|
Name |
Accession |
Description |
Interval |
E-value |
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
6-543 |
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: 716.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672625 6 GNSTLEDSLGQYQRSLRERANRSIHQLKCALREVDATIEEDALDPSTSINVENVDTGVAWHELQHSHAVNQLKALLRQQT 85
Cdd:pfam15964 1 GNSTLEESLGQYQRSLRERANRSIHQLKCALHESDSTISEDEQEESLSSVVQNEDSGSPWSELQHSHAVNQLKALLQQQT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672625 86 STENETSPRRRKLSPSRPSDCEDGSLPTMHNLVPIINDQSQYIHHLEAEVKFCKDELSSMKNRVQVVVLENERLQQELKS 165
Cdd:pfam15964 81 KKENELSPRRRKLSPSRTSEDESSSLPTVHDLVPIINDQSQYIHHLEAEVKFCKEELSEMKQRVQVVVLENEKLQQELKS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672625 166 QRQEETLREQTLLDMSGNVQNSWMkTREDSRVIETTKRPFSHGDAETGKAASTGDADKWRLELERLKLTYEAKTDLLESQ 245
Cdd:pfam15964 161 QTQEETLREQTLLDSSGNMQNSWC-TPEDSRVHQTSKRPASHNLAERLKSATTGEDEKWRLELEKLKLLYEAKTEVLESQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672625 246 LKLLRKDLVEYQKTCEDLKERLKHKESLVTASASSRVGGLCLKCAQHEAVLSQTHNNVHIQTIETLTKERDDLMSVLVSV 325
Cdd:pfam15964 240 VKSLRKDLAESQKTCEDLKERLKHKESLVAASTSSRVGGLCLKCAQHEAVLAQTHTNVHMQTIERLTKERDDLMSALVSV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672625 326 RSSLAEAQERETSAYKQVKHAVQMTEEANFEKTKALIQCEQLRSELERQTDRLEKELASQQEKRALEKEMIKKEVTRERE 405
Cdd:pfam15964 320 RSSLAEAQQRESSAYEQVKQAVQMTEEANFEKTKALIQCEQLKSELERQKERLEKELASQQEKRAQEKEALRKEMKKERE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672625 406 EAEAKMLILSQNIAKLEAEIEKITREKTSAVSQLEEVQNQLASQEMDVTKVCGEMRFQLNKTKMEKDEAEKEHKEYKAKS 485
Cdd:pfam15964 400 ELGATMLALSQNVAQLEAQVEKVTREKNSLVSQLEEAQKQLASQEMDVTKVCGEMRYQLNQTKMKKDEAEKEHREYRTKT 479
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1958672625 486 QKDLEMKDQEIEKLRLELSESTQQVEQEQQKAARARQECLQVTELLGESERQLHLTSL 543
Cdd:pfam15964 480 GRQLEIKDQEIEKLGLELSESKQRLEQAQQDAARAREECLKLTELLGESEHQLHLTRL 537
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
225-518 |
6.99e-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: 62.00 E-value: 6.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672625 225 RLELERLkltyEAKTDLLESQLKLLRKDLVEYQKTCEDLKERLKHKESLvTASASSRVGGLCLKCAQHEavlsqthnnvh 304
Cdd:TIGR02168 676 RREIEEL----EEKIEELEEKIAELEKALAELRKELEELEEELEQLRKE-LEELSRQISALRKDLARLE----------- 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672625 305 iQTIETLTKERDDLMSVLVSVRSSLAEAQERETSAYKQVKHAVQMTEEANFEKTKALIQCEQLRS---ELERQTDRLEKE 381
Cdd:TIGR02168 740 -AEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREaldELRAELTLLNEE 818
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672625 382 LASQQEKRA-LEKEMIKKEVTREREEAEAKmlILSQNIAKLEAEIEKITREKTSAVSQLEEVQNQLASQEmdvtkvcgEM 460
Cdd:TIGR02168 819 AANLRERLEsLERRIAATERRLEDLEEQIE--ELSEDIESLAAEIEELEELIEELESELEALLNERASLE--------EA 888
