|
Name |
Accession |
Description |
Interval |
E-value |
| SH3_MIA3 |
cd11893 |
Src Homology 3 domain of Melanoma Inhibitory Activity 3 protein; MIA3, also called TANGO or ... |
105-168 |
1.26e-39 |
|
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: 141.91 E-value: 1.26e-39
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024390606 105 LMCRGKAMKDFQGPDCRFVNFKKGETVYVYYKLIGMSTELWAGSIGSDFGYFPKDLLEINHNYT 168
Cdd:cd11893 10 LLCRGKAVKDFTGPDCRFLSFKKGETIYVYYKLSGRRTDLWAGSVGFDFGYFPKDLLDVNHLYT 73
|
|
| SH3_MIA2 |
cd11892 |
Src Homology 3 domain of Melanoma Inhibitory Activity 2 protein; MIA2 is expressed ... |
96-168 |
5.21e-24 |
|
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: 97.22 E-value: 5.21e-24
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024390606 96 KCFIKHSIELMCRGKAMKDFQGPDCRFVNFKKGETVYVYYKLIGMSTELWAGSIGSDFGYFPKDLLEINHNYT 168
Cdd:cd11892 1 KCGDPECERLMSRVQAIRDYRGPDCRYLSFKKGDEIIVYYKLSGKREDLWAGSTGKEFGYFPKDAVKVEEVYI 73
|
|
| SH3_MIA_like |
cd11760 |
Src Homology 3 domain of Melanoma Inhibitory Activity protein and similar proteins; MIA is a ... |
105-168 |
1.21e-23 |
|
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: 96.40 E-value: 1.21e-23
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024390606 105 LMCRGKAMKDFQGPDCRFVNFKKGETVYVYYKLIGMSTELWAGSIGSD---FGYFPKDLLEINHNYT 168
Cdd:cd11760 10 PISRARALEDYHGPDCRFLNFKKGDTIYVYSKLAGERQDLWAGSVGGDaglFGYFPKNLVQELKVYE 76
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1349-1725 |
8.12e-15 |
|
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: 80.45 E-value: 8.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1349 KQLAEKIQNLLQEKTEMLDKFSECDEKIKQ-------AKESMKVAQEQKSILSDEIAGLKdtvKELEETNHQLDD---KI 1418
Cdd:TIGR04523 71 NNSNNKIKILEQQIKDLNDKLKKNKDKINKlnsdlskINSEIKNDKEQKNKLEVELNKLE---KQKKENKKNIDKfltEI 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1419 KSLRTMLD--TERKQNAKKQKKLSETQKSLEKFEEAFSMHSAELSEVQIALNESKLSEEKVK--------AELQHVQEEN 1488
Cdd:TIGR04523 148 KKKEKELEklNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKiqknksleSQISELKKQN 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1489 ARLKKSKEQLLKEAEGWSERHTELTEQIKLYRKSQKDIEEALAYKENEIE----VLTNCIMQLKQLDTDsASEAKDGEGL 1564
Cdd:TIGR04523 228 NQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEqnnkKIKELEKQLNQLKSE-ISDLNNQKEQ 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1565 EWSTKddlANGELPDNEKMKTQIKQMMDA-----SRVKTMLSLVEEDRNSLQsklSDEVAARHELEE---QIKKLEHDSS 1636
Cdd:TIGR04523 307 DWNKE---LKSELKNQEKKLEEIQNQISQnnkiiSQLNEQISQLKKELTNSE---SENSEKQRELEEkqnEIEKLKKENQ 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1637 SLQSAKARLENECKTLQQKVEILGELYQQKEMALQKKltQEEYERQEKEQKL-------------SAADEKAVLAIeEVK 1703
Cdd:TIGR04523 381 SYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKL--QQEKELLEKEIERlketiiknnseikDLTNQDSVKEL-IIK 457
|
410 420
....*....|....*....|..
gi 2024390606 1704 VYKQRIQDMEEELQKTERSYKN 1725
Cdd:TIGR04523 458 NLDNTRESLETQLKVLSRSINK 479
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1396-1729 |
4.40e-14 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 78.56 E-value: 4.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1396 EIAGLKDTVKELEETNHQLDDKIKSLRTMLDTERKQNAKKQK-------KLSETQKSLEKFEEAFSMHSAELSEVQIALN 1468
Cdd:TIGR02168 678 EIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKeleelsrQISALRKDLARLEAEVEQLEERIAQLSKELT 757
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1469 ESKLSEEKVKAELQHVQEENARLKKSKEQLLKEAEGWSERHTELTEQIKLYRKSQKDIEEALAYKENEIEVLTNCIMQLK 1548
Cdd:TIGR02168 758 ELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATE 837
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1549 QLDTDSASEAKDGEGLEWSTKDDLANGELPDnEKMKTQIKQMMDASRVktmlslVEEDRNSLQSKLSDEVAARHELEEQI 1628
Cdd:TIGR02168 838 RRLEDLEEQIEELSEDIESLAAEIEELEELI-EELESELEALLNERAS------LEEALALLRSELEELSEELRELESKR 910
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1629 KKLEHDSSSLQSAKARLENECKTLQQkveilgelyqqkemalqkkltqeeyERQEKEQKLSaadEKAVLAIEEVKVYKQR 1708
Cdd:TIGR02168 911 SELRRELEELREKLAQLELRLEGLEV-------------------------RIDNLQERLS---EEYSLTLEEAEALENK 962
|
330 340
....*....|....*....|.
gi 2024390606 1709 IQDMEEELQKTERSYKNQIAA 1729
Cdd:TIGR02168 963 IEDDEEEARRRLKRLENKIKE 983
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1350-1736 |
4.80e-14 |
|
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: 78.19 E-value: 4.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1350 QLAEKIQNLLQEKTEMLDKFSECDEKIKQAKESMKVAQE-------QKSILSDEIAGLKDTVKELEETNHQLDDKIKSLR 1422
Cdd:TIGR02169 678 RLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRkigeiekEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVK 757
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1423 TMLDTERKQNAKKQKKLSETQKSLEKFEEAFSMHsaELSEVQIALNESKLSEEKVKAELQHVQEENARLKKSKEQLLKEA 1502
Cdd:TIGR02169 758 SELKELEARIEELEEDLHKLEEALNDLEARLSHS--RIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEI 835
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1503 EGWSERHTELTEQIKLYRKSQKDIEEALAYKENEIEVLTNcimQLKQLDtdsaSEAKDgeglewstkddlangelpdnek 1582
Cdd:TIGR02169 836 QELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEA---ALRDLE----SRLGD---------------------- 886
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1583 mktqikqmmdasrvktmlslVEEDRNSLQSKLSDEVAARHELEEQIKKLEHDSSSLQSAKARLENECKTLQQkvEILGEL 1662
Cdd:TIGR02169 887 --------------------LKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIED--PKGEDE 944
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024390606 1663 YQQKEMALQKKLTQeeyERQEKEQKLSAADEKAVLAIEEVKVYKQRIQDMEEELQKTE---RSYKNQIAAHEKKAHD 1736
Cdd:TIGR02169 945 EIPEEELSLEDVQA---ELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEeerKAILERIEEYEKKKRE 1018
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1395-1760 |
5.62e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 78.05 E-value: 5.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1395 DEIAGL-------KDTVKELEETNHQL---DDKIKSLRTMLDTERKQ--NAKKQKKLSETQKSLEKFEEAFSMH--SAEL 1460
Cdd:COG1196 162 EEAAGIskykerkEEAERKLEATEENLerlEDILGELERQLEPLERQaeKAERYRELKEELKELEAELLLLKLRelEAEL 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1461 SEVQIALNESKLSEEKVKAELQHVQEENARLKKSKEQLLKEAEgwserhtELTEQIKLYRKSQKDIEEALAYKENEIEVL 1540
Cdd:COG1196 242 EELEAELEELEAELEELEAELAELEAELEELRLELEELELELE-------EAQAEEYELLAELARLEQDIARLEERRREL 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1541 TNcimQLKQLDTDSASEAKDGEGLEwstkddlangelpdnEKMKTQIKQMMDAsrvktmlslvEEDRNSLQSKLSDEVAA 1620
Cdd:COG1196 315 EE---RLEELEEELAELEEELEELE---------------EELEELEEELEEA----------EEELEEAEAELAEAEEA 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1621 RHELEEQIKKLEHDSSSLQSAKARLENECKTLQQKVEILGELyQQKEMALQKKLTQEEYERQEKEQKLSAADEKAVLAIE 1700
Cdd:COG1196 367 LLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEA-EEALLERLERLEEELEELEEALAELEEEEEEEEEALE 445
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1701 EVKVYKQRIQDmEEELQKTERSYKNQIAAHEKKAHDNWLIARSAERALAEEKREAANLRQ 1760
Cdd:COG1196 446 EAAEEEAELEE-EEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYE 504
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1349-1733 |
6.44e-14 |
|
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: 77.37 E-value: 6.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1349 KQLAEKIQNLLQEKTEMLDKFSECDEKIKQAKESMKVAQEQKSILSDE----IAGLKDTVKELEETNHQLDDKIKSLRTM 1424
Cdd:TIGR04523 214 KSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEqnkiKKQLSEKQKELEQNNKKIKELEKQLNQL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1425 ------LDTERKQN---------AKKQKKLSETQKSLEKFEEAFSMHSAELSEVQIALNESKLSEEKVKAELQHVQEENA 1489
Cdd:TIGR04523 294 kseisdLNNQKEQDwnkelkselKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIE 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1490 RLKKSKEQLLKEAEGWSERHTELTEQIKLYRKSQKDIEEALAYKENEIEVLTNCIMQLKQLDTDSASEAKDGEglewsTK 1569
Cdd:TIGR04523 374 KLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLT-----NQ 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1570 DDLANGELPDNEKMKTQIKQmmdasrvktMLSLVEEDRNSLQSKLSDevaarheLEEQIKKLEHDSSSLQSAKARLENEC 1649
Cdd:TIGR04523 449 DSVKELIIKNLDNTRESLET---------QLKVLSRSINKIKQNLEQ-------KQKELKSKEKELKKLNEEKKELEEKV 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1650 KTLQQKVEILgelyQQKEMALQKKLTQEEYERQEKEQKLSAADEkaVLAIEEVKVYKQRIQdmeEELQKTERSYKNQIAA 1729
Cdd:TIGR04523 513 KDLTKKISSL----KEKIEKLESEKKEKESKISDLEDELNKDDF--ELKKENLEKEIDEKN---KEIEELKQTQKSLKKK 583
|
....
