|
Name |
Accession |
Description |
Interval |
E-value |
| SH3_MIA3 |
cd11893 |
Src Homology 3 domain of Melanoma Inhibitory Activity 3 protein; MIA3, also called TANGO or ... |
41-113 |
4.32e-47 |
|
Src Homology 3 domain of Melanoma Inhibitory Activity 3 protein; MIA3, also called TANGO or TANGO1, acts as a tumor suppressor of malignant melanoma. It is downregulated or lost in melanoma cells lines. Unlike other MIA family members, MIA3 is widely expressed except in hematopoietic cells. MIA3 is an ER resident transmembrane protein that is required for the loading of collagen VII into transport vesicles. SNPs in the MIA3 gene have been associated with coronary arterial disease and myocardial infarction. MIA3 contains an N-terminal SH3-like domain, similar to MIA. It is a member of the recently identified family that also includes MIA, MIAL, and MIA2. MIA is a single domain protein that adopts a SH3 domain-like fold; it contains an additional antiparallel beta sheet and two disulfide bonds compared to classical SH3 domains. Unlike classical SH3 domains, MIA does not bind proline-rich ligands.
Pssm-ID: 212826 Cd Length: 73 Bit Score: 163.10 E-value: 4.32e-47
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1201873520 41 RCADPECSKLMCRGKAMKDFQGPDCRFVNFKKGETVYVYYKLIGMSTELWAGSIGSDFGYFPKDLLEINHNYT 113
Cdd:cd11893 1 RCADEECSMLLCRGKAVKDFTGPDCRFLSFKKGETIYVYYKLSGRRTDLWAGSVGFDFGYFPKDLLDVNHLYT 73
|
|
| SH3_MIA2 |
cd11892 |
Src Homology 3 domain of Melanoma Inhibitory Activity 2 protein; MIA2 is expressed ... |
41-113 |
3.49e-29 |
|
Src Homology 3 domain of Melanoma Inhibitory Activity 2 protein; MIA2 is expressed specifically in hepatocytes and its expression is controlled by hepatocyte nuclear factor 1 binding sites in the MIA2 promoter. It inhibits the growth and invasion of hepatocellular carcinomas (HCC) and may act as a tumor suppressor. A mutation in MIA2 in mice resulted in reduced cholesterol and triglycerides. Since MIA2 localizes to ER exit sites, it may function as an ER-to-Golgi trafficking protein that regulates lipid metabolism. MIA2 contains an N-terminal SH3-like domain, similar to MIA. It is a member of the recently identified family that also includes MIA, MIAL, and MIA3 (also called TANGO). MIA is a single domain protein that adopts a SH3 domain-like fold; it contains an additional antiparallel beta sheet and two disulfide bonds compared to classical SH3 domains. Unlike classical SH3 domains, MIA does not bind proline-rich ligands.
Pssm-ID: 212825 Cd Length: 73 Bit Score: 111.85 E-value: 3.49e-29
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1201873520 41 RCADPECSKLMCRGKAMKDFQGPDCRFVNFKKGETVYVYYKLIGMSTELWAGSIGSDFGYFPKDLLEINHNYT 113
Cdd:cd11892 1 KCGDPECERLMSRVQAIRDYRGPDCRYLSFKKGDEIIVYYKLSGKREDLWAGSTGKEFGYFPKDAVKVEEVYI 73
|
|
| SH3_MIA_like |
cd11760 |
Src Homology 3 domain of Melanoma Inhibitory Activity protein and similar proteins; MIA is a ... |
42-113 |
8.09e-29 |
|
Src Homology 3 domain of Melanoma Inhibitory Activity protein and similar proteins; MIA is a single domain protein that adopts a SH3 domain-like fold; it contains an additional antiparallel beta sheet and two disulfide bonds compared to classical SH3 domains. MIA is secreted from malignant melanoma cells and it plays an important role in melanoma development and invasion. MIA is expressed by chondrocytes in normal tissues and may be important in the cartilage cell phenotype. Unlike classical SH3 domains, MIA does not bind proline-rich ligands. MIA is a member of the recently identified family that also includes MIA-like (MIAL), MIA2, and MIA3 (also called TANGO); the biological functions of this family are not yet fully understood.
Pssm-ID: 212694 Cd Length: 76 Bit Score: 111.03 E-value: 8.09e-29
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1201873520 42 CADPECSKLMCRGKAMKDFQGPDCRFVNFKKGETVYVYYKLIGMSTELWAGSIGSD---FGYFPKDLLEINHNYT 113
Cdd:cd11760 2 CADAECSNPISRARALEDYHGPDCRFLNFKKGDTIYVYSKLAGERQDLWAGSVGGDaglFGYFPKNLVQELKVYE 76
|
|
| MIA |
cd11890 |
Melanoma Inhibitory Activity protein; MIA is a single domain protein that adopts a Src ... |
39-128 |
4.44e-17 |
|
Melanoma Inhibitory Activity protein; MIA is a single domain protein that adopts a Src Homology 3 (SH3) domain-like fold; it contains an additional antiparallel beta sheet and two disulfide bonds compared to classical SH3 domains. MIA is secreted from malignant melanoma cells and it plays an important role in melanoma development and invasion. MIA is expressed by chondrocytes in normal tissues and may be important in the cartilage cell phenotype. Unlike classical SH3 domains, MIA does not bind proline-rich ligands. It binds peptide ligands with sequence similarity to type III human fibronectin repeats.
Pssm-ID: 212823 Cd Length: 98 Bit Score: 78.38 E-value: 4.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 39 RKRCADPECSKLMCRGKAMKDFQGPDCRFVNFKKGETVYVYYKLIGMSTELWAGSIGSDF--------GYFPKDLLEINH 110
Cdd:cd11890 1 KKLCADQECSHPISIAVALQDYMAPDCRFIPIQRGQVVYVFSKLKGRGRLFWGGSVQGDYygeqaarlGYFPSSIVQEDQ 80
|
90
....*....|....*...
gi 1201873520 111 NYTNEELELPTEETDFVC 128
Cdd:cd11890 81 YLKPGKVEVKTDKWDFYC 98
|
|
| MIAL |
cd11891 |
Melanoma Inhibitory Activity-Like protein; MIAL is specifically expressed in the cochlea and ... |
42-112 |
2.40e-16 |
|
Melanoma Inhibitory Activity-Like protein; MIAL is specifically expressed in the cochlea and the vestibule of the inner ear and may contribute to inner ear dysfunction in humans. MIAL is a member of the recently identified family that also includes MIA, MIA2, and MIA3 (also called TANGO); MIA is the most studied member of the family. MIA is a single domain protein that adopts a Src Homology 3 (SH3) domain-like fold; it contains an additional antiparallel beta sheet and two disulfide bonds compared to classical SH3 domains. MIA is secreted from malignant melanoma cells and it plays an important role in melanoma development and invasion. MIA is expressed by chondrocytes in normal tissues and may be important in the cartilage cell phenotype. Unlike classical SH3 domains, MIA does not bind proline-rich ligands.
Pssm-ID: 212824 Cd Length: 83 Bit Score: 75.66 E-value: 2.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 42 CADPECSKLMCRGKAMKDFQGPDCRFVNFKKGETVYVYYKLI--GMSTELWAGSIGSD--------FGYFPKDLLEINHN 111
Cdd:cd11891 2 CADEECVYAISLARAEDDYNAPDCRFINIKKGQLIYVYSKLVkeNGAGEFWSGSVYSEryvdqmgiVGYFPSNLVKEQTV 81
|
.
gi 1201873520 112 Y 112
Cdd:cd11891 82 Y 82
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1316-1633 |
3.64e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 78.44 E-value: 3.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1316 KQAK--ESMKVAQEQKNILSDEIAGLKDtvKGLEETNHQLDDKIKSLctmldteRKQNAKKQKKLSETQKSLEKLEEAFS 1393
Cdd:COG1196 207 RQAEkaERYRELKEELKELEAELLLLKL--RELEAELEELEAELEEL-------EAELEELEAELAELEAELEELRLELE 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1394 MHSAELSEVQIALNESKLSEEKVKAELQHVQEENARLKKSKEQLLKEAEGWSERHTELTEQIKLYRKSQKDIEEALAYKE 1473
Cdd:COG1196 278 ELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAE 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1474 NEIEVltncimQLKQLDTDSASEAKKDGEghewstRDDLANGELpdnEKMKTQIKQMMDASRVKTMLSLVEEDRNSLQSK 1553
Cdd:COG1196 358 AELAE------AEEALLEAEAELAEAEEE------LEELAEELL---EALRAAAELAAQLEELEEAEEALLERLERLEEE 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1554 LNDEVAARQELEEQIKKLEHDSCSLQSAKARLENECKTLQQKVEILGELYQQKEMALQKKLTQEEYERQEKEQKLSAADE 1633
Cdd:COG1196 423 LEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEAD 502
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1288-1707 |
1.70e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 76.25 E-value: 1.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1288 KQLAEKIQNLLREKTEMLDKFSECDEKIKQAKESMKVAQEQKNILSDEIAGLKDTVKGLEETNHQLDDKIKSLCTMLdtE 1367
Cdd:TIGR02168 354 ESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKL--E 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1368 RKQNAKKQKKLSETQKSLEKLEEAFSMHSAELSEVQIALNESKLSEEKVKAELQHVQEENARLKKSKE----------QL 1437
Cdd:TIGR02168 432 EAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQEnlegfsegvkAL 511
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1438 LKEAEGWSERHTELTEQIKLYRKSQKDIEEALAYKENEIEVLTN-----CIMQLKQLDT--------DSASEAKKDGEGH 1504
Cdd:TIGR02168 512 LKNQSGLSGILGVLSELISVDEGYEAAIEAALGGRLQAVVVENLnaakkAIAFLKQNELgrvtflplDSIKGTEIQGNDR 591
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1505 EWSTRDDLANGELPDNEKMKTQIKQMMDA-------------------------------------------SRVKTMLS 1541
Cdd:TIGR02168 592 EILKNIEGFLGVAKDLVKFDPKLRKALSYllggvlvvddldnalelakklrpgyrivtldgdlvrpggvitgGSAKTNSS 671
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1542 LVEEDRN----------------SLQSKLNDEVAARQELEEQIKKLEHDSCSLQSAKARLENECKTLQQKVEILGELYQQ 1605
Cdd:TIGR02168 672 ILERRREieeleekieeleekiaELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQ 751
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1606 kemaLQKKLTQEEYERQEKEQKLSAADEKAVLAIEEVKVYKQRIQDMEEELQKTERSY---KNQIAAHEKKAHDNWLIAR 1682
Cdd:TIGR02168 752 ----LSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALdelRAELTLLNEEAANLRERLE 827
|
490 500
....*....|....*....|....*
gi 1201873520 1683 SAERALAEEKREAANLRQKLIEVNQ 1707
Cdd:TIGR02168 828 SLERRIAATERRLEDLEEQIEELSE 852
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1276-1659 |
6.74e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 71.24 E-value: 6.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1276 LSVKSRIYQVTEK--QLAEKIQNLLREKTEMLDKFSECDEKIKQAKESMKVAQEQKNILSDEIAGLKDTVKGLEETNHQL 1353
Cdd:TIGR02168 673 LERRREIEELEEKieELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQL 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1354 DDKIKSLCTMLDTERKQNAKKQKKLSETQKSLEKLEEAFSMHSAELSEVQIALNESKLSEEKVKAELQHVQEENARLKKS 1433
Cdd:TIGR02168 753 SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERR 832
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1434 KEQLLKEAEGWSERHTELTEQIKLYRKSQKDIEEALAYKENEIEVLTNCIMQLKQ-LDTDSASEAKKDGEGHEWSTRDDL 1512
Cdd:TIGR02168 833 IAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEaLALLRSELEELSEELRELESKRSE 912
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1513 ANGELpdnEKMKTQIKQMmdasrvKTMLSLVEEDRNSLQSKLNDEvaARQELEEQIKKLEHDSCSLQSAKARLENecktL 1592
Cdd:TIGR02168 913 LRREL---EELREKLAQL------ELRLEGLEVRIDNLQERLSEE--YSLTLEEAEALENKIEDDEEEARRRLKR----L 977
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1593 QQKVEILGELyqqKEMALqkkltqEEYERQEK------EQK--LSAADEKAVLAIEEV-----KVYKQRIQDMEEELQKT 1659
Cdd:TIGR02168 978 ENKIKELGPV---NLAAI------EEYEELKErydfltAQKedLTEAKETLEEAIEEIdrearERFKDTFDQVNENFQRV 1048
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1287-1691 |
1.85e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 69.78 E-value: 1.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1287 EKQLAEKIQNLLREKTEMLDKFSECDEKIKQAKESMKVAQEQKNilSDEIAGLKDTVKGLEETNHQLDDKIKSLCTMLDT 1366
Cdd:PTZ00121 1389 EKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKK--ADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKA 1466
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1367 ERKQNAKKQKKLSETQKSLEKLEEAFSMHSAELSEVQIALNESKLSEEKVKAELQHVQEE--NARLKKSKEQLLKEAEGW 1444
Cdd:PTZ00121 1467 EEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEakKAEEAKKADEAKKAEEKK 1546
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1445 SERHTELTEQIKLYRKSQKdIEEALAYKENeievltncimqlKQLDTDSASEAKKDGEghewsTRDDLANGELPDNEKMK 1524
Cdd:PTZ00121 1547 KADELKKAEELKKAEEKKK-AEEAKKAEED------------KNMALRKAEEAKKAEE-----ARIEEVMKLYEEEKKMK 1608
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1525 TQIKQMMDASRVKTMLSLVEEDRNSLQSKLNDEVAARQELEEQIKKLEHDSCSLQSAKARLENECKTLQQKVEILGELYQ 1604
Cdd:PTZ00121 1609 AEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEK 1688
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1605 QKEMALQKK---------LTQEEYERQEKEQKLSAADEKAVLAIEEVKVYKQRIQDMEEELQKTERSyKNQIAAHEKKAH 1675
Cdd:PTZ00121 1689 KAAEALKKEaeeakkaeeLKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEE-KKKIAHLKKEEE 1767
|
410
....*....|....*.
gi 1201873520 1676 DNWLIARSAERALAEE 1691
Cdd:PTZ00121 1768 KKAEEIRKEKEAVIEE 1783
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1289-1602 |
1.88e-11 |
|
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: 69.71 E-value: 1.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1289 QLAEKIQNLLREKTEMLDKFSECDEKIKQAKESMKVAQE-------QKNILSDEIAGLKDTVKGLEETNHQLDDKIKSLC 1361
Cdd:TIGR02169 678 RLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRkigeiekEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVK 757
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1362 TMLDTERKQNAKKQKKLS-------------------ETQKSLEKLEEAFSMHSAELSEVQIALNESKLSEEKVKAELQH 1422
Cdd:TIGR02169 758 SELKELEARIEELEEDLHkleealndlearlshsripEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQE 837
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1423 VQEENARLKKSKEQLLKEAEGWSERHTELTEQIKLYRKSQKDIEEALAYKENEIEVLTNCIMQLKQ-LDTDSASEAKKDG 1501
Cdd:TIGR02169 838 LQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERkIEELEAQIEKKRK 917
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1502 EGHEWSTRDDLANGELPDNEKMKTQIK----QMMDASRVKTMLSLVEEDRNSLQSKLNdevAARQELEEQIKKLEhdscS 1577
Cdd:TIGR02169 918 RLSELKAKLEALEEELSEIEDPKGEDEeipeEELSLEDVQAELQRVEEEIRALEPVNM---LAIQEYEEVLKRLD----E 990
|
330 340
....*....|....*....|....*
gi 1201873520 1578 LQSAKARLENECKTLQQKVEILGEL 1602
Cdd:TIGR02169 991 LKEKRAKLEEERKAILERIEEYEKK 1015
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1288-1673 |
1.91e-11 |
|
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: 69.28 E-value: 1.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1288 KQLAEKIQNLLREKTEMLDKFSECDEKIKQAKESMKVAQEQKNILSDE----IAGLKDTVKGLEETNHQLDDK------I 1357
Cdd:TIGR04523 214 KSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEqnkiKKQLSEKQKELEQNNKKIKELekqlnqL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1358 KSLCTMLDTERKQN---------AKKQKKLSETQKSLEKLEEAFSMHSAELSEVQIALNESKLSEEKVKAELQHVQEENA 1428
Cdd:TIGR04523 294 KSEISDLNNQKEQDwnkelkselKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIE 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1429 RLKKSKEQLLKEAEGWSERHTELTEQIKLYRKSQKDIEEALAYKENEIEVLTNCIMQLKQLDTDSASEAKkdgeghewst 1508
Cdd:TIGR04523 374 KLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIK---------- 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1509 rdDLANgelpDNEKMKTQIKQMMDA-SRVKTMLSLVEEDRNSLQSKLNDEVaarQELEEQIKKLEhdscSLQSAKARLEN 1587
Cdd:TIGR04523 444 --DLTN----QDSVKELIIKNLDNTrESLETQLKVLSRSINKIKQNLEQKQ---KELKSKEKELK----KLNEEKKELEE 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1588 ECKTLQQKVEILgelyQQKEMALQKKLTQEEYERQEKEQKLSAADEkaVLAIEEVKVYKQRIQdmeEELQKTERSYKNQI 1667
Cdd:TIGR04523 511 KVKDLTKKISSL----KEKIEKLESEKKEKESKISDLEDELNKDDF--ELKKENLEKEIDEKN---KEIEELKQTQKSLK 581
|
....*.
gi 1201873520 1668 AAHEKK 1673
Cdd:TIGR04523 582 KKQEEK 587
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1288-1665 |
5.05e-11 |
|
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: 68.12 E-value: 5.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1288 KQLAEKIQNLLREKTEMLDKFSECDEKIKQAKESMKVAQEQKNILSDEIAGLKdtvKGLEETNHQLDDKIkslcTMLDTE 1367
Cdd:TIGR04523 78 KILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLE---KQKKENKKNIDKFL----TEIKKK 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1368 RKQNAKKQKKLSETQKSLEKLEEAFSMHSAELSEVQIALNESKLSE-----------------EKVKAELQHVQEENARL 1430
Cdd:TIGR04523 151 EKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLlklelllsnlkkkiqknKSLESQISELKKQNNQL 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1431 KKSKEQLLKEAEGWSERHTELTEQIKLYRKSQKDIEEALAYKENEIE----VLTNCIMQLKQLDTDsASEAKKDGEgHEW 1506
Cdd:TIGR04523 231 KDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEqnnkKIKELEKQLNQLKSE-ISDLNNQKE-QDW 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1507 STRddlANGELPDNEKMKTQIKQMMDA-----SRVKTMLSLVEEDRNSLQsklNDEVAARQELEE---QIKKLEHDSCSL 1578
Cdd:TIGR04523 309 NKE---LKSELKNQEKKLEEIQNQISQnnkiiSQLNEQISQLKKELTNSE---SENSEKQRELEEkqnEIEKLKKENQSY 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1579 QSAKARLENECKTLQQKVEILGELYQQKEMALQKKltQEEYERQEKEQKL-------------SAADEKAVLAIeEVKVY 1645
Cdd:TIGR04523 383 KQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKL--QQEKELLEKEIERlketiiknnseikDLTNQDSVKEL-IIKNL 459
|
410 420
....*....|....*....|
gi 1201873520 1646 KQRIQDMEEELQKTERSYKN 1665
Cdd:TIGR04523 460 DNTRESLETQLKVLSRSINK 479
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1284-1702 |
1.73e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 66.50 E-value: 1.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1284 QVTEKQLAEKIQNLLREKTEMLDKFSECDEKIKQAKESMKVAQEQKNILSDEIAGLKDTVKGLEETNHQLDDKIKSLCTM 1363
Cdd:COG1196 357 EAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEE 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1364 LDTERKQNAKKQKKLSETQKSLEKLEEAFS--MHSAELSEVQIALNESKLSEEKVKAELQHVQEENARLKKSKEQLLKEA 1441
Cdd:COG1196 437 EEEEEEALEEAAEEEAELEEEEEALLELLAelLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLL 516
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1442 EGWSERHTELTEQIKLYRKSQKDIEEALAYKENEI-----EVLTNCIMQLKQ--------LDTDSASEAKKDGEGHEWST 1508
Cdd:COG1196 517 AGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIvveddEVAAAAIEYLKAakagratfLPLDKIRARAALAAALARGA 596
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1509 RDDLANGELPDNEKMKTQIKQMMDASRVKTMLSLVEEDRNSLQSKLNDEVAARQELEEQIkkLEHDSCSLQSAKARLENE 1588
Cdd:COG1196 597 IGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGG--SAGGSLTGGSRRELLAAL 674
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1589 CKTLQQKVEILGELYQQKEMALQKKLTQEEYERQEKEQKLSAADEKAVLAIEEVKVYKQRIQDMEEELQKTERSYKNQIA 1668
Cdd:COG1196 675 LEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALE 754
|
410 420 430
....*....|....*....|....*....|....
gi 1201873520 1669 AHEKKAhdnwliarsaerALAEEKREAANLRQKL 1702
Cdd:COG1196 755 ELPEPP------------DLEELERELERLEREI 776
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1282-1702 |
2.78e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 65.56 E-value: 2.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1282 IYQVTEKQLAEKIQNLLREK----TEMLDKFSECDEKIKQAKESMKV---AQEQKNILSDEIAGLKDTVKGLEETNHQLD 1354
Cdd:COG4717 43 IRAMLLERLEKEADELFKPQgrkpELNLKELKELEEELKEAEEKEEEyaeLQEELEELEEELEELEAELEELREELEKLE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1355 DKIKSLCTM-----LDTERKQNAKKQKKLSETQKSLEKLEEAFSMHSAELSEVQIALNES-KLSEEKVKAELQHVQEENA 1428
Cdd:COG4717 123 KLLQLLPLYqeleaLEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELlEQLSLATEEELQDLAEELE 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1429 RLKKSKEQLLKEAEGWSERHTELTEQIKLYRKSQKDIEEALAYKENEIEVLTNCIMQLKQLDTDSASEAKKDGEGHEWST 1508
Cdd:COG4717 203 ELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLV 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1509 RDDLANGELPDNEKMKTQIKQMMDASRVKTMLSLVEEDRNSLQSKLN--------------DEVAARQELEEQIKKLEHd 1574
Cdd:COG4717 283 LGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGlppdlspeellellDRIEELQELLREAEELEE- 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1575 scslQSAKARLENECKTL--QQKVEILGELYQQKEMALQKKLTQEEYERQEKEQKLSAADEKAVLAIEEVKVYKQRIQDM 1652
Cdd:COG4717 362 ----ELQLEELEQEIAALlaEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEEL 437
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1201873520 1653 EEELQKTERSYKNqiaAHEKKAHDNWLIAR-SAERALAEEKREAANLRQKL 1702
Cdd:COG4717 438 EEELEELEEELEE---LREELAELEAELEQlEEDGELAELLQELEELKAEL 485
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1287-1601 |
3.91e-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: 65.46 E-value: 3.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1287 EKQLAEKIQNLLREKTEM-----LDKFSECDEKIKQAKESMKVAQEQKNILSDEIAGLKDTVKGLEETNHQLDDKIKSLC 1361
Cdd:TIGR02168 208 QAEKAERYKELKAELRELelallVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1362 TMLDTERKQNAKKQKKLSETQKSLEKLEEAFSMHSAELSEVQIALNESKLSEEKVKAELQHVQEENARLKKSKEQLLKEA 1441
Cdd:TIGR02168 288 KELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAEL 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1442 EGWSERHTELTEQIKLYRKsqkdieeALAYKENEIEVLTNCIMQLKQLDTDSASEAKKdgegheWSTRDDLANGELPDNE 1521
Cdd:TIGR02168 368 EELESRLEELEEQLETLRS-------KVAQLELQIASLNNEIERLEARLERLEDRRER------LQQEIEELLKKLEEAE 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1522 KMKTQikqmMDASRVKTMLSLVEEDRNSLQSKLNDEVAARQELEEQIKKLEHDscsLQSAKARLENeCKTLQQKVEILGE 1601
Cdd:TIGR02168 435 LKELQ----AELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERE---LAQLQARLDS-LERLQENLEGFSE 506
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1287-1700 |
4.95e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 65.16 E-value: 4.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1287 EKQLAEKIQNLLREKTEMLDKFSEcdeKIKQAKESMKVAQEQKNiLSDEIAGLKDTVKGLEETNHQLDDKIKSlctmldT 1366
Cdd:PTZ00121 1365 KAEAAEKKKEEAKKKADAAKKKAE---EKKKADEAKKKAEEDKK-KADELKKAAAAKKKADEAKKKAEEKKKA------D 1434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1367 ERKQNAKKQKKLSETQKSLEkleeafsmhsaelsEVQIALNESKLSEEKVKA-ELQHVQEEnarlKKSKEQLLKEAEGWS 1445
Cdd:PTZ00121 1435 EAKKKAEEAKKADEAKKKAE--------------EAKKAEEAKKKAEEAKKAdEAKKKAEE----AKKADEAKKKAEEAK 1496
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1446 ERHTELTEQIKLYRKSQKDIEEALAYKENEIEvltncimqlKQLDTDSASEAKKdgeGHEWSTRDDLANGElpdnEKMKT 1525
Cdd:PTZ00121 1497 KKADEAKKAAEAKKKADEAKKAEEAKKADEAK---------KAEEAKKADEAKK---AEEKKKADELKKAE----ELKKA 1560
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1526 QIKQMMDASRVKtmlslvEEDRNSLQSKLNDEVAARQELEEQIKKLEHDSCSLQSAKARLENECKTlqqKVEILGELYQQ 1605
Cdd:PTZ00121 1561 EEKKKAEEAKKA------EEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKI---KAEELKKAEEE 1631
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1606 KEMALQKKLTQEEYERqeKEQKLSAADEKAVLAIEEVKVYKQRIQDMEEELQKTERSYKNQIAAHEKKAHDnwliARSAE 1685
Cdd:PTZ00121 1632 KKKVEQLKKKEAEEKK--KAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEE----AKKAE 1705
|
410
....*....|....*...
