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672617 486 QKDLEMKDQEIEKLRLELSESTQQVEQEQQKAARARQECLQVTELLGESERQLHLT------------------------ 541
Cdd:pfam15964 480 GRQLEIKDQEIEKLGLELSESKQRLEQAQQDAARAREECLKLTELLGESEHQLHLTrlekesiqqsfsneakaqalqaqq 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672617 542 -------------------------------------------------------RSEIVQLSQEKRYLCDKLEKLQKRN 566
Cdd:pfam15964 560 reqeltqkmqqmeaqhdktvneqyslltsqntfiaklkeecctlakkleeitqksRSEVEQLSQEKEYLQDRLEKLQKRN 639
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958672617 567 DELEDQCVQHGRVHETMKERLRQLDKHGQATAQQLVQLLNKQNQLLLERQNLSEEVDQLRAQ 628
Cdd:pfam15964 640 EELEEQCVQHGRMHERMKQRLRQLDKHCQATAQQLVQLLSKQNQLFKERQNLTEEVQSLRSQ 701
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
308-590 |
1.77e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 70.86 E-value: 1.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672617 308 IETLTKERDDLMSVLVSVRSSLAEAQERETSAYKQVKHAVQMTEEANFEKTKALIQCEQLRSELERQTDRLEkelasQQE 387
Cdd:TIGR02168 679 IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIA-----QLS 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672617 388 KRALEKEMIKKEVTREREEAEAKMLILSQNIAKLEAEIEKITREKTSAVSQLEEVQNQLasqemdvtkvcgemrFQLNKT 467
Cdd:TIGR02168 754 KELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAEL---------------TLLNEE 818
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672617 468 KMEKDEAEKEHKEYKAKSQKDLEMKDQEIEKLRLELSESTQQVEQEQQKAARARQECLQVTELLGESERQLHLTRSEIVQ 547
Cdd:TIGR02168 819 AANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEE 898
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1958672617 548 LSQEKRYLCDKLEKLQKRNDELEDQCVQHGRVHETMKERLRQL 590
Cdd:TIGR02168 899 LSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNL 941
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
367-631 |
9.31e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 68.42 E-value: 9.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672617 367 LRSELERQTDRLEKE-------LASQQEKRALEKEMI----------KKEVTREREEAEAKMLILSQNIAKLEAEIEKIT 429
Cdd:COG1196 194 ILGELERQLEPLERQaekaeryRELKEELKELEAELLllklreleaeLEELEAELEELEAELEELEAELAELEAELEELR 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672617 430 REKTSAVSQLEEVQNQLASQEMDVTKVCGEMRFQLNKTKMEKDEAEKEHKEyKAKSQKDLEMKDQEIEKLRLELSESTQQ 509
Cdd:COG1196 274 LELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEE-LAELEEELEELEEELEELEEELEEAEEE 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672617 510 VEQEQQKAARARQECLQVTELLGESERQLHLTRSEIVQLSQEKRYLCDKLEKLQKRNDELEDQcvqhgrvHETMKERLRQ 589
Cdd:COG1196 353 LEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLER-------LERLEEELEE 425
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1958672617 590 LDKHGQATAQQLVQLLNKQNQLLLERQNLSEEVDQLRAQRRE 631
Cdd:COG1196 426 LEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAE 467
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
400-631 |
4.27e-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: 4.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672617 400 VTREREEAEAKMLILSQNIAKLEAEIEKIT---REKTSAVSQLEEVQNQLASQEMDVTKVCGEMRFQLNKTKMEKDEAEK 476
Cdd:TIGR02168 661 ITGGSAKTNSSILERRREIEELEEKIEELEekiAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEA 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672617 477 EHkeykAKSQKDLEMKDQEIEKLRLELSESTQQVEQEQQKAARARQECLQVTELLGESERQLHLTRSEIVQLSQEKRYLC 556
Cdd:TIGR02168 741 EV----EQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLN 816
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958672617 557 DKLEKLQKRNDELEDQCVQHGRVHETMKERLRQLDKHGQATAQQLVQLLNKQNQLLLERQNLSEEVDQLRAQRRE 631
Cdd:TIGR02168 817 EEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALAL 891
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
329-572 |
1.07e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 64.96 E-value: 1.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672617 329 LAEAQERETSAYKQVKHAVQMTEEANFEKTKALIQCEQLRSELERQTDRLEkelASQQEKRALEKEMIKKEVTREREEAE 408
Cdd:COG1196 234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELE---EAQAEEYELLAELARLEQDIARLEER 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672617 409 AKMLilSQNIAKLEAEIEKITREKTSAVSQLEEVQNQLASQEMDVTKVcGEMRFQLNKTKMEKDEAEKEHKEYKAKSQKD 488
Cdd:COG1196 311 RREL--EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEA-EAELAEAEEALLEAEAELAEAEEELEELAEE 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672617 489 LEMKDQEIEKLRLELSESTQQVEQEQQKAARARQECLQVTELLGESERQLHLTRSEIVQLSQEKRYLCDKLEKLQKRNDE 568
Cdd:COG1196 388 LLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAE 467
|
....