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1958672625 461 RFQLNKTKMEKDEAEKEHKEYKAKSQKDLEMKDQEIEKLRLELSESTQQVEQEQQKAA 518
Cdd:TIGR02168 889 LALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLS 946
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
228-538 |
7.72e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 61.88 E-value: 7.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672625 228 LERLK-LTYEaktdlLESQLKLLRKD---LVEYQKtcedLKERLKHKESLVTASAssrvgglcLKCAQHEAVLSQTHNNV 303
Cdd:COG1196 188 LERLEdILGE-----LERQLEPLERQaekAERYRE----LKEELKELEAELLLLK--------LRELEAELEELEAELEE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672625 304 HIQTIETLTKERDDLMSVLVSVRSSLAEAQERETSAykQVKHAVQMTEEANFEKTKALIQceQLRSELERQTDRLEKELA 383
Cdd:COG1196 251 LEAELEELEAELAELEAELEELRLELEELELELEEA--QAEEYELLAELARLEQDIARLE--ERRRELEERLEELEEELA 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672625 384 SQQEKRALEKEMIkKEVTREREEAEAKMLILSQNIAKLEAEIEKITREKTSAVSQLEEVQNQLASQEMDvtkvcgemRFQ 463
Cdd:COG1196 327 ELEEELEELEEEL-EELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRA--------AAE 397
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958672625 464 LNKTKMEKDEAEKEHKEYKAKSQKDLEMKDQEIEKLRLELSESTQQVEQEQQKAARARQECLQVTELLGESERQL 538
Cdd:COG1196 398 LAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEA 472
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
329-553 |
5.22e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.18 E-value: 5.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672625 329 LAEAQERETSAYKQVKHAVQMTEEANFEKTKALIQCEQLRSELERQTDRLEkelASQQEKRALEKEMIKKEVTREREEAE 408
Cdd:COG1196 234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELE---EAQAEEYELLAELARLEQDIARLEER 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672625 409 AKMLilSQNIAKLEAEIEKITREKTSAVSQLEEVQNQLASQEMDVTKVcGEMRFQLNKTKMEKDEAEKEHKEYKAKSQKD 488
Cdd:COG1196 311 RREL--EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEA-EAELAEAEEALLEAEAELAEAEEELEELAEE 387
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958672625 489 LEMKDQEIEKLRLELSESTQQVEQEQQKAARARQECLQVTELLGESERQLHLTSLSLCLERESHR 553
Cdd:COG1196 388 LLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEA 452
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
356-538 |
4.33e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 53.15 E-value: 4.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672625 356 EKTKALIQCEQLRSELERQTDRLEK--ELASQQEKRALEKEMIKKEVTRE-REEAEAKMLILSQNIAKLEAEIEKITREK 432
Cdd:TIGR02169 231 EKEALERQKEAIERQLASLEEELEKltEEISELEKRLEEIEQLLEELNKKiKDLGEEEQLRVKEKIGELEAEIASLERSI 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672625 433 TSAVSQLEEVQNQLASQEMdvtkvcgemrfQLNKTKMEKDEAEKEHKEYkaksQKDLEMKDQEIEKLRLELSESTQQVEQ 512
Cdd:TIGR02169 311 AEKERELEDAEERLAKLEA-----------EIDKLLAEIEELEREIEEE----RKRRDKLTEEYAELKEELEDLRAELEE 375
|
170 180
....*....|....*....|....*.