gi 1201873520 1686 ---RALAEEKREAANLRQ 1700
Cdd:PTZ00121 1706 elkKKEAEEKKKAEELKK 1723
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1314-1669 |
6.72e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 64.69 E-value: 6.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1314 KIKQAKESMKVAQEQKNILSDEIAGLKDTVKGLEETNHQLddkikslctmldteRKQNAKKQKKLSETQKSLEKLEEAFS 1393
Cdd:TIGR02168 678 EIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQL--------------RKELEELSRQISALRKDLARLEAEVE 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1394 MHSAELSEVQIALNESKLSEEKVKAELQHVQEENARLKKSKEQLLKEAEGWSERHTELTEQIKLYRKSQKDIEEALAYKE 1473
Cdd:TIGR02168 744 QLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLR 823
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1474 NEIEVLTNCIMQLKQLDTDSASEAKKdgeghewsTRDDLANgelpdnekmktqikqmmdasrvktmlslVEEDRNSLQSK 1553
Cdd:TIGR02168 824 ERLESLERRIAATERRLEDLEEQIEE--------LSEDIES----------------------------LAAEIEELEEL 867
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1554 LNDEVAARQELEEQIKKLEHDscsLQSAKARLENECKTLQQKVEILGELYQQKEmALQKKLTQEEYERQEKEQKL----S 1629
Cdd:TIGR02168 868 IEELESELEALLNERASLEEA---LALLRSELEELSEELRELESKRSELRRELE-ELREKLAQLELRLEGLEVRIdnlqE 943
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1201873520 1630 AADEKAVLAIEEVKVYKQRIQDMEEELQKTERSYKNQIAA 1669
Cdd:TIGR02168 944 RLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKE 983
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1287-1704 |
8.08e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 64.31 E-value: 8.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1287 EKQLAEKIQNL------LREKTEMLDKFSECDEKIKQAKESMKVAQEQKNILSDEIAGLKDTVKGLEETNHQLDDKIKSL 1360
Cdd:PRK03918 199 EKELEEVLREIneisseLPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEEL 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1361 ctmldterKQNAKKQKKLSETQKSLEKLEEAFSMHSAELSEVQIALneSKLSEEkvKAELQHVQEENARLKKSKEQLLKE 1440
Cdd:PRK03918 279 --------EEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRL--SRLEEE--INGIEERIKELEEKEERLEELKKK 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1441 AEGWSERHTELTEQIKLYRKSQKDIEEALAYKE----NEIEVLTNCImqlkqldtDSASEAKKDGEGHEWSTRDDLANGE 1516
Cdd:PRK03918 347 LKELEKRLEELEERHELYEEAKAKKEELERLKKrltgLTPEKLEKEL--------EELEKAKEEIEEEISKITARIGELK 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1517 LPDNEKMKTqIKQMMDASRVKTMLS--LVEEDRNSLQSKLNDEVAarqELEEQIKKLEhdscslqSAKARLENECKTLQQ 1594
Cdd:PRK03918 419 KEIKELKKA-IEELKKAKGKCPVCGreLTEEHRKELLEEYTAELK---RIEKELKEIE-------EKERKLRKELRELEK 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1595 KVEILGELYQQKEMALQKKLTQEEYERQEKEqKLSAADEKAVLAIEEVKVYKQRIQDMEEELQKTErSYKNQIAAHEKKA 1674
Cdd:PRK03918 488 VLKKESELIKLKELAEQLKELEEKLKKYNLE-ELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLE-ELKKKLAELEKKL 565
|
410 420 430
....*....|....*....|....*....|
gi 1201873520 1675 HDnwliarsAERALAEEKREAANLRQKLIE 1704
Cdd:PRK03918 566 DE-------LEEELAELLKELEELGFESVE 588
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1289-1488 |
9.31e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 64.19 E-value: 9.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1289 QLAEKIQNLLREKTEMLDKFSECDEKIKQAKESMKVAQEQKNILSDEIAGLKDTVKGLEETNHQLDDKIKSLCTMLDTER 1368
Cdd:COG1196 271 ELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAE 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1369 KQNAKKQKKLSETQKSLEKLEEAFSMHSAELSEVQIALNESKLSEEKVKAELQHVQEENARLKKSKEQLLKEAEGWSERH 1448
Cdd:COG1196 351 EELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEAL 430
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1201873520 1449 TELTEQIKLYRKSQKDIEEALAYKENEIEVLTNCIMQLKQ 1488
Cdd:COG1196 431 AELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLE 470
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
1277-1664 |
1.14e-09 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 63.17 E-value: 1.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1277 SVKSRIYQVTEKQLAEKIQNLLREKTEMLDKFSECDEKIKQAKEsMKVAQEQKNILSDEIAGLKDTVKGLEETNhqldDK 1356
Cdd:pfam05622 55 TPGGKKYLLLQKQLEQLQEENFRLETARDDYRIKCEELEKEVLE-LQHRNEELTSLAEEAQALKDEMDILRESS----DK 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1357 IKSLCTMLDTERKQ-----NAKKQKKLSE------TQKSLEKLEEAFSMHSA----ELSEVQIALNESKLSEEKVKA--- 1418
Cdd:pfam05622 130 VKKLEATVETYKKKledlgDLRRQVKLLEernaeyMQRTLQLEEELKKANALrgqlETYKRQVQELHGKLSEESKKAdkl 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1419 --ELQHVQEENARLKKSKEQLLkeaegwSERHT--ELTEQIKLYRKSQKDIEEALAYKENEIEVLTNCIMQLKQLDTDSA 1494
Cdd:pfam05622 210 efEYKKLEEKLEALQKEKERLI------IERDTlrETNEELRCAQLQQAELSQADALLSPSSDPGDNLAAEIMPAEIREK 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1495 -----SEAKKDGEGHEWSTRDDLA--NGELPD----NEKMKTQIKqmMDASRVKTMLSLVEEDRNSLQ---SKLNDEVAA 1560
Cdd:pfam05622 284 lirlqHENKMLRLGQEGSYRERLTelQQLLEDanrrKNELETQNR--LANQRILELQQQVEELQKALQeqgSKAEDSSLL 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1561 RQELEEQIKKLEHDSCSLQSAKARLENECKTLQQKVeilgelyQQKEMALQKKLTQEEYERQEKEQKLSAADEKA----- 1635
Cdd:pfam05622 362 KQKLEEHLEKLHEAQSELQKKKEQIEELEPKQDSNL-------AQKIDELQEALRKKDEDMKAMEERYKKYVEKAksvik 434
|
410 420 430
....*....|....*....|....*....|....*.
gi 1201873520 1636 -------VLAIEEVKVYKQRIQDMEEELQKTERSYK 1664
Cdd:pfam05622 435 tldpkqnPASPPEIQALKNQLLEKDKKIEHLERDFE 470
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1374-1716 |
1.41e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 63.42 E-value: 1.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1374 KQKKlsetQKSLEKLEEAfsmhSAELSEVQIALNE-----SKLSEEKVKAELQHVQEENARLKKsKEQLLKEAEGWSERH 1448
Cdd:COG1196 171 KERK----EEAERKLEAT----EENLERLEDILGElerqlEPLERQAEKAERYRELKEELKELE-AELLLLKLRELEAEL 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1449 TELTEQIKLYRKSQKDIEEALAYKENEIEVLtncimQLKQLDTDSASEAKKDGEghewstrddlangelpdnEKMKTQIK 1528
Cdd:COG1196 242 EELEAELEELEAELEELEAELAELEAELEEL-----RLELEELELELEEAQAEE------------------YELLAELA 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1529 QMmdasrvktmlslvEEDRNSLQSKLNDEVAARQELEEQIKKLEHDSCSLQSAKARLENECKTLQQKVEILgelyQQKEM 1608
Cdd:COG1196 299 RL-------------EQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEA----EAELA 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1609 ALQKKLTQEEYERQEKEQKLSAADEKAVLAIEEVKVYKQRIQDMEEELQKTERSYKNQIAAHEKKAHDnwliARSAERAL 1688
Cdd:COG1196 362 EAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEA----LAELEEEE 437
|
330 340
....*....|....*....|....*...
gi 1201873520 1689 AEEKREAANLRQKLIEVNQKNIMLQRPL 1716
Cdd:COG1196 438 EEEEEALEEAAEEEAELEEEEEALLELL 465
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1374-1658 |
2.89e-09 |
|
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: 62.38 E-value: 2.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1374 KQKKLSETQKSLEKLEEAFSMHSAELSEVQIALNESKLSEEKVKAELQHVQEENARLKKSKEqllkeaegwserhtELTE 1453
Cdd:TIGR02168 237 LREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEIS--------------RLEQ 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1454 QIKLYRKSQKDIEEALAYKENEIEVLtncimqLKQLDTDSASEAKKDGEGHEWSTRDDLANGELpdnEKMKTQIKQMmda 1533
Cdd:TIGR02168 303 QKQILRERLANLERQLEELEAQLEEL------ESKLDELAEELAELEEKLEELKEELESLEAEL---EELEAELEEL--- 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1534 srvKTMLSLVEEDRNSLQSKLNdevaarqELEEQIKKLEHDSCSLQSAKARLENECKTLQQKVEILGELYQQKEM-ALQK 1612
Cdd:TIGR02168 371 ---ESRLEELEEQLETLRSKVA-------QLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELkELQA 440
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1201873520 1613 KLTQEEYERQEKEQKLSAADEKAVLAIEEVKVYKQRIQDMEEELQK 1658
Cdd:TIGR02168 441 ELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQ 486
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1283-1565 |
4.30e-09 |
|
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: 4.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1283 YQVTEKQLAEKIQNLLREKTEMLDKFSECDEKIKQAKESMKVAQEQKNILSDEIAGLKDTVKGLEETNHQLDDKIKSLCT 1362
Cdd:TIGR02168 244 LQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEA 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1363 MLDTERKQNAKKQKKLSETQKSLEKLEEAFSMHSAELSEVQIALNESKLSEEKVKAELQHVQEENARLKKSKEQllkeae 1442
Cdd:TIGR02168 324 QLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIAS------ 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1443 gwserhteLTEQIKLYRKSQKDIEEALAYKENEIEVLtNCIMQLKQLDTDSASEAKKDGEGHEWSTRDDLANGELPDNEK 1522
Cdd:TIGR02168 398 --------LNNEIERLEARLERLEDRRERLQQEIEEL-LKKLEEAELKELQAELEELEEELEELQEELERLEEALEELRE 468
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1201873520 1523 MKTQIKQMMDAsrvktmlslVEEDRNSLQSKLNDEVAARQELE 1565
Cdd:TIGR02168 469 ELEEAEQALDA---------AERELAQLQARLDSLERLQENLE 502
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1287-1714 |
5.53e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 61.70 E-value: 5.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1287 EKQLAEKIQNLLREKTEMLDKFSECDEKIKQAKESMKVAQEQKNilSDEIAGLKDTVKGLEETNHQLDDKIKSLCTmldT 1366
Cdd:PTZ00121 1300 EKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKK--AAEAAKAEAEAAADEAEAAEEKAEAAEKKK---E 1374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1367 ERKQNAKKQKKLSETQKSLEKLEEAFSMHSAELSEVQIALNESKLSEE-KVKAELQHVQEE---NARLKKSKEQLLKEAE 1442
Cdd:PTZ00121 1375 EAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEaKKKAEEKKKADEakkKAEEAKKADEAKKKAE 1454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1443 GW--SERHTELTEQIKLYRKSQKDIEEALAYKEneievltncIMQLKQLDTDSASEAKKDGEghEWSTRDDLANGElpdn 1520
Cdd:PTZ00121 1455 EAkkAEEAKKKAEEAKKADEAKKKAEEAKKADE---------AKKKAEEAKKKADEAKKAAE--AKKKADEAKKAE---- 1519
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1521 EKMKTQIKQMMDASRVKTMLSLVEEDRNSLQSKLNDEVAARQELE--EQIKKLEHDScslQSAKARLENECKTLQQKVEI 1598
Cdd:PTZ00121 1520 EAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKkaEEAKKAEEDK---NMALRKAEEAKKAEEARIEE 1596
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1599 LGELYQQKEMALQKKLTQEEYERQEKEQKLSAADEKavlaieevKVYKQRIQDMEEELQKTERSYKNQIAAHEKKAHdnw 1678
Cdd:PTZ00121 1597 VMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEK--------KKVEQLKKKEAEEKKKAEELKKAEEENKIKAAE--- 1665
|
410 420 430
....*....|....*....|....*....|....*.
gi 1201873520 1679 lIARSAEralaEEKREAANLRQKLIEVNQKNIMLQR 1714
Cdd:PTZ00121 1666 -EAKKAE----EDKKKAEEAKKAEEDEKKAAEALKK 1696
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1288-1673 |
7.01e-09 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 61.14 E-value: 7.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1288 KQLAEKIQNLLREKTEMLDKFSECDEK-IKQAKESMKVAQEQKNILSDEIAGLKDTVKGLEETNHQLDDKIKslcTMLDT 1366
Cdd:pfam02463 652 VSLEEGLAEKSEVKASLSELTKELLEIqELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELL---ADRVQ 728
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1367 ERKQNAKKQKKLSETQKSLEKLEEAFSMHSAELSEVQIA---LNESKLSEEKVKAELQHVQEENARLKKSKEQLLKEAEg 1443
Cdd:pfam02463 729 EAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSelsLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALE- 807
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1444 wserhTELTEQIKLYRKSQKDIEEALAYKENEIEvltncimqlkqLDTDSASEAKKDGEGHEWSTRDDLANGELPDNEKM 1523
Cdd:pfam02463 808 -----EELKEEAELLEEEQLLIEQEEKIKEEELE-----------ELALELKEEQKLEKLAEEELERLEEEITKEELLQE 871
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1524 KTQIKQMMDASRVKTMLSLVE-EDRNSLQSKLNDEVAARQELEEQIKKLEHDSCSLqsakarlENECKTLQQKVEILGEL 1602
Cdd:pfam02463 872 LLLKEEELEEQKLKDELESKEeKEKEEKKELEEESQKLNLLEEKENEIEERIKEEA-------EILLKYEEEPEELLLEE 944
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1201873520 1603 YQQKEMALQKKLTQEEYERQEKEQKLSAAdEKAVLAIEEVKVYKQRIQDMEEELQKTERSYKNQIAAHEKK 1673
Cdd:pfam02463 945 ADEKEKEENNKEEEEERNKRLLLAKEELG-KVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEE 1014
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1299-1663 |
8.36e-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: 60.85 E-value: 8.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1299 REKTEMLDKFS---ECDEKIKQAKESMKVAQEQKNILSDEIAGLKDTVKGLE-ETNHQL----------DDKIKSLCTML 1364
Cdd:TIGR02169 153 VERRKIIDEIAgvaEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRrEREKAEryqallkekrEYEGYELLKEK 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1365 DTERKQNAKKQKKLSETQKSLEKLEEAFSMHSAELSEVQIALNE-----SKLSEEK---VKAELQHVQEENARLKKSKEQ 1436
Cdd:TIGR02169 233 EALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEElnkkiKDLGEEEqlrVKEKIGELEAEIASLERSIAE 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1437 LLKEAEGWSERHTELTEQIKLYRKSQKDIEEALAYKENEIEVLTNCIMQLKQLDTDSASEAK-KDGEGHEWstRDDLang 1515
Cdd:TIGR02169 313 KERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEeVDKEFAET--RDEL--- 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1516 elpdnekmktqikqmmdaSRVKTMLSLVEEDRNSLQSKLNDEVAARQELEEQIKKLEHDSCSLQSAKARLENECKTLQQK 1595
Cdd:TIGR02169 388 ------------------KDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALE 449
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1596 VEilgelyqqkemalqkkltqeeyerqEKEQKLSAAdeKAVLAIEEVKVY--KQRIQDMEEELQKTERSY 1663
Cdd:TIGR02169 450 IK-------------------------KQEWKLEQL--AADLSKYEQELYdlKEEYDRVEKELSKLQREL 492
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1289-1597 |
1.19e-08 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 60.42 E-value: 1.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1289 QLAEKIQNLLREKTEMLDKFSECDEKIKQAKESMKVAQEQKNILSDEIAGLKDTVKGLE-------ETNHQLDDKIKSlc 1361
Cdd:TIGR04523 339 QLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLEskiqnqeKLNQQKDEQIKK-- 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1362 tmLDTERKQNAKKQKKLSETqksLEKLEEAFSMHSAELSEVQIALNESKLSEEKVKAELQHVQEENARLKKSKEQLLKEA 1441
Cdd:TIGR04523 417 --LQQEKELLEKEIERLKET---IIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKEL 491
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1442 EGWSERHTELTEQIKLYRKSQKDIEEALAYKENEIEVLTNCIMQLKQLDTDSASEAKKDGEGHEWSTRDDLANGELPDNE 1521
Cdd:TIGR04523 492 KSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEKEIDEKNKEIE 571
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1201873520 1522 KMKTQIKQMMDA-SRVKTMLSLVEEDRNSLQSKLNDEVAARQELEEQIKKLEHDSCSLQSAKARLENECKTLQQKVE 1597
Cdd:TIGR04523 572 ELKQTQKSLKKKqEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVK 648
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1278-1661 |
2.02e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 59.67 E-value: 2.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1278 VKSRIYQVTEKQLAEKIQNLLREKTEMLDKFSECDEKIKQAKESMKVA----------QEQKNILSDEIAGLKDTVKGLE 1347
Cdd:PRK02224 192 LKAQIEEKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEAdevleeheerREELETLEAEIEDLRETIAETE 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1348 ETNHQLDDKIKSLCTMLDTERKQNAKKQKKLSETQKSLEKLEEAFSMHSAELSEVQIALNESKLSeekvkaeLQHVQEEN 1427
Cdd:PRK02224 272 REREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVA-------AQAHNEEA 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1428 ARLKKSKEQLLKEAEGWSERHTELTEQIKLYRKSQKDIEEALAYKENEIEVL----TNCIMQLKQLDT--DSASEAKKDG 1501
Cdd:PRK02224 345 ESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELrerfGDAPVDLGNAEDflEELREERDEL 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1502 EGHEWSTRDDLANGE--------LPDNEKMKTQIKQMMDASRVKTmLSLVEEDRNSLQSKLNDEVAARQELEEQIKKLEh 1573
Cdd:PRK02224 425 REREAELEATLRTARerveeaeaLLEAGKCPECGQPVEGSPHVET-IEEDRERVEELEAELEDLEEEVEEVEERLERAE- 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1574 dscSLQSAKARLEneckTLQQKVEILGELYQQKEMALQKKLTQEEYER----------QEKEQKLSAADEKAVLAIEEVK 1643
Cdd:PRK02224 503 ---DLVEAEDRIE----RLEERREDLEELIAERRETIEEKRERAEELReraaeleaeaEEKREAAAEAEEEAEEAREEVA 575
|
410
....*....|....*...