gi 1958672617 569 LEDQ 572
Cdd:COG1196 468 LLEE 471
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
356-630 |
1.39e-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: 64.70 E-value: 1.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672617 356 EKTKALIQCEQLRSELERQTDRLEK--ELASQQEKRALEKEMIKKEVTRE-REEAEAKMLILSQNIAKLEAEIEKITREK 432
Cdd:TIGR02169 231 EKEALERQKEAIERQLASLEEELEKltEEISELEKRLEEIEQLLEELNKKiKDLGEEEQLRVKEKIGELEAEIASLERSI 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672617 433 TSAVSQLEEVQNQLASQEMdvtkvcgemrfQLNKTKMEKDEAEKEHKEYkaksQKDLEMKDQEIEKLRLELSESTQQVEQ 512
Cdd:TIGR02169 311 AEKERELEDAEERLAKLEA-----------EIDKLLAEIEELEREIEEE----RKRRDKLTEEYAELKEELEDLRAELEE 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672617 513 EQQKAARARQECLQ-------VTELLGESERQLHLTRSEIVQLSQEKRYLCDKLEKLQKRNDELEDQCVQHGRVHETMKE 585
Cdd:TIGR02169 376 VDKEFAETRDELKDyreklekLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEW 455
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1958672617 586 RLRQLDKHGQATAQQLVQLLNKQNQLLLERQNLSEEVDQLRAQRR 630
Cdd:TIGR02169 456 KLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQAR 500
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
355-628 |
2.45e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 63.92 E-value: 2.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672617 355 FEKTKALIQCEQLRSELERQTDRLEKELASQQEKRALEKEMIKKEVTRErEEAEAKMLILSQNIAKLEAEIEKITREKTS 434
Cdd:TIGR02168 673 LERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKEL-EELSRQISALRKDLARLEAEVEQLEERIAQ 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672617 435 AVSQLEEVQNQLASQEMDVTkvcgemrfqlnktkmEKDEAEKEHKEYKAKSQKDLEMKDQEIEKLRLELSESTQQVEQEQ 514
Cdd:TIGR02168 752 LSKELTELEAEIEELEERLE---------------EAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLN 816
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672617 515 QKAARARQECLQVTELLGESERQLHLTRSEIVQLSQEKRYLCDKLEKLQKRNDELEDQCVQHGRVHETMKERLRQLDKHG 594
Cdd:TIGR02168 817 EEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSEL 896
|
250 260 270
....*....|....*....|....*....|....
gi 1958672617 595 QATAQQLVQLLNKQNQLLLERQNLSEEVDQLRAQ 628
Cdd:TIGR02168 897 EELSEELRELESKRSELRRELEELREKLAQLELR 930
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
242-551 |
4.75e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 62.65 E-value: 4.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672617 242 LESQLKLLRKD---LVEYQKtcedLKERLKHKESLVTASAssrvgglcLKCAQHEAVLSQTHNNVHIQTIETLTKERDDL 318
Cdd:COG1196 198 LERQLEPLERQaekAERYRE----LKEELKELEAELLLLK--------LRELEAELEELEAELEELEAELEELEAELAEL 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672617 319 MSVLVSVRSSLAEAQERETSAykQVKHAVQMTEEANFEKTKALIQceQLRSELERQTDRLEKELASQQEKRALEKEMIkK 398
Cdd:COG1196 266 EAELEELRLELEELELELEEA--QAEEYELLAELARLEQDIARLE--ERRRELEERLEELEEELAELEEELEELEEEL-E 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672617 399 EVTREREEAEAKMLILSQNIAKLEAEIEKITREKTSAVSQLEEVQNQLASQEMDvtkvcgemRFQLNKTKMEKDEAEKEH 478
Cdd:COG1196 341 ELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRA--------AAELAAQLEELEEAEEAL 412
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958672617 479 KEYKAKSQKDLEMKDQEIEKLRLELSESTQQVEQEQQKAARARQECLQVTELLGESERQLHLTRSEIVQLSQE 551
Cdd:COG1196 413 LERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEE 485
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
369-631 |
1.45e-09 |
|
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: 61.24 E-value: 1.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672617 369 SELERQTDRLEKELASQQEKRALEKEMIKKEVT---REREEAEAKMLILSQNIAKLEAEIEKITREKTSAVSQLEEVQNQ 445
Cdd:TIGR02169 194 DEKRQQLERLRREREKAERYQALLKEKREYEGYellKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQL 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672617 446 LASQEMDVTKVCGEMRFQLnKTKMEKDEAEKEHKEYK-AKSQKDLEMKDQEIEKLRLELSESTQQVEQEQQKAARARQEC 524
Cdd:TIGR02169 274 LEELNKKIKDLGEEEQLRV-KEKIGELEAEIASLERSiAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRR 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672617 525 LQVTELLGESERQLHLTRSEIVQLSQEKRYLCDKLEKLQKRNDELEDQCVQHGRVHETMKERLRQLDKHGQATAQQLVQL 604
Cdd:TIGR02169 353 DKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGI 432
|
250 260
....*....|....*....|....*..