gi 1958672625 513 EQQKAARARQECLQVTELLGESERQL 538
Cdd:TIGR02169 376 VDKEFAETRDELKDYREKLEKLKREI 401
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
400-545 |
7.19e-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: 52.37 E-value: 7.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672625 400 VTREREEAEAKMLILSQNIAKLEAEIEKIT---REKTSAVSQLEEVQNQLASQEMDVTKVCGEMRFQLNKTKMEKDEAEK 476
Cdd:TIGR02168 661 ITGGSAKTNSSILERRREIEELEEKIEELEekiAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEA 740
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958672625 477 EHKEYK----------AKSQKDLEMKDQEIEKLRLELSESTQQVEQEQQKAARARQECLQVTELLGESERQLHLTSLSL 545
Cdd:TIGR02168 741 EVEQLEeriaqlskelTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEA 819
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
308-540 |
7.25e-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: 52.37 E-value: 7.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672625 308 IETLTKERDDLMSVLVSVRSSLAEAQERETSAYKQVKHAVQMTEEANFEKTKALIQCEQL---RSELERQTDRLEKELAS 384
Cdd:TIGR02168 262 LQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELeaqLEELESKLDELAEELAE 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672625 385 QQEKraleKEMIKKEVTRERE---EAEAKMLILSQNIAKLEAEIEKITREKTSAVSQLEEVQNQLASQEMDVTKVCGEmr 461
Cdd:TIGR02168 342 LEEK----LEELKEELESLEAeleELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDR-- 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672625 462 fqLNKTKMEKDEAEKEHKEY-KAKSQKDLEMKDQEIEKLRLELSESTQQVEQEQQKAARARQECLQVTELLGESERQLHL 540
Cdd:TIGR02168 416 --RERLQQEIEELLKKLEEAeLKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDS 493
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
294-538 |
5.65e-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: 49.45 E-value: 5.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672625 294 AVLSQTHNNVHIQTIETLTKERddlmsvLVSVRSSLAEAQERETSAYKQVKhavQMTEEANFEKTKALIQCEQLRSELER 373
Cdd:pfam12128 256 AELRLSHLHFGYKSDETLIASR------QEERQETSAELNQLLRTLDDQWK---EKRDELNGELSAADAAVAKDRSELEA 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672625 374 QTDRLEKELASQQEKRALEKEMIKkEVTREREEAEAKMLILSQNIAKLEAEIE------------KITREKTSAVSQLEE 441
Cdd:pfam12128 327 LEDQHGAFLDADIETAAADQEQLP-SWQSELENLEERLKALTGKHQDVTAKYNrrrskikeqnnrDIAGIKDKLAKIREA 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672625 442 VQNQLASQEMDVTKVCGEMRFQLNKTKMEKDEAEKEHKE-------------YKAKSQKDLEMKDQEIEKLRLELSESTQ 508
Cdd:pfam12128 406 RDRQLAVAEDDLQALESELREQLEAGKLEFNEEEYRLKSrlgelklrlnqatATPELLLQLENFDERIERAREEQEAANA 485
|
250 260 270
....*....|....*....|....*....|
gi 1958672625 509 QVEQEQQKAARARQECLQVTELLGESERQL 538
Cdd:pfam12128 486 EVERLQSELRQARKRRDQASEALRQASRRL 515
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
366-523 |
1.95e-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: 47.07 E-value: 1.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672625 366 QLRSELERQTDRLEKELASQQEKRALEKEMiKKEVTREREEAEAKMLILSQNIAKLEAEIEKITREKTSAVSQLEEVQNQ 445
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKE-EKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672625 446 LASQEMDVTKV---------CGEMRFQLNKTKMEKD-----------EAEKEHKEYKAKSQKDLEMKDQEIEKLRLELSE 505
Cdd:COG4942 99 LEAQKEELAELlralyrlgrQPPLALLLSPEDFLDAvrrlqylkylaPARREQAEELRADLAELAALRAELEAERAELEA 178
|
170
....*....|....*...
gi 1958672625 506 STQQVEQEQQKAARARQE 523
Cdd:COG4942 179 LLAELEEERAALEALKAE 196
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
355-538 |
2.69e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 47.36 E-value: 2.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672625 355 FEKTKALIQCEQLRSELERQTDRLEKELAS--------QQEKRALEKEMIKKE------------VTREREEAEAKMLIL 414
Cdd:TIGR02168 673 LERRREIEELEEKIEELEEKIAELEKALAElrkeleelEEELEQLRKELEELSrqisalrkdlarLEAEVEQLEERIAQL 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672625 415 SQNIAKLEAEIEKITREKTSAVSQLEEVQNQLASQEMDVTkvcgEMRFQLNKTKMEKDEAEKEHKEYKAKSQK---DLEM 491
Cdd:TIGR02168 753 SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIE----QLKEELKALREALDELRAELTLLNEEAANlreRLES 828