gi 1201873520 1644 VYKQRIQDMEEELQKTER 1661
Cdd:PRK02224 576 ELNSKLAELKERIESLER 593
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1313-1708 |
2.12e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 59.77 E-value: 2.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1313 EKIKQAKESMKVAQEQKNIlsdEIAGLKDTVKGLEETNHQLDDKIKSLCTMLDTERK----QNAKKQKKLSETQKSLE-- 1386
Cdd:PTZ00121 1112 EEARKAEEAKKKAEDARKA---EEARKAEDARKAEEARKAEDAKRVEIARKAEDARKaeeaRKAEDAKKAEAARKAEEvr 1188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1387 ------KLEEAFSMHSAELSEVQIALNESKLSEEKVKAELQHVQEEnARLKKSKEQLLKEAEGWSERHTELTEQIKLYRK 1460
Cdd:PTZ00121 1189 kaeelrKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEE-AKKDAEEAKKAEEERNNEEIRKFEEARMAHFAR 1267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1461 SQKDIEEALAYKENEIEVLTncimQLKQLDTDSASEAKKDGEGHEWSTRDDLANGELpdnEKMKTQIKQMMDASRVKTml 1540
Cdd:PTZ00121 1268 RQAAIKAEEARKADELKKAE----EKKKADEAKKAEEKKKADEAKKKAEEAKKADEA---KKKAEEAKKKADAAKKKA-- 1338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1541 slvEEDRNSLQSKLNDEVAARQELEEQIKKLEHDSCSLQSAKARLEneckTLQQKVEILGELYQQKEMALQKKLTQEEYE 1620
Cdd:PTZ00121 1339 ---EEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKAD----AAKKKAEEKKKADEAKKKAEEDKKKADELK 1411
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1621 RQEKEQKlsAADEKAVLAiEEVKVYKQRIQDMEEELQKTERSYKNQIAAHEKKAHDNWLIARSAERA--LAEEKREAANL 1698
Cdd:PTZ00121 1412 KAAAAKK--KADEAKKKA-EEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAkkKAEEAKKADEA 1488
|
410
....*....|
gi 1201873520 1699 RQKLIEVNQK 1708
Cdd:PTZ00121 1489 KKKAEEAKKK 1498
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1307-1710 |
2.56e-08 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 59.26 E-value: 2.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1307 KFSECDEKIKQAKESMKVAQE-----QKNILSDE--IAGLKDTVKGLEETNHQLDDKIKSLCTMLD-------------- 1365
Cdd:TIGR04523 34 EEKQLEKKLKTIKNELKNKEKelknlDKNLNKDEekINNSNNKIKILEQQIKDLNDKLKKNKDKINklnsdlskinseik 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1366 TERKQNAKKQKKLSETQKSLEKLEEAFSMHSAELSEVQIALNES--------------KLSEEKVKAELQHVQEENARLK 1431
Cdd:TIGR04523 114 NDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLnnkyndlkkqkeelENELNLLEKEKLNIQKNIDKIK 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1432 K---SKEQLLKEAEGWSERHTELTEQIKLYRKSQKDIEEALAYKENEIEVLTNCIMQLKQLDTDSASEAKKDGEGHEWST 1508
Cdd:TIGR04523 194 NkllKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQ 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1509 RD-DLANGELPDNEK----MKTQI------KQMMDASRVKTMLSLVEEDRNSLQSKLNDEVAARQELEEQIKKLEHDSCS 1577
Cdd:TIGR04523 274 KElEQNNKKIKELEKqlnqLKSEIsdlnnqKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTN 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1578 LQSAKARLENECKTLQQKVEILGELYQQKemalQKKLTQEEYERQEKEQKLSAADEKAVLAIEEVKVYKQRIQDMEEELQ 1657
Cdd:TIGR04523 354 SESENSEKQRELEEKQNEIEKLKKENQSY----KQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIE 429
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1201873520 1658 ----------KTERSYKNQIAAHEKKAHDNWLIARSAERALAEEKREAANLRQKLiEVNQKNI 1710
Cdd:TIGR04523 430 rlketiiknnSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNL-EQKQKEL 491
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1281-1706 |
5.97e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.02 E-value: 5.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1281 RIYQVTEKQLAEKIQNLLREKTEMLDKFSECDEKIKQAKESMKVAQEQKNILSDEIAGLKDTVKGLEETNHQLDDKIKSL 1360
Cdd:COG1196 235 RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRREL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1361 CTMLDTERKQNAKKQKKLSETQKSLEKLEEAFSMHSAELSEVQIALNESKLSEEKVKAELQHVQEENARLKKSKEQLLKE 1440
Cdd:COG1196 315 EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRA 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1441 AEgwserhtELTEQIKLYRKSQKDIEEALAYKENEIEvltncimqlkQLDTDSASEAKKDGEGHEwsTRDDLANGELPDN 1520
Cdd:COG1196 395 AA-------ELAAQLEELEEAEEALLERLERLEEELE----------ELEEALAELEEEEEEEEE--ALEEAAEEEAELE 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1521 EKMKTQIKQMMDASRVktmLSLVEEDRNSLQSKLNDEVAARQELEEQIKKLEHDScslQSAKARLENEcktLQQKVEILG 1600
Cdd:COG1196 456 EEEEALLELLAELLEE---AALLEAALAELLEELAEAAARLLLLLEAEADYEGFL---EGVKAALLLA---GLRGLAGAV 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1601 ELYQQKEMALQKKLtqEEYERQEKEQKLSAADEKAVLAIEEVKvykqriqdmEEELQKTERSYKNQIAAHEKKAHDNWLI 1680
Cdd:COG1196 527 AVLIGVEAAYEAAL--EAALAAALQNIVVEDDEVAAAAIEYLK---------AAKAGRATFLPLDKIRARAALAAALARG 595
|
410 420
....*....|....*....|....*.
gi 1201873520 1681 ARSAERALAEEKREAANLRQKLIEVN 1706
Cdd:COG1196 596 AIGAAVDLVASDLREADARYYVLGDT 621
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1276-1713 |
9.91e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 57.39 E-value: 9.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1276 LSVKSRIYQVTEKQLAEKIQNLLREKTEMLDKFSECDEKIKQAkeSMKVAQeqkniLSDEIAGLKDTVKGLEETNHQLDD 1355
Cdd:TIGR02169 376 VDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRL--SEELAD-----LNAAIAGIEAKINELEEEKEDKAL 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1356 KIKslctmldterkqnaKKQKKLSETQKSLEKLEEAFSMHSAELSEVQIALNESKLSEEKVKAELQHVQEENARLKKSKE 1435
Cdd:TIGR02169 449 EIK--------------KQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEE 514
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1436 QLLKEAEGwseRHTELTEQIKLYRKSQKDIEEALAYKENEIEVLTN-----CI------------------MQLKQLDTD 1492
Cdd:TIGR02169 515 VLKASIQG---VHGTVAQLGSVGERYATAIEVAAGNRLNNVVVEDDavakeAIellkrrkagratflplnkMRDERRDLS 591
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1493 SASEA-------------KKDGEGHEWSTRDDL------ANGELPDNEKMKTQIKQMMDASRVKTMLSLVEEDRNSLQSK 1553
Cdd:TIGR02169 592 ILSEDgvigfavdlvefdPKYEPAFKYVFGDTLvvedieAARRLMGKYRMVTLEGELFEKSGAMTGGSRAPRGGILFSRS 671
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1554 LNDEVaarQELEEQIKKLEHDSCSLQSAKARLENECKTLQQKVEIL----------GELYQQKEMALQKKLTQEEYERQE 1623
Cdd:TIGR02169 672 EPAEL---QRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDAsrkigeiekeIEQLEQEEEKLKERLEELEEDLSS 748
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1624 KEQKLSAADEKAVLAIEEVKVYKQRIQDMEEELQKTERSY--------KNQIAAHEKKAHDNWLIARSAERALAEEKREA 1695
Cdd:TIGR02169 749 LEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLshsripeiQAELSKLEEEVSRIEARLREIEQKLNRLTLEK 828
|
490
....*....|....*...
gi 1201873520 1696 ANLRQKLIEVNQKNIMLQ 1713
Cdd:TIGR02169 829 EYLEKEIQELQEQRIDLK 846
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1284-1661 |
1.34e-07 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 56.90 E-value: 1.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1284 QVTEKQLAEKIQNLLREKTEML-DKFSECDEKIKQAKESMKVAQEQKN----------------ILSDEIAGLKDTVKGL 1346
Cdd:TIGR00618 454 EKLEKIHLQESAQSLKEREQQLqTKEQIHLQETRKKAVVLARLLELQEepcplcgscihpnparQDIDNPGPLTRRMQRG 533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1347 EETNHQLDDKIKSLCTMLDTERKQNAKKQKKLSETQKSLEKLEEAFSMHSAELSEVQ------IALNESKLSEEKVKAEL 1420
Cdd:TIGR00618 534 EQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQnitvrlQDLTEKLSEAEDMLACE 613
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1421 QHVQEENARLK------------KSKEQLLKEAEGWSERHTELTEQIKLYRKSQKDIEE--------ALAYKENEIEVLT 1480
Cdd:TIGR00618 614 QHALLRKLQPEqdlqdvrlhlqqCSQELALKLTALHALQLTLTQERVREHALSIRVLPKellasrqlALQKMQSEKEQLT 693
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1481 NCIMQLKQLDTDSASEAKKDGEG----HEWSTRDDLANGELPDNEKMKTQIKQMMDASRVKTMLSLVEEDRNSlqsklND 1556
Cdd:TIGR00618 694 YWKEMLAQCQTLLRELETHIEEYdrefNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNN-----NE 768
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1557 EVAARQELEEQIKKLEHDSCSLQSAKARLENECKTLQQKVEilgelyQQKEMALQKKLTQEEYERQEKEQKLSAADEKAV 1636
Cdd:TIGR00618 769 EVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIG------QEIPSDEDILNLQCETLVQEEEQFLSRLEEKSA 842
|
410 420
....*....|....*....|....*...
gi 1201873520 1637 LAIE---EVKVYKQRIQDMEEELQKTER 1661
Cdd:TIGR00618 843 TLGEithQLLKYEECSKQLAQLTQEQAK 870
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1288-1477 |
2.19e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 55.54 E-value: 2.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1288 KQLAEKIQNLLREKTEMLDKFSECDEKIKQAKESMKVAQEQKNILSDEIAGLKDTVKGLE----ETNHQLDDKIKSLCTM 1363
Cdd:COG4942 37 AELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRaeleAQKEELAELLRALYRL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1364 LDTER----------KQNAKKQKKLSETQKSLEKLEEAFSMHSAELSEVQIALNESKLSEEKVKAELQHVQEENARLKKS 1433
Cdd:COG4942 117 GRQPPlalllspedfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAE 196
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1201873520 1434 KEQLLKEAEgwsERHTELTEQIKLYRKSQKDIEEALAYKENEIE 1477
Cdd:COG4942 197 RQKLLARLE---KELAELAAELAELQQEAEELEALIARLEAEAA 237
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1291-1489 |
2.31e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 55.16 E-value: 2.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1291 AEKIQNLLREKTEMLDKFSECDEKIKQAKESMKVAQEQKNILSDEIAGLKDTVKGLEETNHQLDDKIKSLCTMLDTERKQ 1370
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1371 NAKKQKKLSETQKSLEKLEE----AFSMHSAELSEVQIAL-------NESKLSEEKVKAELQHVQEENARLKKSKEQLLK 1439
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRqpplALLLSPEDFLDAVRRLqylkylaPARREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1440 EAEGWSERHTELTEQIKLYRKSQKDIEEALAYKENEIEVLTNCIMQLKQL 1489
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEAL 228
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1287-1700 |
2.41e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 56.30 E-value: 2.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1287 EKQLAEKIQNllrekTEMLDKFSECDEKIKQAKESMKVAQEQKNilSDEIAGLKDTVKGLEETNHQLDDKIKslctmldt 1366
Cdd:PTZ00121 1241 EAKKAEEERN-----NEEIRKFEEARMAHFARRQAAIKAEEARK--ADELKKAEEKKKADEAKKAEEKKKAD-------- 1305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1367 ERKQNAKKQKKLSETQKSLEKLEEAFSMHSAELSEVQIALNESKLSEEKVKAELQHVQEENARLKKSKEQLLKEAEGWSE 1446
Cdd:PTZ00121 1306 EAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKK 1385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1447 RHTELTEQIKLYRKSQKDIEEALAYKENEIEVLTNCIMQLKQLDTDSASEAKKDGEGhewSTRDDLANGELPDNEKMKTQ 1526
Cdd:PTZ00121 1386 KAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEE---AKKADEAKKKAEEAKKAEEA 1462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1527 IKQMMDASRVKTMLSLVEEDRNSLQSKLNDEVAARQELE-----------EQIKKLEHDSCSLQSAKARLENECKTLQQK 1595
Cdd:PTZ00121 1463 KKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEakkaaeakkkaDEAKKAEEAKKADEAKKAEEAKKADEAKKA 1542
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1596 VEI--LGELYQQKEMALQKKLTQEEYERQEKEQKLSAADEKAVL-AIEEVKVYKQRIQDMEEELQKTERSYKNQ---IAA 1669
Cdd:PTZ00121 1543 EEKkkADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAkKAEEARIEEVMKLYEEEKKMKAEEAKKAEeakIKA 1622
|
410 420 430
....*....|....*....|....*....|..
gi 1201873520 1670 HE-KKAHDNWLIARSAERALAEEKREAANLRQ 1700
Cdd:PTZ00121 1623 EElKKAEEEKKKVEQLKKKEAEEKKKAEELKK 1654
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1298-1691 |
2.57e-07 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 55.29 E-value: 2.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1298 LREKTEMLDKFSEcdEKIKQAKESMKVAQEQKNILSDEIAGLKDTVKGLEETnhqlddkikslctmLDTERKQNAKKQKK 1377
Cdd:COG4372 18 LRPKTGILIAALS--EQLRKALFELDKLQEELEQLREELEQAREELEQLEEE--------------LEQARSELEQLEEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1378 LSETQKSLEKLEEAFSMHSAELSEVQialneskLSEEKVKAELQHVQEENARLKKSKEQLlkeaegwSERHTELTEQIKL 1457
Cdd:COG4372 82 LEELNEQLQAAQAELAQAQEELESLQ-------EEAEELQEELEELQKERQDLEQQRKQL-------EAQIAELQSEIAE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1458 YRKSQKDIEEALAYKENEIEVLTNCIMQLKQLDTDSASEAKKdgeghewstrdDLANGELPDNEKMKTQIKQMMDASRVK 1537
Cdd:COG4372 148 REEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELL-----------KEANRNAEKEEELAEAEKLIESLPREL 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1538 TMLSLVEEDRNSLQSKLNDEVAARQELEEQIKKLEHDSCSLQSAKARLENECKTLQQKVEILGELYQQKEMALQKKLTQE 1617
Cdd:COG4372 217 AEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELK 296
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1201873520 1618 EYERQEKEQKLSAADEKAVLAIEEVKVYKQRIQDMEEELQKTERSYKNQIAAHEKKAHDNWLIARSAERALAEE 1691
Cdd:COG4372 297 LLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGVADG 370
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1284-1651 |
3.03e-07 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 55.80 E-value: 3.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1284 QVTEKQLAEKIQNLLREKTEMLDKFSECDEKIKQakesmkvaqeqkniLSDEIAGLKDTVKGLEETNHQLDDKIKSLCTM 1363
Cdd:TIGR04523 306 QDWNKELKSELKNQEKKLEEIQNQISQNNKIISQ--------------LNEQISQLKKELTNSESENSEKQRELEEKQNE 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1364 LDTERKQNAKKQKKLSETQKSLEKLEeafsmhsaelSEVQIALNESKLSEEKVKAelqhVQEENARLKKSKEQLLKEAEG 1443
Cdd:TIGR04523 372 IEKLKKENQSYKQEIKNLESQINDLE----------SKIQNQEKLNQQKDEQIKK----LQQEKELLEKEIERLKETIIK 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1444 WSERHTELTEQIKLYRKSQKDIEEALAYKENEIEVLTNCIMQLKQ-LDTDSASEAKKDGEGHEWSTRDDLANGELPDNEK 1522
Cdd:TIGR04523 438 NNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQnLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTK 517
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1523 MKTQIKQMMDA-----SRVKTMLSLVEEDRNSLQSKLNDEVAAR--QELEEQIKKLEHDSCSLQSAKARLENECKTLQQK 1595
Cdd:TIGR04523 518 KISSLKEKIEKlesekKEKESKISDLEDELNKDDFELKKENLEKeiDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKE 597
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1201873520 1596 VEILGELYQQKEMaLQKKLTQEEYERQEKEQKLSAADEKAVLAIEEVKVYKQRIQD 1651
Cdd:TIGR04523 598 KKDLIKEIEEKEK-KISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKE 652
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1287-1709 |
3.92e-07 |
|
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: 55.61 E-value: 3.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1287 EKQLAEKIQNLLREKTEMLDKFSECDEKIKQAKESMKVAQEQKNilSDEIAGLKDTVKGLEETNHQL----DDKIKSLCT 1362
Cdd:pfam12128 345 DQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQN--NRDIAGIKDKLAKIREARDRQlavaEDDLQALES 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1363 MLDTERKQ---NAKKQKKLSETQKSLEKLEEAFSMHSAELSEvQIALNESKL-----SEEKVKAELQHVQEENARLKKSK 1434
Cdd:pfam12128 423 ELREQLEAgklEFNEEEYRLKSRLGELKLRLNQATATPELLL-QLENFDERIerareEQEAANAEVERLQSELRQARKRR 501
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1435 EQ----LLKEAEGWSERHTELTE-QIKLYRKSQKDIE----EALAYKENEIEVLTNCIMQLKQLDTdSASEAKKDGEGHE 1505
Cdd:pfam12128 502 DQaseaLRQASRRLEERQSALDElELQLFPQAGTLLHflrkEAPDWEQSIGKVISPELLHRTDLDP-EVWDGSVGGELNL 580
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1506 WSTRDDLANGELPDNEKMKTQIKQMMDAsrvktmlslveedrnsLQSKLNDEVAARQELEEQI----KKLEHDSCSLQSA 1581
Cdd:pfam12128 581 YGVKLDLKRIDVPEWAASEEELRERLDK----------------AEEALQSAREKQAAAEEQLvqanGELEKASREETFA 644
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1582 KARLENECKTLQQkveiLGELYQQKEMALQKKLTQEEYERQEKEQKLSAadekavlaieEVKVYKQRIQDMEEELQKTER 1661
Cdd:pfam12128 645 RTALKNARLDLRR----LFDEKQSEKDKKNKALAERKDSANERLNSLEA----------QLKQLDKKHQAWLEEQKEQKR 710
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1201873520 1662 SYKNQIAAHEK---KAHDNWLIARSAERALAEEKREAanlRQKLIEVNQKN 1709
Cdd:pfam12128 711 EARTEKQAYWQvveGALDAQLALLKAAIAARRSGAKA---ELKALETWYKR 758
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1379-1696 |
4.72e-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: 55.07 E-value: 4.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1379 SETQKSLEKLEEAfsmhsaelsEVQIALNESKLSEekVKAELQHVQEEnaRLKKSKEQLLK----EAEGWserhtELTEQ 1454
Cdd:TIGR02169 170 RKKEKALEELEEV---------EENIERLDLIIDE--KRQQLERLRRE--REKAERYQALLkekrEYEGY-----ELLKE 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1455 IKLYRKSQKDIEEALAYKENEIEVLTNCIMQLKQldtdsASEAKKDgeghewsTRDDLAngelpdnekmkTQIKQMMD-- 1532
Cdd:TIGR02169 232 KEALERQKEAIERQLASLEEELEKLTEEISELEK-----RLEEIEQ-------LLEELN-----------KKIKDLGEee 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1533 ASRVKTMLSLVEEDRNSLQSKLNDEVAARQELEEQIKKLEHDSCSLQSAKARLENECKTLQQKVEILGELY---QQKEMA 1609
Cdd:TIGR02169 289 QLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYaelKEELED 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1610 LQKKLTQEEYERQEKEQKLSAADEKavlaIEEVKVYKQRIQDMEEELQKTERSYKNQIAAHEKKAHDnwliARSAERALA 1689
Cdd:TIGR02169 369 LRAELEEVDKEFAETRDELKDYREK----LEKLKREINELKRELDRLQEELQRLSEELADLNAAIAG----IEAKINELE 440
|
....*..
gi 1201873520 1690 EEKREAA 1696
Cdd:TIGR02169 441 EEKEDKA 447
|
|
| SH3_2 |
pfam07653 |
Variant SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in ... |
53-108 |
6.21e-07 |
|
Variant SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in signal transduction related to cytoskeletal organization. First described in the Src cytoplasmic tyrosine kinase. The structure is a partly opened beta barrel.