gi 1958672617 605 LNKQNQLLLERQNLSEEVDQLRAQRRE 631
Cdd:TIGR02169 433 EAKINELEEEKEDKALEIKKQEWKLEQ 459
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
227-518 |
1.58e-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: 58.14 E-value: 1.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672617 227 ELERLKLTYEAKTDLLESQLKLLRKDLVEYQKTCEDLKERLKHKESLVTASASSRVgglclkcaqheavlsqthnnVHIQ 306
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLA--------------------RLEA 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672617 307 TIETLTKERDDLMSVLVSVRSSLAEAQERETSAYKQVKHAVQMTEEANFEKTKALIQCEQLRS---ELERQTDRLEKELA 383
Cdd:TIGR02168 741 EVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREaldELRAELTLLNEEAA 820
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672617 384 SQQEKRA-LEKEMIKKEVTREREEAEAKmlILSQNIAKLEAEIEKITREKTSAVSQLEEVQNQLASQEmdvtkvcgEMRF 462
Cdd:TIGR02168 821 NLRERLEsLERRIAATERRLEDLEEQIE--ELSEDIESLAAEIEELEELIEELESELEALLNERASLE--------EALA 890
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958672617 463 QLNKTKMEKDEAEKEHKEYKAKSQKDLEMKDQEIEKLRLELSESTQQVEQEQQKAA 518
Cdd:TIGR02168 891 LLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLS 946
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
328-601 |
2.41e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 57.37 E-value: 2.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672617 328 SLAEAQERETSAYKQVKHAVQMTEEANFEKTKALIQCEQLRS---ELERQTDRLEKEL-ASQQEKRALEKEmiKKEVTRE 403
Cdd:TIGR02168 233 RLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLevsELEEEIEELQKELyALANEISRLEQQ--KQILRER 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672617 404 REEAEAKMLILSQNIAKLEAEIEKITREKTSAVSQLEEVQNQLASQEMDVTKVCGEMRFQLNKTKMEKDEAEKEHKEY-K 482
Cdd:TIGR02168 311 LANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVaQ 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672617 483 AKSQKDLEMKDQEIEKLRLELSESTQQVEQEQQKAARARQECLQVTEL---LGESERQLHLTRSEIVQLSQEKRYLCDKL 559
Cdd:TIGR02168 391 LELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELqaeLEELEEELEELQEELERLEEALEELREEL 470
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1958672617 560 EKLQKRNDELEDQCVQHGRVHETMKERLRQLDKHGQATAQQL 601
Cdd:TIGR02168 471 EEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALL 512
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
366-565 |
4.03e-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: 55.93 E-value: 4.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672617 366 QLRSELERQTDRLEKELASQQEKRALEKEMiKKEVTREREEAEAKMLILSQNIAKLEAEIEKITREKTSAVSQLEEVQNQ 445
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKE-EKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672617 446 LASQEMDVTKV---------CGEMRFQLNKTKMEKD-----------EAEKEHKEYKAKSQKDLEMKDQEIEKLRLELSE 505
Cdd:COG4942 99 LEAQKEELAELlralyrlgrQPPLALLLSPEDFLDAvrrlqylkylaPARREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672617 506 STQQVEQEQQKAARARQEclqVTELLGESERQLHLTRSEIVQLSQEKRYLCDKLEKLQKR 565
Cdd:COG4942 179 LLAELEEERAALEALKAE---RQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
366-628 |
7.13e-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: 7.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672617 366 QLRSeLERQTDRLEKELASQQEKRALEKEMIKKEVTREREEAEA----------KMLILSQNIAKLEAEIEKITREKTSA 435
Cdd:TIGR02168 201 QLKS-LERQAEKAERYKELKAELRELELALLVLRLEELREELEElqeelkeaeeELEELTAELQELEEKLEELRLEVSEL 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672617 436 VSQLEEVQNQLASQEMDVTKVCGEMRFQLNK------------TKMEKDEAEKEHKEYK-AKSQKDLEMKDQEIEKLRLE 502
Cdd:TIGR02168 280 EEEIEELQKELYALANEISRLEQQKQILRERlanlerqleeleAQLEELESKLDELAEElAELEEKLEELKEELESLEAE 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672617 503 LSESTQQVEQEQQKAARARQECLQVTELLGESERQLHLTRSEIVQLSQEKRYLCDKLEKLQKRNDELEDQCVQH-----G 577
Cdd:TIGR02168 360 LEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAelkelQ 439
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1958672617 578 RVHETMKERLRQLDKHGQATAQQLVQLLNKQNQLLLERQNLSEEVDQLRAQ 628
Cdd:TIGR02168 440 AELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQAR 490
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
397-628 |
9.99e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 51.98 E-value: 9.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672617 397 KKEVTREREEAEAKMLILSQNIAKLEAEIEKITREKTSAV------SQLEEVQNQLASQEMDvtkvcgEMRFQLNKTKME 470
Cdd:TIGR02168 174 RKETERKLERTRENLDRLEDILNELERQLKSLERQAEKAErykelkAELRELELALLVLRLE------ELREELEELQEE 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672617 471 KDEAEKEHKEYKAKsqkdLEMKDQEIEKLRLELSESTQQVEQEQQkaararqECLQVTELLGESERQLHLTRSEIVQLSQ 550
Cdd:TIGR02168 248 LKEAEEELEELTAE----LQELEEKLEELRLEVSELEEEIEELQK-------ELYALANEISRLEQQKQILRERLANLER 316
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958672617 551 EKRYLCDKLEKLQKRNDELEDQCVQHGRVHETMKERLRQLDKHGQATAQQLVQLLNKQNQLLLERQNLSEEVDQLRAQ 628
Cdd:TIGR02168 317 QLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQ 394
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
294-550 |
3.41e-06 |
|
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: 50.22 E-value: 3.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672617 294 AVLSQTHNNVHIQTIETLTKERddlmsvLVSVRSSLAEAQERETSAYKQVKhavQMTEEANFEKTKALIQCEQLRSELER 373
Cdd:pfam12128 256 AELRLSHLHFGYKSDETLIASR------QEERQETSAELNQLLRTLDDQWK---EKRDELNGELSAADAAVAKDRSELEA 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672617 374 QTDRLEKELASQQEKRALEKEMIKkEVTREREEAEAKMLILSQNIAKLEAEIE------------KITREKTSAVSQLEE 441
Cdd:pfam12128 327 LEDQHGAFLDADIETAAADQEQLP-SWQSELENLEERLKALTGKHQDVTAKYNrrrskikeqnnrDIAGIKDKLAKIREA 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672617 442 VQNQLASQEMDVTKVCGEMRFQLNKTKMEKDEAEKEHKE-------------YKAKSQKDLEMKDQEIEKLRLELSESTQ 508
Cdd:pfam12128 406 RDRQLAVAEDDLQALESELREQLEAGKLEFNEEEYRLKSrlgelklrlnqatATPELLLQLENFDERIERAREEQEAANA 485
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1958672617 509 QVEQEQQKAARARQECLQVTELLGESERQLHLTRSEIVQLSQ 550
Cdd:pfam12128 486 EVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELEL 527
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
403-628 |
5.80e-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: 5.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672617 403 EREEAEAKMLILSQNIAKLEAEIEKITREKTSAVSQLEEVQNQLASQEMdvtkvcgemrfQLNKTKMEKDEAEKEHKEyk 482