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1958672625 492 KDQEIEKLRLELSESTQQVEQEQQKAARARQECLQVTELLGESERQL 538
Cdd:TIGR02168 829 LERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESEL 875
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
124-490 |
2.76e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 47.36 E-value: 2.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672625 124 QSQYIHHLEAEVKFCKDELSSMKNRVQVVVLENERLQQELKSQRQEETLREQTLLDMSGNVQNSWMKTREDSRVIETTKR 203
Cdd:TIGR02168 675 RRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSK 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672625 204 PFSHGDAE-TGKAASTGDADKWRLELERLKLTYEAKTDLLESQLKLLRKDLVEYQKTCEDLKERLkhkeslvtASASSRV 282
Cdd:TIGR02168 755 ELTELEAEiEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEA--------ANLRERL 826
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672625 283 GGLclkcaQHEAVLSQTHNNVHIQTIETLTKERDDLMSVLVSVRSSLAEAQERETSAYKQVKHAVQMTEEANFEKTKA-- 360
Cdd:TIGR02168 827 ESL-----ERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELse 901
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672625 361 -LIQCEQLRSELERQTDRLEKELASQQEKRALEKEMIKKEVTREREEAEAKMLILSQNIAKLEAEIEKITREKTSAVSQL 439
Cdd:TIGR02168 902 eLRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKI 981
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1958672625 440 EEVQNqlasqemdvtkvcgemrfqLNKTKMEKDEAEKEHKEYKAKSQKDLE 490
Cdd:TIGR02168 982 KELGP-------------------VNLAAIEEYEELKERYDFLTAQKEDLT 1013
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
308-444 |
4.08e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.45 E-value: 4.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672625 308 IETLTKERDDLMSVLVSVRSSLAEAQEREtSAYKQVKHAVQMTEEANFEktkaLIQCEQLRSELERQTDRLEKELASQQE 387
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAEL-DALQERREALQRLAEYSWD----EIDVASAEREIAELEAELERLDASSDD 686
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958672625 388 KRALEKEmiKKEVTREREEAEAKMLILSQNIAKLEAEIEKITREKTSAVSQLEEVQN 444
Cdd:COG4913 687 LAALEEQ--LEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAED 741
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
322-480 |
1.59e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.38 E-value: 1.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672625 322 LVSVRSSLAEAQERETSAYKQVKHAvqmTEEANFEKTKALIQC----EQLRSELERQTDRLEKELAsQQEKRALEKEMI- 396
Cdd:PRK12704 23 FVRKKIAEAKIKEAEEEAKRILEEA---KKEAEAIKKEALLEAkeeiHKLRNEFEKELRERRNELQ-KLEKRLLQKEENl 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672625 397 ---KKEVTREREEAEAKMLILSQNIAKLEAEIEKITREKTSAVSQLEEVQNQLASQ--EMDVTKVCGEMRFQ----LNKT 467
Cdd:PRK12704 99 drkLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAEEakEILLEKVEEEARHEaavlIKEI 178
|
170
....*....|....
gi 1958672625 468 KME-KDEAEKEHKE 480
Cdd:PRK12704 179 EEEaKEEADKKAKE 192
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
225-538 |
2.82e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 43.95 E-value: 2.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672625 225 RLELERLKLTYEAKTDLLESQLKLLRKDLVEYQKTCEDLKER---LKHKESLVTASASSRVGGLCLKCAQHEAVLSQTHN 301
Cdd:pfam15921 330 RSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQEsgnLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTG 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672625 302 NVhiQTIETLTKERDD-------LMSVLVSVRSSLAEAQERETSAYKQVKHAVQMTEE--ANFEKTKALIQ--CEQLRSE 370
Cdd:pfam15921 410 NS--ITIDHLRRELDDrnmevqrLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSltAQLESTKEMLRkvVEELTAK 487
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672625 371 ---LERQTDRLEKELASQQEK-RALEKemIKKEVTREREEAEAKMlilsQNIAKLEAEIEKITREKTSA------VSQLE 440
Cdd:pfam15921 488 kmtLESSERTVSDLTASLQEKeRAIEA--TNAEITKLRSRVDLKL----QELQHLKNEGDHLRNVQTECealklqMAEKD 561
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672625 441 EVQNQLASQEMDVTKVCGEMRFQLNKTKMEKDEAEKEHKEYKAKSQKDLEMKDQEIEKLRlELSESTQQVEQEQQKAARA 520
Cdd:pfam15921 562 KVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIR-ELEARVSDLELEKVKLVNA 640
|
330
....*....|....*...