gi 2024390606 1730 HEKK 1733
Cdd:TIGR04523 584 QEEK 587
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1349-1715 |
3.04e-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: 75.48 E-value: 3.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1349 KQLAEKIQNLLQEKTEMLDKFSECDEKIKQAKE-------SMKVAQEQKSILSDEIAGLKDTVKELEETNHQLDDKIKSL 1421
Cdd:TIGR02168 687 EELEEKIAELEKALAELRKELEELEEELEQLRKeleelsrQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEEL 766
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1422 RTMLDTERKQNAKKQKKLSETQKSLEKFEEAFSMHSAELSEVQIALNEsklseekVKAELQHVQEENARLKKSKEQLLKE 1501
Cdd:TIGR02168 767 EERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTL-------LNEEAANLRERLESLERRIAATERR 839
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1502 AEGWSERHTELTEQIKLYRKSQKDIEEALAYKENEIEVLTNCIMQLkqldtdsaseakdgeglewstkddlangelpdne 1581
Cdd:TIGR02168 840 LEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASL---------------------------------- 885
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1582 kmktqikqmmdasrvktmlslvEEDRNSLQSKLSDEVAARHELEEQIKKLEHDSSSLQSAKARLENECKTLQQKV----E 1657
Cdd:TIGR02168 886 ----------------------EEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIdnlqE 943
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024390606 1658 ILGELYQQKEMALQKKLTQEEYERQEKEQKLSAADEK-----AV--LAIEEVKVYKQRIQDMEEE 1715
Cdd:TIGR02168 944 RLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKikelgPVnlAAIEEYEELKERYDFLTAQ 1008
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1348-1769 |
4.93e-13 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 75.18 E-value: 4.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1348 EKQLAEKIQNLLQEKTEMLDKFSECDEKIKQAKESMKVAQEQKSilSDEIAGLKDTVKELEETNHQLDDKIKSLRTMLDT 1427
Cdd:PTZ00121 1389 EKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKK--ADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKA 1466
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1428 ERKQNAKKQKKLSETQKSLEKFEEAFSMHSAELSEVQIALNESKLSEEKVKAELQHVQEE--NARLKKSKEQLLKEAEGW 1505
Cdd:PTZ00121 1467 EEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEakKAEEAKKADEAKKAEEKK 1546
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1506 SERHTELTEQIKLYRKSQKdIEEALAYKENeievltncimqlKQLDTDSASEAKDGEGLEWSTKDDLANGElpdnEKMKT 1585
Cdd:PTZ00121 1547 KADELKKAEELKKAEEKKK-AEEAKKAEED------------KNMALRKAEEAKKAEEARIEEVMKLYEEE----KKMKA 1609
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1586 QIKQMMDASRVKTMLSLVEEDRNSLQSKLSDEVAARHELEEQIKKLEHDSSSLQSAKARLENECKTLQQKVEILGELYQQ 1665
Cdd:PTZ00121 1610 EEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKK 1689
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1666 KEMALQKK---------LTQEEYERQEKEQKLSAADEKAVLAIEEVKVYKQRIQDMEEELQKTERSyKNQIAAHEKKAHD 1736
Cdd:PTZ00121 1690 AAEALKKEaeeakkaeeLKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEE-KKKIAHLKKEEEK 1768
|
410 420 430
....*....|....*....|....*....|...
gi 2024390606 1737 NWLIARSAERALAEEKREAANLRQKlMEVNQKT 1769
Cdd:PTZ00121 1769 KAEEIRKEKEAVIEEELDEEDEKRR-MEVDKKI 1800
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1360-1712 |
1.15e-12 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 73.56 E-value: 1.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1360 QEKTEMLDKFS---ECDEKIKQAKESMKVAQEQKSILSDEIAGLKDTVKELE-ETNHQLddKIKSLRTML-DTE------ 1428
Cdd:TIGR02169 153 VERRKIIDEIAgvaEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRrEREKAE--RYQALLKEKrEYEgyellk 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1429 -----RKQNAKKQKKLSETQKSLEKFEEAFSMHSAELSEVQIALNE-----SKLSEEK---VKAELQHVQEENARLKKSK 1495
Cdd:TIGR02169 231 ekealERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEElnkkiKDLGEEEqlrVKEKIGELEAEIASLERSI 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1496 EQLLKEAEGWSERHTELTEQIKLYRKSQKDIEEALAYKENEIEVLTNCIMQLKQLDTDSASEAKdgeglEWSTKDDLANG 1575
Cdd:TIGR02169 311 AEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELE-----EVDKEFAETRD 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1576 ELPDNEKMKTQIKQMMDASrvKTMLSLVEEDRNSLQSKLSDEVAARHELEEQIKKLEHDSSSLQSAKARLENECKTLQQK 1655
Cdd:TIGR02169 386 ELKDYREKLEKLKREINEL--KRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAAD 463
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 2024390606 1656 VEIlgelYQQKEMALQKKLTQEEYERQEKEQKLSAAdEKAVLAIEEVKVYKQRIQDM 1712
Cdd:TIGR02169 464 LSK----YEQELYDLKEEYDRVEKELSKLQRELAEA-EAQARASEERVRGGRAVEEV 515
|
|
| MIAL |
cd11891 |
Melanoma Inhibitory Activity-Like protein; MIAL is specifically expressed in the cochlea and ... |
109-167 |
1.73e-12 |
|
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: 64.88 E-value: 1.73e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024390606 109 GKAMKDFQGPDCRFVNFKKGETVYVYYKLI--GMSTELWAGSIGSD--------FGYFPKDLLEINHNY 167
Cdd:cd11891 14 ARAEDDYNAPDCRFINIKKGQLIYVYSKLVkeNGAGEFWSGSVYSEryvdqmgiVGYFPSNLVKEQTVY 82
|
|
| MIA |
cd11890 |
Melanoma Inhibitory Activity protein; MIA is a single domain protein that adopts a Src ... |
110-183 |
8.73e-12 |
|
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: 63.36 E-value: 8.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 110 KAMKDFQGPDCRFVNFKKGETVYVYYKLIGMSTELWAGSIGSDF--------GYFPKDLLEINHNYTNEELELPTEETDF 181
Cdd:cd11890 17 VALQDYMAPDCRFIPIQRGQVVYVFSKLKGRGRLFWGGSVQGDYygeqaarlGYFPSSIVQEDQYLKPGKVEVKTDKWDF 96
|
..
gi 2024390606 182 VC 183
Cdd:cd11890 97 YC 98
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1348-1774 |
9.68e-12 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 70.94 E-value: 9.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1348 EKQLAEKIQNLLQEKTEMLDKFSECDEKIKQAKESMKVAQEQKSILSDEIAGLKDTVKELE--ETNHQLDDKIKSLRTML 1425
Cdd:PTZ00121 1300 EKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEaaEEKAEAAEKKKEEAKKK 1379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1426 DTERKQNAKKQKKLSETQKSLEKFEEAFSMHSAELSEVQIALNESKLSEEKVKAELQHVQEENAR----LKKSKEQlLKE 1501
Cdd:PTZ00121 1380 ADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKkadeAKKKAEE-AKK 1458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1502 AEGWSERHTELTEQIKLYRKSQKDIEEALAYKENEIEVLTNCIMQLKQLDTDSASEAKDGEglEWSTKDDLANGElpdnE 1581
Cdd:PTZ00121 1459 AEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAE--EAKKADEAKKAE----E 1532
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1582 KMKTQIKQMMDASRVKTMLSLVEEDRNSLQSKLSDEvaARHELEEQIKKLEHDSSSLQSAKARLENECKTLQQKVEILGE 1661
Cdd:PTZ00121 1533 AKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEE--AKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAE 1610
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1662 LYQQKEMALQK--KLTQEEYERQEKEQkLSAADEKAVLAIEEVKVYKQRIQDMEEELQKTERSYKNQiAAHEKKAHDNWL 1739
Cdd:PTZ00121 1611 EAKKAEEAKIKaeELKKAEEEKKKVEQ-LKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKK-AEEAKKAEEDEK 1688
|
410 420 430
....*....|....*....|....*....|....*
gi 2024390606 1740 IARSAERALAEEKREAANLRQKLMEVNQKTIMLQR 1774
Cdd:PTZ00121 1689 KAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKK 1723
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1348-1774 |
1.19e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 70.56 E-value: 1.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1348 EKQLAEKIQNLLQEKTEMLDKFSEcdeKIKQAKESMKVAQEQKSiLSDEIAGLKDTVKELEETNHQLDDKIKSlrtmldT 1427
Cdd:PTZ00121 1365 KAEAAEKKKEEAKKKADAAKKKAE---EKKKADEAKKKAEEDKK-KADELKKAAAAKKKADEAKKKAEEKKKA------D 1434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1428 ERKQNAKKQKKLSETQKSLEkfeeafsmhsaelsEVQIALNESKLSEEKVKA-ELQHVQEEnarlKKSKEQLLKEAEGWS 1506
Cdd:PTZ00121 1435 EAKKKAEEAKKADEAKKKAE--------------EAKKAEEAKKKAEEAKKAdEAKKKAEE----AKKADEAKKKAEEAK 1496
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1507 ERHTELTEQIKLYRKSQKDIEEALAYKENEIEvltncimqlKQLDTDSASEAKDGEglEWSTKDDLANGElpdnEKMKTQ 1586
Cdd:PTZ00121 1497 KKADEAKKAAEAKKKADEAKKAEEAKKADEAK---------KAEEAKKADEAKKAE--EKKKADELKKAE----ELKKAE 1561
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1587 IKQMMDASRVKtmlslvEEDRNSLQSKLSDEVAARHELEEQIKKLEHDSSSLQSAKARLENECKTlqqKVEILGELYQQK 1666
Cdd:PTZ00121 1562 EKKKAEEAKKA------EEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKI---KAEELKKAEEEK 1632
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1667 EMALQKKLTQEEYERqeKEQKLSAADEKAVLAIEEVKVYKQRIQDMEEELQKTERSYKNQIAAHEKKAHDnwliARSAE- 1745
Cdd:PTZ00121 1633 KKVEQLKKKEAEEKK--KAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEE----AKKAEe 1706
|
410 420 430
....*....|....*....|....*....|.