Pssm-ID: 429575 [Multi-domain] Cd Length: 54 Bit Score: 47.98 E-value: 6.21e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1201873520 53 RGKAMKDFQGPDCRFVNFKKGETVYVYYKLIGmstELWAGSIGSDFGYFPKDLLEI 108
Cdd:pfam07653 1 YGRVIFDYVGTDKNGLTLKKGDVVKVLGKDND---GWWEGETGGRVGLVPSTAVEE 53
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1715-1921 |
6.48e-07 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 54.94 E-value: 6.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1715 PLIVKPTPGRPDRQVPPRRvplsrdgsFGPSPVSGGNPSPTQMMEVPSRPLSAPQREGSRGEFGTvvDGPPAPRRPPELP 1794
Cdd:PHA03247 2554 PLPPAAPPAAPDRSVPPPR--------PAPRPSEPAVTSRARRPDAPPQSARPRAPVDDRGDPRG--PAPPSPLPPDTHA 2623
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1795 GRMSVPDLGPAVASLISSGPRTSSPATAKDRALSPKEPEAPCVTTDSPSSIEPATVTVGPKGPPSFPGTPVMTSPVMgpp 1874
Cdd:PHA03247 2624 PDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLTSLAD--- 2700
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1201873520 1875 ppppvnygpppaPFPGHYGPRPLPVPLVCGAPLP--PPAARDFLPGPPL 1921
Cdd:PHA03247 2701 ------------PPPPPPTPEPAPHALVSATPLPpgPAAARQASPALPA 2737
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1293-1727 |
7.13e-07 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 54.46 E-value: 7.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1293 KIQNLLREKTEMLDKFsecdeKIKQAKESMKVAQEQKNILSDEIAGLKDTVKGLEETNHQLDDKIKSLCTMLDTERKQNA 1372
Cdd:PRK04778 83 DIEEQLFEAEELNDKF-----RFRKAKHEINEIESLLDLIEEDIEQILEELQELLESEEKNREEVEQLKDLYRELRKSLL 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1373 KKQKKLSETQKSLEK-LEEAfsmhSAELSEVqIALNESKlSEEKVKAELQHVQEENARLKKSKEQ---LLKEAEgwserh 1448
Cdd:PRK04778 158 ANRFSFGPALDELEKqLENL----EEEFSQF-VELTESG-DYVEAREILDQLEEELAALEQIMEEipeLLKELQ------ 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1449 TELTEQIK-L---YRK--------SQKDIEEALAYKENEIEvltNCIMQLKQLDTDSASEAkkdgeghewstrddlange 1516
Cdd:PRK04778 226 TELPDQLQeLkagYRElveegyhlDHLDIEKEIQDLKEQID---ENLALLEELDLDEAEEK------------------- 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1517 lpdNEKMKTQIKQMMDAsrvktmlslveedrnslqskLNDEVAARQELEEQIKKlehdscsLQSAKARLENECKTLQQKV 1596
Cdd:PRK04778 284 ---NEEIQERIDQLYDI--------------------LEREVKARKYVEKNSDT-------LPDFLEHAKEQNKELKEEI 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1597 EILGELYQQKEMALQKkltQEEYERQEKEqkLSAADEKAVLAIEEVKVYKQRIQDMEEELQKTERsyknQIAAHEKKAHD 1676
Cdd:PRK04778 334 DRVKQSYTLNESELES---VRQLEKQLES--LEKQYDEITERIAEQEIAYSELQEELEEILKQLE----EIEKEQEKLSE 404
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1201873520 1677 NwLIARSAERALAEEKreAANLRQKLIEVnqKNIMLQRPLivkptPGRPDR 1727
Cdd:PRK04778 405 M-LQGLRKDELEAREK--LERYRNKLHEI--KRYLEKSNL-----PGLPED 445
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1720-2008 |
7.41e-07 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 54.94 E-value: 7.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1720 PTPGRPDRQVPPRRVPLSRDGSFGPSPVSggnpsptqmmevPSRPLSAPQREGSRGEFGTVVD--GPPAPRRPPELPGRM 1797
Cdd:PHA03247 2647 PPPERPRDDPAPGRVSRPRRARRLGRAAQ------------ASSPPQRPRRRAARPTVGSLTSlaDPPPPPPTPEPAPHA 2714
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1798 SVP--DLGPAVASLISSGPRT----SSPATAKDRAL--SPKEPEAPCVTTDSPSSIEPATVTVGPkgPPSFPGTPVMTSP 1869
Cdd:PHA03247 2715 LVSatPLPPGPAAARQASPALpaapAPPAVPAGPATpgGPARPARPPTTAGPPAPAPPAAPAAGP--PRRLTRPAVASLS 2792
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1870 VMGPPPPPPVNYGPPPAPFPG-------HYGPRPLPVPLVCGAPLPPPAARDFLPgPPLGMRDLPPGPLPPLpdprsyRR 1942
Cdd:PHA03247 2793 ESRESLPSPWDPADPPAAVLApaaalppAASPAGPLPPPTSAQPTAPPPPPGPPP-PSLPLGGSVAPGGDVR------RR 2865
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1201873520 1943 GPPHFRPPGPPGPRAYPPGPPLPPPASRdyaPSRNRDLPPAGPRDYPAGPPPPPAGSKDYTQPPAQ 2008
Cdd:PHA03247 2866 PPSRSPAAKPAAPARPPVRRLARPAVSR---STESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQ 2928
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1286-1596 |
7.90e-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: 54.69 E-value: 7.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1286 TEKQLAEKIQNLLREKTEMldKFSECDEKIKQAKESMKVAQEQKNILSDEIAGLKDTVKGLEETNHQLDDKIKSLCTMLD 1365
Cdd:TIGR02169 205 REREKAERYQALLKEKREY--EGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIK 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1366 --TERKQNAKkQKKLSETQKSLEKLEEAFSMHSAELSEVQIALNESKLSEEKVKAELQHVQEENARLKKSKEQLLKEAEG 1443
Cdd:TIGR02169 283 dlGEEEQLRV-KEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAE 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1444 WSERHTELTEQIKLYRKSQKDIEEALAYKENEIEVLTNCIMQLK-QLDTDSASEAKKDGEGHEwstrddlANGELPDNEK 1522
Cdd:TIGR02169 362 LKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKrELDRLQEELQRLSEELAD-------LNAAIAGIEA 434
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1201873520 1523 MKTQIKQMMDASRVKtmLSLVEEDRNSLQSKLNDEVAARQELEEQIKKLEHDSCSLQSAKARLENECKTLQQKV 1596
Cdd:TIGR02169 435 KINELEEEKEDKALE--IKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERV 506
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1712-1932 |
1.54e-06 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 53.79 E-value: 1.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1712 LQRPLIVKPTPG-RPDRQVPPRRVPLSRDGSFGPSPVSGGNPSPTQMMEVPSRPlSAPQREGSRgefgTVVDGPPA---P 1787
Cdd:PHA03247 2698 LADPPPPPPTPEpAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATP-GGPARPARP----PTTAGPPApapP 2772
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1788 RRPPELPGRMSVPdlgPAVASLISSGPRTSSPATAKDRALSPKEPEAPCVTTDSPSSIEPATVTVGPKGPPSFPG--TPV 1865
Cdd:PHA03247 2773 AAPAAGPPRRLTR---PAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGppPPS 2849
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1201873520 1866 MTSPVMGPPPPPPVNYGPPPAPFPGHYGPRPLPVPLVCGAPLPPPAARDFLPGPPLGMRDLPPGPLP 1932
Cdd:PHA03247 2850 LPLGGSVAPGGDVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPP 2916
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1543-1704 |
1.56e-06 |
|
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: 53.52 E-value: 1.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1543 VEEDRNSLQSKLNDEVAARQELEEQIKKLEHDSCSLQSAKARLENECKTLQQKVEILG---ELYQQKEMALQKKLTQEEY 1619
Cdd:TIGR02168 244 LQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEqqkQILRERLANLERQLEELEA 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1620 ERQEKEQKLSAADEKAVLAIEEVKVYKQRIQDMEEELQKTERSYKNQIAAHEKKahDNWLIARSAERALAEEKREAANLR 1699
Cdd:TIGR02168 324 QLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEEL--EEQLETLRSKVAQLELQIASLNNE 401
|
....*
gi 1201873520 1700 QKLIE 1704
Cdd:TIGR02168 402 IERLE 406
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1276-1502 |
1.82e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 53.10 E-value: 1.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1276 LSVKSRIYQVTEKQLAEKIQNLLREKTEMLDKFSECDEKIKQAKESMKVAQEQKNILSDEIAGLKDTVKGLEETNHQLDD 1355
Cdd:TIGR04523 396 LESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSR 475
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1356 KIKSLCTMLDTERKQNAKKQKKLSETQKSLEKLEEAFSMHSAELSEvqIALNESKLSEEKVKAELQHVQEENARLKK--- 1432
Cdd:TIGR04523 476 SINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISS--LKEKIEKLESEKKEKESKISDLEDELNKDdfe 553
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1201873520 1433 -SKEQLLKEAEGWSERHTELTEQIKLYRKSQKDIEEALAYKENEIEVLTNCI----MQLKQLdTDSASEAKKDGE 1502
Cdd:TIGR04523 554 lKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIeekeKKISSL-EKELEKAKKENE 627
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1277-1625 |
1.97e-06 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 53.20 E-value: 1.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1277 SVKSRIYQVTEKQLAEkiqnlLREKTEMLDKFSECDEKIKQAKESM-KVAQE----------QKNILSDEIAGLKDTVKG 1345
Cdd:pfam15921 437 AMKSECQGQMERQMAA-----IQGKNESLEKVSSLTAQLESTKEMLrKVVEEltakkmtlesSERTVSDLTASLQEKERA 511
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1346 LEETNHQL--------------------DDKIKSLCTMLDTERKQNAKKQKKLSETQKSLEKLEEAFSMH---------- 1395
Cdd:pfam15921 512 IEATNAEItklrsrvdlklqelqhlkneGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHgrtagamqve 591
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1396 ----SAELSEVQIALNESKLSEEKVKA------------ELQHVQEENA---------RLKKSKEQLLKEAEGWSERHTE 1450
Cdd:pfam15921 592 kaqlEKEINDRRLELQEFKILKDKKDAkirelearvsdlELEKVKLVNAgserlravkDIKQERDQLLNEVKTSRNELNS 671
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1451 LTEQIKLYRKSQKDieealayKENEIEVLTNCI-MQLKQldtdSASEAKKdgeghewsTRDDLANGELPDNEKMKTQIKQ 1529
Cdd:pfam15921 672 LSEDYEVLKRNFRN-------KSEEMETTTNKLkMQLKS----AQSELEQ--------TRNTLKSMEGSDGHAMKVAMGM 732
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1530 MMDASRVKTMLSLVEEDRNSLQSKLNDEVAARQELEEQIKKLEHDSCSLQSAKARLENECKTLQQKVEILGELYQQKEMA 1609
Cdd:pfam15921 733 QKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVA 812
|
410 420
....*....|....*....|.
gi 1201873520 1610 LQKKL-----TQEEYERQEKE 1625
Cdd:pfam15921 813 LDKASlqfaeCQDIIQRQEQE 833
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1285-1658 |
2.75e-06 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 52.16 E-value: 2.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1285 VTEKQLAEkIQNLLREKTEMLDKFsecdeKIKQAKESMKVAQEQKNILSDEIAGLKDTVKGLEETNHQLDDKIKSLCTML 1364
Cdd:pfam06160 57 IVTKSLPD-IEELLFEAEELNDKY-----RFKKAKKALDEIEELLDDIEEDIKQILEELDELLESEEKNREEVEELKDKY 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1365 DTERKQNAKKQKKLSETQKSLEK----LEEAFSMHSaELSEVQialnesklSEEKVKAELQHVQEENARLKKSKEQ---L 1437
Cdd:pfam06160 131 RELRKTLLANRFSYGPAIDELEKqlaeIEEEFSQFE-ELTESG--------DYLEAREVLEKLEEETDALEELMEDippL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1438 LKEAEgwserhTELTEQIK----LYRKSQK--------DIEEALAYKENEIEvltNCIMQLKQLDTDSASEAKKDGEG-- 1503
Cdd:pfam06160 202 YEELK------TELPDQLEelkeGYREMEEegyalehlNVDKEIQQLEEQLE---ENLALLENLELDEAEEALEEIEEri 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1504 --------HEWSTRDDLangelpdnEKMKTQIKQMMDASRVKTMLSLVEEDRNSLQSKLNDEVAAR-QELEEQIKKLEHD 1574
Cdd:pfam06160 273 dqlydlleKEVDAKKYV--------EKNLPEIEDYLEHAEEQNKELKEELERVQQSYTLNENELERvRGLEKQLEELEKR 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1575 scsLQSAKARLENECKTLQQKVEILGELYQQKEmALQKKltQEEYerQEKEQKLSaADEKAvlAIEEVKVYKQRIQDMEE 1654
Cdd:pfam06160 345 ---YDEIVERLEEKEVAYSELQEELEEILEQLE-EIEEE--QEEF--KESLQSLR-KDELE--AREKLDEFKLELREIKR 413
|
....
gi 1201873520 1655 ELQK 1658
Cdd:pfam06160 414 LVEK 417
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
378-879 |
2.96e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.84 E-value: 2.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 378 EYVNGATELynqRDNEEERDSDALITKdafSENKKSGDSVTTdmfESEETKEKRDEVmpvsKREAPAATQLDDLSEELIG 457
Cdd:PTZ00121 1287 EEKKKADEA---KKAEEKKKADEAKKK---AEEAKKADEAKK---KAEEAKKKADAA----KKKAEEAKKAAEAAKAEAE 1353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 458 RESVDAGDPDSKEKTNKTEQFEEQLMTD------ETVLHTKELKSTTVPDPRvlpgPGDDLKFKSFVESKQDALSPPGGD 531
Cdd:PTZ00121 1354 AAADEAEAAEEKAEAAEKKKEEAKKKADaakkkaEEKKKADEAKKKAEEDKK----KADELKKAAAAKKKADEAKKKAEE 1429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 532 MNKSPggvplAEMEKEKEKFEDDTLKESSESNLKHRKLWEKMKEKGKAKYEPSGDVPAKPVEDVQNASQSDAGDTDLLKD 611
Cdd:PTZ00121 1430 KKKAD-----EAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKK 1504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 612 KLEEGMPALE---------REILRHEEDLEQTGEAD--------HENQKPISVKKEPEIKRGNLKETPANEGDPSHRGA- 673
Cdd:PTZ00121 1505 AAEAKKKADEakkaeeakkADEAKKAEEAKKADEAKkaeekkkaDELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAe 1584
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 674 ----AEQPRPWENETEY-SEADVKEELSRNLGKMTIFEESIEKSSPEEKSKSTAPNTNAENSTQQGTVHTDNEDSG---R 745
Cdd:PTZ00121 1585 eakkAEEARIEEVMKLYeEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKikaA 1664
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 746 NLGTNSAREKTLRLELQSEEPDAEGdpdlKQEEELLEDENAASAKLLQARLANVQGNAQTIKSTNPELEVLSEAVSGTAN 825
Cdd:PTZ00121 1665 EEAKKAEEDKKKAEEAKKAEEDEKK----AAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAE 1740
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1201873520 826 PTYETGEETNSFSEEAKKISRVQDAQETGNKEVDEP----VSEDSKLDEIEHVMEDDK 879
Cdd:PTZ00121 1741 EDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEkeavIEEELDEEDEKRRMEVDK 1798
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1286-1708 |
3.03e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 52.42 E-value: 3.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1286 TEKQLAEKIQNLLREKTEMLDKFSECDEKIKQAKESMKVAQEQKNILSDEIAGLKDTVKGLEETNHQLDDKIKSLCTMLD 1365
Cdd:pfam05483 367 TEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQ 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1366 TERKQNAKKQKKLSETQKS----LEKLEEAFS-MHSAELSEVQIALNESKLSEEKVKA---------ELQHVQEENARLK 1431
Cdd:pfam05483 447 AREKEIHDLEIQLTAIKTSeehyLKEVEDLKTeLEKEKLKNIELTAHCDKLLLENKELtqeasdmtlELKKHQEDIINCK 526
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1432 KSKEQLLKEAEGWSERHTELTEQIKLYRKSqkdieeaLAYKENEIEVltncimqlkQLDTdsaSEAKKDGEGHEWSTRDD 1511
Cdd:pfam05483 527 KQEERMLKQIENLEEKEMNLRDELESVREE-------FIQKGDEVKC---------KLDK---SEENARSIEYEVLKKEK 587
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1512 LANGELPDNEKMKTQIKqmmdaSRVKTMLSLVEEDRnSLQSKLNDEVAARQELEEQIKKLEHDscsLQSAKARLENECKT 1591
Cdd:pfam05483 588 QMKILENKCNNLKKQIE-----NKNKNIEELHQENK-ALKKKGSAENKQLNAYEIKVNKLELE---LASAKQKFEEIIDN 658
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1592 LQQKVEIlgelyqqkemalqKKLTQEEYeRQEKEQKLSAADEKAVLAIEEVKVYKQRIQDMEEELQKTERSYKNQIaaHE 1671
Cdd:pfam05483 659 YQKEIED-------------KKISEEKL-LEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKII--EE 722
|
410 420 430
....*....|....*....|....*....|....*....
gi 1201873520 1672 KKAHDNWLIARSAERALAEE--KREAANLRQKLIEVNQK 1708
Cdd:pfam05483 723 RDSELGLYKNKEQEQSSAKAalEIELSNIKAELLSLKKQ 761
|
|
| Drf_FH1 |
pfam06346 |
Formin Homology Region 1; This region is found in some of the Diaphanous related formins (Drfs) ... |
1784-1923 |
3.03e-06 |
|
Formin Homology Region 1; This region is found in some of the Diaphanous related formins (Drfs). It consists of low complexity repeats of around 12 residues.
Pssm-ID: 461881 [Multi-domain] Cd Length: 157 Bit Score: 49.10 E-value: 3.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1784 PPaprrPPELPGRMSVPDLGPAV-----ASLISSGPRTSSPATAKDRALSPKePEAPCVTTDSPSSIEPATVTVGPkgPP 1858
Cdd:pfam06346 1 PP----PPPLPGDSSTIPLPPGAciptpPPLPGGGGPPPPPPLPGSAAIPPP-PPLPGGTSIPPPPPLPGAASIPP--PP 73
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1201873520 1859 SFPGTPVMTSPvmgppppppvnygpppAPFPGHYG--PRPLPVPLVCGAPLPPPAardfLPGPPlGM 1923
Cdd:pfam06346 74 PLPGSTGIPPP----------------PPLPGGAGipPPPPPLPGGAGVPPPPPP----LPGGP-GI 119
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1368-1708 |
3.87e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.45 E-value: 3.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1368 RKQNAKKQKKLSETQKSLEKLEEAFSMHSAELSEVQIALNESKLSEEKVKAELQHVQEENARLKKS-KEQLLKEAEgwSE 1446
Cdd:PTZ00121 1104 KKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEArKAEDAKKAE--AA 1181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1447 RHTELTEQIKLYRKSQ--KDIEEALAYKE-NEIEVLTNCIMQLKQLDTDSASEAKKDGEGHEWSTrddlangELPDNEKM 1523
Cdd:PTZ00121 1182 RKAEEVRKAEELRKAEdaRKAEAARKAEEeRKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAE-------EERNNEEI 1254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1524 KTQIKQMMDASRVKTMLSLVEEDRNSLQSKLNDEVAARQELEEQIKKLEHDSCSLQSAKARLENECKTLQQKVEILGELY 1603
Cdd:PTZ00121 1255 RKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAA 1334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1604 QQKEMALQKKLTQEEYERQEKEQKLSAADEKA---VLAIEEVKVYKQRIQDMEEELQKTERSYKNqiaAHEKKAHDNWLI 1680
Cdd:PTZ00121 1335 KKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAeaaEKKKEEAKKKADAAKKKAEEKKKADEAKKK---AEEDKKKADELK 1411
|
330 340
....*....|....*....|....*...
gi 1201873520 1681 ARSAERALAEEKREAANLRQKLIEVNQK 1708
Cdd:PTZ00121 1412 KAAAAKKKADEAKKKAEEKKKADEAKKK 1439
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1284-1707 |
4.78e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 51.65 E-value: 4.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1284 QVTEKQlaEKIQNLLREKTEMLDKFSECDEKIKQAKESMKVAQEQKNILSDEIAGLKDTVKGLEETNHQLDDKI----KS 1359
Cdd:pfam05483 248 QITEKE--NKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLqiatKT 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1360 LCTMldTERKqnakkqkklsETQksLEKLEEAFSMHSAELSEVQIALNESklsEEKVKAELQhvqeenaRLKKSKEQLLK 1439
Cdd:pfam05483 326 ICQL--TEEK----------EAQ--MEELNKAKAAHSFVVTEFEATTCSL---EELLRTEQQ-------RLEKNEDQLKI 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1440 EAEGWSERHTELTEQIKLYRKSQKDIEE---------ALAYKENEIEVLTNCIMQLKQLDTDSASEAKKdgEGHEWSTRD 1510
Cdd:pfam05483 382 ITMELQKKSSELEEMTKFKNNKEVELEElkkilaedeKLLDEKKQFEKIAEELKGKEQELIFLLQAREK--EIHDLEIQL 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1511 DLANGELPDNEKMKTQIKQMMDASRVKTMLSLVEEDRNSLQSKLNDEVAARQELEeqIKKLEHDSCSLQSAKARLENECK 1590
Cdd:pfam05483 460 TAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLE--LKKHQEDIINCKKQEERMLKQIE 537
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1591 TLQQK-------VEILGELYQQKEMALQKKLTQEEYERQEKEQKLSAADEKAVLAIEEVKVYKQRIQDME---EELQKTE 1660
Cdd:pfam05483 538 NLEEKemnlrdeLESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNkniEELHQEN 617
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1661 RSYKNQIAAHEKKAHDNWLIARSAERALAEEKR---EAANLRQKLIEVNQ 1707
Cdd:pfam05483 618 KALKKKGSAENKQLNAYEIKVNKLELELASAKQkfeEIIDNYQKEIEDKK 667
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1277-1670 |
4.96e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.99 E-value: 4.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1277 SVKSRIYQVTEKQLAEKIQNLLREKTEMLDKFSECDEKIKQAKEsmKVAQEQKNILSDEIAGLKDTVKGLEETNHQLDDK 1356
Cdd:PRK03918 376 RLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKK--EIKELKKAIEELKKAKGKCPVCGRELTEEHRKEL 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1357 IKSLCTMLDTERKQNAKKQKKLSETQKSLEKLEEAFSMHSAELSEVQIALNESKLSEEKVKAELQHVQEENARLKKSKEQ 1436
Cdd:PRK03918 454 LEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEK 533
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1437 LLKeAEGWSERHTELTEQIKLYRKSQKDIEEALAYKENEievLTNCIMQLKQLDTDSASEAKKdgeghewstrddlange 1516
Cdd:PRK03918 534 LIK-LKGEIKSLKKELEKLEELKKKLAELEKKLDELEEE---LAELLKELEELGFESVEELEE----------------- 592
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1517 lpdnekmktQIKQMMDASRVKTMLSLVEEDRNSLQSKLNDEvaaRQELEEQIKKLEHDSCSLQSAKARLEN-ECKTLQQK 1595
Cdd:PRK03918 593 ---------RLKELEPFYNEYLELKDAEKELEREEKELKKL---EEELDKAFEELAETEKRLEELRKELEElEKKYSEEE 660
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1596 VEILGELYQQKEMALQKKLTQ-EEYERQEKEQKLSAADEKAVLaiEEVKVYKQRIQDME------EELQKTERSYKNQIA 1668
Cdd:PRK03918 661 YEELREEYLELSRELAGLRAElEELEKRREEIKKTLEKLKEEL--EEREKAKKELEKLEkalervEELREKVKKYKALLK 738
|
..
gi 1201873520 1669 AH 1670
Cdd:PRK03918 739 ER 740
|
|
| EzrA |
COG4477 |
Septation ring formation regulator EzrA [Cell cycle control, cell division, chromosome ... |
1373-1698 |
5.10e-06 |
|
Septation ring formation regulator EzrA [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443574 [Multi-domain] Cd Length: 567 Bit Score: 51.38 E-value: 5.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1373 KKQKKLSETQKSLEKLEEafsmhsaELSEVQIALNESKLSEEKVKAELQHVQEenaRLKKSKEQLLKEAEGWSERHTELT 1452
Cdd:COG4477 101 KAKKALDEIEQLLDEIEE-------EIEEILEELEELLESEEKNREEIEELKE---KYRELRKTLLAHRHSFGPAAEELE 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1453 EQIKLY---------RKSQKDIEEA---LAYKENEIEVLTNCI----MQLKQLDTDSASEAKKDGEGHEWSTRD--DLAN 1514
Cdd:COG4477 171 KQLEELepefeefeeLTESGDYLEAreiLEQLEEELNALEELMeeipPLLKELQTELPDQLEELKSGYREMKEQgyVLEH 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1515 GELPDN-EKMKTQIKQMMDA------SRVKTMLSLVEEDRNSLQSKLNDEVAARQELEEQIKKLEHDscsLQSAKARLEN 1587
Cdd:COG4477 251 LNIEKEiEQLEEQLKEALELleeldlDEAEEELEEIEEEIDELYDLLEKEVEAKKYVDKNQEELEEY---LEHLKEQNRE 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1588 ecktLQQKVEILGELYQ--QKEMALQKKLTQE--EYERQEKEQKLSAADEKAV--LAIEEVKVYKQRIQDMEEELQKTER 1661
Cdd:COG4477 328 ----LKEEIDRVQQSYRlnENELEKVRNLEKQieELEKRYDEIDERIEEEKVAysELQEELEEIEEQLEEIEEEQEEFSE 403
|
330 340 350
....*....|....*....|....*....|....*....
gi 1201873520 1662 SYKNqIAAHEKKAHDNwliARSAERALAEEKR--EAANL 1698
Cdd:COG4477 404 KLKS-LRKDELEAREK---LDELKKKLREIKRrlEKSNL 438
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
1725-1911 |
5.37e-06 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 51.71 E-value: 5.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1725 PDRQVPPRRVPLSRDGSFGPSPVSGGNPSPTqmmEVPSRPLSAPqREGSRGEFGTVVDGPPAPRRPPELPGRMSVPDLGP 1804
Cdd:PHA03307 61 ACDRFEPPTGPPPGPGTEAPANESRSTPTWS---LSTLAPASPA-REGSPTPPGPSSPDPPPPTPPPASPPPSPAPDLSE 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1805 AVASLISSGPR--TSSPATAKDRALSPkEPEAPCVTTDSPSSIEPATVTVGPKGPPSFPGTPvmtspvmgppppppvnyg 1882
Cdd:PHA03307 137 MLRPVGSPGPPpaASPPAAGASPAAVA-SDAASSRQAALPLSSPEETARAPSSPPAEPPPST------------------ 197
|
170 180
....*....|....*....|....*....
gi 1201873520 1883 pppAPFPGHYGPRPLPVPLVCGAPLPPPA 1911
Cdd:PHA03307 198 ---PPAAASPRPPRRSSPISASASSPAPA 223
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1284-1632 |
9.55e-06 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 50.94 E-value: 9.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1284 QVTEKQLAEKIQNLLREK-----TEMLDKFSECdEKIKQAKESMKVAQE-QKNILSDEIAGLKDTVKGLEETNHQLDDKI 1357
Cdd:pfam01576 167 NLAEEEEKAKSLSKLKNKheamiSDLEERLKKE-EKGRQELEKAKRKLEgESTDLQEQIAELQAQIAELRAQLAKKEEEL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1358 KSLCTMLDTERKQNAKKQKKLSETQKSLEKLEEAFSMHSA----------ELSEVQIALN---ESKLSEEKVKAELQHVQ 1424
Cdd:pfam01576 246 QAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAarnkaekqrrDLGEELEALKtelEDTLDTTAAQQELRSKR 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1425 E-ENARLKKSKEQLLKEAEG----WSERHT----ELTEQIKLYRKSQKDIEEALAYKENEIEVLTNCIMQLKQLDTDSAS 1495
Cdd:pfam01576 326 EqEVTELKKALEEETRSHEAqlqeMRQKHTqaleELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEH 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1496 EAKK-DGEGHEWSTR---DDLANGELPD----------------NEKMKTQIKQMMDASRVK------------------ 1537
Cdd:pfam01576 406 KRKKlEGQLQELQARlseSERQRAELAEklsklqselesvssllNEAEGKNIKLSKDVSSLEsqlqdtqellqeetrqkl 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1538 ---TMLSLVEEDRNSLQSKLNDEVAARQELEEQI-----------KKLEHDSCSLQSakarLENECKTLQQKVEILGELY 1603
Cdd:pfam01576 486 nlsTRLRQLEDERNSLQEQLEEEEEAKRNVERQLstlqaqlsdmkKKLEEDAGTLEA----LEEGKKRLQRELEALTQQL 561
|
410 420
....*....|....*....|....*....