gi 1958672625 521 RQECLQVTELLGESERQL 538
Cdd:pfam15921 641 GSERLRAVKDIKQERDQL 658
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
399-549 |
4.13e-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: 42.44 E-value: 4.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672625 399 EVTREREEAEAKMLILSQNIAKLEAEIEKITREKTSAVSQLEEVQNQLASQEMDVTKVCGEMRFQLNKTKMEKDEAEKEH 478
Cdd:pfam09787 51 ELRQERDLLREEIQKLRGQIQQLRTELQELEAQQQEEAESSREQLQELEEQLATERSARREAEAELERLQEELRYLEEEL 130
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958672625 479 KEYKAKSQKDLEMKDQEIEKLRLELSESTQQVEQEQQKAARARqeclQVTELLGESERQLHL-----TSLSLCLER 549
Cdd:pfam09787 131 RRSKATLQSRIKDREAEIEKLRNQLTSKSQSSSSQSELENRLH----QLTETLIQKQTMLEAlstekNSLVLQLER 202
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
225-450 |
5.56e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 43.12 E-value: 5.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672625 225 RLELERLKLTYEAKTDLLESQLKLLRKDLVEYQKTCEDLKERLKHKE---------------SLVTASASSRVGGLCLKC 289
Cdd:TIGR02168 255 LEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEqqkqilrerlanlerQLEELEAQLEELESKLDE 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672625 290 AQHEAVLSQTHNNVHIQTIETLTKERDDLMSVLVSVRSSLAEAQERETSAYKQVKHAVQMTEEANFEKTKALIQCEQLRS 369
Cdd:TIGR02168 335 LAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLED 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672625 370 ELERQTDRLEKELASQQEKRALEKEMIKKEVTREREEAEAKMLILSQNIAKLEAEIEKITREKTSAVSQLEEVQNQLASQ 449
Cdd:TIGR02168 415 RRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSL 494
|
.
gi 1958672625 450 E 450
Cdd:TIGR02168 495 E 495
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
306-520 |
6.93e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.06 E-value: 6.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672625 306 QTIETLTKERDDLMSVLVSVRSSLAEAQERETSAYKQVKHAVQMTEEANFEKTKALIQCEQLRSELERQTDRLEKELASQ 385
Cdd:COG4942 34 QEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRAL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672625 386 QEKRALEKEMIK------KEVTREREEAEAKMLILSQNIAKLEAEIEKITREKTSAVSQLEEVQNQLASQEmdvtkvcgE 459
Cdd:COG4942 114 YRLGRQPPLALLlspedfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELE--------E 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958672625 460 MRFQLNKTKMEKDEAEKEHKEYKAKSQKDLEMKDQEIEKLRLELSESTQQVEQEQQKAARA 520
Cdd:COG4942 186 ERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
361-547 |
7.21e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.45 E-value: 7.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672625 361 LIQCEQLRSELERQTDRLEKELASQQEKRALEKEMIKKEVTREREEAEAKMLILSQNIAKLEAEIEKITREKTSAVSQLE 440
Cdd:COG4717 70 LKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672625 441 EVQNQLAsqemDVTKVCGEMRFQLNKTKMEKDEAEKEHKEYKAKSQKDLEMKDQEIEKLRLELSESTQQVEQEQQKAARA 520
Cdd:COG4717 150 ELEERLE----ELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEEL 225
|
170 180
....*....|....*....|....*....
gi 1958672625 521 RQEC--LQVTELLGESERQLHLTSLSLCL 547
Cdd:COG4717 226 EEELeqLENELEAAALEERLKEARLLLLI 254
|
|
| PRK00247 |
PRK00247 |
putative inner membrane protein translocase component YidC; Validated |
361-521 |
7.25e-04 |
|
putative inner membrane protein translocase component YidC; Validated
Pssm-ID: 178945 [Multi-domain] Cd Length: 429 Bit Score: 42.15 E-value: 7.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672625 361 LIQCEQLRSELERQTDRLEKELASQQEKRAL--EKEMIKKEVTREREEAEAKMLILSQNIAKLEAEIEKITREKTSAVSQ 438
Cdd:PRK00247 263 LIQNIIMYLILERKYPLTDEFKEHHAEQRAQyrEKQKEKKAFLWTLRRNRLRMIITPWRAPELHAENAEIKKTRTAEKNE 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672625 439 LEEVQNQLASQEMDVTKVCGEMRFQLNKTKMEKDEAEKEHKEYKAKSQKDLEMKDQEIEKLRLELSESTQQVEQEQQKAA 518
Cdd:PRK00247 343 AKARKKEIAQKRRAAEREINREARQERAAAMARARARRAAVKAKKKGLIDASPNEDTPSENEESKGSPPQVEATTTAEPN 422
|
...