gi 2024390606 1746 --RALAEEKREAANLRQKLMEVNQKTIMLQR 1774
Cdd:PTZ00121 1707 lkKKEAEEKKKAEELKKAEEENKIKAEEAKK 1737
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1368-1767 |
1.25e-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: 70.05 E-value: 1.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1368 KFSECDEKIKQAKESMKVAQE-----QKSILSDE--IAGLKDTVKELEETNHQLDDKIKSLRTMLD-------------- 1426
Cdd:TIGR04523 34 EEKQLEKKLKTIKNELKNKEKelknlDKNLNKDEekINNSNNKIKILEQQIKDLNDKLKKNKDKINklnsdlskinseik 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1427 TERKQNAKKQKKLSETQKSLEKFEEAFSMHSAELSEVQIALNES--------------KLSEEKVKAELQHVQEENARLK 1492
Cdd:TIGR04523 114 NDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLnnkyndlkkqkeelENELNLLEKEKLNIQKNIDKIK 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1493 K---SKEQLLKEAEGWSERHTELTEQIKLYRKSQKDIEEALAYKENEIEVLTNCIMQLK-QLDTDSASEAKDGEGLEWST 1568
Cdd:TIGR04523 194 NkllKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQtQLNQLKDEQNKIKKQLSEKQ 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1569 KD-DLANGELPDNEK----MKTQI------KQMMDASRVKTMLSLVEEDRNSLQSKLSDEVAARHELEEQIKKLEHDSSS 1637
Cdd:TIGR04523 274 KElEQNNKKIKELEKqlnqLKSEIsdlnnqKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTN 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1638 LQSAKARLENECKTLQQKVEILGELYQQKemalQKKLTQEEYERQEKEQKLSAADEKAVLAIEEVKVYKQRIQDMEEELQ 1717
Cdd:TIGR04523 354 SESENSEKQRELEEKQNEIEKLKKENQSY----KQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIE 429
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1718 ----------KTERSYKNQIAAHEKKAHDNWLIARSAERALAEEKREAANLRQKLMEVNQ 1767
Cdd:TIGR04523 430 rlketiiknnSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQK 489
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1348-1768 |
3.40e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 68.94 E-value: 3.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1348 EKQLAEKIQNL------LQEKTEMLDKFSECDEKIKQAKESMKVAQEQKSILSDEIAGLKDTVKELEETNHQLDDKIKSL 1421
Cdd:PRK03918 199 EKELEEVLREIneisseLPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEEL 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1422 RTMLD--TERKQNAKKQKKLS----ETQKSLEKFEEAFSMHSAELSEVQ--IALNESKLSE-EKVKAELQHVQEENARLK 1492
Cdd:PRK03918 279 EEKVKelKELKEKAEEYIKLSefyeEYLDELREIEKRLSRLEEEINGIEerIKELEEKEERlEELKKKLKELEKRLEELE 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1493 KSKE------QLLKEAEGWSERHTELT-----EQIKLYRKSQKDIEEALAYKENEIEVLTNCIMQLKqldtDSASEAKDG 1561
Cdd:PRK03918 359 ERHElyeeakAKKEELERLKKRLTGLTpekleKELEELEKAKEEIEEEISKITARIGELKKEIKELK----KAIEELKKA 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1562 EG--------LEWSTKDDLAN---GELPDNEK-MKTQIKQMMDASRVKTMLS--LVEEDRNSLQSKLSDEV-AARHELEE 1626
Cdd:PRK03918 435 KGkcpvcgreLTEEHRKELLEeytAELKRIEKeLKEIEEKERKLRKELRELEkvLKKESELIKLKELAEQLkELEEKLKK 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1627 -QIKKLEHDSSSLQSAKAR---LENECKTLQQKVEILGELYQQKEmALQKKLTQEEYERQEKEQKLSaadEKAVLAIEEV 1702
Cdd:PRK03918 515 yNLEELEKKAEEYEKLKEKlikLKGEIKSLKKELEKLEELKKKLA-ELEKKLDELEEELAELLKELE---ELGFESVEEL 590
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024390606 1703 kvyKQRIQDMEEELQK--TERSYKNQIAAHEKKAHDNWLIARSAERALAEEKREAANLRQKLMEVNQK 1768
Cdd:PRK03918 591 ---EERLKELEPFYNEylELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKK 655
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1350-1565 |
4.87e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 68.42 E-value: 4.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1350 QLAEKIQNLLQEKTEMLDKFSECDEKIKQAKESMKVAQEQKSILSDEIAGLKDTVKELEETNHQLDDKIKSLRTMLDTER 1429
Cdd:COG1196 271 ELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAE 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1430 KQNAKKQKKLSETQKSLEKFEEAFSMHSAELSEVQIALNESKLSEEKVKAELQHVQEENARLKKSKEQLLKEAEGWSERH 1509
Cdd:COG1196 351 EELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEAL 430
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2024390606 1510 TELTEQIKLYRKSQKDIEEALAYKENEIEVLTNCIMQLKQLDTDSASEAKDGEGLE 1565
Cdd:COG1196 431 AELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEEL 486
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1337-1733 |
7.54e-11 |
|
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: 67.69 E-value: 7.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1337 LSVKSRMYQVTEKQLAEKIQN-LLQEKTEMLDKFSECDEKIKQAKESMKVAQEQKSILSDEIAGLKDTVKELEETNHQLD 1415
Cdd:pfam02463 645 ESGLRKGVSLEEGLAEKSEVKaSLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLA 724
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1416 DKIKSLRTMLDTERKQNakKQKKLSETQKSLEKFEEAFSmhsAELSEVQIALNESKLSEEKVKAELQHVQEENARLKKSK 1495
Cdd:pfam02463 725 DRVQEAQDKINEELKLL--KQKIDEEEEEEEKSRLKKEE---KEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQ 799
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1496 EQLLKEAEgwserhTELTEQIKLYRKSQKDIEEALAYKENEIEvltncimqlkQLDTDSASEAKDGEGLEWSTKDDLANG 1575
Cdd:pfam02463 800 EEELRALE------EELKEEAELLEEEQLLIEQEEKIKEEELE----------ELALELKEEQKLEKLAEEELERLEEEI 863
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1576 ELPDNEKMKTQIKQMMDASRVKTMLSLVE-EDRNSLQSKLSDEVAARHELEEQIKKLEHDSSSLqsakarlENECKTLQQ 1654
Cdd:pfam02463 864 TKEELLQELLLKEEELEEQKLKDELESKEeKEKEEKKELEEESQKLNLLEEKENEIEERIKEEA-------EILLKYEEE 936
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024390606 1655 KVEILGELYQQKEMALQKKLTQEEYERQEKEQKLSAAdEKAVLAIEEVKVYKQRIQDMEEELQKTERSYKNQIAAHEKK 1733
Cdd:pfam02463 937 PEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELG-KVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEE 1014
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1348-1762 |
1.07e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 66.71 E-value: 1.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1348 EKQLAEKIQNLL----QEKTEMLDKFSECDEKIKQAKESMKV---AQEQKSILSDEIAGLKDTVKELEETNHQLDDKIKS 1420
Cdd:COG4717 48 LERLEKEADELFkpqgRKPELNLKELKELEEELKEAEEKEEEyaeLQEELEELEEELEELEAELEELREELEKLEKLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1421 LRTM-----LDTERKQNAKKQKKLSETQKSLEKFEEAFSMHSAELSEVQIALNES-KLSEEKVKAELQHVQEENARLKKS 1494
Cdd:COG4717 128 LPLYqeleaLEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELlEQLSLATEEELQDLAEELEELQQR 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1495 KEQLLKEAEGWSERHTELTEQIKLYRKSQKDIEEALAYKENEIE-VLTNCIMQLKQLDTDSASEAKDGEGLEWSTKDDLA 1573
Cdd:COG4717 208 LAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLlLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLA 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1574 NGELPDNEKMKTQIKQMMDASRVKTMLSLVEEDRNSLQSKLS-DEVAARHELEEQIKKLEHdsssLQSAKARLENECKTL 1652
Cdd:COG4717 288 LLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGlPPDLSPEELLELLDRIEE----LQELLREAEELEEEL 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1653 QQKV------EILGELYQQKEMALQKKLTQEEyERQEKEQKLSAADE---------KAVLAIEEVKVYKQRIQDMEEELQ 1717
Cdd:COG4717 364 QLEEleqeiaALLAEAGVEDEEELRAALEQAE-EYQELKEELEELEEqleellgelEELLEALDEEELEEELEELEEELE 442
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 2024390606 1718 KTERSYKNqiaAHEKKAHDNWLIAR-SAERALAEEKREAANLRQKL 1762
Cdd:COG4717 443 ELEEELEE---LREELAELEAELEQlEEDGELAELLQELEELKAEL 485
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1348-1647 |
1.23e-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: 67.00 E-value: 1.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1348 EKQLAEKIQNLLQEKTEM-----LDKFSECDEKIKQAKESMKVAQEQKSILSDEIAGLKDTVKELEETNHQLDDKIKSLR 1422
Cdd:TIGR02168 208 QAEKAERYKELKAELRELelallVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1423 TMLDTERKQNAKKQKKLSETQKSLEKFEEAFSMHSAELSEVQIALNESKLSEEKVKAELQHVQEENARLKKSKEQLLKEA 1502
Cdd:TIGR02168 288 KELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAEL 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1503 EGWSERHTELTEQIKLYRKSQKDIEEALAYKENEIEVLTNcimQLKQLDTDSASEAKDGEGLEwstkddlanGELPDNEK 1582