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALAR-----------RIRALEQELAALEAELAE-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672617 483 akSQKDLEMKDQEIEKLRLELSEstqQVEQEQQKAARARQECLQVTELLGESERQLHLTRSEIVQLSQEKRYLCDKLEKL 562
Cdd:COG4942 88 --LEKEIAELRAELEAQKEELAE---LLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAEL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958672617 563 QKRNDELEDQCVQHGRVHETMKERLRQLDKHGQATAQQLVQLLNKQNQLLLERQNLSEEVDQLRAQ 628
Cdd:COG4942 163 AALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEAL 228
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
363-565 |
1.74e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.99 E-value: 1.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672617 363 QCEQLRsELERQTDRLEKELASQQEKRALEKEMIKKEVTREREEAEAKMLILSQNIAKLEAEIEKITREKTSAVSQLEEV 442
Cdd:COG4913 250 QIELLE-PIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDEL 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672617 443 QNQLASQEMDvtkvcgemrfQLNKTKMEKDEAEKEHKEYKAKSQKDlemkDQEIEKLRLELSESTQQVEQEQQKAARARQ 522
Cdd:COG4913 329 EAQIRGNGGD----------RLEQLEREIERLERELEERERRRARL----EALLAALGLPLPASAEEFAALRAEAAALLE 394
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1958672617 523 eclQVTELLGESERQLHLTRSEIVQLSQEKRYLCDKLEKLQKR 565
Cdd:COG4913 395 ---ALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
225-572 |
3.77e-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: 47.04 E-value: 3.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672617 225 RLELERLKLTYEAKTDLLESQLKLLRKDLVEYQKTCEDLKER---LKHKESLVTASASSRVGGLCLKCAQHEAVLSQTHN 301
Cdd:pfam15921 330 RSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQEsgnLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTG 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672617 302 NVhiQTIETLTKERDD-------LMSVLVSVRSSLAEAQERETSAYKQVKHAVQMTEE--ANFEKTKALIQ--CEQLRSE 370
Cdd:pfam15921 410 NS--ITIDHLRRELDDrnmevqrLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSltAQLESTKEMLRkvVEELTAK 487
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672617 371 ---LERQTDRLEKELASQQEK-RALEKemIKKEVTREREEAEAKMlilsQNIAKLEAEIEKITREKTSA------VSQLE 440
Cdd:pfam15921 488 kmtLESSERTVSDLTASLQEKeRAIEA--TNAEITKLRSRVDLKL----QELQHLKNEGDHLRNVQTECealklqMAEKD 561
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672617 441 EVQNQLASQEMDVTKVCGEMRFQLNKTKMEKDEAEKEHKEYKAKSQKDLEMKDQEIEKLRlELSESTQQVEQEQQKAARA 520
Cdd:pfam15921 562 KVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIR-ELEARVSDLELEKVKLVNA 640
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672617 521 RQECLQVTELLGESERQL----HLTRSEIVQLSQE----KRYLCDKLEKLQKRNDELEDQ 572
Cdd:pfam15921 641 GSERLRAVKDIKQERDQLlnevKTSRNELNSLSEDyevlKRNFRNKSEEMETTTNKLKMQ 700
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
370-592 |
6.43e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 45.78 E-value: 6.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672617 370 ELERQTDRLEKELASQQEKRALEKEMIkkevtrerEEAEAKMlilSQNIAKLEAEIEKITREKTSAVSQLEEVQNQLASQ 449
Cdd:PHA02562 178 ELNQQIQTLDMKIDHIQQQIKTYNKNI--------EEQRKKN---GENIARKQNKYDELVEEAKTIKAEIEELTDELLNL 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672617 450 EM---DVTKVCGEMRFQLNKTKMEKDEAEKEHKEYKAKS-----QKDLEMKDQEIEKLRLELSESTQQVEQEQQkaarAR 521
Cdd:PHA02562 247 VMdieDPSAALNKLNTAAAKIKSKIEQFQKVIKMYEKGGvcptcTQQISEGPDRITKIKDKLKELQHSLEKLDT----AI 322
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958672617 522 QECLQVTELLGESERQLHLTRSEIVQLSQEKRYLCDKLEKLQKRNDELEDQCVQHGRVHETMKERLRQLDK 592
Cdd:PHA02562 323 DELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVK 393
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
489-628 |
8.30e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.06 E-value: 8.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672617 489 LEMKDQEIEKLRLELSESTQQVE--QEQQKAARARQECLQVTELLGESERQLHLTRSEIVQLSQEkrylcdkLEKLQKRN 566
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEalEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAE-------LERLDASS 684
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958672617 567 DELEdqcvqhgrvheTMKERLRQLDKHGQATAQQLVQLLNKQNQLLLERQNLSEEVDQLRAQ 628
Cdd:COG4913 685 DDLA-----------ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDR 735
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
124-490 |
1.20e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 45.43 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672617 124 QSQYIHHLEAEVKFCKDELSSMKNRVQVVVLENERLQQELKSQRQEETLREQTLLDMSGNVQNSWMKTREDSRVIETTKR 203
Cdd:TIGR02168 675 RRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSK 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672617 204 PFSHGDAE-TGKAASTGDADKWRLELERLKLTYEAKTDLLESQLKLLRKDLVEYQKTCEDLKERLkhkeslvtASASSRV 282
Cdd:TIGR02168 755 ELTELEAEiEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEA--------ANLRERL 826
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672617 283 GGLclkcaQHEAVLSQTHNNVHIQTIETLTKERDDLMSVLVSVRSSLAEAQERETSAYKQVKHAVQMTEEANFEKTKA-- 360
Cdd:TIGR02168 827 ESL-----ERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELse 901
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672617 361 -LIQCEQLRSELERQTDRLEKELASQQEKRALEKEMIKKEVTREREEAEAKMLILSQNIAKLEAEIEKITREKTSAVSQL 439
Cdd:TIGR02168 902 eLRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKI 981
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1958672617 440 EEVQNqlasqemdvtkvcgemrfqLNKTKMEKDEAEKEHKEYKAKSQKDLE 490
Cdd:TIGR02168 982 KELGP-------------------VNLAAIEEYEELKERYDFLTAQKEDLT 1013
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
322-480 |
2.96e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.61 E-value: 2.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672617 322 LVSVRSSLAEAQERETSAYKQVKHAvqmTEEANFEKTKALIQC----EQLRSELERQTDRLEKELAsQQEKRALEKEMI- 396
Cdd:PRK12704 23 FVRKKIAEAKIKEAEEEAKRILEEA---KKEAEAIKKEALLEAkeeiHKLRNEFEKELRERRNELQ-KLEKRLLQKEENl 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672617 397 ---KKEVTREREEAEAKMLILSQNIAKLEAEIEKITREKTSAVSQLEEVQNQLASQ--EMDVTKVCGEMRFQ----LNKT 467
Cdd:PRK12704 99 drkLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAEEakEILLEKVEEEARHEaavlIKEI 178
|
170
....*....|....