gi 1958672625 519 RAR 521
Cdd:PRK00247 423 REP 425
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
359-523 |
7.36e-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: 41.45 E-value: 7.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672625 359 KALIQCEQLRSELERQTDRLEKELAsQQEKRALEKEMIKKEVTREREEAEAKMLILSQNIAKLEAEIEKITREKtsavsQ 438
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELA-ALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNK-----E 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672625 439 LEEVQNQLASQEMDVTkvcgemrfQLNKTKMEKDEAEKEHKEYKAKSQKDLEMKDQEIEKLRLELSESTQQVEQEQQKAA 518
Cdd:COG1579 91 YEALQKEIESLKRRIS--------DLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELE 162
|
....*
gi 1958672625 519 RARQE 523
Cdd:COG1579 163 AEREE 167
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
236-431 |
1.05e-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: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672625 236 EAKTDLLESQLKLLRKDLVEYQKTCEDLKERLKHKESLvtASASSRVGGLCLKCAQHEAVLSQthnnvhiqtIETLTKER 315
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQER--REALQRLAEYSWDEIDVASAERE---------IAELEAEL 677
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672625 316 DDL---MSVLVSVRSSLAEAQERETSAYKQVKHAVQMTEEANFEKTKALIQCEQLRSELERQTDRLEKELASQQEKRaLE 392
Cdd:COG4913 678 ERLdasSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEER-FA 756
|
170 180 190
....*....|....*....|....*....|....*....
gi 1958672625 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 |
1.08e-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: 41.67 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672625 227 ELERLKLTYEAKTDLLESQLKLLRKDLVEYQKTCEDLKERLKhkESLVTASASSRVGGLCLKCAQHEAVLSQTHnnvhIQ 306
Cdd:COG4942 66 ALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELA--ELLRALYRLGRQPPLALLLSPEDFLDAVRR----LQ 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672625 307 TIETLTKERDDLMSVLVSVRSSLAEAQERETSAYKQVKHAVQMTEEANFEKTKALIQCEQLRSELERQTDRLEKELASQQ 386
Cdd:COG4942 140 YLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQ 219
|
170 180
....*....|....*....|...
gi 1958672625 387 EKRALEKEMIKKEVTREREEAEA 409
Cdd:COG4942 220 QEAEELEALIARLEAEAAAAAER 242
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
242-513 |
2.07e-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: 41.21 E-value: 2.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672625 242 LESQLKLLRKDLVEYQKTCEDLKERLKHKESLVTASASSrvgglcLKCAQHEAVLSQTHNNVHIQTIETLTKERDDLMSV 321
Cdd:TIGR02169 672 EPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQE------LSDASRKIGEIEKEIEQLEQEEEKLKERLEELEED 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672625 322 LVSVRSSLAEAQ------ERETSAYKQVKHAVQMTEEANF---------EKTKALIQCEQLRSELERQTDRLEKELASQQ 386
Cdd:TIGR02169 746 LSSLEQEIENVKselkelEARIEELEEDLHKLEEALNDLEarlshsripEIQAELSKLEEEVSRIEARLREIEQKLNRLT 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672625 387 EKRALEKEmikkevtrEREEAEAKMLILSQNIAKLEAEIEKITREKTSAVSQLEEVQNQLAsqemdvtkvcgEMRFQLNK 466
Cdd:TIGR02169 826 LEKEYLEK--------EIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALR-----------DLESRLGD 886
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1958672625 467 TKMEKDEAEKEHKEYKAKSQkDLEMKDQEIEKLRLELSESTQQVEQE 513
Cdd:TIGR02169 887 LKKERDELEAQLRELERKIE-ELEAQIEKKRKRLSELKAKLEALEEE 932
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
336-523 |
2.42e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.89 E-value: 2.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672625 336 ETSAYKQVKHAVQMTEEANFEKTKALIQCEQLRSELERQTDRLEK-ELASQQEKRALEKEMIKKEVTREREEAEAKmlil 414
Cdd:PTZ00121 1538 EAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKaEEAKKAEEARIEEVMKLYEEEKKMKAEEAK---- 1613
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672625 415 sqniaklEAEIEKITREKTSAVSQLEEVQNQLASQEMDVTKVCGEMRFQLNKTKMEKDEAEKEHKEYKAKSQkdlEMKDQ 494
Cdd:PTZ00121 1614 -------KAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAE---EAKKA 1683
|
170 180
....*....|....*....|....*....