Cdd:TIGR02168 368 EELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEA---RLERLEDRRERLQQEIEELL---------KKLEEAEL 435
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024390606 1583 MKTQikqmMDASRVKTMLSLVEEDRNSLQSKLSDEVAARHELEEQIKKLEHDSSSLQSAKARLEN 1647
Cdd:TIGR02168 436 KELQ----AELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLER 496
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1349-1768 |
1.48e-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: 67.00 E-value: 1.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1349 KQLAEKIQNLLQEKTEMLDKFSECDEKIKQAKESMKVAQEQKSILSDEIAGLKDTVKELEETNHQLDDKIKSLRTMLdtE 1428
Cdd:TIGR02168 354 ESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKL--E 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1429 RKQNAKKQKKLSETQKSLEKFEEAFSMHSAELSEVQIALNESKLSEEKVKAELQHVQEENARLKKSKE----------QL 1498
Cdd:TIGR02168 432 EAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQEnlegfsegvkAL 511
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1499 LKEAEGWSERHTELTEQIKLYRKSQKDIEEALAYKENEIEVLTN-----CIMQLKQ------------LDTDSASEAKDG 1561
Cdd:TIGR02168 512 LKNQSGLSGILGVLSELISVDEGYEAAIEAALGGRLQAVVVENLnaakkAIAFLKQnelgrvtflpldSIKGTEIQGNDR 591
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1562 EGLEWSTK-----------------------------DDLANG------------------------------------- 1575
Cdd:TIGR02168 592 EILKNIEGflgvakdlvkfdpklrkalsyllggvlvvDDLDNAlelakklrpgyrivtldgdlvrpggvitggsaktnss 671
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1576 ------ELPDNEK-------------------------MKTQIKQMMDA--------SRVKTMLSLVEEDRNSLQSKLSD 1616
Cdd:TIGR02168 672 ilerrrEIEELEEkieeleekiaelekalaelrkeleeLEEELEQLRKEleelsrqiSALRKDLARLEAEVEQLEERIAQ 751
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1617 EVAARHELEEQIKKLEHDSSSLQSAKARLENECKTLQQKVE-ILGELYQQKEM--ALQKKLTQEEYERQEKEQKLSAADE 1693
Cdd:TIGR02168 752 LSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEqLKEELKALREAldELRAELTLLNEEAANLRERLESLER 831
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024390606 1694 KAVLAIEEVKVYKQRIQDMEEELQKTERSYKNQIAAHEK--KAHDNWLIAR-SAERALAEEKREAANLRQKLMEVNQK 1768
Cdd:TIGR02168 832 RIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEEleSELEALLNERaSLEEALALLRSELEELSEELRELESK 909
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1344-1758 |
1.51e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 66.63 E-value: 1.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1344 YQVTEKQLAEkIQNLLQEKTEMLDKF----SECDEKIKQAKESM-KVAQEQKSI------LSDEIAGLKDTVKELEETNh 1412
Cdd:PRK03918 160 YENAYKNLGE-VIKEIKRRIERLEKFikrtENIEELIKEKEKELeEVLREINEIsselpeLREELEKLEKEVKELEELK- 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1413 qldDKIKSLRTMLDTERKQNAKKQKKLSETQKSLEKFEEafsmHSAELSEVQIALNESKLSEE---KVKAELQHVQEENA 1489
Cdd:PRK03918 238 ---EEIEELEKELESLEGSKRKLEEKIRELEERIEELKK----EIEELEEKVKELKELKEKAEeyiKLSEFYEEYLDELR 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1490 RLKKSKEQLLKEAEGWSERHTELTEQIKLYRKSQKDIEEaLAYKENEIEVLTNCIMQLKQLDTDSASEAKDGEGLewsTK 1569
Cdd:PRK03918 311 EIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKE-LEKRLEELEERHELYEEAKAKKEELERLKKRLTGL---TP 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1570 DDLANgELPDNEKMKTQIkqMMDASRVKTMLSLVEEDRNSLQSKLSD-------------EVAARHELE------EQIKK 1630
Cdd:PRK03918 387 EKLEK-ELEELEKAKEEI--EEEISKITARIGELKKEIKELKKAIEElkkakgkcpvcgrELTEEHRKElleeytAELKR 463
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1631 LEHDSSSLQSAKARLENECKTLQQKVEILGELYQQKEMALQKKLTQEEYERQEKEqKLSAADEKAVLAIEEVKVYKQRIQ 1710
Cdd:PRK03918 464 IEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLE-ELEKKAEEYEKLKEKLIKLKGEIK 542
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 2024390606 1711 DMEEELQKTErSYKNQIAAHEKKAHDnwliarsAERALAEEKREAANL 1758
Cdd:PRK03918 543 SLKKELEKLE-ELKKKLAELEKKLDE-------LEEELAELLKELEEL 582
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1374-1730 |
2.32e-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: 66.23 E-value: 2.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1374 EKIKQAKesmkvAQEQKSILsDEIAGL-------KDTVKELEETNH---QLDDKIKSLRTMLDTERKQ--NAKKQKKLSE 1441
Cdd:TIGR02168 147 SEIIEAK-----PEERRAIF-EEAAGIskykerrKETERKLERTREnldRLEDILNELERQLKSLERQaeKAERYKELKA 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1442 TQKSLEKFEEAFSMHSA--ELSEVQIALNESKLSEEKVKAELQHVQEENARLKKskeqllkeaegwseRHTELTEQIKLY 1519
Cdd:TIGR02168 221 ELRELELALLVLRLEELreELEELQEELKEAEEELEELTAELQELEEKLEELRL--------------EVSELEEEIEEL 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1520 RKSQKDIEEALAYKENEIEVLTNcimQLKQLDTDSasEAKDGEGLEWSTKDDLANGELPDNEKMKTQIKQMMDAsrvktM 1599
Cdd:TIGR02168 287 QKELYALANEISRLEQQKQILRE---RLANLERQL--EELEAQLEELESKLDELAEELAELEEKLEELKEELES-----L 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1600 LSLVEEDRNSLQSKLSDEVAARHELEEQIKKLEHDSSSLQSAKARLENECKTLQQKVEILGELYQQKEMALQKKLTQEEY 1679
Cdd:TIGR02168 357 EAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELK 436
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 2024390606 1680 ERQEKEQKLSAADEKAVLAIEEVKVYKQRIQDMEEELQKTERSYKNQIAAH 1730
Cdd:TIGR02168 437 ELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQL 487
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1345-1538 |
2.79e-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: 65.85 E-value: 2.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1345 QVTEKQLAEKIQNLLQEKTEMLDKFSECDEKIKQAKESMKVAQEQKSILSDEIAGLKDTVKELEETNHQLDDKIKSLRtm 1424
Cdd:TIGR02168 753 SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLE-- 830
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1425 ldterKQNAKKQKKLSETQKSLEKFEEAFSMHSAELSEVQIALNESKLSEEKVKAELQHVQEENARLKKSKEQLLKEAEG 1504
Cdd:TIGR02168 831 -----RRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRE 905
|
170 180 190
....*....|....*....|....*....|....
gi 2024390606 1505 WSERHTELTEQIKLYRKSQKDIEEALAYKENEIE 1538
Cdd:TIGR02168 906 LESKRSELRRELEELREKLAQLELRLEGLEVRID 939
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
428-946 |
2.97e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 65.93 E-value: 2.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 428 ESKHHKLDEYANGATELhnQRDNEEERDSDVLitKDAFSENKKSGDSVNVDMFESEQTKEKRDEAMPVSK--------KE 499
Cdd:PTZ00121 1367 EAAEKKKEEAKKKADAA--KKKAEEKKKADEA--KKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKadeakkkaEE 1442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 500 APTATQLDDLSEELSRREPVGASDPDAKEKTNKTEQFEEQLLTDETVLHPEELKSTAvpdppvlhspgDGLKFKSFVEGK 579
Cdd:PTZ00121 1443 AKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKA-----------DEAKKAAEAKKK 1511
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 580 QDAL-----SPPAGDVNQSPEGVLLAETEKEEEKFGGDTLKESSEnnfkHRKLWEKMKEKGKAKYEPSGDVLAKPVEDVQ 654
Cdd:PTZ00121 1512 ADEAkkaeeAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEE----LKKAEEKKKAEEAKKAEEDKNMALRKAEEAK 1587
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 655 NTSQSDTGDTDllkdKLEQEMPVVEKEILRQEEDLK----QTREADHENQRPISVKKEPEIERGSMKETSADERDPSRRG 730
Cdd:PTZ00121 1588 KAEEARIEEVM----KLYEEEKKMKAEEAKKAEEAKikaeELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKA 1663
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 731 AAEQPRPWENETEYSEADVKEELSRNLGKMTIFE-------ERIEKSSPEEKSKS-------------AAQNTNAENSTQ 790
Cdd:PTZ00121 1664 AEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEaeeakkaEELKKKEAEEKKKAeelkkaeeenkikAEEAKKEAEEDK 1743
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 791 QGTAHTDNEDSDRNLGTSSARETTLRLELQSEEPDAEEDPDLKQEEELLEDENAASAKLLQARLANIQ-GNAQTTRstnp 869
Cdd:PTZ00121 1744 KKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIeGGKEGNL---- 1819
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 870 dlgVLSEAVSGTVNPTYETGEKTNSFSEDTKEISRVQ-----DAHEVGNKEVDKPVSEDTKLDEIEHVMED------NKE 938
Cdd:PTZ00121 1820 ---VINDSKEMEDSAIKEVADSKNMQLEEADAFEKHKfnknnENGEDGNKEADFNKEKDLKEDDEEEIEEAdeiekiDKD 1896
|
....*...