gi 1201873520 1604 QQKEMALQKKLTQEEYERQEKEQKLSAAD 1632
Cdd:pfam01576 562 EEKAAAYDKLEKTKNRLQQELDDLLVDLD 590
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1291-1716 |
1.15e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 50.74 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1291 AEKIQNLLREKTEMLDKFSECDEKIkqAKESMKVAQEQKNILSDEIAGLKDTVKGLEETNHQLddkikslcTMLDTERKQ 1370
Cdd:TIGR00618 185 EFAKKKSLHGKAELLTLRSQLLTLC--TPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYL--------TQKREAQEE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1371 NAKKQKKLSETQKSLEKLEEafsmHSAELSEVQIALNESKlSEEKVKAELQHV-------QEENARLKKSKEQLLKEAEg 1443
Cdd:TIGR00618 255 QLKKQQLLKQLRARIEELRA----QEAVLEETQERINRAR-KAAPLAAHIKAVtqieqqaQRIHTELQSKMRSRAKLLM- 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1444 wserHTELTEQIKLYRKSQKDIEEALAYKENEIEVLTNcimqlKQLDTDSASEAKKDGEGHEWSTRDDLANgeLPDNEKM 1523
Cdd:TIGR00618 329 ----KRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHE-----VATSIREISCQQHTLTQHIHTLQQQKTT--LTQKLQS 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1524 KTQIKQMMDASRVKTMLSLVEedRNSLQSKLndeVAARQELEEQIKKLE----HDSCSLQSAKAR----------LENEC 1589
Cdd:TIGR00618 398 LCKELDILQREQATIDTRTSA--FRDLQGQL---AHAKKQQELQQRYAElcaaAITCTAQCEKLEkihlqesaqsLKERE 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1590 KTLQQKVEILGELYQQKEMALQKKLTQEEYERQ------EKEQKLSAADEKAVLA------IEEVKVYKQRIQDMEEELQ 1657
Cdd:TIGR00618 473 QQLQTKEQIHLQETRKKAVVLARLLELQEEPCPlcgsciHPNPARQDIDNPGPLTrrmqrgEQTYAQLETSEEDVYHQLT 552
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1201873520 1658 kTERSYKNQIAAHEKKAHDNWLIARSAERALAEEKREAANLRQKLIEVNQKNIMLQRPL 1716
Cdd:TIGR00618 553 -SERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDML 610
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1287-1661 |
1.43e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 50.56 E-value: 1.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1287 EKQLAEkiQNLLREKTEmLDKFSeCDEKIKQAKESMKVAQEQKNILSDEIAGLKDTVKGLEETNHQLDDKIKSLCTMLDT 1366
Cdd:pfam01576 109 EEQLDE--EEAARQKLQ-LEKVT-TEAKIKKLEEDILLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNK 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1367 ERKQNAKKQKKLSETQKSLEKLEEAFSMHSAELSEVQIALNESKLSEEKVKAELQHVQEE----NARLKKS---KEQLLK 1439
Cdd:pfam01576 185 HEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEElqaaLARLEEEtaqKNNALK 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1440 ---EAEGWSERHTELTEQIKLYR----KSQKDIEEALAYKENEIEvltncimqlKQLDTDSASE---AKKDGEGHEWSTr 1509
Cdd:pfam01576 265 kirELEAQISELQEDLESERAARnkaeKQRRDLGEELEALKTELE---------DTLDTTAAQQelrSKREQEVTELKK- 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1510 ddlangELPDNEKMKTQIKQMMDASRVKTMLSLVEEDRNSLQSKLNDEvAARQELEEQIKKLEHDSCSLQSAKARLENEC 1589
Cdd:pfam01576 335 ------ALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLE-KAKQALESENAELQAELRTLQQAKQDSEHKR 407
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1201873520 1590 KTLQQKVEILGELYQQKEMA---LQKKLTQEEYERQEKEQKLSAADEKAVLAIEEVKVYKQRIQDMEEELQKTER 1661
Cdd:pfam01576 408 KKLEGQLQELQARLSESERQraeLAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETR 482
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1313-1700 |
1.94e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.14 E-value: 1.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1313 EKIKQAKESMKVAQEQK--NILSDEIAGLKDTVKGLEETNHQLDDKIKSLCTMLDTERKQNAKKQKKLSETQKSLEKLEE 1390
Cdd:PTZ00121 1197 EDARKAEAARKAEEERKaeEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEE 1276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1391 AFSMHSAELSEVQIALNESKLSEEKVKAELQHVQEENAR----LKKSKEQLLKEAEGWSERHTELTEQIKLYRKSQKDIE 1466
Cdd:PTZ00121 1277 ARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKkadeAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAA 1356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1467 EALAYKENEievltncimqlKQLDTDSASEAKKDGeghewstrddlangelpDNEKMKTQIKQMMDASRVKTmlslvEED 1546
Cdd:PTZ00121 1357 DEAEAAEEK-----------AEAAEKKKEEAKKKA-----------------DAAKKKAEEKKKADEAKKKA-----EED 1403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1547 RNSLQsKLNDEVAARQELEEQIKKLEHDSCSLQS-AKARLENECKTLQQKVEILGELYQQKEMALQKKLTQEEYERQEKE 1625
Cdd:PTZ00121 1404 KKKAD-ELKKAAAAKKKADEAKKKAEEKKKADEAkKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEA 1482
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1201873520 1626 QKLSAADEKAvlaiEEVKVYKQRIQDMEEELQKTERSYKnqiaAHEKKAHDNWLIARSAERA----LAEEKREAANLRQ 1700
Cdd:PTZ00121 1483 KKADEAKKKA----EEAKKKADEAKKAAEAKKKADEAKK----AEEAKKADEAKKAEEAKKAdeakKAEEKKKADELKK 1553
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1513-1749 |
2.99e-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: 48.61 E-value: 2.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1513 ANGELPDNEKMKTQIKQMMDASRVKtmLSLVEEDRNSLQSKLNDEVAARQELEEQIKKLEHDSCSLQSAKARLENECKTL 1592
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKE--LAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1593 QQKVEILGELYQQKEMALQKK---------LTQEE----YERQEKEQKLSAADEKavlAIEEVKVYKQRIQDMEEELQKT 1659
Cdd:COG4942 96 RAELEAQKEELAELLRALYRLgrqpplallLSPEDfldaVRRLQYLKYLAPARRE---QAEELRADLAELAALRAELEAE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1660 ERSYKNQIAAHEKKAHDNWLIARSAERALAEEKREAANLRQKLIEVNQKNIMLQRpLIVKPTPGRPDRQVPPRRVPLSRD 1739
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEA-LIARLEAEAAAAAERTPAAGFAAL 251
|
250
....*....|
gi 1201873520 1740 GSFGPSPVSG 1749
Cdd:COG4942 252 KGKLPWPVSG 261
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1391-1635 |
3.34e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.29 E-value: 3.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1391 AFSMHSAELSEVQIALNESKLSEekVKAELQHVQEENARLKKSKEQLLKEAEGWSERHTELTEQIKlyrKSQKDIEEAla 1470
Cdd:COG3883 5 ALAAPTPAFADPQIQAKQKELSE--LQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEID---KLQAEIAEA-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1471 ykENEIEVLTNcimQLKQLdtdsASEAKKDGEGHewSTRDDLANGELPDN--EKMkTQIKQMMDASR-----VKTMLSLV 1543
Cdd:COG3883 78 --EAEIEERRE---ELGER----ARALYRSGGSV--SYLDVLLGSESFSDflDRL-SALSKIADADAdlleeLKADKAEL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1544 EEDRNSLQSKLNDEVAARQELEEQIKKLEHDSCSLQSAKARLENECKTLQQKVEILGELYQQKEMALQKKLTQEEYERQE 1623
Cdd:COG3883 146 EAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAA 225
|
250
....*....|..
gi 1201873520 1624 KEQKLSAADEKA 1635
Cdd:COG3883 226 AAAAAAAAAAAA 237
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1274-1705 |
3.37e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 49.27 E-value: 3.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1274 TCLSVKSRIYQvTEKQLAE---KIQNLLRE-KTEMLDKFSECDEKIKQAKESMKVAQEQKNILSDEIAGLKDtvkgLEET 1349
Cdd:TIGR00606 678 SCCPVCQRVFQ-TEAELQEfisDLQSKLRLaPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPE----LRNK 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1350 NHQLDDKIKslctmldtERKQNAKKQKKLSETQKSLEKLEEAFSMHSAELSEVQIALNESKLSEEKVKAELQHVQeenar 1429
Cdd:TIGR00606 753 LQKVNRDIQ--------RLKNDIEEQETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGSD----- 819
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1430 LKKSKEQLLKEAEGWSERHTELTEQIKLYRKSQKDIEEA---LAYKENEIEV----LTNCIMQLKQLDTDSASEAKKDGE 1502
Cdd:TIGR00606 820 LDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQiqhLKSKTNELKSeklqIGTNLQRRQQFEEQLVELSTEVQS 899
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1503 GHewSTRDDLANGELPDNE-KMKTQIKQMMDASRVKTMLSLVEEDRNSLQSKLNDEVAARQELEEQIKK-----LEHDSC 1576
Cdd:TIGR00606 900 LI--REIKDAKEQDSPLETfLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDgkddyLKQKET 977
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1577 SLQSAKARLEnECKTLQQKV-EILGELYQ------QKEMALQKKLTQEEYERQEKEQKLSAADEKAVLAIEEVKVYKQRI 1649
Cdd:TIGR00606 978 ELNTVNAQLE-ECEKHQEKInEDMRLMRQdidtqkIQERWLQDNLTLRKRENELKEVEEELKQHLKEMGQMQVLQMKQEH 1056
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1201873520 1650 QDMEEELQKTERSYkNQIAAHEKKAHDNWLIARsAERALAEEKREAANLRQKLIEV 1705
Cdd:TIGR00606 1057 QKLEENIDLIKRNH-VLALGRQKGYEKEIKHFK-KELREPQFRDAEEKYREMMIVM 1110
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1547-1708 |
4.63e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.47 E-value: 4.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1547 RNSLQSKLNDEVAARQELEEQIKKLEHDscsLQSAKARLENecktLQQKVEIL-----GELYQQKEMALQKKLTQEEYER 1621
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKE---LEEAEAALEE----FRQKNGLVdlseeAKLLLQQLSELESQLAEARAEL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1622 QEKEQKLSAADEK---------AVLAIEEVKVYKQRIQDMEEELQKTERSYKNQ----IAAHEKKAHDNWLIARSAERAL 1688
Cdd:COG3206 236 AEAEARLAALRAQlgsgpdalpELLQSPVIQQLRAQLAELEAELAELSARYTPNhpdvIALRAQIAALRAQLQQEAQRIL 315
|
170 180
....*....|....*....|
gi 1201873520 1689 AEEKREAANLRQKLIEVNQK 1708
Cdd:COG3206 316 ASLEAELEALQAREASLQAQ 335
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1291-1571 |
4.81e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.76 E-value: 4.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1291 AEKIQNLLREKTEMLDKFSECDEKIKQAKESMKVAQEQKNILS--DEIAGLKDTVKGLEETNHQLDDKIKSL---CTMLD 1365
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQrlAEYSWDEIDVASAEREIAELEAELERLdasSDDLA 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1366 TERKQNAKKQKKLSETQKSLEKLEEAFSMHSAELSEVQIALNEskLSEEKVKAELQHVQEENARLKKSKEQLLKEaegws 1445
Cdd:COG4913 689 ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDE--LQDRLEAAEDLARLELRALLEERFAAALGD----- 761
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1446 ERHTELTEQIklyRKSQKDIEEALAYKENEIEvltNCIMQLKQLDTDSASEAKKDGEG-HEWSTR-DDLANGELPDNE-K 1522
Cdd:COG4913 762 AVERELRENL---EERIDALRARLNRAEEELE---RAMRAFNREWPAETADLDADLESlPEYLALlDRLEEDGLPEYEeR 835
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1201873520 1523 MKTQIKQMMdasrvktmlslvEEDRNSLQSKLNDEvaaRQELEEQIKKL 1571
Cdd:COG4913 836 FKELLNENS------------IEFVADLLSKLRRA---IREIKERIDPL 869
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
1582-1708 |
5.62e-05 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 47.77 E-value: 5.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1582 KARLENeCKTLQQKVEilgELYQQKEMALQKKLTQEE--YERQEKEQKLSAA--DEKAVLAIEEVKVYKQriQDMEEELQ 1657
Cdd:PRK11637 166 QARQET-IAELKQTRE---ELAAQKAELEEKQSQQKTllYEQQAQQQKLEQArnERKKTLTGLESSLQKD--QQQLSELR 239
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1201873520 1658 KTERSYKNQIAAHEKKAHdnwliARsAERalaeEKREAANLRQKLIEVNQK 1708
Cdd:PRK11637 240 ANESRLRDSIARAEREAK-----AR-AER----EAREAARVRDKQKQAKRK 280
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1414-1696 |
6.60e-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: 47.45 E-value: 6.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1414 EKVKAELQHVQEENARLKKSKEQLLKEAEGWSERHTELTEQIKLYRKSQKDIEEALAYKENEIEVLTnciMQLKQLDTDS 1493
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELE---KEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1494 ASEakkdgeghewstRDDLAngelpdneKMKTQIKQMMDASRVKTMLSlvEEDRNSLQSKLNDEVAARQELEEQIKKLEH 1573
Cdd:COG4942 100 EAQ------------KEELA--------ELLRALYRLGRQPPLALLLS--PEDFLDAVRRLQYLKYLAPARREQAEELRA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1574 DSCSLQSAKARLENEcktlqqkveilgelyqqkemalQKKLTQEEYERQEKEQKLSAAdekavlaieevkvyKQRIQDME 1653
Cdd:COG4942 158 DLAELAALRAELEAE----------------------RAELEALLAELEEERAALEAL--------------KAERQKLL 201
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1201873520 1654 EELQKTERSYKNQIAAHEKKAHD-NWLIARSAERALAEEKREAA 1696
Cdd:COG4942 202 ARLEKELAELAAELAELQQEAEElEALIARLEAEAAAAAERTPA 245
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1312-1705 |
7.85e-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: 7.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1312 DEKIKQAKESMKVAQEQKNILSDEIAGLKDTVKGLEETNHQLD-DKIKSLCTMLDTERKQNAKKQKKLSETQKSLEKLEE 1390
Cdd:COG4913 294 EAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEALLAALGL 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1391 AFSMHSAELSEVQIALNESKlseEKVKAELQHVQEENARLKKSKEQLLKEAEGWSERHTELTEQIKLYRKSQ----KDIE 1466
Cdd:COG4913 374 PLPASAEEFAALRAEAAALL---EALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLlalrDALA 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1467 EALAYKENEIEVLtnC-IMQLKQLDTD---------------------------SASEAKKDGEGHEW----STRDDLAN 1514
Cdd:COG4913 451 EALGLDEAELPFV--GeLIEVRPEEERwrgaiervlggfaltllvppehyaaalRWVNRLHLRGRLVYervrTGLPDPER 528
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1515 GELPDN---EKMKT-----------QIKQMMDASRVKTmlslVEE------------------------DRNSLQSKL-- 1554
Cdd:COG4913 529 PRLDPDslaGKLDFkphpfrawleaELGRRFDYVCVDS----PEElrrhpraitragqvkgngtrhekdDRRRIRSRYvl 604
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1555 -NDEVAARQELEEQIKKLEHDSCSLQSAKARLENECKTLQQKVEILGELYQQKEMALQKKLTQEEYERQEKE-QKLSAAD 1632
Cdd:COG4913 605 gFDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAElERLDASS 684
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1633 EKAVLAIEEVKVYKQRIQDMEEELQKTERSY---KNQIAAHEK-------KAHDNWLIARSAERALAEEKREAANLRQKL 1702
Cdd:COG4913 685 DDLAALEEQLEELEAELEELEEELDELKGEIgrlEKELEQAEEeldelqdRLEAAEDLARLELRALLEERFAAALGDAVE 764
|
...
gi 1201873520 1703 IEV 1705
Cdd:COG4913 765 REL 767
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1408-1704 |
9.15e-05 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 47.66 E-value: 9.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1408 ESKLSEEKVKAELQHVQEENARLKKSKEQLLKEAegwSERHTELTEQIKLYRKSQKDIEEALAYKENEIEVLTNCIMQLK 1487
Cdd:pfam02463 164 GSRLKRKKKEALKKLIEETENLAELIIDLEELKL---QELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERID 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1488 QLDTDSASE-AKKDGEGHEWSTRDDLANGELPDNEKMKTQIKQM-MDASRVKTMLSLVEEDRNSLQSKLNDEVAARQELE 1565
Cdd:pfam02463 241 LLQELLRDEqEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQeEELKLLAKEEEELKSELLKLERRKVDDEEKLKESE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1566 EQIKKLEHDSCSLQSAKARLENECKTLQQKVEILGELYQQKEMALQKKLTQEE---YERQEKEQKLSAADEKAVLAIEEV 1642
Cdd:pfam02463 321 KEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEellAKKKLESERLSSAAKLKEEELELK 400
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1201873520 1643 KVYKQRIQDMEEELQKTERSYKNQIAAHEKKAHDNWLIARSAERALAEEKREAANLRQKLIE 1704
Cdd:pfam02463 401 SEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLK 462
|
|
| PHA03379 |
PHA03379 |
EBNA-3A; Provisional |
1722-1922 |
1.02e-04 |
|
EBNA-3A; Provisional
Pssm-ID: 223066 [Multi-domain] Cd Length: 935 Bit Score: 47.36 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1722 PGrPDRQVPPRRVPLSRDGSFGPSPVSGGNPSPTqmmEVPS------RPLSAPQREGSRGEFGTVVDGP------PAPRR 1789
Cdd:PHA03379 464 PC-PVAQLPPGPLQDLEPGDQLPGVVQDGRPACA---PVPApagpivRPWEASLSQVPGVAFAPVMPQPmpvepvPVPTV 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1790 PPELPGRMSVPDL---GPAVASLI-------------SSGPRTSSPATAKDRaLSPKEPEAPCVTtdSPSSIEPATVT-V 1852
Cdd:PHA03379 540 ALERPVCPAPPLIamqGPGETSGIvrvrerwrpapwtPNPPRSPSQMSVRDR-LARLRAEAQPYQ--ASVEVQPPQLTqV 616
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1201873520 1853 GPKGPPSFPGTPVMTSPVMGPPPPPPVNYGPPPAP-FPGHYGPRPLPVPLVCGAPLPPPAArDFLPGPPLG 1922
Cdd:PHA03379 617 SPQQPMEYPLEPEQQMFPGSPFSQVADVMRAGGVPaMQPQYFDLPLQQPISQGAPLAPLRA-SMGPVPPVP 686
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1303-1707 |
1.09e-04 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 47.44 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1303 EMLDKFSEcDEKIKQAKESMKVAQEQKNILS----DEIAGLKDTVKGLEETNHQLDDKIKSLCTMLDTERKQNAKKQKKL 1378
Cdd:pfam07111 128 EMVRKNLE-EGSQRELEEIQRLHQEQLSSLTqaheEALSSLTSKAEGLEKSLNSLETKRAGEAKQLAEAQKEAELLRKQL 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1379 SETQKSLE---KLEEAFSMHSAELSEVQIALNESKLSEEKVKAELQHVQEENARLKKSKEQL------------LKEAE- 1442
Cdd:pfam07111 207 SKTQEELEaqvTLVESLRKYVGEQVPPEVHSQTWELERQELLDTMQHLQEDRADLQATVELLqvrvqslthmlaLQEEEl 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1443 -----------------------GWSERHTELTEQIKL----YRKSQKDIEEALAYKENEIEVLTNCIMQLKQLDTDSAS 1495
Cdd:pfam07111 287 trkiqpsdslepefpkkcrsllnRWREKVFALMVQLKAqdleHRDSVKQLRGQVAELQEQVTSQSQEQAILQRALQDKAA 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1496 EAKKDgeghewstRDDLANGELPDNEKMKTQIKQMMDASRVKTMLSLVEEDRNSLQSKLNDEVAARQELEEQIKKLEHDs 1575
Cdd:pfam07111 367 EVEVE--------RMSAKGLQMELSRAQEARRRQQQQTASAEEQLKFVVNAMSSTQIWLETTMTRVEQAVARIPSLSNR- 437
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1576 cslQSAKARLENECKTLQQKVEILGELYQQK------------EMALQKKLTQEEYERQEKEQKLSA--ADEKAVLAIEE 1641
Cdd:pfam07111 438 ---LSYAVRKVHTIKGLMARKVALAQLRQEScpppppappvdaDLSLELEQLREERNRLDAELQLSAhlIQQEVGRAREQ 514
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1642 VKVYKQRI----QDMEEELQKTERSYKNQIAAHEkkahdnwliarSAERALAEEKREAANLRQKLIEVNQ 1707
Cdd:pfam07111 515 GEAERQQLsevaQQLEQELQRAQESLASVGQQLE-----------VARQGQQESTEEAASLRQELTQQQE 573
|
|
| PHA03378 |
PHA03378 |
EBNA-3B; Provisional |
1714-1854 |
1.12e-04 |
|
EBNA-3B; Provisional
Pssm-ID: 223065 [Multi-domain] Cd Length: 991 Bit Score: 47.37 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1714 RPLIVKPTPGRPDRQVPPR-RVPLSRDGSFGPSPVSGGNPSPTQMMEVPSRPLSAPQregsrgefgtvvdGPPAPRRPPE 1792
Cdd:PHA03378 735 RPPAAAPGRARPPAAAPGRaRPPAAAPGRARPPAAAPGAPTPQPPPQAPPAPQQRPR-------------GAPTPQPPPQ 801
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1201873520 1793 -LPGRMSV------PDLGPA---VASLISSGPRTSSPATAKDRALspkEPEAPCVTTDSPSSIEPATVTVGP 1854
Cdd:PHA03378 802 aGPTSMQLmpraapGQQGPTkqiLRQLLTGGVKRGRPSLKKPAAL---ERQAAAGPTPSPGSGTSDKIVQAP 870
|
|
| ADIP |
pfam11559 |
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ... |
1548-1658 |
1.18e-04 |
|
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at cell-cell adherens junctions, and in Sch. pombe and other fungi where it anchors spindle-pole bodies to spindle microtubules. It is a coiled-coil structure, and in pombe, it is required for anchoring the minus end of spindle microtubules to the centrosome equivalent, the spindle-pole body. The name ADIP derives from the family being composed of Afadin- and alpha -Actinin-Binding Proteins localized at Cell-Cell Adherens Junctions.