gi 1958672617 468 KME-KDEAEKEHKE 480
Cdd:PRK12704 179 EEEaKEEADKKAKE 192
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
399-580 |
2.96e-04 |
|
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: 43.21 E-value: 2.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672617 399 EVTREREEAEAKMLILSQNIAKLEAEIEKITREKTSAVSQLEEVQNQLASQEMDVTKVCGEMRFQLNKTKMEKDEAEKEH 478
Cdd:pfam09787 51 ELRQERDLLREEIQKLRGQIQQLRTELQELEAQQQEEAESSREQLQELEEQLATERSARREAEAELERLQEELRYLEEEL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672617 479 KEYKAKSQKDLEMKDQEIEKLRLELSESTQQVEQEQQKAARARqeclQVTELLGESERQLHltrseivQLSQEKRYLCDK 558
Cdd:pfam09787 131 RRSKATLQSRIKDREAEIEKLRNQLTSKSQSSSSQSELENRLH----QLTETLIQKQTMLE-------ALSTEKNSLVLQ 199
|
170 180
....*....|....*....|..
gi 1958672617 559 LEKLQKRNDELEDQCVQHGRVH 580
Cdd:pfam09787 200 LERMEQQIKELQGEGSNGTSIN 221
|
|
| PRK00247 |
PRK00247 |
putative inner membrane protein translocase component YidC; Validated |
383-521 |
9.43e-04 |
|
putative inner membrane protein translocase component YidC; Validated
Pssm-ID: 178945 [Multi-domain] Cd Length: 429 Bit Score: 42.15 E-value: 9.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672617 383 ASQQEKRAL--EKEMIKKEVTREREEAEAKMLILSQNIAKLEAEIEKITREKTSAVSQLEEVQNQLASQEMDVTKVCGEM 460
Cdd:PRK00247 285 EHHAEQRAQyrEKQKEKKAFLWTLRRNRLRMIITPWRAPELHAENAEIKKTRTAEKNEAKARKKEIAQKRRAAEREINRE 364
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958672617 461 RFQLNKTKMEKDEAEKEHKEYKAKSQKDLEMKDQEIEKLRLELSESTQQVEQEQQKAARAR 521
Cdd:PRK00247 365 ARQERAAAMARARARRAAVKAKKKGLIDASPNEDTPSENEESKGSPPQVEATTTAEPNREP 425
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
329-568 |
9.88e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.44 E-value: 9.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672617 329 LAEAQE-RETSAYKQVKHAVQMTEEANFEKTKALI--QCEQLRSELERQTDRLEKELASQQEKRAlEKEMIKKEVTRERE 405
Cdd:PTZ00121 1551 LKKAEElKKAEEKKKAEEAKKAEEDKNMALRKAEEakKAEEARIEEVMKLYEEEKKMKAEEAKKA-EEAKIKAEELKKAE 1629
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672617 406 EAEAKMLILSQNIA---------KLEAEIEKITREKTSAVSQLEEVQNQLASQEMDVTKVCGEmrfQLNKTKMEKDEAEK 476
Cdd:PTZ00121 1630 EEKKKVEQLKKKEAeekkkaeelKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAE---ALKKEAEEAKKAEE 1706
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672617 477 EHKEYKAKSQKDLEMKDQEiEKLRLELSESTQQVEQEQQKAARARQEclqvtelLGESERQLHLTRSEIVQLSQEKRYLC 556
Cdd:PTZ00121 1707 LKKKEAEEKKKAEELKKAE-EENKIKAEEAKKEAEEDKKKAEEAKKD-------EEEKKKIAHLKKEEEKKAEEIRKEKE 1778
|
250
....*....|..
gi 1958672617 557 DKLEKLQKRNDE 568
Cdd:PTZ00121 1779 AVIEEELDEEDE 1790
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
473-630 |
1.17e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.21 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672617 473 EAEKEHKEYKAKSQkDLEMKDQEIEKLRLELSEstQQVEQEQQKAARARQECLQVTELLGESERQLHLTRSEIVQLSQEK 552
Cdd:COG4913 256 PIRELAERYAAARE-RLAELEYLRAALRLWFAQ--RRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQI 332
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958672617 553 RYLC-DKLEKLQKRNDELEDQCVQHGRVHETMKERLRQLDKHGQATAQQLVQLLNKQNQLLLERQNLSEEVDQLRAQRR 630
Cdd:COG4913 333 RGNGgDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAE 411
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
225-450 |
1.32e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 41.97 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672617 225 RLELERLKLTYEAKTDLLESQLKLLRKDLVEYQKTCEDLKERLKHKE---------------SLVTASASSRVGGLCLKC 289
Cdd:TIGR02168 255 LEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEqqkqilrerlanlerQLEELEAQLEELESKLDE 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672617 290 AQHEAVLSQTHNNVHIQTIETLTKERDDLMSVLVSVRSSLAEAQERETSAYKQVKHAVQMTEEANFEKTKALIQCEQLRS 369
Cdd:TIGR02168 335 LAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLED 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672617 370 ELERQTDRLEKELASQQEKRALEKEMIKKEVTREREEAEAKMLILSQNIAKLEAEIEKITREKTSAVSQLEEVQNQLASQ 449
Cdd:TIGR02168 415 RRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSL 494
|
.