gi 2024390606 939 SSEAEEPS 946
Cdd:PTZ00121 1897 DIEREIPN 1904
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1348-1766 |
4.07e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 65.34 E-value: 4.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1348 EKQLAEKIQNLLQEKTEMLDKFSECDEKIKQAKEsmkvAQEQKSILSDEIAGLKDTVKELEETNHQLDDKIKSLRTMLDT 1427
Cdd:COG1196 350 EEELEEAEAELAEAEEALLEAEAELAEAEEELEE----LAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEE 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1428 ERKQNAKKQKKLSETQKSLEKFEEAFSMHSAELSEVQIALNESKLSEEKVKAELQHVQEENARLK---KSKEQLLKEAEG 1504
Cdd:COG1196 426 LEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAarlLLLLEAEADYEG 505
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1505 WSERHTELTEQIKLYRKSQKDIEEALAYKENEIEVLTNCIMQLKQLDTDSASEAKDGEGLEWSTK---------DDLANG 1575
Cdd:COG1196 506 FLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKagratflplDKIRAR 585
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1576 ELPDNEKMKTQIKQMM----------DASRVKTMLSLVEEDRNSLQSKLSDEVAARHELEEQIKKLEHD------SSSLQ 1639
Cdd:COG1196 586 AALAAALARGAIGAAVdlvasdlreaDARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEggsaggSLTGG 665
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1640 SAKARLENECKTLQQKVEILGELYQQKEMALQKKLTQEEYERQEKEQKLSAADEKAVLAIEEVKVYKQRIQDMEEELQKT 1719
Cdd:COG1196 666 SRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEE 745
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1720 ERSYKNQIAAHEKKAhdnwliarsaerALAEEKREAANLRQKLME---VN 1766
Cdd:COG1196 746 ELLEEEALEELPEPP------------DLEELERELERLEREIEAlgpVN 783
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1354-1774 |
4.46e-10 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 64.86 E-value: 4.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1354 KIQNLLQEKTEMLDKFsecdeKIKQAKESMKVAQEQKSILSDEIAGLKDTVKELEETNHQLDDKIKSLRTMLDTERKQNA 1433
Cdd:PRK04778 83 DIEEQLFEAEELNDKF-----RFRKAKHEINEIESLLDLIEEDIEQILEELQELLESEEKNREEVEQLKDLYRELRKSLL 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1434 KKQKKLSETQKSLEKFEEAFsmhSAELSEVqIALNESKlSEEKVKAELQHVQEENARLKKSKEQ---LLKEAEgwserhT 1510
Cdd:PRK04778 158 ANRFSFGPALDELEKQLENL---EEEFSQF-VELTESG-DYVEAREILDQLEEELAALEQIMEEipeLLKELQ------T 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1511 ELTEQIK-L---YRK--------SQKDIEEALAYKENEIEvltNCIMQLKQLDTDSASEAkdgeglewstkddlangelp 1578
Cdd:PRK04778 227 ELPDQLQeLkagYRElveegyhlDHLDIEKEIQDLKEQID---ENLALLEELDLDEAEEK-------------------- 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1579 dNEKMKTQIKQMMDAsrvktmlslveedrnslqskLSDEVAARHELEEQIKKLehdSSSLQSAKARLenecKTLQQKVEI 1658
Cdd:PRK04778 284 -NEEIQERIDQLYDI--------------------LEREVKARKYVEKNSDTL---PDFLEHAKEQN----KELKEEIDR 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1659 LGELYQQKEMALQKkltQEEYERQEKEqkLSAADEKAVLAIEEVKVYKQRIQDMEEELQKTERSYKNQiaaHEKkahdnw 1738
Cdd:PRK04778 336 VKQSYTLNESELES---VRQLEKQLES--LEKQYDEITERIAEQEIAYSELQEELEEILKQLEEIEKE---QEK------ 401
|
410 420 430
....*....|....*....|....*....|....*.
gi 2024390606 1739 liARSAERALAEEKREAanlRQKLMEVNQKTIMLQR 1774
Cdd:PRK04778 402 --LSEMLQGLRKDELEA---REKLERYRNKLHEIKR 432
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1345-1724 |
8.22e-10 |
|
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: 64.27 E-value: 8.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1345 QVTEKQLAEKIQNLLQEKTEMLDKFSECDEKIKQakesmkvaqeqksiLSDEIAGLKDTVKELEETNHQLDDKIKSLRTM 1424
Cdd:TIGR04523 306 QDWNKELKSELKNQEKKLEEIQNQISQNNKIISQ--------------LNEQISQLKKELTNSESENSEKQRELEEKQNE 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1425 LDTERKQNAKKQKKLSETQKSLEKFEeafsmhsaelSEVQIALNESKLSEEKVKaelqhvqeenaRLKKSKEQLLKEaeg 1504
Cdd:TIGR04523 372 IEKLKKENQSYKQEIKNLESQINDLE----------SKIQNQEKLNQQKDEQIK-----------KLQQEKELLEKE--- 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1505 wserHTELTEQIKLYRKSQKDIEEALAYKENEIEVLTNCIMQLK-QLDTDSASEAKDGEGLEWSTKddlangELPDNEKM 1583
Cdd:TIGR04523 428 ----IERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLEtQLKVLSRSINKIKQNLEQKQK------ELKSKEKE 497
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1584 KTQIKQmmdasrVKTMLSLVEEDRNSLQSKLSDEVaarHELEEQIKKLEHDSSSLQSAKARLENECKTLQQKVEILGely 1663
Cdd:TIGR04523 498 LKKLNE------EKKELEEKVKDLTKKISSLKEKI---EKLESEKKEKESKISDLEDELNKDDFELKKENLEKEIDE--- 565
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024390606 1664 QQKEMAlQKKLTQEEYER-QEKEQKLSAADEKAVLAI-EEVKVYKQRIQDMEEELQKTERSYK 1724
Cdd:TIGR04523 566 KNKEIE-ELKQTQKSLKKkQEEKQELIDQKEKEKKDLiKEIEEKEKKISSLEKELEKAKKENE 627
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
1338-1724 |
9.78e-10 |
|
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: 63.55 E-value: 9.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1338 SVKSRMYQVTEKQLAEKIQNLLQEKTEMLDKFSECDEKIKQAKEsMKVAQEQKSILSDEIAGLKDTVKELEETNhqldDK 1417
Cdd:pfam05622 55 TPGGKKYLLLQKQLEQLQEENFRLETARDDYRIKCEELEKEVLE-LQHRNEELTSLAEEAQALKDEMDILRESS----DK 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1418 IKSLRTMLDTERKQ-----NAKKQKKLSE------TQKSLEKFEEAFSMHSA----ELSEVQIALNESKLSEEKVKA--- 1479
Cdd:pfam05622 130 VKKLEATVETYKKKledlgDLRRQVKLLEernaeyMQRTLQLEEELKKANALrgqlETYKRQVQELHGKLSEESKKAdkl 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1480 --ELQHVQEENARLKKSKEQLLkeaegwSERHT--ELTEQIKLYRKSQKDIEEALAYKENEIEVLTNCIMQLKQLDTDSA 1555
Cdd:pfam05622 210 efEYKKLEEKLEALQKEKERLI------IERDTlrETNEELRCAQLQQAELSQADALLSPSSDPGDNLAAEIMPAEIREK 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1556 -----SEAKD-GEGLEWSTKDDLA--NGELPD----NEKMKTQIKqmMDASRVKTMLSLVEEDRNSLQ---SKLSDEVAA 1620
Cdd:pfam05622 284 lirlqHENKMlRLGQEGSYRERLTelQQLLEDanrrKNELETQNR--LANQRILELQQQVEELQKALQeqgSKAEDSSLL 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1621 RHELEEQIKKLEHDSSSLQSAKARLENECKTLQQKVeilgelyQQKEMALQKKLTQEEYERQEKEQKLSAADEKA----- 1695
Cdd:pfam05622 362 KQKLEEHLEKLHEAQSELQKKKEQIEELEPKQDSNL-------AQKIDELQEALRKKDEDMKAMEERYKKYVEKAksvik 434
|
410 420 430
....*....|....*....|....*....|....*.