Pssm-ID: 463295 [Multi-domain] Cd Length: 151 Bit Score: 44.23 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1548 NSLQSKLNDEVAARQELEEQIKKLEHDSCSLQSAKARLENECKTLQQKVeilgELYQQKEMALQKKL-TQEEYERQEKE- 1625
Cdd:pfam11559 41 YELLQQRDRDLEFRESLNETIRTLEAEIERLQSKIERLKTQLEDLEREL----ALLQAKERQLEKKLkTLEQKLKNEKEe 116
|
90 100 110
....*....|....*....|....*....|....*
gi 1201873520 1626 -QKL-SAADEKAVLAIEEVKVYKQRIQDMEEELQK 1658
Cdd:pfam11559 117 lQRLkNALQQIKTQFAHEVKKRDREIEKLKERLAQ 151
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1292-1607 |
1.46e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.96 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1292 EKIQNLLREKTEMLD--KFSECDEKIKQAK--ESMKVAQEQKNILSDEIAGLKDTVKGLEEtnhqlddKIKSLctmldte 1367
Cdd:PRK02224 436 RTARERVEEAEALLEagKCPECGQPVEGSPhvETIEEDRERVEELEAELEDLEEEVEEVEE-------RLERA------- 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1368 rkqnakkqKKLSETQKSLEKLEEafsmhSAELSEVQIALNESKLSEEKVKAElqhvqeenaRLKKSKEQLLKEAEGWSER 1447
Cdd:PRK02224 502 --------EDLVEAEDRIERLEE-----RREDLEELIAERRETIEEKRERAE---------ELRERAAELEAEAEEKREA 559
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1448 HTELTEQIKLYRKSQKDIEEALAYKENEIEVLTNCIMQLkqldtdSASEAKKDGEGHEWSTRDDLAngELPDNEKMKTQI 1527
Cdd:PRK02224 560 AAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLL------AAIADAEDEIERLREKREALA--ELNDERRERLAE 631
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1528 KQmmdaSRVKTMLSLVEEDR-NSLQSKLNDEVAARQELEEQIKKLEHDSCSLQSAKARLENECK----------TLQQKV 1596
Cdd:PRK02224 632 KR----ERKRELEAEFDEARiEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEeleelrerreALENRV 707
|
330
....*....|.
gi 1201873520 1597 EILGELYQQKE 1607
Cdd:PRK02224 708 EALEALYDEAE 718
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1550-1710 |
1.90e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.83 E-value: 1.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1550 LQSKLNDEVAAR--QELEEQIKKLEHDSCSLQSAKARLENECKTLQQKVEILGELYQQ----KEMALQKKLTQEEYERQE 1623
Cdd:COG4913 277 LRAALRLWFAQRrlELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGnggdRLEQLEREIERLERELEE 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1624 KEQKLSAADEKAvlaieevKVYKQRIQDMEE---ELQKTERSYKNQIAAHEKKAHDNwliARSAERALAEEKREAANLRQ 1700
Cdd:COG4913 357 RERRRARLEALL-------AALGLPLPASAEefaALRAEAAALLEALEEELEALEEA---LAEAEAALRDLRRELRELEA 426
|
170
....*....|..
gi 1201873520 1701 KL--IEVNQKNI 1710
Cdd:COG4913 427 EIasLERRKSNI 438
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
1369-1664 |
1.95e-04 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 46.61 E-value: 1.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1369 KQNAKKQKKLSETQKSLEKLEEAFSMHSAELSE--VQIALNESKLSEEKVKAELQHVQEENARLKKSKEQLLKEAEGWSE 1446
Cdd:COG5022 817 ACIIKLQKTIKREKKLRETEEVEFSLKAEVLIQkfGRSLKAKKRFSLLKKETIYLQSAQRVELAERQLQELKIDVKSISS 896
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1447 RHTELTEQIKLYRKSQKDIEEALAykeNEIEVLTNCIMQLKQL----DTDSASEAKKdgeghewsTRDDLANGELPDNEK 1522
Cdd:COG5022 897 LKLVNLELESEIIELKKSLSSDLI---ENLEFKTELIARLKKLlnniDLEEGPSIEY--------VKLPELNKLHEVESK 965
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1523 MKTQIKQMMDA--------SRVKTMLSLVEEDRNSLQSKLnDEVAARQELEEQIKKLEHDSCSLQSAKARLENECKTLQ- 1593
Cdd:COG5022 966 LKETSEEYEDLlkkstilvREGNKANSELKNFKKELAELS-KQYGALQESTKQLKELPVEVAELQSASKIISSESTELSi 1044
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1201873520 1594 ----QKVEILGELyqqKEMALQKKLTQEEYERqekeqKLSAADEKAVLAIEEVKVYKQRIQDMEEELQKTERSYK 1664
Cdd:COG5022 1045 lkplQKLKGLLLL---ENNQLQARYKALKLRR-----ENSLLDDKQLYQLESTENLLKTINVKDLEVTNRNLVKP 1111
|
|
| Taxilin |
pfam09728 |
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain ... |
1280-1594 |
2.17e-04 |
|
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain in its C-terminal half and is ubiquitously expressed. It is a novel binding partner of several syntaxin family members and is possibly involved in Ca2+-dependent exocytosis in neuroendocrine cells. Gamma-taxilin, described as leucine zipper protein Factor Inhibiting ATF4-mediated Transcription (FIAT), localizes to the nucleus in osteoblasts and dimerizes with ATF4 to form inactive dimers, thus inhibiting ATF4-mediated transcription.
Pssm-ID: 462861 [Multi-domain] Cd Length: 302 Bit Score: 45.33 E-value: 2.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1280 SRIYQVTEKQLAEKIQNLLREKTEMLDKFSE-----------CDEKIKQAK----ESMKVAQEQKNILSDEIAGLKDTVK 1344
Cdd:pfam09728 34 MKRLQKDLKKLKKKQDQLQKEKDQLQSELSKailakskleklCRELQKQNKklkeESKKLAKEEEEKRKELSEKFQSTLK 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1345 GLEET-NHQLDDKIKSlctmldteRKQNAKKQKKLSETQKSLEKLEEAF-SMHsaELSEVQIALNESKLSEEKVKAELQH 1422
Cdd:pfam09728 114 DIQDKmEEKSEKNNKL--------REENEELREKLKSLIEQYELRELHFeKLL--KTKELEVQLAEAKLQQATEEEEKKA 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1423 VQEENARLKKSKEQLlkeaEGWSERHTELTEQIKLYRKSQKDIEEALAyKENEIevltncIMQLKQldtdsaseakkdge 1502
Cdd:pfam09728 184 QEKEVAKARELKAQV----QTLSETEKELREQLNLYVEKFEEFQDTLN-KSNEV------FTTFKK-------------- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1503 ghewstrddlangelpDNEKMKTQIKQmmdasrvktmlslVEEDRNSLQSK-------LNDEVAARQELEEQIKKLehds 1575
Cdd:pfam09728 239 ----------------EMEKMSKKIKK-------------LEKENLTWKRKweksnkaLLEMAEERQKLKEELEKL---- 285
|
330
....*....|....*....
gi 1201873520 1576 cslQSAKARLENECKTLQQ 1594
Cdd:pfam09728 286 ---QKKLEKLENLCRALQA 301
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1298-1710 |
2.42e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 46.58 E-value: 2.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1298 LREKTEMLDKFSECDEKIK--QAKESMK-VAQEQKNILSDEIAGLKdTVKGLEETNHQLDDKIKSLCTMLDTERKQNAKK 1374
Cdd:TIGR00606 165 LSEGKALKQKFDEIFSATRyiKALETLRqVRQTQGQKVQEHQMELK-YLKQYKEKACEIRDQITSKEAQLESSREIVKSY 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1375 QKKLSETQKSLEKLEEAFSmHSAELSEVQIALNESKLSEEKVKAELQHVQEENARLKKSKEQLLKEAEGWSERHTElTEQ 1454
Cdd:TIGR00606 244 ENELDPLKNRLKEIEHNLS-KIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVREKE-REL 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1455 IKLYRKSQKDIEEALAYKENEIEVLTNCIMQLKQLDTDSASEAKKDGEGHEWSTRDDLANGEL-PDNEK-----MKTQIK 1528
Cdd:TIGR00606 322 VDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERgPFSERqiknfHTLVIE 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1529 QMMDASRVKTMLSLVEEDRNSLQSKLNDEVAARQE------------LEEQIKKLEHDSCSLQSAKARLENECKTLQQKV 1596
Cdd:TIGR00606 402 RQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKglgrtielkkeiLEKKQEELKFVIKELQQLEGSSDRILELDQELR 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1597 EILGELYQQKEMAL-QKKLTQEEYERQEK---EQKLSAADEKAVLAIEEVKVYKQRIQDMEEELQKTERSYKNQIAAHE- 1671
Cdd:TIGR00606 482 KAERELSKAEKNSLtETLKKEVKSLQNEKadlDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDe 561
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1201873520 1672 ----------KKAHDNWLIARSAERALAEEKREAANLRQKLIEVNQKNI 1710
Cdd:TIGR00606 562 ltsllgyfpnKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHI 610
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1543-1673 |
2.51e-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: 44.92 E-value: 2.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1543 VEEDRNSLQSKLNDEVAARQELEEQIKKLEHDSCSLQSAKARLEN---------ECKTLQQKVEILGELYQQKEmalqKK 1613
Cdd:COG1579 36 LEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEqlgnvrnnkEYEALQKEIESLKRRISDLE----DE 111
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1614 LTQEEYERQEKEQKLSAADEKAVLAIEEVKVYKQRIQDMEEELQKTERSYKNQIAAHEKK 1673
Cdd:COG1579 112 ILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAK 171
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1283-1704 |
2.62e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 46.21 E-value: 2.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1283 YQVTEKQLAEKIQNLLREKTEMLDKFSECDEKIKQAKESMKVAQEQKNILSDEIAGLKDTVKGLEEtnhqlddKIKSLCT 1362
Cdd:TIGR02169 390 YREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEW-------KLEQLAA 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1363 MLDTERKQNAKKQKKLSETQKSLEKLEEAFSMHSAELSEVQIALNESKLSEEKVKAELQHVQEENARLKKSKEQLLK--- 1439
Cdd:TIGR02169 463 DLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGERYATaie 542
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1440 ------------EAEGWSERHTELTEQIKLYRKS--------QKDIEEALAYKENEIEVLTNCI---------------- 1483
Cdd:TIGR02169 543 vaagnrlnnvvvEDDAVAKEAIELLKRRKAGRATflplnkmrDERRDLSILSEDGVIGFAVDLVefdpkyepafkyvfgd 622
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1484 ----------------MQLKQLDTD----------------SASEAKKDGEGHEWSTRDDLA--NGELPDNEKMKTQIKQ 1529
Cdd:TIGR02169 623 tlvvedieaarrlmgkYRMVTLEGElfeksgamtggsraprGGILFSRSEPAELQRLRERLEglKRELSSLQSELRRIEN 702
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1530 MMDA-----SRVKTMLSLVEEDRNSLQSKLNDEVAARQELEEQIKKLEHDSCSLQSAKARLENECKTLQQKV----EILG 1600
Cdd:TIGR02169 703 RLDElsqelSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLhkleEALN 782
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1601 ELYQQKEMALQKKLtQEEYERQEKE-QKLSAADEKAVLAIEEVKVYKQRIQDMEEELQKTERSYKNQIAAHEKKAHDNWL 1679
Cdd:TIGR02169 783 DLEARLSHSRIPEI-QAELSKLEEEvSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNG 861
|
490 500
....*....|....*....|....*
gi 1201873520 1680 IARSAERALAEEKREAANLRQKLIE 1704
Cdd:TIGR02169 862 KKEELEEELEELEAALRDLESRLGD 886
|
|
| PHA03379 |
PHA03379 |
EBNA-3A; Provisional |
1719-1864 |
2.68e-04 |
|
EBNA-3A; Provisional
Pssm-ID: 223066 [Multi-domain] Cd Length: 935 Bit Score: 46.20 E-value: 2.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1719 KPTPG--RPDRQVPPRRVPLSRDGSFGPSPVSGGNPSPTQMMEvpsrplSAPQREGSRGEFGTVVDGPPAPRRPPE---- 1792
Cdd:PHA03379 410 EPTYGtpRPPVEKPRPEVPQSLETATSHGSAQVPEPPPVHDLE------PGPLHDQHSMAPCPVAQLPPGPLQDLEpgdq 483
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1201873520 1793 LPGRMSVPDLGPAVASLISSG---PRTSSPATAKDRALSPKEPEapcvttdsPSSIEPATVTVGPKGPPSFPGTP 1864
Cdd:PHA03379 484 LPGVVQDGRPACAPVPAPAGPivrPWEASLSQVPGVAFAPVMPQ--------PMPVEPVPVPTVALERPVCPAPP 550
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1288-1653 |
3.45e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 45.81 E-value: 3.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1288 KQLAEKIQNLLREKTEMLDKFSECD---EKIKQAKESMKVAQEQKNILSDEIAGLKDTVKGLEE------------TNHQ 1352
Cdd:TIGR00606 747 PELRNKLQKVNRDIQRLKNDIEEQEtllGTIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQqaaklqgsdldrTVQQ 826
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1353 LDDKIKSLCTMLDTERKQNAKKQKKLSETQKSLEKLEEAFSMHSAELSEVQIALNESKLSEEKVKAELQHVQEENARLKK 1432
Cdd:TIGR00606 827 VNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKD 906
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1433 SKEQLLKEAEGWSERHTELTEQIKLYRKSQKDIEEALAYKENEIEVLTNCIMQLKQLDTDSASEAKKDGEghewsTRDDL 1512
Cdd:TIGR00606 907 AKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDDYLKQKE-----TELNT 981
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1513 ANGELPDNEKMKTQIKQMMDASRVKTMLSLVEE----DRNSLQSKLNDEVAARQELEEQIKKLEHDSC-SLQSAKARLEN 1587
Cdd:TIGR00606 982 VNAQLEECEKHQEKINEDMRLMRQDIDTQKIQErwlqDNLTLRKRENELKEVEEELKQHLKEMGQMQVlQMKQEHQKLEE 1061
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1201873520 1588 ECKTL-QQKVEILGelyQQKEMALQKKLtqeeYERQEKEQKLSAADEKAVLAIEEVKVYKQRIQDME 1653
Cdd:TIGR00606 1062 NIDLIkRNHVLALG---RQKGYEKEIKH----FKKELREPQFRDAEEKYREMMIVMRTTELVNKDLD 1121
|
|
| MISS |
pfam15822 |
MAPK-interacting and spindle-stabilising protein-like; MISS is a family of eukaryotic ... |
1798-1920 |
3.76e-04 |
|
MAPK-interacting and spindle-stabilising protein-like; MISS is a family of eukaryotic MAPK-interacting and spindle-stabilising protein-like proteins. MISS is rich in prolines and has four potential MAPK-phosphorylation sites, a MAPK-docking site, a PEST sequence (PEST motif) and a bipartite nuclear localization signal. The endogenous protein accumulates during mouse meiotic maturation and is found as discrete dots on the MII spindle. MISS is the first example of a physiological MAPK-substrate that is stabilized in MII that specifically regulates MII spindle integrity during the CSF arrest.
Pssm-ID: 318115 [Multi-domain] Cd Length: 238 Bit Score: 44.21 E-value: 3.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1798 SVPDLGPAVASLISSgPRTSSPATAKDRALSPKEPEAP-CVTTDSPSSIEPATVTVGPkgPPS--FPGTPVmtspvmgpp 1874
Cdd:pfam15822 6 ALPEQSPAKTSAVSN-PKPGQPPQGWPGSNPWNNPSAPpAVPSGLPPSTAPSTVPFGP--APTgmYPSIPL--------- 73
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1201873520 1875 ppppvnygppPAPFPGHYGPRPlPVPLVC---GAPLPPPAARDflPGPP 1920
Cdd:pfam15822 74 ----------TGPSPGPPAPFP-PSGPSCpppGGPYPAPTVPG--PGPI 109
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
1334-1450 |
3.80e-04 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 45.07 E-value: 3.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1334 DEIAGLKDTVKGLEETNHQLDDKIKSLCTMLDTERKQNAKKQKKLSETQKSLEKLEEAFSMHSAELSEVQiaLNESKLSE 1413
Cdd:PRK11637 170 ETIAELKQTREELAAQKAELEEKQSQQKTLLYEQQAQQQKLEQARNERKKTLTGLESSLQKDQQQLSELR--ANESRLRD 247
|
90 100 110
....*....|....*....|....*....|....*..
gi 1201873520 1414 EKVKAElqhvQEENARlkksKEQLLKEAEGWSERHTE 1450
Cdd:PRK11637 248 SIARAE----REAKAR----AEREAREAARVRDKQKQ 276
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1403-1700 |
4.01e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 45.50 E-value: 4.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1403 QIALNESKLSEEKVKAELQHVQEENARLKKSKEQLLKEAEGWSERHTELTEQIKLYRKSQKDIEEalayKENEIEvltnc 1482
Cdd:pfam17380 281 QKAVSERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAME----RERELE----- 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1483 imQLKQLDTDSASEAKKDGE-GHEWSTRDDLANGELPDNEKmKTQIKQMMDASRVKTMLSLVEEDRNSLQSKLNDEVAAR 1561
Cdd:pfam17380 352 --RIRQEERKRELERIRQEEiAMEISRMRELERLQMERQQK-NERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAE 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1562 QE--LEEQIKKLEHDScslQSAKARLENECKTLQQKVEILgelYQQKEMALQKKLTQEEYERQEK----------EQKLS 1629
Cdd:pfam17380 429 QEeaRQREVRRLEEER---AREMERVRLEEQERQQQVERL---RQQEEERKRKKLELEKEKRDRKraeeqrrkilEKELE 502
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1201873520 1630 AADEKAVLAIEEVKVYKQRIQDM------EEELQKTERSYKNQIAAHEKKAHDNWLIARSAERA-LAEEKREAANLRQ 1700
Cdd:pfam17380 503 ERKQAMIEEERKRKLLEKEMEERqkaiyeEERRREAEEERRKQQEMEERRRIQEQMRKATEERSrLEAMEREREMMRQ 580
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1364-1708 |
4.80e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.14 E-value: 4.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1364 LDTERKQNAKKQKKLSETQKSLEKLEEAFSMHSAELSEVQIALNESKLSEEKVKAElQHVQEENARLkkskEQLLKEAEG 1443
Cdd:COG4717 83 AEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALE-AELAELPERL----EELEERLEE 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1444 WSERHTELTEQIKLYRKSQKDIEEALAYKENEIEV-LTNCIMQLKQLdtdSASEAKKDGEGHEWSTRDDLANGELPDNEK 1522
Cdd:COG4717 158 LRELEEELEELEAELAELQEELEELLEQLSLATEEeLQDLAEELEEL---QQRLAELEEELEEAQEELEELEEELEQLEN 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1523 MKT------QIKQMMDASRVKTMLSLVEEDRNSLQSKLNDEVAA------------------RQELEEQIKKLEHDSCSL 1578
Cdd:COG4717 235 ELEaaaleeRLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVlflvlgllallflllareKASLGKEAEELQALPALE 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1579 QSAKARLENECKTLQ----QKVEILGELYQQ---------KEMALQKKLTQEEYErQEKEQKLSAAD-------EKAVLA 1638
Cdd:COG4717 315 ELEEEELEELLAALGlppdLSPEELLELLDRieelqellrEAEELEEELQLEELE-QEIAALLAEAGvedeeelRAALEQ 393
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1639 IEEVKVYKQRIQDMEEELQKTERSYKNQIAAHEKKAHDNWLiaRSAERALAEEKREAANLRQKLIEVNQK 1708
Cdd:COG4717 394 AEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEEL--EELEEELEELEEELEELREELAELEAE 461
|
|
| MISS |
pfam15822 |
MAPK-interacting and spindle-stabilising protein-like; MISS is a family of eukaryotic ... |
1720-1920 |
4.97e-04 |
|
MAPK-interacting and spindle-stabilising protein-like; MISS is a family of eukaryotic MAPK-interacting and spindle-stabilising protein-like proteins. MISS is rich in prolines and has four potential MAPK-phosphorylation sites, a MAPK-docking site, a PEST sequence (PEST motif) and a bipartite nuclear localization signal. The endogenous protein accumulates during mouse meiotic maturation and is found as discrete dots on the MII spindle. MISS is the first example of a physiological MAPK-substrate that is stabilized in MII that specifically regulates MII spindle integrity during the CSF arrest.