gi 1958672617 450 E 450
Cdd:TIGR02168 495 E 495
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
236-573 |
1.32e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.95 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672617 236 EAKTDLLESQLKLLRKDLVEYQKTCEDLKERLKHKESLVTAsassrvgGLCLKCAQheavlsQTHNNVHIQTIETLTKER 315
Cdd:PRK02224 411 EDFLEELREERDELREREAELEATLRTARERVEEAEALLEA-------GKCPECGQ------PVEGSPHVETIEEDRERV 477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672617 316 DDLMSVLVSVRSSLAEAQERETSAYKQVKHAVQMTEEAnfEKTKALIQ-CEQLRSELERQTDRLEkELASQQEKRALEKE 394
Cdd:PRK02224 478 EELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLE--ERREDLEElIAERRETIEEKRERAE-ELRERAAELEAEAE 554
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672617 395 MIKKEVTREREEAEAKMlilsQNIAKLEAEIEKITrektSAVSQLEEVQNQLASQEMdvtkvCGEMRFQLNKTKMEKDEA 474
Cdd:PRK02224 555 EKREAAAEAEEEAEEAR----EEVAELNSKLAELK----ERIESLERIRTLLAAIAD-----AEDEIERLREKREALAEL 621
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672617 475 EKEHKEYkaksqkdLEMKDQEIEKLRLELSEStqQVEQEQQKAARARQECLQVTELLGESERQLHLTRSEIVQLSQEkry 554
Cdd:PRK02224 622 NDERRER-------LAEKRERKRELEAEFDEA--RIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENE--- 689
|
330
....*....|....*....
gi 1958672617 555 lCDKLEKLQKRNDELEDQC 573
Cdd:PRK02224 690 -LEELEELRERREALENRV 707
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
482-631 |
1.42e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 41.29 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672617 482 KAKSQKDLEMKDQEIEKLRLELSESTQQVEQEQQKAARARQECLQVTELLGESERQLHLTRSEIVQLSQEKRYLCDKLEK 561
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672617 562 LQK-------------RNDELE-----DQCVQHGRVHETMKERLRQLDKHGQATAQQLVQLLNKQNQLLLERQNLSEEVD 623
Cdd:COG4942 102 QKEelaellralyrlgRQPPLAlllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLA 181
|
....*...
gi 1958672617 624 QLRAQRRE 631
Cdd:COG4942 182 ELEEERAA 189
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
306-564 |
1.81e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 41.54 E-value: 1.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672617 306 QTIETLTKERDDLMSVLVSVRSSLAEAQ------ERETSAYKQ-----------VKHAVQMTEEANFEKTKALIQCEQLR 368
Cdd:TIGR04523 342 EQISQLKKELTNSESENSEKQRELEEKQneieklKKENQSYKQeiknlesqindLESKIQNQEKLNQQKDEQIKKLQQEK 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672617 369 SELERQTDRLEKELASQQ------EKRALEKEMIKKEVTREREEAEAKMLILSQNIAKLEAEIEKITRE---KTSAVSQL 439
Cdd:TIGR04523 422 ELLEKEIERLKETIIKNNseikdlTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKElksKEKELKKL 501
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672617 440 EEVQNQLASQEMDVTKVCGEMRFQLNKTKMEKDEAEKEHKEYKAKSQKD------------LEMKDQEIEKLRLELSEST 507
Cdd:TIGR04523 502 NEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDdfelkkenlekeIDEKNKEIEELKQTQKSLK 581
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958672617 508 QQVEQEQQKAARARQECLQV-------TELLGESERQLHLTRSEIVQLSQEKRYLCDKLEKLQK 564
Cdd:TIGR04523 582 KKQEEKQELIDQKEKEKKDLikeieekEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQ 645
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
228-454 |
1.82e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.54 E-value: 1.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672617 228 LERLKLTYEAKTDLLESQLKLLRKDLVEYQKTCEDLKErlkhkeslvtasassrvgglclkcaQHEAVLSQTHNNVHIQT 307
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQ-------------------------KNGLVDLSEEAKLLLQQ 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672617 308 IETLTKErddlmsvLVSVRSSLAEAQERETSAYKQVKHAVQMTEEANfeKTKALIQCEQLRSELERQTDRLEK------- 380
Cdd:COG3206 221 LSELESQ-------LAEARAELAEAEARLAALRAQLGSGPDALPELL--QSPVIQQLRAQLAELEAELAELSArytpnhp 291
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958672617 381 ELASQQEKRALEKEMIKKEVTREREEAEAKMLILSQNIAKLEAEIEKITREktsaVSQLEEVQNQLASQEMDVT 454
Cdd:COG3206 292 DVIALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEAR----LAELPELEAELRRLEREVE 361
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
459-553 |
2.16e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 41.22 E-value: 2.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672617 459 EMRFQLNKTKMEKDEAEKEHKEykaKSQKDLEMKDQEIEKLRLELSESTQQVEQEQQKAAR---ARQECLQVTELLGESE 535
Cdd:COG0542 415 ELERRLEQLEIEKEALKKEQDE---ASFERLAELRDELAELEEELEALKARWEAEKELIEEiqeLKEELEQRYGKIPELE 491
|
90
....*....|....*...