gi 1958672625 495 EIEKLRLElsESTQQVEQEQQKAARARQE 523
Cdd:PTZ00121 1684 EEDEKKAA--EALKKEAEEAKKAEELKKK 1710
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
363-539 |
2.50e-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: 2.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672625 363 QCEQLRsELERQTDRLEKELASQQEKRALEKEMIKKEVTREREEAEAKMLILSQNIAKLEAEIEKITREKTSAVSQLEEV 442
Cdd:COG4913 250 QIELLE-PIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDEL 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672625 443 QNQLASQEMDvtkvcgemrfQLNKTKMEKDEAEKEHKEYKAKSQKDlemkDQEIEKLRLELSESTQQVEQEQQKAARARQ 522
Cdd:COG4913 329 EAQIRGNGGD----------RLEQLEREIERLERELEERERRRARL----EALLAALGLPLPASAEEFAALRAEAAALLE 394
|
170
....*....|....*..
gi 1958672625 523 ECLQVTELLGESERQLH 539
Cdd:COG4913 395 ALEEELEALEEALAEAE 411
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
370-516 |
2.65e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 40.38 E-value: 2.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672625 370 ELERQTDRLEKELASQQEKRALEKEMIkkevtrerEEAEAKMlilSQNIAKLEAEIEKITREKTSAVSQLEEVQNQLASQ 449
Cdd:PHA02562 178 ELNQQIQTLDMKIDHIQQQIKTYNKNI--------EEQRKKN---GENIARKQNKYDELVEEAKTIKAEIEELTDELLNL 246
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958672625 450 EM---DVTKVCGEMRFQLNKTKMEKDEAEKEHKEYKAKS-----QKDLEMKDQEIEKLRLELSESTQQVEQEQQK 516
Cdd:PHA02562 247 VMdieDPSAALNKLNTAAAKIKSKIEQFQKVIKMYEKGGvcptcTQQISEGPDRITKIKDKLKELQHSLEKLDTA 321
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
365-523 |
4.07e-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: 39.99 E-value: 4.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672625 365 EQLRSELERQTDrLEKELASQQEKRALEKEMIKKEVTREREEAEAKMLILSQNIAKLEAEIEKITREKTSAVSQLEEVQN 444
Cdd:pfam05262 184 EALREDNEKGVN-FRRDMTDLKERESQEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAKNLPK 262
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958672625 445 QLASQEMDVTKvcgemRFQLNKtkmeKDEAEKEHKEYKAKSQKDLEMKDQEIEKLRLELSESTQQVEQEQQKAARARQE 523
Cdd:pfam05262 263 PADTSSPKEDK-----QVAENQ----KREIEKAQIEIKKNDEEALKAKDHKAFDLKQESKASEKEAEDKELEAQKKREP 332
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
365-526 |
4.55e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.00 E-value: 4.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672625 365 EQLRSELERQTDRLEKELASQQEK-RALEKEMikkEVTRERE---EAEAKMLILSQNIAKLEAEIEKITREKTSAVSQLE 440
Cdd:COG3206 167 ELRREEARKALEFLEEQLPELRKElEEAEAAL---EEFRQKNglvDLSEEAKLLLQQLSELESQLAEARAELAEAEARLA 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672625 441 EVQNQLASQEMDVTKVCG-----EMRFQLNKTKMEKDEAEK----EHKEYKAksqkdlemKDQEIEKLRLELSESTQQVE 511
Cdd:COG3206 244 ALRAQLGSGPDALPELLQspviqQLRAQLAELEAELAELSArytpNHPDVIA--------LRAQIAALRAQLQQEAQRIL 315
|
170
....*....|....*...
gi 1958672625 512 QE---QQKAARARQECLQ 526
Cdd:COG3206 316 ASleaELEALQAREASLQ 333
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
228-455 |
5.59e-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: 5.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672625 228 LERLKLTYEAKTDLLESQLKLLRKDLVEYQKTCEDLKErlkhkeslvtasassrvgglclkcaQHEAVLSQTHNNVHIQT 307
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQ-------------------------KNGLVDLSEEAKLLLQQ 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672625 308 IETLTKERDDLMSVLVSVRSSLAEAQERETSAYKQVKHAVQMTEEANFEKTKALIQcEQLRSELERQTD------RLEKE 381
Cdd:COG3206 221 LSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELE-AELAELSARYTPnhpdviALRAQ 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672625 382 LASQQEKRALEKEMIKKEVTREREEAEAKMLILSQNIAKL----------EAEIEKITREKTSAVSQLEEVQNQLasQEM 451
Cdd:COG3206 300 IAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLearlaelpelEAELRRLEREVEVARELYESLLQRL--EEA 377
|
....