Pssm-ID: 318115 [Multi-domain] Cd Length: 238 Bit Score: 43.82 E-value: 4.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1720 PTPGRPDRQVP----------PRRVPLSRDGSFGPSPVSGGnPSPTQMMevPSRPLSAPQrEGSRGEF------------ 1777
Cdd:pfam15822 21 PKPGQPPQGWPgsnpwnnpsaPPAVPSGLPPSTAPSTVPFG-PAPTGMY--PSIPLTGPS-PGPPAPFppsgpscpppgg 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1778 ---GTVVDGP------PAPRRP-PELPGRMSVPDlGPAVASliSSGPRTSSPATAKDRALSPKEPeAPCVTTDSPSSIEP 1847
Cdd:pfam15822 97 pypAPTVPGPgpigpyPTPNMPfPELPRPYGAPT-DPAAAA--PSGPWGSMSSGPWAPGMGGQYP-APNMPYPSPGPYPA 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1201873520 1848 ATVTVGPKGPPSFP-GTpvMTSPVMGPPPPPPVNYGPPPAPFPGHYGPRPLPVPlvCGAPLPPPaardfLPGPP 1920
Cdd:pfam15822 173 VPPPQSPGAAPPVPwGT--VPPGPWGPPAPYPDPTGSYPMPGLYPTPNNPFQVP--SGPSGAPP-----MPGGP 237
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1293-1469 |
5.37e-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: 43.76 E-value: 5.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1293 KIQNLLREKTEMLDKFSECDEKIKQAKESMKVAQEQKNILSDEIAGLKDTVKGLEETNHQLDDKIKSlctmlDTERKQNA 1372
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKK-----YEEQLGNV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1373 KKQKKLSETQKSLEKLEEAFSMHSAELSEVQIALNESKLSEEKVKAELQHVQEENARLKKSKEQLLKEAEgwsERHTELT 1452
Cdd:COG1579 86 RNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELE---AELEELE 162
|
170
....*....|....*..
gi 1201873520 1453 EQIKLYRKSqkdIEEAL 1469
Cdd:COG1579 163 AEREELAAK---IPPEL 176
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1288-1622 |
5.40e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.14 E-value: 5.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1288 KQLAEKIQNLLREKT--------EMLDKFSECDEKIKQAKESMKVAQEQKNILSDEIAGLKDtvkglEETNHQLDDKIKS 1359
Cdd:COG4717 173 AELQEELEELLEQLSlateeelqDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLEN-----ELEAAALEERLKE 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1360 LCTM---------LDTERKQNAKKQKKLSETQKSL--------EKLEEAFSMHSAELSEVQIALNESKLSEEKVKAELQH 1422
Cdd:COG4717 248 ARLLlliaaallaLLGLGGSLLSLILTIAGVLFLVlgllallfLLLAREKASLGKEAEELQALPALEELEEEELEELLAA 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1423 VQEENARLKKSKEQLLKEAEGWSERHTELTEQIKlyrksqkdiEEALAYKENEIEVLtncimqLKQLDTDSASE----AK 1498
Cdd:COG4717 328 LGLPPDLSPEELLELLDRIEELQELLREAEELEE---------ELQLEELEQEIAAL------LAEAGVEDEEElraaLE 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1499 KDGEGHEWSTRDDLANGELPDNEKMKTQIKQMMDASRVKTMLSLVEEDRNSLQSKLNDEVAARQELEEQIKKLEHDScSL 1578
Cdd:COG4717 393 QAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDG-EL 471
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1201873520 1579 QSAKARLEneckTLQQKVEILGELYQQKEMALQK-KLTQEEYERQ 1622
Cdd:COG4717 472 AELLQELE----ELKAELRELAEEWAALKLALELlEEAREEYREE 512
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1558-1709 |
5.46e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 45.06 E-value: 5.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1558 VAARQELEEQIKKLEHDSCSLQSAKARLENEcktLQQKVEILGELYQQ-KEMALQ-KKLTQEEYER-QEKEQKLSAADEK 1634
Cdd:TIGR02169 229 LKEKEALERQKEAIERQLASLEEELEKLTEE---ISELEKRLEEIEQLlEELNKKiKDLGEEEQLRvKEKIGELEAEIAS 305
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1201873520 1635 AVLAIEEvkvYKQRIQDMEEELQKTE---RSYKNQIAAHEKKAHDNWLIARSAERALAEEKREAANLRQKLIEVNQKN 1709
Cdd:TIGR02169 306 LERSIAE---KERELEDAEERLAKLEaeiDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEF 380
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1288-1473 |
5.59e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.44 E-value: 5.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1288 KQLAEKIQNLLREKTEMLDKFSECDEKIKQAKESMKVAQEQKNILSDEIAGLKDTVKGLEEtnhQLDDKIKSL------- 1360
Cdd:COG3883 26 SELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERRE---ELGERARALyrsggsv 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1361 ------------------CTMLDTERKQNAKKQKKLSETQKSLEKLEEAFSMHSAELSEVQIALNESKLSEEKVKAELqh 1422
Cdd:COG3883 103 syldvllgsesfsdfldrLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQ-- 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1201873520 1423 vQEENARLKKSKEQLLKEAEGWSERHTELTEQIKLYRKSQKDIEEALAYKE 1473
Cdd:COG3883 181 -EALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAA 230
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1312-1481 |
5.63e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.44 E-value: 5.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1312 DEKIKQAKESMKVAQEQKNILSDEIAGLKDTVKGLEETNHQLDDKIKSLCTMLDTERKQNAKKQKKLSETQKSLEKLEEA 1391
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1392 FSMHSAELSEVQIALNESKLSE------------EKVKAELQHVQEENARLKKSKEQLLKEAEgwserhtELTEQIKLYR 1459
Cdd:COG3883 95 LYRSGGSVSYLDVLLGSESFSDfldrlsalskiaDADADLLEELKADKAELEAKKAELEAKLA-------ELEALKAELE 167
|
170 180
....*....|....*....|..
gi 1201873520 1460 KSQKDIEEALAYKENEIEVLTN 1481
Cdd:COG3883 168 AAKAELEAQQAEQEALLAQLSA 189
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1273-1613 |
6.00e-04 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 45.04 E-value: 6.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1273 RTClsvKSRIYQ-VTEKQLAEKIQNLLREKTEMLDKFSECDEKIKQAKESMK-VAQEQKNIlsdEIAGLKdtvkgleeTN 1350
Cdd:TIGR01612 1402 EEC---KSKIEStLDDKDIDECIKKIKELKNHILSEESNIDTYFKNADENNEnVLLLFKNI---EMADNK--------SQ 1467
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1351 HQLDDKIKSLCTMLD---TERKQNAKKQKKLS----ETQKSLEKLEEAFSMHSAELSEVqiaLNesKLSEEKVKAELqhv 1423
Cdd:TIGR01612 1468 HILKIKKDNATNDHDfniNELKEHIDKSKGCKdeadKNAKAIEKNKELFEQYKKDVTEL---LN--KYSALAIKNKF--- 1539
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1424 qeenARLKKSKEQLLKEAEGWSERHT---ELTEQ-IKLYRKSQKDIEEALAYKENEIEVLTNCIMQLKQLDTD--SASEA 1497
Cdd:TIGR01612 1540 ----AKTKKDSEIIIKEIKDAHKKFIleaEKSEQkIKEIKKEKFRIEDDAAKNDKSNKAAIDIQLSLENFENKflKISDI 1615
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1498 KKDgeghewstrddlANGELPDNEKMKTQIKQMMDASRvKTMLSLVEEDRNSLQSKLNDEVAARQELEEQIKKLEhdscS 1577
Cdd:TIGR01612 1616 KKK------------INDCLKETESIEKKISSFSIDSQ-DTELKENGDNLNSLQEFLESLKDQKKNIEDKKKELD----E 1678
|
330 340 350
....*....|....*....|....*....|....*.
gi 1201873520 1578 LQSAKARLENECKTLQQKVEIlGELYQQKEMALQKK 1613
Cdd:TIGR01612 1679 LDSEIEKIEIDVDQHKKNYEI-GIIEKIKEIAIANK 1713
|
|
| HlpA |
COG2825 |
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ... |
1579-1667 |
6.59e-04 |
|
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 442073 [Multi-domain] Cd Length: 171 Bit Score: 42.52 E-value: 6.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1579 QSAKARLENECKTLQQKVEILGELYQQKEMALQKK---LTQEeyERQEKEQKLSAADEKavlaieevkvYKQRIQDMEEE 1655
Cdd:COG2825 42 KAAQKKLEKEFKKRQAELQKLEKELQALQEKLQKEaatLSEE--ERQKKERELQKKQQE----------LQRKQQEAQQD 109
|
90
....*....|..
gi 1201873520 1656 LQKTERSYKNQI 1667
Cdd:COG2825 110 LQKRQQELLQPI 121
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1286-1655 |
7.23e-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: 44.72 E-value: 7.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1286 TEKQLAEKIQNLLRE----KTEMLDKFSECDEKIKQAKESM----KVAQEQKNILSD--EIAGLKDTVKGLEETNH--QL 1353
Cdd:pfam15921 139 SQEDLRNQLQNTVHEleaaKCLKEDMLEDSNTQIEQLRKMMlsheGVLQEIRSILVDfeEASGKKIYEHDSMSTMHfrSL 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1354 DDKIKSLCTMLDTE---------------RKQNAKKQKKLSET-QKSLEKLEEAFSMHSAELSEVQIALNESKLSEEKVK 1417
Cdd:pfam15921 219 GSAISKILRELDTEisylkgrifpvedqlEALKSESQNKIELLlQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQ 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1418 AELQHVQEEnARLKKS--KEQLLKEAEGWSERHTELTEQIKLYRKSQKDIEEALAYKENEI-EVLT----------NCIM 1484
Cdd:pfam15921 299 SQLEIIQEQ-ARNQNSmyMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELtEARTerdqfsqesgNLDD 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1485 QLKQLDTDSASEAKKDGEGHEWSTR---DDLANGELPDNEKMKTQIKQMmdasRVKTMLSLVEEDRNSLQSKLNDEVAAR 1561
Cdd:pfam15921 378 QLQKLLADLHKREKELSLEKEQNKRlwdRDTGNSITIDHLRRELDDRNM----EVQRLEALLKAMKSECQGQMERQMAAI 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1562 QELEEQIKKlehdscsLQSAKARLENECKTLQQKVEILgelyqqkemaLQKKLTQEEYER---------QEKEQKLSAAD 1632
Cdd:pfam15921 454 QGKNESLEK-------VSSLTAQLESTKEMLRKVVEEL----------TAKKMTLESSERtvsdltaslQEKERAIEATN 516
|
410 420
....*....|....*....|...
gi 1201873520 1633 EKAVLAIEEVKVYKQRIQDMEEE 1655
Cdd:pfam15921 517 AEITKLRSRVDLKLQELQHLKNE 539
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1293-1692 |
7.67e-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: 44.72 E-value: 7.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1293 KIQNLLREKTEML-DKFSECDEKIKQAKESMKVAQEQKNILSDEIAGLKDTVKGLEETNHQLDDKikslctmLDTERKQN 1371
Cdd:pfam15921 328 QLRSELREAKRMYeDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKE-------LSLEKEQN 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1372 AKK--------------QKKLSETQKSLEKLEeafSMHSAELSEVQIALNESKLSEEKVKAELQHVQEENARLKKSKEQL 1437
Cdd:pfam15921 401 KRLwdrdtgnsitidhlRRELDDRNMEVQRLE---ALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEML 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1438 LKEAEgwserhtELTEQIKLYRKSQK---DIEEALAYKENEIEVLTNCIMQLKqldtdSASEAKKDGEGHEWSTRDDLAN 1514
Cdd:pfam15921 478 RKVVE-------ELTAKKMTLESSERtvsDLTASLQEKERAIEATNAEITKLR-----SRVDLKLQELQHLKNEGDHLRN 545
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1515 GElPDNEKMKTQikqMMDASRVKTMLSLVEEDRNSLQSKLNDEVAARQ----ELEEQIKKLEHDSCSLQSAKARLENECK 1590
Cdd:pfam15921 546 VQ-TECEALKLQ---MAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQvekaQLEKEINDRRLELQEFKILKDKKDAKIR 621
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1591 TLQQKVEILgELYQQKEM-ALQKKLTQEEYERQEKEQKLSaadekavlaieEVKVYKQRIQDMEEELQKTERSYKNQIAA 1669
Cdd:pfam15921 622 ELEARVSDL-ELEKVKLVnAGSERLRAVKDIKQERDQLLN-----------EVKTSRNELNSLSEDYEVLKRNFRNKSEE 689
|
410 420
....*....|....*....|...
gi 1201873520 1670 HEKKAHDNWLIARSAERALAEEK 1692
Cdd:pfam15921 690 METTTNKLKMQLKSAQSELEQTR 712
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
1562-1701 |
9.99e-04 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 43.33 E-value: 9.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1562 QELEEQIKKLEHD--------SCSLQSAKARLENECKTLQQKVEILGELYQQKEmALQKKLTQEEYERQEKEQKLSAADE 1633
Cdd:cd16269 127 APLEEKISQGSYSvpggyqlyLEDREKLVEKYRQVPRKGVKAEEVLQEFLQSKE-AEAEAILQADQALTEKEKEIEAERA 205
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1201873520 1634 KAVLAIEEVKVYKQRIQDMEEELQKTERSYKNQIAAHEKK-AHDNWLIARSAERALAEEKREAANLRQK 1701
Cdd:cd16269 206 KAEAAEQERKLLEEQQRELEQKLEDQERSYEEHLRQLKEKmEEERENLLKEQERALESKLKEQEALLEE 274
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
1510-1709 |
1.00e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 44.15 E-value: 1.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1510 DDLANGELPDNEKMKTQIKQMMDA-SRVKTMLSLVEEDRNSLQSKLNDEVAARQE-----LEEQIKKLEHDSCSLQSAKA 1583
Cdd:PRK05771 38 EELSNERLRKLRSLLTKLSEALDKlRSYLPKLNPLREEKKKVSVKSLEELIKDVEeelekIEKEIKELEEEISELENEIK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1584 RLENECKTLqqkvEILGELyqqkEMALQKKLTQE-------EYERQEKEQKLSAADEKAVLAIEEVK--------VYKQR 1648
Cdd:PRK05771 118 ELEQEIERL----EPWGNF----DLDLSLLLGFKyvsvfvgTVPEDKLEELKLESDVENVEYISTDKgyvyvvvvVLKEL 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1201873520 1649 IQDMEEELQKTErsYKNQIAAHEKKAHDnwLIARSAERaLAEEKREAANLRQKLIEVNQKN 1709
Cdd:PRK05771 190 SDEVEEELKKLG--FERLELEEEGTPSE--LIREIKEE-LEEIEKERESLLEELKELAKKY 245
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
1714-1917 |
1.18e-03 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 44.10 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1714 RPLIVKPTPGRPDRQVPPRRVPLSRDGSFGPSPVSGGN--PSPTQMMEVPSRPLSAPQREGSRGEFGTVVDGPPAPRRPP 1791
Cdd:PRK12323 386 APAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAParRSPAPEALAAARQASARGPGGAPAPAPAPAAAPAAAARPA 465
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1792 elpgrmsVPDLGPAVASLISSGPRTSSPATAK--DRALSPKEPEAPCVTTDSPSSIEPAtvtvgPKGPPSFPGTPVMTSP 1869
Cdd:PRK12323 466 -------AAGPRPVAAAAAAAPARAAPAAAPApaDDDPPPWEELPPEFASPAPAQPDAA-----PAGWVAESIPDPATAD 533
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1201873520 1870 VMGPPPPPPVNYGPPPAPfpghyGPRPLPVPLVcgAPLPPPAARDFLP 1917
Cdd:PRK12323 534 PDDAFETLAPAPAAAPAP-----RAAAATEPVV--APRPPRASASGLP 574
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1414-1714 |
1.42e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 43.81 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1414 EKVKAELQHVQEENARLKKSKEQLLKEAEGWSERHTELTEQIKLYRKSQKDIEEALAYKENEIEVLTNCIMQLKQLDTD- 1492
Cdd:pfam02463 629 LKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQRe 708
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1493 SASEAKKDGEGHEWSTR-----DDLANGELPDNEKMKTQIKQMMDASRVKTMLSLVEEDRNSLQSKLNDEVAARQELEEQ 1567
Cdd:pfam02463 709 KEELKKLKLEAEELLADrvqeaQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKV 788
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1568 IKKLEHDscslqsaKARLENECKTLQQKVEILGELYQQKEMALQKKLTQEEYERQEKEQKLSAADEKAVLAIEEVKVYKQ 1647
Cdd:pfam02463 789 EEEKEEK-------LKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEE 861
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1201873520 1648 RIQDMEEELQKTERSYKNQIAAHEKKAHdnwliarsaeraLAEEKreaanlrqkliEVNQKNIMLQR 1714
Cdd:pfam02463 862 EITKEELLQELLLKEEELEEQKLKDELE------------SKEEK-----------EKEEKKELEEE 905
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1364-1663 |
1.47e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.79 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1364 LDTERKQNAKKQKKLSETQKSLEKLEEAFSMHSAE-LS-------EVQIALNESKLSEEKVKAELQHVQEENAR--LKKS 1433
Cdd:PRK04863 791 LRAEREELAERYATLSFDVQKLQRLHQAFSRFIGShLAvafeadpEAELRQLNRRRVELERALADHESQEQQQRsqLEQA 870
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1434 KEQL-----------LKEAEGWSERHTELTEQIKLYRKSQKDIEE---ALAYKENEIEVLTNCIMQLKQLDTDSAsEAKK 1499
Cdd:PRK04863 871 KEGLsalnrllprlnLLADETLADRVEEIREQLDEAEEAKRFVQQhgnALAQLEPIVSVLQSDPEQFEQLKQDYQ-QAQQ 949
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1500 DGE-------------------GHEWSTRDDLANGELpdNEKMKTQIKQM-MDASRVKTMLSLVEE---DRNSLQSKLND 1556
Cdd:PRK04863 950 TQRdakqqafaltevvqrrahfSYEDAAEMLAKNSDL--NEKLRQRLEQAeQERTRAREQLRQAQAqlaQYNQVLASLKS 1027
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1557 EVAA----RQELEEQIKKLEHDSCSLQSAKARLENEckTLQQKveiLGELYQQKEmALQKKLTQEEYERQEKEQKLSAAD 1632
Cdd:PRK04863 1028 SYDAkrqmLQELKQELQDLGVPADSGAEERARARRD--ELHAR---LSANRSRRN-QLEKQLTFCEAEMDNLTKKLRKLE 1101
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1201873520 1633 EKAVLAIEEVKVYKQRIQ---------DMEEELQKTERSY 1663
Cdd:PRK04863 1102 RDYHEMREQVVNAKAGWCavlrlvkdnGVERRLHRRELAY 1141
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1288-1634 |
1.61e-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: 43.35 E-value: 1.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1288 KQLAEKIQNLLREKTEMLDKFSECDEKIKQAKESMKVAQEQKNILSDEIAGLKDTVKGLEETNHQLDDKIKSLCTMLD-- 1365
Cdd:pfam07888 76 RELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELErm 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1366 TERKQNAKKQKKLSETQKslEKLEEAFSMHSAELSEVQIALNESKLSEEKVKAELQHVQEENARLKKS----------KE 1435
Cdd:pfam07888 156 KERAKKAGAQRKEEEAER--KQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKlttahrkeaeNE 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1436 QLLKEAEGWSERHTELTEQIKLYRksqKDIEEALAYKENEIEVLTNCIMQLKQLDTD--SASEAKKDGEGHEWSTRDDLA 1513
Cdd:pfam07888 234 ALLEELRSLQERLNASERKVEGLG---EELSSMAAQRDRTQAELHQARLQAAQLTLQlaDASLALREGRARWAQERETLQ 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1514 NGELPDNEKMKTQIKQMMdasrvktmlslveedrnSLQSKLNDEVAARQELEEQIKKlEHDSCSLQSAKARLEnecktLQ 1593
Cdd:pfam07888 311 QSAEADKDRIEKLSAELQ-----------------RLEERLQEERMEREKLEVELGR-EKDCNRVQLSESRRE-----LQ 367
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1201873520 1594 QKVEILGELYQQKEMALQKKLTQEEYERQEKEQKLSAADEK 1634
Cdd:pfam07888 368 ELKASLRVAQKEKEQLQAEKQELLEYIRQLEQRLETVADAK 408
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1339-1672 |
1.89e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 43.35 E-value: 1.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1339 LKDTVKGLEETNHQLD---DKIKSLCTMLDTERKQNAKKQKKLSETQKSLEKLEEAFSMHSAELSEVQIALNE-SKLSEE 1414
Cdd:PRK01156 171 LKDVIDMLRAEISNIDyleEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNElSSLEDM 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1415 KVKAELQhVQEENARLkKSKEQLLKEAEGWSERHTELT--------EQIKLYRKSQKDIE---EALAYKENEIEVLTNCI 1483
Cdd:PRK01156 251 KNRYESE-IKTAESDL-SMELEKNNYYKELEERHMKIIndpvyknrNYINDYFKYKNDIEnkkQILSNIDAEINKYHAII 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1484 MQLKQLDTDSASEAKKDGEGHEWST-RDDLANGELP--------DNEKMKTQ---IKQMMDASRVKTMLSLVEEDRNSLQ 1551
Cdd:PRK01156 329 KKLSVLQKDYNDYIKKKSRYDDLNNqILELEGYEMDynsylksiESLKKKIEeysKNIERMSAFISEILKIQEIDPDAIK 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1552 SKLNDEVAARQELEEQIKKLEHDSCSLQSAKARLENECKTLQ--------------QKVEILGELYQQKEMALQKKLTQE 1617
Cdd:PRK01156 409 KELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNgqsvcpvcgttlgeEKSNHIINHYNEKKSRLEEKIREI 488
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1201873520 1618 EYE----RQEKEQKLSAADEKAVLAIEEVKVYKQRIQDMEEELQKTERSYKNQIAAHEK 1672
Cdd:PRK01156 489 EIEvkdiDEKIVDLKKRKEYLESEEINKSINEYNKIESARADLEDIKIKINELKDKHDK 547
|
|
| OmpH |
pfam03938 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
1579-1667 |
1.91e-03 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 461098 [Multi-domain] Cd Length: 140 Bit Score: 40.64 E-value: 1.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1579 QSAKARLENECKTLQQKVEILGELYQQKEMALQKKLTQEEYERQEKEQKLSAADEKavlaieevkvYKQRIQDMEEELQK 1658
Cdd:pfam03938 18 KAAQAQLEKKFKKRQAELEAKQKELQKLYEELQKDGALLEEEREEKEQELQKKEQE----------LQQLQQKAQQELQK 87
|
....*....
gi 1201873520 1659 TERSYKNQI 1667
Cdd:pfam03938 88 KQQELLQPI 96
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1290-1634 |
1.94e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 43.27 E-value: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1290 LAEKiQNLLREKTEMLDKFSEcdEK------IKQAKESMKVAQEQKNILSDEIAGLKDTVKGLEETNHQLDDKIKSLCTM 1363
Cdd:pfam10174 354 LEEK-ESFLNKKTKQLQDLTE--EKstlageIRDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTD 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1364 LDTERKQNAKKQKKLSETQKSLEKLEEAFSMHSAE-LSEVQIALNESKLSEEKVKAELQHVQEENARLKKSKEQ------ 1436
Cdd:pfam10174 431 SSNTDTALTTLEEALSEKERIIERLKEQREREDRErLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHasslas 510
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1437 -------LLKEAEGWSERHTEltEQIKLYRKSQKDIEEALAYKENE-----IEVLTNCIMQLK------QLDTDSASEAK 1498
Cdd:pfam10174 511 sglkkdsKLKSLEIAVEQKKE--ECSKLENQLKKAHNAEEAVRTNPeindrIRLLEQEVARYKeesgkaQAEVERLLGIL 588
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1499 KDGEGHEWSTRDDLANGELPDNEKMKTQIK-----QMMDASRVKTMLSLVEEDRNSLQSKLNDevAARQELEEQIKKLEH 1573
Cdd:pfam10174 589 REVENEKNDKDKKIAELESLTLRQMKEQNKkvaniKHGQQEMKKKGAQLLEEARRREDNLADN--SQQLQLEELMGALEK 666
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1201873520 1574 DSCSLQSAKARLENECKTLQQKVEILGELYQQKEMALqkkltqEEYERQEKEQKLSAADEK 1634
Cdd:pfam10174 667 TRQELDATKARLSSTQQSLAEKDGHLTNLRAERRKQL------EEILEMKQEALLAAISEK 721
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1543-1714 |
3.07e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 41.83 E-value: 3.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1543 VEEDRNSLQSKLNDEVAARQELEEQIKKLEHDSCSLQSAKARLENECKTLQQkveilgelyqqkEMALQKKLTQEEYerq 1622
Cdd:pfam00038 80 LRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKE------------ELAFLKKNHEEEV--- 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1623 eKEQKLSAADEKAVLaieEVKVYKQriQDMEEELQKTERSYKnQIAAHEKKAHDNWLIARSAERALAEEkREAANLRQKL 1702
Cdd:pfam00038 145 -RELQAQVSDTQVNV---EMDAARK--LDLTSALAEIRAQYE-EIAAKNREEAEEWYQSKLEELQQAAA-RNGDALRSAK 216
|
170
....*....|..