gi 1958672617 536 RQLHLTRSEIVQLSQEKR 553
Cdd:COG0542 492 KELAELEEELAELAPLLR 509
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
486-629 |
2.16e-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: 2.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672617 486 QKDLEMKDQEIEKLRLELSESTQQVEQEQQKAARARQECLQVTELLGESERQlhltrsEIVQLSQEKRYLCDKLEKLQKR 565
Cdd:COG4913 287 QRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGD------RLEQLEREIERLERELEERERR 360
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958672617 566 NDELEDQCVQHG-----------RVHETMKERLRQLDKHGQATAQQLVQLLNKQNQLLLERQNLSEEVDQLRAQR 629
Cdd:COG4913 361 RARLEALLAALGlplpasaeefaALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRK 435
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
306-520 |
2.23e-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: 40.90 E-value: 2.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672617 306 QTIETLTKERDDLMSVLVSVRSSLAEAQERETSAYKQVKHAVQMTEEANFEKTKALIQCEQLRSELERQTDRLEKELASQ 385
Cdd:COG4942 34 QEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRAL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672617 386 QEKRALEKEMIK------KEVTREREEAEAKMLILSQNIAKLEAEIEKITREKTSAVSQLEEVQNQLASQEmdvtkvcgE 459
Cdd:COG4942 114 YRLGRQPPLALLlspedfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELE--------E 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958672617 460 MRFQLNKTKMEKDEAEKEHKEYKAKSQKDLEMKDQEIEKLRLELSESTQQVEQEQQKAARA 520
Cdd:COG4942 186 ERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
483-631 |
2.33e-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: 40.52 E-value: 2.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672617 483 AKSQKDLEMKDQEIEKLRLELSESTQQVEQEQQKAARARQECLQVTELLGESERQLHLTRSEIVQLSQEKRYLCDKLEKL 562
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958672617 563 QKRNDELEDQcvqhgrvhetMKERLRQLDKHGQATAQQLVQLLNKQNQLLLERQNLSEEVDQLRAQRRE 631
Cdd:COG4942 96 RAELEAQKEE----------LAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEE 154
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
361-549 |
2.35e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.91 E-value: 2.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672617 361 LIQCEQLRSELERQTDRLEKELASQQEKRALEKEMIKKEVTREREEAEAKMLILSQNIAKLEAEIEKITREKTSAVSQLE 440
Cdd:COG4717 70 LKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672617 441 EVQNQLAsqemDVTKVCGEMRFQLNKTKMEKDEAEKEHKEYKAKSQKDLEMKDQEIEKLRLELSESTQQVEQEQQKAARA 520
Cdd:COG4717 150 ELEERLE----ELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEEL 225
|
170 180 190
....*....|....*....|....*....|.
gi 1958672617 521 RQEC--LQVTELLGESERQLHLTRSEIVQLS 549
Cdd:COG4717 226 EEELeqLENELEAAALEERLKEARLLLLIAA 256
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
236-431 |
2.91e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.67 E-value: 2.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672617 236 EAKTDLLESQLKLLRKDLVEYQKTCEDLKERLKHKESLvtASASSRVGGLCLKCAQHEAVLSQthnnvhiqtIETLTKER 315
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQER--REALQRLAEYSWDEIDVASAERE---------IAELEAEL 677
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672617 316 DDL---MSVLVSVRSSLAEAQERETSAYKQVKHAVQMTEEANFEKTKALIQCEQLRSELERQTDRLEKELASQQEKRaLE 392
Cdd:COG4913 678 ERLdasSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEER-FA 756
|
170 180 190
....*....|....*....|....*....|....*....
gi 1958672617 393 KEMIKKEVTREREEAEAKMLILSQNIAKLEAEIEKITRE 431
Cdd:COG4913 757 AALGDAVERELRENLEERIDALRARLNRAEEELERAMRA 795
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
227-409 |
3.30e-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: 40.13 E-value: 3.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672617 227 ELERLKLTYEAKTDLLESQLKLLRKDLVEYQKTCEDLKERLKhkESLVTASASSRVGGLCLKCAQHEAVLSQTHnnvhIQ 306
Cdd:COG4942 66 ALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELA--ELLRALYRLGRQPPLALLLSPEDFLDAVRR----LQ 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672617 307 TIETLTKERDDLMSVLVSVRSSLAEAQERETSAYKQVKHAVQMTEEANFEKTKALIQCEQLRSELERQTDRLEKELASQQ 386
Cdd:COG4942 140 YLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQ 219
|
170 180
....*....|....*....|...
gi 1958672617 387 EKRALEKEMIKKEVTREREEAEA 409
Cdd:COG4942 220 QEAEELEALIARLEAEAAAAAER 242
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
463-630 |
5.00e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 39.75 E-value: 5.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672617 463 QLNKTKMEKDEAEKEHKEYKAKsQKDLEMKDQEIEKLRLELSESTQQVEQ--EQQKAARARQECLQVTELLGESERQLHL 540
Cdd:COG4717 72 ELKELEEELKEAEEKEEEYAEL-QEELEELEEELEELEAELEELREELEKleKLLQLLPLYQELEALEAELAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672617 541 TRSEIVQLSQekryLCDKLEKLQKRNDELEDQCVQHGRVH-ETMKERLRQLDKHGQATAQQLVQLLNKQNQLLLERQNLS 619
Cdd:COG4717 151 LEERLEELRE----LEEELEELEAELAELQEELEELLEQLsLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELE 226
|
170
....*....|.