gi 2024390606 1696 -------VLAIEEVKVYKQRIQDMEEELQKTERSYK 1724
Cdd:pfam05622 435 tldpkqnPASPPEIQALKNQLLEKDKKIEHLERDFE 470
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1390-1751 |
1.96e-09 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 61.84 E-value: 1.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1390 KSILSDEIAGLKDTVKELEETNHQLDDK---IKSLRTMLDTERKQNAKKQKKLSETQKSLEKFEEAFSMHSAELSEVQia 1466
Cdd:COG4372 30 SEQLRKALFELDKLQEELEQLREELEQAreeLEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQ-- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1467 lneskLSEEKVKAELQHVQEENARLKKSKEQLlkeaegwSERHTELTEQIKLYRKSQKDIEEALAYKENEIEVLTNcimQ 1546
Cdd:COG4372 108 -----EEAEELQEELEELQKERQDLEQQRKQL-------EAQIAELQSEIAEREEELKELEEQLESLQEELAALEQ---E 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1547 LKQLDTDSASEAKDGEGLEwstkddlANGELPDNEKMKTQIKQMMDASRVKTMLSLVEEDRNSLQSKLSDEVAARHELEE 1626
Cdd:COG4372 173 LQALSEAEAEQALDELLKE-------ANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1627 QIKKLEHDSSSLQSAKARLENECKTLQQKVEILGELYQQKEMALQKKLTQEEYERQEKEQKLSAADEKAVLAIEEVKVYK 1706
Cdd:COG4372 246 EDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELA 325
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 2024390606 1707 QRIQDMEEELQKTERSYKNQIAAHEKKAHDNWLIARSAERALAEE 1751
Cdd:COG4372 326 KKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGVADG 370
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1349-1764 |
2.27e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 62.77 E-value: 2.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1349 KQLAEKIQNLLQEKTEMLDKFSECDEKIKQAKESMKVAQEQkSILSDEIAGLKDTVKELEETNHQLDDKIKSLRTMLDTE 1428
Cdd:PRK03918 255 RKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEY-IKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKEL 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1429 RKQNAKK----------QKKLSETQKSLEKFEEAFSM------HSAELSEVQIALNESKLSE-----EKVKAELQHVQEE 1487
Cdd:PRK03918 334 EEKEERLeelkkklkelEKRLEELEERHELYEEAKAKkeelerLKKRLTGLTPEKLEKELEElekakEEIEEEISKITAR 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1488 NARLKKSKEQL------LKEAEG--------WSERHTEltEQIKLYRKSQKDIEEALAYKENEIEVLTNcimQLKQLDTD 1553
Cdd:PRK03918 414 IGELKKEIKELkkaieeLKKAKGkcpvcgreLTEEHRK--ELLEEYTAELKRIEKELKEIEEKERKLRK---ELRELEKV 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1554 SASEAkdgeglEWSTKDDLAngELPDNEKMKTQIKQMMDASRVKTMLSLVEEDRNSLQSKLS---DEVAARHELEEQIKK 1630
Cdd:PRK03918 489 LKKES------ELIKLKELA--EQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKslkKELEKLEELKKKLAE 560
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1631 LEHDSSSLQSAKARLENECKTLQQK-VEILGELYQQKEMALQK--KLTQEEYERQEKEQKLSAADEKAVLAIEEVKVYKQ 1707
Cdd:PRK03918 561 LEKKLDELEEELAELLKELEELGFEsVEELEERLKELEPFYNEylELKDAEKELEREEKELKKLEEELDKAFEELAETEK 640
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 2024390606 1708 RIQDMEEELQKTERSYKNQiaAHEKKaHDNWLIARSAERALAEEKREAANLRQKLME 1764
Cdd:PRK03918 641 RLEELRKELEELEKKYSEE--EYEEL-REEYLELSRELAGLRAELEELEKRREEIKK 694
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1348-1788 |
2.34e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 62.65 E-value: 2.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1348 EKQLAEKIQNLLQEKTEMLDKFSECDEKIKQAKESMKVAQEQKSILSDEIAGLKDTVKELEETNHQLDDKIKSLRTMLDT 1427
Cdd:COG1196 311 RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLE 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1428 ERKQNAKKQKKLSETQKSL-------EKFEEAFSMHSAELSEVQIALNESKLSEEKVKAELQHVQEENARLKKSKEQLLK 1500
Cdd:COG1196 391 ALRAAAELAAQLEELEEAEeallerlERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLE 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1501 EAEGWSERHTELTEQIKLYRKSQKDIEEALAYKENEIEVLTNCIMQLKQ--LDTDSASEAKDGEGLEWSTKDDLANGELP 1578
Cdd:COG1196 471 EAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLrgLAGAVAVLIGVEAAYEAALEAALAAALQN 550
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1579 DNEKMKTQIKQMMDASRVK-----TMLSLVEEDRNSLQSKLSDEVA----------ARHELEEQIKKLEHDSSSLQSAKA 1643
Cdd:COG1196 551 IVVEDDEVAAAAIEYLKAAkagraTFLPLDKIRARAALAAALARGAigaavdlvasDLREADARYYVLGDTLLGRTLVAA 630
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1644 RLENECKTLQQKVEILGELYQQKEMALQKKLTQEEYERQEKEQKLSAADEKAVLAIEEVKVYKQRIQDMEEELQKTERSY 1723
Cdd:COG1196 631 RLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELA 710
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024390606 1724 KNQIAAHEkkahdnwliarsAERALAEEKREAANLRQKLMEVNQKTIMLQRPLIVKPTPGRPDRQ 1788
Cdd:COG1196 711 EAEEERLE------------EELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLE 763
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1339-1721 |
2.47e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 62.75 E-value: 2.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1339 VKSRMYQVTEKQLAEKIQNLLQEKTEMLDKFSECDEKIKQAKESMKVA----------QEQKSILSDEIAGLKDTVKELE 1408
Cdd:PRK02224 192 LKAQIEEKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEAdevleeheerREELETLEAEIEDLRETIAETE 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1409 ETNHQLDDKIKSLRTMLDTERKQNAKKQKKLSETQKSLEKFEEAFSMHSAELSEVQIALNESKLSE-------EKVKAEL 1481
Cdd:PRK02224 272 REREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAqahneeaESLREDA 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1482 QHVQEENARLKKSKEQLLKEAEGWSERHTELTEQIKLYRKSQKDIEEALAYKENEIEVLTNCIMQLKQLDTDSASEAKDG 1561
Cdd:PRK02224 352 DDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAEL 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1562 EGLEWSTKDDLANGE-LPDNEKMKTQIKQMMDASRVKTmlslVEEDRNSLqSKLSDEVAarhELEEQIKKLEHDSSSLQS 1640
Cdd:PRK02224 432 EATLRTARERVEEAEaLLEAGKCPECGQPVEGSPHVET----IEEDRERV-EELEAELE---DLEEEVEEVEERLERAED 503
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1641 AKArLENECKTLQQKVEILGELYQQKEMALQKKLTQEEYER----------QEKEQKLSAADEKAVLAIEEVKVYKQRIQ 1710
Cdd:PRK02224 504 LVE-AEDRIERLEERREDLEELIAERRETIEEKRERAEELReraaeleaeaEEKREAAAEAEEEAEEAREEVAELNSKLA 582
|
410
....*....|.
gi 2024390606 1711 DMEEELQKTER 1721
Cdd:PRK02224 583 ELKERIESLER 593
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1374-1768 |
2.87e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 62.85 E-value: 2.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1374 EKIKQAKESMKVAQEQKSIlsdEIAGLKDTVKELEETNHQLDDKIKSLRTMLDTERK----QNAKKQKKLSETQKSLE-- 1447
Cdd:PTZ00121 1112 EEARKAEEAKKKAEDARKA---EEARKAEDARKAEEARKAEDAKRVEIARKAEDARKaeeaRKAEDAKKAEAARKAEEvr 1188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1448 ------KFEEAFSMHSAELSEVQIALNESKLSEEKVKAELQHVQEEnarlKKSKEQLLKEAEgwSERHTELTEQIKLYRK 1521
Cdd:PTZ00121 1189 kaeelrKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEE----AKKDAEEAKKAE--EERNNEEIRKFEEARM 1262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1522 SQKDIEEAL--AYKENEIEVLTNCIMQLKQLDTDSASEAKDGEGLEWSTKDDLANGELpdnEKMKTQIKQMMDASRVKTm 1599
Cdd:PTZ00121 1263 AHFARRQAAikAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEA---KKKAEEAKKKADAAKKKA- 1338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1600 lslvEEDRNSLQSKLSDEVAARHELEEQIKKLEHDSSSLQSAKARLEneckTLQQKVEILGELYQQKEMALQKKLTQEEY 1679
Cdd:PTZ00121 1339 ----EEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKAD----AAKKKAEEKKKADEAKKKAEEDKKKADEL 1410
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1680 ERQEKEQKLSaadEKAVLAIEEVKVYKQRIQDMEEELQKTERSYKNQIAAHEKKAHDNWLIARSAERA--LAEEKREAAN 1757
Cdd:PTZ00121 1411 KKAAAAKKKA---DEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAkkKAEEAKKADE 1487
|
410
....*....|.
gi 2024390606 1758 LRQKLMEVNQK 1768
Cdd:PTZ00121 1488 AKKKAEEAKKK 1498
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1345-1721 |
4.14e-09 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 61.68 E-value: 4.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1345 QVTEKQLAEKiQNLLQEKTEM---LDKFSECDEKIKQAKESMKV-AQEQKSILSDEIAGLK-----------DTVKELEE 1409
Cdd:pfam05557 58 RLLEKREAEA-EEALREQAELnrlKKKYLEALNKKLNEKESQLAdAREVISCLKNELSELRrqiqraelelqSTNSELEE 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1410 TNHQLDDKIKSLRTMldTERKQN-AKKQKKLSETQKSLEKFEEAFSMHSAElSEVQIALNESKLSEEKVKAELQHVQEEN 1488
Cdd:pfam05557 137 LQERLDLLKAKASEA--EQLRQNlEKQQSSLAEAEQRIKELEFEIQSQEQD-SEIVKNSKSELARIPELEKELERLREHN 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1489 ARLKKSKE--QLLKE-AEGWserhtelteQIKLYRksQKDIEEALAYKENEIEVLTNCIMQLKQLDTDSaseakdgeGLE 1565
Cdd:pfam05557 214 KHLNENIEnkLLLKEeVEDL---------KRKLER--EEKYREEAATLELEKEKLEQELQSWVKLAQDT--------GLN 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1566 WSTKDDLANgelpdnekmktQIKQMMdasrvKTMLSLVEEdRNSLQSKLSDEVAARHELEEQIKKLEHDSSSLQSAKARL 1645
Cdd:pfam05557 275 LRSPEDLSR-----------RIEQLQ-----QREIVLKEE-NSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRH 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1646 ENECKTLQQKVEILG---ELYQQKEMALQKKLTQEEYERQEKEQKLSAAD-------------EKAVLAIEEVKVYKQRI 1709
Cdd:pfam05557 338 KALVRRLQRRVLLLTkerDGYRAILESYDKELTMSNYSPQLLERIEEAEDmtqkmqahneemeAQLSVAEEELGGYKQQA 417
|
410
....*....|..