gi 1201873520 1703 IEVNQKNIMLQR 1714
Cdd:pfam00038 217 EEITELRRTIQS 228
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1288-1644 |
3.10e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 42.64 E-value: 3.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1288 KQLAEKIQNLLREKTEMLDkfsecdEKIKQAKESMKVAQEQKNILSDEIaglkdtvkglEETNHQLDDKIKSLCTMLDTE 1367
Cdd:COG5185 249 AQTSDKLEKLVEQNTDLRL------EKLGENAESSKRLNENANNLIKQF----------ENTKEKIAEYTKSIDIKKATE 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1368 RKQNakkQKKLSETQKSLE-KLEEAFSMHSAELSEVQIALNESKLSEEKVKAELQHVQEENaRLKKSKEQLLKEAEGWSE 1446
Cdd:COG5185 313 SLEE---QLAAAEAEQELEeSKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEV-ELSKSSEELDSFKDTIES 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1447 RHTELTEQIKLYRKSQKDIEEALA--YKENEIEvLTNCIMQLKQLDTD-SASEAKKDGEGHEWSTRDDLANgelpDNEKM 1523
Cdd:COG5185 389 TKESLDEIPQNQRGYAQEILATLEdtLKAADRQ-IEELQRQIEQATSSnEEVSKLLNELISELNKVMREAD----EESQS 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1524 KTQIKQMMDASRVKTMLSLVEEDRNSLQSKLNDEVAARQELEEQIKKLEHDSCSLQSAKARLENECKTLQQKVEILGELY 1603
Cdd:COG5185 464 RLEEAYDEINRSVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLERQLEGVRSKLDQVAESLKDFMRARGYAHILALEN 543
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1201873520 1604 QQKEMALQKKLT-----QEEYERQEKEQKLSAADEKAVLAIEEVKV 1644
Cdd:COG5185 544 LIPASELIQASNaktdgQAANLRTAVIDELTQYLSTIESQQAREDP 589
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1281-1435 |
3.19e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.46 E-value: 3.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1281 RIYQVTEKQLAEKIQNLLRE-KTEMLDKFSECDEKIKQAKESMkvaQEQKNILSDEIAGLKDTVKGLEETNHQLDDKIKS 1359
Cdd:PRK12704 42 RILEEAKKEAEAIKKEALLEaKEEIHKLRNEFEKELRERRNEL---QKLEKRLLQKEENLDRKLELLEKREEELEKKEKE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1360 lctmLDTERKQNAKKQKKLSE-TQKSLEKLEEAFSMHSAELSEVQIALNESKLSEEkvKAELQHVQEENARL---KKSKE 1435
Cdd:PRK12704 119 ----LEQKQQELEKKEEELEElIEEQLQELERISGLTAEEAKEILLEKVEEEARHE--AAVLIKEIEEEAKEeadKKAKE 192
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1339-1588 |
3.21e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 42.31 E-value: 3.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1339 LKDTVKGLEETNHQLDDKIKSLCTMLDTERK----QNAKKQKKLSETQKSLEKLEEAFSMHSAELSEVQIALNESKLSEE 1414
Cdd:PHA02562 172 NKDKIRELNQQIQTLDMKIDHIQQQIKTYNKnieeQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1415 KVKAELQHVQEENARLKKSKEQLLKEAEGWSERHT--ELTEQIklyrKSQKDIEEALAYKeneievLTNCIMQLKQLDTD 1492
Cdd:PHA02562 252 DPSAALNKLNTAAAKIKSKIEQFQKVIKMYEKGGVcpTCTQQI----SEGPDRITKIKDK------LKELQHSLEKLDTA 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1493 SASEAKKDgegHEWSTRDDLANGelpdnekMKTQIkqmmdaSRVKTMLSLVEEDRNSLQSKLNDEVAARQELEEQIKKLE 1572
Cdd:PHA02562 322 IDELEEIM---DEFNEQSKKLLE-------LKNKI------STNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQ 385
|
250
....*....|....*.
gi 1201873520 1573 HDSCSLQSAKARLENE 1588
Cdd:PHA02562 386 DELDKIVKTKSELVKE 401
|
|
| PTZ00449 |
PTZ00449 |
104 kDa microneme/rhoptry antigen; Provisional |
1722-1922 |
3.62e-03 |
|
104 kDa microneme/rhoptry antigen; Provisional
Pssm-ID: 185628 [Multi-domain] Cd Length: 943 Bit Score: 42.37 E-value: 3.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1722 PGRPDRQVPPRRVPLSRDGSFG--------PSPVSGGNPSPTQMMEVPSRPlsAPQREGSRGEFGTVVDGPPAPRRP--- 1790
Cdd:PTZ00449 511 PEGPEASGLPPKAPGDKEGEEGehedskesDEPKEGGKPGETKEGEVGKKP--GPAKEHKPSKIPTLSKKPEFPKDPkhp 588
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1791 --------------PELPGRMSVPDLgPAVASLISSGPRTSSPATAKdRALSPKEPEAPcVTTDSPSSIEPATVTVGPKG 1856
Cdd:PTZ00449 589 kdpeepkkpkrprsAQRPTRPKSPKL-PELLDIPKSPKRPESPKSPK-RPPPPQRPSSP-ERPEGPKIIKSPKPPKSPKP 665
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1201873520 1857 P--PSFPGT---PVMTSPVMGPPPPPPVNYGPPPAPFPGHYGPRPLPVPLVCGAPLPPPAARD-FLPGPPLG 1922
Cdd:PTZ00449 666 PfdPKFKEKfydDYLDAAAKSKETKTTVVLDESFESILKETLPETPGTPFTTPRPLPPKLPRDeEFPFEPIG 737
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1720-2005 |
3.88e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 42.62 E-value: 3.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1720 PTPGRPDRQVPPrrvPLSRDGSFGPSPVSGGNPSPTQMMEVPsRPLSAPQREgSRGEFGTVVDGPPAPRRPPELPGRMSV 1799
Cdd:PHA03247 2614 PSPLPPDTHAPD---PPPPSPSPAANEPDPHPPPTVPPPERP-RDDPAPGRV-SRPRRARRLGRAAQASSPPQRPRRRAA 2688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1800 PdlgPAVASLISSG-----PRTSSPATakdRALSPKEPeAPCVTTDSPSSIEPATVTVGPKGPPSFPGTPVmtspvmgpp 1874
Cdd:PHA03247 2689 R---PTVGSLTSLAdppppPPTPEPAP---HALVSATP-LPPGPAAARQASPALPAAPAPPAVPAGPATPG--------- 2752
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1875 ppppvnygpppapfpghyGPRPLPVPLVCGAPLPPPAARDFLPGPPlgmRDLPPGPLPPLPDPRSYRRGPPHFRPPGPPG 1954
Cdd:PHA03247 2753 ------------------GPARPARPPTTAGPPAPAPPAAPAAGPP---RRLTRPAVASLSESRESLPSPWDPADPPAAV 2811
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1201873520 1955 PRAYPPGPPLPPPASRDYAPSRNRDLPPAgprdypagppPPPAGSKDYTQP 2005
Cdd:PHA03247 2812 LAPAAALPPAASPAGPLPPPTSAQPTAPP----------PPPGPPPPSLPL 2852
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1363-1708 |
4.18e-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: 4.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1363 MLDTERKQNA-----KKQKKLSETQKSLEKLEEAFSMHSAELSEVQIALNESKLseEKVKAELQHVQEENARLKKSKEQL 1437
Cdd:COG4913 244 LEDAREQIELlepirELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAEL--EELRAELARLEAELERLEARLDAL 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1438 lkeaegwSERHTELTEQIklyRKSQKDIEEALaykENEIEVLtncimqlkqldtdsasEAKKDGEGHEWSTRDDLANG-- 1515
Cdd:COG4913 322 -------REELDELEAQI---RGNGGDRLEQL---EREIERL----------------ERELEERERRRARLEALLAAlg 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1516 -ELPDNEK----MKTQIKQMMDAsrVKTMLSLVEEDRNSLQSKLNDEVAARQELEEQIKKLEH-DSC---SLQSAKARLE 1586
Cdd:COG4913 373 lPLPASAEefaaLRAEAAALLEA--LEEELEALEEALAEAEAALRDLRRELRELEAEIASLERrKSNipaRLLALRDALA 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1587 NECKTLQQKVEILGELYQQKE------------------------------------MALQKKLTQEEYERQEKEQKLSA 1630
Cdd:COG4913 451 EALGLDEAELPFVGELIEVRPeeerwrgaiervlggfaltllvppehyaaalrwvnrLHLRGRLVYERVRTGLPDPERPR 530
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1631 ADEKAV---LAIEEVKVY---KQRIQ--------DMEEELQKTERS------YKNQIAAHEKKAHD----NWLIARSAER 1686
Cdd:COG4913 531 LDPDSLagkLDFKPHPFRawlEAELGrrfdyvcvDSPEELRRHPRAitragqVKGNGTRHEKDDRRrirsRYVLGFDNRA 610
|
410 420
....*....|....*....|..
gi 1201873520 1687 ALAEEKREAANLRQKLIEVNQK 1708
Cdd:COG4913 611 KLAALEAELAELEEELAEAEER 632
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1288-1470 |
4.43e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.97 E-value: 4.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1288 KQLAEKIQNLLREKTEMLDK--------FSECDEKIKQAKESMKVAQEQKNILSdEIAGLKDTVKGLEETNHQLDDKIKS 1359
Cdd:PRK03918 559 AELEKKLDELEEELAELLKEleelgfesVEELEERLKELEPFYNEYLELKDAEK-ELEREEKELKKLEEELDKAFEELAE 637
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1360 LCTMLDTERKQNAKKQKKLSEtqKSLEKLEEAFSMHSAELSEVQIALNESKLSEEKVKAELQHVQEENARLKKSKEQlLK 1439
Cdd:PRK03918 638 TEKRLEELRKELEELEKKYSE--EEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKE-LE 714
|
170 180 190
....*....|....*....|....*....|.
gi 1201873520 1440 EAEGWSERHTELTEQIKLYRKSQKdiEEALA 1470
Cdd:PRK03918 715 KLEKALERVEELREKVKKYKALLK--ERALS 743
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1286-1716 |
4.99e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 41.88 E-value: 4.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1286 TEKQLAEKIQNLLREKTEMLDKfsecDEKIKQAKESMKVAQEQKNilsdEIAGLKDTVKGLEETNHQLDDKiKSLCTMLD 1365
Cdd:TIGR00618 416 TSAFRDLQGQLAHAKKQQELQQ----RYAELCAAAITCTAQCEKL----EKIHLQESAQSLKEREQQLQTK-EQIHLQET 486
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1366 TERKQNAKKQKKLSETQKSLEK--LEEAFSMHSAELSE-----VQIALNESKL---SEEKVKAELQHVQEENARLKKSKE 1435
Cdd:TIGR00618 487 RKKAVVLARLLELQEEPCPLCGscIHPNPARQDIDNPGpltrrMQRGEQTYAQletSEEDVYHQLTSERKQRASLKEQMQ 566
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1436 QLLKEAEGWSERHTELTEQIKLYRKSQKDIeealaykeneievltncimqLKQLDTDSASEAKKDGEGHEWSTR--DDLA 1513
Cdd:TIGR00618 567 EIQQSFSILTQCDNRSKEDIPNLQNITVRL--------------------QDLTEKLSEAEDMLACEQHALLRKlqPEQD 626
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1514 NGELPDNEKMKTQIKQMMDASRVKTMLSLVEED-RNSLQSKLNDEVAARQELEEQIKKLEHDSCSLQSAKARLENECKTL 1592
Cdd:TIGR00618 627 LQDVRLHLQQCSQELALKLTALHALQLTLTQERvREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLL 706
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1593 QQKVEILGEL------YQQKEMALQKKLTQE---------EYERQEKEQ-KLSA-----ADEKAVLAIEEVKVYKQRIQD 1651
Cdd:TIGR00618 707 RELETHIEEYdrefneIENASSSLGSDLAARedalnqslkELMHQARTVlKARTeahfnNNEEVTAALQTGAELSHLAAE 786
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1201873520 1652 ME---EELQKTERSYKNQIAAHEKKAHDNWLIARSAERALAEEKreaANLRQKLIEVNQKNIMLQRPL 1716
Cdd:TIGR00618 787 IQffnRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEE---EQFLSRLEEKSATLGEITHQL 851
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
1720-1984 |
5.07e-03 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 42.08 E-value: 5.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1720 PTPGrPDRQVPPRRVPLSRDGSFGPSPVSGGNPSPTQMMEVPSRPLSAPQREGSR---------GEFGTVVDGPPAPRRP 1790
Cdd:PHA03307 128 PSPA-PDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQAALPLSSPEEtarapssppAEPPPSTPPAAASPRP 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1791 PE--------------LPGRMSVPDLGPAVASLISS-------GPRTSSP---------ATAKDRALSPKEPEAPCVTTD 1840
Cdd:PHA03307 207 PRrsspisasasspapAPGRSAADDAGASSSDSSSSessgcgwGPENECPlprpapitlPTRIWEASGWNGPSSRPGPAS 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1841 SPSSIEPAtvtvGPKGPPSFPGTPVMTSPVMGPPPPPPVNYGPPPAPFPGHYGPRPLPVPL--VCGAPLPPPAARDFLPG 1918
Cdd:PHA03307 287 SSSSPRER----SPSPSPSSPGSGPAPSSPRASSSSSSSRESSSSSTSSSSESSRGAAVSPgpSPSRSPSPSRPPPPADP 362
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1201873520 1919 PPLGMRD--LPPGPLPPLPDPRSYRRGPPHFRPPGPPGPR-------AYPPGPPLPPPASRDYAPSRNRDLPPAG 1984
Cdd:PHA03307 363 SSPRKRPrpSRAPSSPAASAGRPTRRRARAAVAGRARRRDatgrfpaGRPRPSPLDAGAASGAFYARYPLLTPSG 437
|
|
| PHA03378 |
PHA03378 |
EBNA-3B; Provisional |
1720-1919 |
5.11e-03 |
|
EBNA-3B; Provisional
Pssm-ID: 223065 [Multi-domain] Cd Length: 991 Bit Score: 41.98 E-value: 5.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1720 PTPGRPDRQVPPRRVPL-SRDGSFGPSPVSGGNP--SPTQMMEVPSRPLSAPQREGSRGEfgtvvdgpPAPRRP-PELPG 1795
Cdd:PHA03378 565 PAPGLGPLQIQPLTSPTtSQLASSAPSYAQTPWPvpHPSQTPEPPTTQSHIPETSAPRQW--------PMPLRPiPMRPL 636
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1796 RMSVPDLGPAVASLISSGPRTSSPATAKDRALSPKEPEAPCVTTDS--------PSSIEPATVTVGPKGPPSFPGTPVMT 1867
Cdd:PHA03378 637 RMQPITFNVLVFPTPHQPPQVEITPYKPTWTQIGHIPYQPSPTGANtmlpiqwaPGTMQPPPRAPTPMRPPAAPPGRAQR 716
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1868 SPVMGPPPPPPVNYGPPPAPFPGHYGPRPLPV--------PLVCGAPLPPPAARDFLPGP 1919
Cdd:PHA03378 717 PAAATGRARPPAAAPGRARPPAAAPGRARPPAaapgrarpPAAAPGRARPPAAAPGAPTP 776
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1720-1895 |
5.71e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 41.85 E-value: 5.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1720 PTPGRPDRQVPPRRVPLSRDGSFGP-------SPVSGGNPSPTQMMEVPSRPLSAPQREGSRGEFGTVVDGPPAPRRPPE 1792
Cdd:PHA03247 2834 AQPTAPPPPPGPPPPSLPLGGSVAPggdvrrrPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQA 2913
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1793 LPGRMSVPDLgpavaslissgPRTSSPATAKDRALSPKEPEAPcvTTDSPSSIEPATVTVGPKGPPSFPGTPVMTSPVMG 1872
Cdd:PHA03247 2914 PPPPQPQPQP-----------PPPPQPQPPPPPPPRPQPPLAP--TTDPAGAGEPSGAVPQPWLGALVPGRVAVPRFRVP 2980
|
170 180
....*....|....*....|...
gi 1201873520 1873 PPPPPPVNYGPPPAPFPGHYGPR 1895
Cdd:PHA03247 2981 QPAPSREAPASSTPPLTGHSLSR 3003
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1371-1707 |
6.30e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.68 E-value: 6.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1371 NAKKQKKLSETQKSLEKLEEAFSMHSAELSEVQIALNESKLSEEKVKAELQHV--QEENARLKKSKEQLLKEAEGWSERH 1448
Cdd:COG4717 69 NLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLekLLQLLPLYQELEALEAELAELPERL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1449 TELTEQIKLYRKSQKDIEEAlaykENEIEVLTNCIMQLKQLDTDSASEAKKDgeghewsTRDDLangelpdnEKMKTQIK 1528
Cdd:COG4717 149 EELEERLEELRELEEELEEL----EAELAELQEELEELLEQLSLATEEELQD-------LAEEL--------EELQQRLA 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1529 QMMDA-SRVKTMLSLVEEDRNSLQSKLndevaARQELEEQIKKLEHDS------CSLQSAKARLENECKTL--------- 1592
Cdd:COG4717 210 ELEEElEEAQEELEELEEELEQLENEL-----EAAALEERLKEARLLLliaaalLALLGLGGSLLSLILTIagvlflvlg 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1593 ----------QQKVEILGELYQQKEMALQKKLTQEEYERQEKEQKLSAADEK-----AVLAIEEVKVYKQRIQDMEEELQ 1657
Cdd:COG4717 285 llallflllaREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPeelleLLDRIEELQELLREAEELEEELQ 364
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1658 KTERSYKNQIAAHEKKAHDnwliaRSAERALAEEKREAANLRQKLIEVNQ 1707
Cdd:COG4717 365 LEELEQEIAALLAEAGVED-----EEELRAALEQAEEYQELKEELEELEE 409
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1407-1670 |
6.43e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.82 E-value: 6.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1407 NESKLseEKVKAELQHVQEENARLKKSKEQLLKEAEGWSERHTELtEQIKLYRKSQKDIEEAlaykENEIEVLTNcimQL 1486
Cdd:COG4913 608 NRAKL--AALEAELAELEEELAEAEERLEALEAELDALQERREAL-QRLAEYSWDEIDVASA----EREIAELEA---EL 677
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1487 KQLDTDSaseakkdgeghewstrDDLAngelpdnekmktqikqmmdasrvktmlslveedrnSLQSKLNDEVAARQELEE 1566
Cdd:COG4913 678 ERLDASS----------------DDLA-----------------------------------ALEEQLEELEAELEELEE 706
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1567 QIKKLEHDSCSLQSAKARLENECKTLQQKVEILGELyqqkemalqkkltQEEYERQEKEQKLSAADEKAVLAiEEVKVYK 1646
Cdd:COG4913 707 ELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDL-------------ARLELRALLEERFAAALGDAVER-ELRENLE 772
|
250 260
....*....|....*....|....
gi 1201873520 1647 QRIQDMEEELQKTERSYKNQIAAH 1670
Cdd:COG4913 773 ERIDALRARLNRAEEELERAMRAF 796
|
|
| Gag_spuma |
pfam03276 |
Spumavirus gag protein; |
1756-1924 |
6.67e-03 |
|
Spumavirus gag protein;
Pssm-ID: 460872 [Multi-domain] Cd Length: 614 Bit Score: 41.27 E-value: 6.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1756 QMMEVPSRPLSAPQREGSRGEFGTVVDGPPAPRRPPELPGRMSVPDLGPAVASLISSGPRTSSPATAKDRALSPKEPeaP 1835
Cdd:pfam03276 154 EIQEIELLALREQEAEALRIGLAEISPGAQGGIPPGASFSGLPSLPAIGGIHLPAIPGIHARAPPGNIARSLGDDIM--P 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1836 CVTTDSPSSIEPAtvtvGPKGPP-SF-PGTPVMT-SPVMGPPPPPPVNYGPPPAPFPGHYGPRPLPVPLVCGAPLPPPAA 1912
Cdd:pfam03276 232 SLGDAGMPQPRFA----FHPGNPfAEaEGHPFAEaEGERPRDIPRAPRIDAPSAPAIPAIQPIAPPMIPPIGAPIPIPHG 307
|
170
....*....|..
gi 1201873520 1913 RDFLPGPPLGMR 1924
Cdd:pfam03276 308 ASIPGEHIRNPR 319
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1373-1672 |
7.71e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 41.31 E-value: 7.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1373 KKQKKLSETQKSLEKLEEAFsmhsAELSEVQIALNESKLSEEKVKAELQHVQEENARLKKSKEQLLKEAEGWSERHTELT 1452
Cdd:pfam01576 16 KVKERQQKAESELKELEKKH----QQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHELESRLEEEEERS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1453 EQIKLYRKSQ----KDIEEALAYKENEIEVLtncimQLKQLDTDSasEAKKdgeghewsTRDDLANGElPDNEKMKTQIK 1528
Cdd:pfam01576 92 QQLQNEKKKMqqhiQDLEEQLDEEEAARQKL-----QLEKVTTEA--KIKK--------LEEDILLLE-DQNSKLSKERK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1529 QMMD-ASRVKTMLSLVEEDRNSLQSKLNDEVAARQELEEQIKKLEHDSCSLQSAKARLENECKTLQqkvEILGELYQQKE 1607
Cdd:pfam01576 156 LLEErISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQ---EQIAELQAQIA 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1201873520 1608 mALQKKLTQEEYERQEKEQKLSAADEKAVLAIEEVKVYKQRIQDMEEELQkTERSYKNQIAAHEK 1672
Cdd:pfam01576 233 -ELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLE-SERAARNKAEKQRR 295
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1288-1499 |
8.32e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 40.66 E-value: 8.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1288 KQLAEKIQNLLREKTEMLdkfsecdEKIKQAKESMKVAQEQKNILSDEIAGLKDTVKGLEETN---HQLDDKIKSLCTML 1364
Cdd:COG1340 53 KELREEAQELREKRDELN-------EKVKELKEERDELNEKLNELREELDELRKELAELNKAGgsiDKLRKEIERLEWRQ 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1365 DTErKQNAKKQKKL----SETQKSLEKLEEAFSMHSaELSEVQIALNESKLSEEKVKAELQHVQEENARLKKSKEQLLKE 1440
Cdd:COG1340 126 QTE-VLSPEEEKELvekiKELEKELEKAKKALEKNE-KLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKE 203
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1201873520 1441 AEGWSERHTELTEQIKLYRKSQKDIEEALAYKENEIEVLTNCIMQLKQLDTDSASEAKK 1499
Cdd:COG1340 204 ADELRKEADELHKEIVEAQEKADELHEEIIELQKELRELRKELKKLRKKQRALKREKEK 262
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1365-1499 |
8.88e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.92 E-value: 8.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1365 DTERKQNAKKQKKLSETQKSLEKLEEAFSmhsaelSEVQIALNESKLSEEKVKAELQHVQEENARLKKSKEQLLKEAEGW 1444
Cdd:PRK12704 46 EAKKEAEAIKKEALLEAKEEIHKLRNEFE------KELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKEL 119
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1201873520 1445 SERHTELTEQiklyrksQKDIEEALAYKENEIEVltncIMQLkqldtdSASEAKK 1499
Cdd:PRK12704 120 EQKQQELEKK-------EEELEELIEEQLQELER----ISGL------TAEEAKE 157
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
1563-1705 |
9.39e-03 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 40.42 E-value: 9.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1563 ELEEQIKKLEHDscsLQSAKARLENECKTLQQKVEILGELYQQKEMALQKKLTQEEYERQEKEQKLSAADEKAVLAIE-E 1641
Cdd:COG1566 80 DLQAALAQAEAQ---LAAAEAQLARLEAELGAEAEIAAAEAQLAAAQAQLDLAQRELERYQALYKKGAVSQQELDEARaA 156
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1201873520 1642 VKVYKQRIQDMEEELQKTersyKNQIAAHEKKAhdnwliARSAERALAEEKREAANLRQKLIEV 1705
Cdd:COG1566 157 LDAAQAQLEAAQAQLAQA----QAGLREEEELA------AAQAQVAQAEAALAQAELNLARTTI 210
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1563-1708 |
9.71e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 41.20 E-value: 9.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201873520 1563 ELEEQIKKLEhdscsLQSAKA----RLENECKTLQqkVEILGELYQQKE---MALQKKLTQEEYERQEKEQKLSAADEKa 1635
Cdd:TIGR02168 197 ELERQLKSLE-----RQAEKAerykELKAELRELE--LALLVLRLEELReelEELQEELKEAEEELEELTAELQELEEK- 268
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1201873520 1636 vlaIEEVKVYKQRIQDMEEELQKTERSYKNQIAA--HEKKAHDNWLiaRSAERALAEEKREAANLRQKLIEVNQK 1708
Cdd:TIGR02168 269 ---LEELRLEVSELEEEIEELQKELYALANEISRleQQKQILRERL--ANLERQLEELEAQLEELESKLDELAEE 338
|
|
| |