gi 1958672625 452 DVTK 455
Cdd:COG3206 378 RLAE 381
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
459-539 |
5.75e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 39.68 E-value: 5.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672625 459 EMRFQLNKTKMEKDEAEKEHKEykaKSQKDLEMKDQEIEKLRLELSESTQQVEQEQQKAAR---ARQECLQVTELLGESE 535
Cdd:COG0542 415 ELERRLEQLEIEKEALKKEQDE---ASFERLAELRDELAELEEELEALKARWEAEKELIEEiqeLKEELEQRYGKIPELE 491
|
....
gi 1958672625 536 RQLH 539
Cdd:COG0542 492 KELA 495
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
327-537 |
6.41e-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: 39.11 E-value: 6.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672625 327 SSLAEAQERETSAYKQVKHAVQMTEEANFEKTKALIQCEQLRSELERQTDRLEKELASQQEKRAlEKEMIKKEVTREREE 406
Cdd:pfam07888 34 NRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHE-ELEEKYKELSASSEE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672625 407 AEAKMLILSQNIAKLEAEIEkitrektsavsQLEEVQNQLASQEMDVTKVCGEMRFQLNKTKMEKDEAEKEHKEYKAKsq 486
Cdd:pfam07888 113 LSEEKDALLAQRAAHEARIR-----------ELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAK-- 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1958672625 487 kdLEMKDQEIEKLRLELSESTQQVEQEQQKAARARQECLQVTELLGESERQ 537
Cdd:pfam07888 180 --LQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRK 228
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
366-516 |
6.73e-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: 39.28 E-value: 6.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672625 366 QLRSELERQTDR---LEKELAS-QQEKRALEKEMikKEVTREREEAEAKMLILSQNIAKLEAEIEKITREKTSAVSQLEE 441
Cdd:TIGR02169 671 SEPAELQRLRERlegLKRELSSlQSELRRIENRL--DELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSS 748
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958672625 442 VQNQLASQEMDVTKVCGEM-RFQLNKTKMEKDEAEKEHKEYKAKSQKdLEMKDQEIEKLRLELSESTQQVEQEQQK 516
Cdd:TIGR02169 749 LEQEIENVKSELKELEARIeELEEDLHKLEEALNDLEARLSHSRIPE-IQAELSKLEEEVSRIEARLREIEQKLNR 823
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
316-450 |
8.90e-03 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 38.49 E-value: 8.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672625 316 DDLMSVLVSVRSSLAEAQERETSAYKQVKHAVQMTE-EANFEKTKAliQCEQLRSELERQTDRLEKELASQQEKRALEke 394
Cdd:COG1566 79 TDLQAALAQAEAQLAAAEAQLARLEAELGAEAEIAAaEAQLAAAQA--QLDLAQRELERYQALYKKGAVSQQELDEAR-- 154
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958672625 395 mikkevtREREEAEAKMLILSQNIAKLEAEIEKITrEKTSAVSQLEEVQNQLASQE 450
Cdd:COG1566 155 -------AALDAAQAQLEAAQAQLAQAQAGLREEE-ELAAAQAQVAQAEAALAQAE 202
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
359-513 |
9.66e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 38.74 E-value: 9.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672625 359 KALIQCEQLRSELERQTDRLEKELASQQEK-RALE----------KEMIKKEV---TREREEAEAKMLILSQNIAKLEAE 424
Cdd:COG4913 295 AELEELRAELARLEAELERLEARLDALREElDELEaqirgnggdrLEQLEREIerlERELEERERRRARLEALLAALGLP 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672625 425 IEKITREKTSAVSQLEEVQNQLASQEMDVTKVCGEMRFQLNKTKMEKDEAEKEHKEYKAKsQKDLemkDQEIEKLRLELS 504
Cdd:COG4913 375 LPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERR-KSNI---PARLLALRDALA 450
|
....*....
gi 1958672625 505 ESTQQVEQE 513
Cdd:COG4913 451 EALGLDEAE 459
|
|
| |