gi 2024390606 1710 QDMEEELQKTER 1721
Cdd:pfam05557 418 QTLERELQALRQ 429
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1348-1737 |
4.23e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 62.08 E-value: 4.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1348 EKQLAEKIQNLLQEKTEMlDKFSECDEKIKQAKESMKVAQEQKSilSDEIAGLKDTVKELEETNHQLDD-KIKSLRTMLD 1426
Cdd:PTZ00121 1429 EKKKADEAKKKAEEAKKA-DEAKKKAEEAKKAEEAKKKAEEAKK--ADEAKKKAEEAKKADEAKKKAEEaKKKADEAKKA 1505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1427 TERKQNAKKQKKLSETQKS--LEKFEEAFSMHSAELSEVQIALNESKLSEEKVKAELQHVQEENARLKKSKEQLLKEAEG 1504
Cdd:PTZ00121 1506 AEAKKKADEAKKAEEAKKAdeAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEE 1585
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1505 WSERHTELTEQIKLYRKSQKDIEEALAYKENEIEVLTNcimQLKQldtdSASEAKDGEGLEWSTKDDLANGELPDNEKMK 1584
Cdd:PTZ00121 1586 AKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAE---ELKK----AEEEKKKVEQLKKKEAEEKKKAEELKKAEEE 1658
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1585 TQIKQMMDASRVKtmlslvEEDRNSLQSKLSDEvaARHELEEQIKKLEHDSSSLQSAKARLENECKTLQQkVEILGELYQ 1664
Cdd:PTZ00121 1659 NKIKAAEEAKKAE------EDKKKAEEAKKAEE--DEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEE-LKKAEEENK 1729
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024390606 1665 QKEMALQKKLTQE----EYERQEKEQKLSAADEKAVLAIEEVKVYKQRIQDMEEELQKTERSYKNQIAAHEKKAHDN 1737
Cdd:PTZ00121 1730 IKAEEAKKEAEEDkkkaEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDN 1806
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1352-1578 |
5.92e-09 |
|
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: 60.55 E-value: 5.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1352 AEKIQNLLQEKTEMLDKFSECDEKIKQAKESMKVAQEQKSILSDEIAGLKDTVKELEETNHQLDDKIKSLRTMLDTERKQ 1431
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1432 NAKKQKKLSE----TQKSLEKFEEAFSMHSAELSEVQIAL-------NESKLSEEKVKAELQHVQEENARLKKSKEQLLK 1500
Cdd:COG4942 99 LEAQKEELAEllraLYRLGRQPPLALLLSPEDFLDAVRRLqylkylaPARREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024390606 1501 EAEGWSERHTELTEQIKLYRKSQKDIEEALAYKENEIEVLTNCIMQLKQLDTDSASEAKDGEGLEWSTKDDLANGELP 1578
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGKLP 256
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1346-1737 |
7.65e-09 |
|
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: 60.64 E-value: 7.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1346 VTEKQLAEkIQNLLQEKTEMLDKFsecdeKIKQAKESMKVAQEQKSILSDEIAGLKDTVKELEETNHQLDDKIKSLRTML 1425
Cdd:pfam06160 57 IVTKSLPD-IEELLFEAEELNDKY-----RFKKAKKALDEIEELLDDIEEDIKQILEELDELLESEEKNREEVEELKDKY 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1426 DTERKQNAKKQKKLSETQKSLEKfeeafsmhsaELSEVQIALNE-SKLSE----EKVKAELQHVQEENARLKKSKEQ--- 1497
Cdd:pfam06160 131 RELRKTLLANRFSYGPAIDELEK----------QLAEIEEEFSQfEELTEsgdyLEAREVLEKLEEETDALEELMEDipp 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1498 LLKEAEgwserhTELTEQIK----LYRKSQK--------DIEEALAYKENEIEvltNCIMQLKQLDTDSASEAkdgegle 1565
Cdd:pfam06160 201 LYEELK------TELPDQLEelkeGYREMEEegyalehlNVDKEIQQLEEQLE---ENLALLENLELDEAEEA------- 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1566 wstkddlangelpdNEKMKTQIKQMMDAsrvktmlslveedrnslqskLSDEVAARHELEEQIKKLEhdsSSLQSAKARL 1645
Cdd:pfam06160 265 --------------LEEIEERIDQLYDL--------------------LEKEVDAKKYVEKNLPEIE---DYLEHAEEQN 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1646 enecKTLQQKVEILGELYQ------QKEMALQKKLTQEEYERQEKEQKLsaADEKAV--LAIEEVKVYKQRIQDMEEElQ 1717
Cdd:pfam06160 308 ----KELKEELERVQQSYTlnenelERVRGLEKQLEELEKRYDEIVERL--EEKEVAysELQEELEEILEQLEEIEEE-Q 380
|
410 420
....*....|....*....|
gi 2024390606 1718 KTERSYKNQIAAHEKKAHDN 1737
Cdd:pfam06160 381 EEFKESLQSLRKDELEAREK 400
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1337-1656 |
1.22e-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: 60.47 E-value: 1.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1337 LSVKSRMYQVTEKQLaEKIQNLLQEKTEMLDKFSECDEKIKQAKESM-----KVAQEQKSILSDEIAGLKDTVKELEETN 1411
Cdd:TIGR02169 225 GYELLKEKEALERQK-EAIERQLASLEEELEKLTEEISELEKRLEEIeqlleELNKKIKDLGEEEQLRVKEKIGELEAEI 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1412 HQLDDKIKSLRTMLDTERKQNAKKQKKLSETQKSLEKFEEAFSMHSAELSEVQIALNESKLSEEKVKAELQHVQEENARL 1491
Cdd:TIGR02169 304 ASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAET 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1492 KKSKEQLLKEAEGWSERHTELTEQIKLYRKSQKDIEEALAYKENEIEVLtncIMQLKQLDTDsaseakdgeglewstKDD 1571
Cdd:TIGR02169 384 RDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGI---EAKINELEEE---------------KED 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1572 LAngelpdnEKMKTQikqmmdasrvktmlslvEEDRNSLQSKLSDEVAARHELEEQIKKLEHDSSSLQSAKARLENECKT 1651
Cdd:TIGR02169 446 KA-------LEIKKQ-----------------EWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARA 501
|
....*
gi 2024390606 1652 LQQKV 1656
Cdd:TIGR02169 502 SEERV 506
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1366-1776 |
1.69e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 60.08 E-value: 1.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1366 LDKFSECDEKIKQAKESMKVAQEQKSILSDEIAGLKDTVKELEETNHQLDDKIKSLRTMLDTERKQNAKKQKKLSETQKS 1445
Cdd:PRK03918 157 LDDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEEL 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1446 LEKFEEafsmhsaelSEVQIALNESKLS--EEKVKAELQHVQEENARLKKSKEQL--LKEAEGWSERHTELTEQIKLYRK 1521
Cdd:PRK03918 237 KEEIEE---------LEKELESLEGSKRklEEKIRELEERIEELKKEIEELEEKVkeLKELKEKAEEYIKLSEFYEEYLD 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1522 SQKDIEEALAYKENEIEVLtncIMQLKQLDTDSaSEAKDGEGLEWSTKDDLAngELPDNEKMKTQIKQMMD-ASRVKTML 1600
Cdd:PRK03918 308 ELREIEKRLSRLEEEINGI---EERIKELEEKE-ERLEELKKKLKELEKRLE--ELEERHELYEEAKAKKEeLERLKKRL 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1601 SLVEEDRnsLQSKLSDEVAARHELEEQIKKLEHDSSSLQSAKARLE---NECKTLQQKVEILG-ELYQQKEMALQKKLTq 1676
Cdd:PRK03918 382 TGLTPEK--LEKELEELEKAKEEIEEEISKITARIGELKKEIKELKkaiEELKKAKGKCPVCGrELTEEHRKELLEEYT- 458
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1677 EEYERQEKEQKlsaadekavLAIEEVKVYKQRIQDMEEELQKTERSYKNQIAAHEKKAHDNWLIARSAERaLAEEKREAA 1756
Cdd:PRK03918 459 AELKRIEKELK---------EIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEE-LEKKAEEYE 528
|
410 420
....*....|....*....|
gi 2024390606 1757 NLRQKLMEVNQKTIMLQRPL 1776
Cdd:PRK03918 529 KLKEKLIKLKGEIKSLKKEL 548
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1347-1768 |
1.70e-08 |
|
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: 59.74 E-value: 1.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1347 TEKQLAEKIQNLLQEKTEMLDKFSECDEKIKQAKESMKVAQEQKSILSDEIAGLKDTVKELEETNHQLDDKIKSLRTMLD 1426
Cdd:pfam05483 367 TEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQ 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1427 TERKQNAKKQKKLSETQKSLEKF-----EEAFSMHSAELSEVQIALNESKLSEEKVKA---------ELQHVQEENARLK 1492
Cdd:pfam05483 447 AREKEIHDLEIQLTAIKTSEEHYlkeveDLKTELEKEKLKNIELTAHCDKLLLENKELtqeasdmtlELKKHQEDIINCK 526
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1493 KSKEQLLKEAEGWSERHTELTEQIKLYRKSqkdieeaLAYKENEIevltncimqlkQLDTDSASEAKDGEGLEWSTKDDL 1572
Cdd:pfam05483 527 KQEERMLKQIENLEEKEMNLRDELESVREE-------FIQKGDEV-----------KCKLDKSEENARSIEYEVLKKEKQ 588
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1573 ANGELPDNEKMKTQIKqmmdaSRVKTMLSLVEEDRnSLQSKLSDEVAARHELEEQIKKLEHDsssLQSAKARLENECKTL 1652
Cdd:pfam05483 589 MKILENKCNNLKKQIE-----NKNKNIEELHQENK-ALKKKGSAENKQLNAYEIKVNKLELE---LASAKQKFEEIIDNY 659
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1653 QQKVEIlgelyqqkemalqKKLTQEEYeRQEKEQKLSAADEKAVLAIEEVKVYKQRIQDMEEELQKTERSYKNQIaaHEK 1732
Cdd:pfam05483 660 QKEIED-------------KKISEEKL-LEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKII--EER 723
|
410 420 430
....*....|....*....|....*....|....*...