gi 1958672617 620 EEVDQLRAQRR 630
Cdd:COG4717 227 EELEQLENELE 237
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
365-570 |
6.42e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 39.61 E-value: 6.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672617 365 EQLRSELERQTDRLEKELASQQEK-RALEKEMikkEVTRERE---EAEAKMLILSQNIAKLEAEIEKITREKTSAVSQLE 440
Cdd:COG3206 167 ELRREEARKALEFLEEQLPELRKElEEAEAAL---EEFRQKNglvDLSEEAKLLLQQLSELESQLAEARAELAEAEARLA 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672617 441 EVQNQLASQEMDVTKVCG-----EMRFQLNKTKMEKDEAEK----EHKEYKAksqkdlemKDQEIEKLRLELSESTQQVE 511
Cdd:COG3206 244 ALRAQLGSGPDALPELLQspviqQLRAQLAELEAELAELSArytpNHPDVIA--------LRAQIAALRAQLQQEAQRIL 315
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958672617 512 QE---QQKAARARQECL--QVTELLGESeRQLHLTRSEIVQLSQEKRYLCDKLEKLQKRNDELE 570
Cdd:COG3206 316 ASleaELEALQAREASLqaQLAQLEARL-AELPELEAELRRLEREVEVARELYESLLQRLEEAR 378
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
242-513 |
7.11e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 39.67 E-value: 7.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672617 242 LESQLKLLRKDLVEYQKTCEDLKERLKHKESLVTASASSrvgglcLKCAQHEAVLSQTHNNVHIQTIETLTKERDDLMSV 321
Cdd:TIGR02169 672 EPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQE------LSDASRKIGEIEKEIEQLEQEEEKLKERLEELEED 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672617 322 LVSVRSSLAEAQ------ERETSAYKQVKHAVQMTEEANF---------EKTKALIQCEQLRSELERQTDRLEKELASQQ 386
Cdd:TIGR02169 746 LSSLEQEIENVKselkelEARIEELEEDLHKLEEALNDLEarlshsripEIQAELSKLEEEVSRIEARLREIEQKLNRLT 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672617 387 EKRALEKEmikkevtrEREEAEAKMLILSQNIAKLEAEIEKITREKTSAVSQLEEVQNQLAsqemdvtkvcgEMRFQLNK 466
Cdd:TIGR02169 826 LEKEYLEK--------EIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALR-----------DLESRLGD 886
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1958672617 467 TKMEKDEAEKEHKEYKAKsQKDLEMKDQEIEKLRLELSESTQQVEQE 513
Cdd:TIGR02169 887 LKKERDELEAQLRELERK-IEELEAQIEKKRKRLSELKAKLEALEEE 932
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
365-523 |
7.71e-03 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 39.22 E-value: 7.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672617 365 EQLRSELERQTDrLEKELASQQEKRALEKEMIKKEVTREREEAEAKMLILSQNIAKLEAEIEKITREKTSAVSQLEEVQN 444
Cdd:pfam05262 184 EALREDNEKGVN-FRRDMTDLKERESQEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAKNLPK 262
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958672617 445 QLASQEMDVTKvcgemRFQLNKtkmeKDEAEKEHKEYKAKSQKDLEMKDQEIEKLRLELSESTQQVEQEQQKAARARQE 523
Cdd:pfam05262 263 PADTSSPKEDK-----QVAENQ----KREIEKAQIEIKKNDEEALKAKDHKAFDLKQESKASEKEAEDKELEAQKKREP 332
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
350-630 |
8.91e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 39.29 E-value: 8.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672617 350 TEEANFEKTKALIQcEQLRSELERQTDRLEKELASQQEKRALEKemikkevtREREEAEAKMLILSQNIAKLEAEIEKIT 429
Cdd:COG5022 815 YLACIIKLQKTIKR-EKKLRETEEVEFSLKAEVLIQKFGRSLKA--------KKRFSLLKKETIYLQSAQRVELAERQLQ 885
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672617 430 REKTSA--VSQLEEVQNQLASQEMDVTKvcgemrfqlnktkmekDEAEKEHKEYKAKSQKDLEMKDQeIEKLRLELSEST 507
Cdd:COG5022 886 ELKIDVksISSLKLVNLELESEIIELKK----------------SLSSDLIENLEFKTELIARLKKL-LNNIDLEEGPSI 948
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672617 508 QQVEQE-----QQKAARARQECLQVTELL---GESERQLHLTRSEIVQLSQEKRYLCDKLEKLQKRNDELEDQCVQHGRV 579
Cdd:COG5022 949 EYVKLPelnklHEVESKLKETSEEYEDLLkksTILVREGNKANSELKNFKKELAELSKQYGALQESTKQLKELPVEVAEL 1028
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1958672617 580 HETMKerlrqLDKHGQATAQQLVQLLNKQNQLLLERQNLSEEVDQLRAQRR 630
Cdd:COG5022 1029 QSASK-----IISSESTELSILKPLQKLKGLLLLENNQLQARYKALKLRRE 1074
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
363-552 |
9.00e-03 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 39.16 E-value: 9.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672617 363 QCEQLRSELERQTDRLEKELASQQEKRALEKEMiKKEVTREREEAEAKMLILSQniaKLEAEIEKITREKTSAVSQLEEV 442
Cdd:pfam15709 342 RAEMRRLEVERKRREQEEQRRLQQEQLERAEKM-REELELEQQRRFEEIRLRKQ---RLEEERQRQEEEERKQRLQLQAA 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672617 443 QNQLASQEMDVTKVCGEMRFQLNKTKMEKDEAEKEHkeykaksQKDLEMKDQEIEKLRLELSEStQQVEQEQQKAARARQ 522
Cdd:pfam15709 418 QERARQQQEEFRRKLQELQRKKQQEEAERAEAEKQR-------QKELEMQLAEEQKRLMEMAEE-ERLEYQRQKQEAEEK 489
|
170 180 190
....*....|....*....|....*....|
gi 1958672617 523 ECLQVTELLGESERQLHLTRSEIVQLSQEK 552
Cdd:pfam15709 490 ARLEAEERRQKEEEAARLALEEAMKQAQEQ 519
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
438-565 |
9.70e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 39.04 E-value: 9.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672617 438 QLEEVQNQLASQEMdvtkvcgEMRFQLNKTKMEKDEAEKEHKEYKAKSQKDLEMKDQEIEKLrlelsestqqvEQEQQKA 517
Cdd:PRK00409 517 KLNELIASLEELER-------ELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEA-----------EKEAQQA 578
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1958672617 518 -ARARQECLQVTELLGESERQLHLTRSEiVQLSQEKRYLCDKLEKLQKR 565
Cdd:PRK00409 579 iKEAKKEADEIIKELRQLQKGGYASVKA-HELIEARKRLNKANEKKEKK 626
|
|
| |