gi 2024390606 1733 KAHDNWLIARSAERALAEE--KREAANLRQKLMEVNQK 1768
Cdd:pfam05483 724 DSELGLYKNKEQEQSSAKAalEIELSNIKAELLSLKKQ 761
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1337-1773 |
2.12e-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: 59.70 E-value: 2.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1337 LSVKSRMYQVTEKQLAEKIQNLLQEKTEMLDKFSECDEKIKQAkeSMKVAQeqksiLSDEIAGLKDTVKELEETNHQLDD 1416
Cdd:TIGR02169 376 VDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRL--SEELAD-----LNAAIAGIEAKINELEEEKEDKAL 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1417 KIKslrtmldterkqnaKKQKKLSETQKSLEKFEEAFSMHSAELSEVQIALNESKLSEEKVKAELQHVQEENARLKKSKE 1496
Cdd:TIGR02169 449 EIK--------------KQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEE 514
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1497 QLLKEAEGwseRHTELTEQIKLYRKSQKDIEEALAYKENEIEVLTN-----CIMQLKQLDTDSA---------SEAKDGE 1562
Cdd:TIGR02169 515 VLKASIQG---VHGTVAQLGSVGERYATAIEVAAGNRLNNVVVEDDavakeAIELLKRRKAGRAtflplnkmrDERRDLS 591
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1563 GL-------------EWSTK---------------DDLANG-ELPDNEKMKTQIKQMMDASRVKTMLSLVEEDRNSLQSK 1613
Cdd:TIGR02169 592 ILsedgvigfavdlvEFDPKyepafkyvfgdtlvvEDIEAArRLMGKYRMVTLEGELFEKSGAMTGGSRAPRGGILFSRS 671
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1614 LSDEVAarhELEEQIKKLEHDSSSLQSAKARLENECKTLQQKVEIL----------GELYQQKEMALQKKLTQEEYERQE 1683
Cdd:TIGR02169 672 EPAELQ---RLRERLEGLKRELSSLQSELRRIENRLDELSQELSDAsrkigeiekeIEQLEQEEEKLKERLEELEEDLSS 748
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1684 KEQKLSAADEKAVLAIEEVKVYKQRIQDMEEELQKTERSY--------KNQIAAHEKKAHDNWLIARSAERALAEEKREA 1755
Cdd:TIGR02169 749 LEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLshsripeiQAELSKLEEEVSRIEARLREIEQKLNRLTLEK 828
|
490
....*....|....*...
gi 2024390606 1756 ANLRQKLMEVNQKTIMLQ 1773
Cdd:TIGR02169 829 EYLEKEIQELQEQRIDLK 846
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1337-1592 |
2.50e-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: 2.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1337 LSVKSRMYQVTEKQLAEKIQNLLQEKTEMLDKFSECDEKIKQAKESMKVAQEQKSILSDEIAGLKDTVKELEETNHQLDD 1416
Cdd:TIGR04523 396 LESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSR 475
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1417 KIKSLRTMLDTERKQNAKKQKKLSETQKSLEKFEEAFSMHSAELSEvqIALNESKLSEEKVKAELQHVQEENARLKK--- 1493
Cdd:TIGR04523 476 SINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISS--LKEKIEKLESEKKEKESKISDLEDELNKDdfe 553
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1494 -SKEQLLKEAEGWSERHTELTEQIKLYRKSQKDIEEALAYKENEIEVLTNCI----MQLKQLDTDSASEAKDGEGLEwST 1568
Cdd:TIGR04523 554 lKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIeekeKKISSLEKELEKAKKENEKLS-SI 632
|
250 260
....*....|....*....|....
gi 2024390606 1569 KDDLANGElpdnEKMKTQIKQMMD 1592
Cdd:TIGR04523 633 IKNIKSKK----NKLKQEVKQIKE 652
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1600-1762 |
3.69e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.79 E-value: 3.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1600 LSLVEEDRNSLQSKLSDEVAARHELEEQIKKLEHDSSSLQSAKARLENECKTLQQKVEILG----------ELYQQKEMA 1669
Cdd:COG1196 234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLaelarleqdiARLEERRRE 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1670 LQKKLTQEEYERQEKEQKLSAADEKAVLAIEEVKVYKQRIQDMEEELQKTERSYKNQIAAHEKKAHDnwliARSAERALA 1749
Cdd:COG1196 314 LEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE----LEELAEELL 389
|
170
....*....|...
gi 2024390606 1750 EEKREAANLRQKL 1762
Cdd:COG1196 390 EALRAAAELAAQL 402
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1775-1983 |
4.20e-08 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 58.80 E-value: 4.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1775 PLIVKPTPGRPDRQVPPRRvplsrdgsfgPSPvsggNPSPTQMMEVPSRPLSAPQREGSRAEFGTVVD--GPPAPRRPPE 1852
Cdd:PHA03247 2554 PLPPAAPPAAPDRSVPPPR----------PAP----RPSEPAVTSRARRPDAPPQSARPRAPVDDRGDprGPAPPSPLPP 2619
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1853 LPGRMSVPDLGPAVA--SLISSGPRTSSPATAKDRAPSPKEPEAPRVTTDSPSSIEPATVNVGPKGPPSFPGTPVMTSPV 1930
Cdd:PHA03247 2620 DTHAPDPPPPSPSPAanEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLTSLA 2699
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2024390606 1931 LgppppppvnygpppapfPGHYGPGPRPLPVPLVCGAPLP--PPAARDFLPGPSL 1983
Cdd:PHA03247 2700 D-----------------PPPPPPTPEPAPHALVSATPLPpgPAAARQASPALPA 2737
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1430-1776 |
6.67e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 58.16 E-value: 6.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1430 KQNAKKQKKLSETQKSLEKFEEAFSMHSAELSEVQIALNESKLSEEKVKAELQHVQEEnaRLKKSKEQLLK----EAEGW 1505
Cdd:TIGR02169 149 SMSPVERRKIIDEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRRE--REKAERYQALLkekrEYEGY 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1506 serhtELTEQIKLYRKSQKDIEEALAYKENEIEVLTnciMQLKQLDTDSASEAKDGEGLEWSTKDdlangeLPDNEkmkt 1585
Cdd:TIGR02169 227 -----ELLKEKEALERQKEAIERQLASLEEELEKLT---EEISELEKRLEEIEQLLEELNKKIKD------LGEEE---- 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1586 qikqmmdASRVKTMLSLVEEDRNSLQSKLSDEVAARHELEEQIKKLEHDSSSLQSAKARLENECKTLQQKVEILGELY-- 1663
Cdd:TIGR02169 289 -------QLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYae 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1664 -QQKEMALQKKLTQEEYERQEKEQKLSAADEKavlaIEEVKVYKQRIQDMEEELQKTERSYKNQIAAHEKKAHDnwliAR 1742
Cdd:TIGR02169 362 lKEELEDLRAELEEVDKEFAETRDELKDYREK----LEKLKREINELKRELDRLQEELQRLSEELADLNAAIAG----IE 433
|
330 340 350
....*....|....*....|....*....|....*...
gi 2024390606 1743 SAERALAEEKREAA----NLRQKLMEVNQKTIMLQRPL 1776
Cdd:TIGR02169 434 AKINELEEEKEDKAleikKQEWKLEQLAADLSKYEQEL 471
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1348-1755 |
9.34e-08 |
|
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: 57.54 E-value: 9.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1348 EKQLAEKIQNLLQEKTEMLDKFSECDEKIKQAKESMKVAQEQKsiLSDEIAGLKD--------TVKELEETNHQLDDKIK 1419
Cdd:pfam12128 345 DQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQ--NNRDIAGIKDklakireaRDRQLAVAEDDLQALES 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1420 SLRTMLDTErKQNAKKQKKLSETQKSLEKFEEAFSMHSAELSEvQIALNESKL-----SEEKVKAELQHVQEENARLKKS 1494
Cdd:pfam12128 423 ELREQLEAG-KLEFNEEEYRLKSRLGELKLRLNQATATPELLL-QLENFDERIerareEQEAANAEVERLQSELRQARKR 500
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1495 KEQ----LLKEAEGWSERHTELTE-QIKLYRKSQKDIE----EALAYKENEIEVLTNCIMQLKQLDTDSASEAKDGEGLE 1565
Cdd:pfam12128 501 RDQaseaLRQASRRLEERQSALDElELQLFPQAGTLLHflrkEAPDWEQSIGKVISPELLHRTDLDPEVWDGSVGGELNL 580
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1566 WSTKDDLANGELPDNEKMKTQIKQMMDAsrvktmlslVEEDrnsLQSKLSDEVAARHELEEQIKKLEHDSSSLQSAKARL 1645
Cdd:pfam12128 581 YGVKLDLKRIDVPEWAASEEELRERLDK---------AEEA---LQSAREKQAAAEEQLVQANGELEKASREETFARTAL 648
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1646 ENECKTLQQkveiLGELYQQKEMALQKKLTQEEYERQEKEQKLSAadekavlaieEVKVYKQRIQDMEEELQKTERSYKN 1725
Cdd:pfam12128 649 KNARLDLRR----LFDEKQSEKDKKNKALAERKDSANERLNSLEA----------QLKQLDKKHQAWLEEQKEQKREART 714
|
410 420 430
....*....|....*....|....*....|...
gi 2024390606 1726 QIAAHEK---KAHDNWLIARSAERALAEEKREA 1755
Cdd:pfam12128 715 EKQAYWQvveGALDAQLALLKAAIAARRSGAKA 747
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1338-1730 |
1.00e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 57.38 E-value: 1.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1338 SVKSRMYQVTEKQLAEKIQNLLQEKTEMLDKFSECDEKIKQakesmkvaqeqksiLSDEIAGLKDTVKELEETNhqldDK 1417
Cdd:PRK03918 376 RLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGE--------------LKKEIKELKKAIEELKKAK----GK 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1418 IKSLRTMLDTERKQN--AKKQKKLSETQKSLEKFEEAFSMHSAELSEVQIALNESK--LSEEKVKAELQHVQEENARLKK 1493
Cdd:PRK03918 438 CPVCGRELTEEHRKEllEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESelIKLKELAEQLKELEEKLKKYNL 517
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1494 SK-EQLLKEAEGWSERHTELTEQIKLYRKSQKDIEEAlaykENEIEVLTNcimQLKQLDTDSASEAKDGEGLEWSTKDDL 1572
Cdd:PRK03918 518 EElEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEEL----KKKLAELEK---KLDELEEELAELLKELEELGFESVEEL 590
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1573 angelpdnekmKTQIKQMMDASRVKTMLSLVEEDRNSLQSKLSDEvaaRHELEEQIKKLEHDSSSLQSAKARLEN-ECKT 1651
Cdd:PRK03918 591 -----------EERLKELEPFYNEYLELKDAEKELEREEKELKKL---EEELDKAFEELAETEKRLEELRKELEElEKKY 656
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1652 LQQKVEILGELYQQKEMALQKKLTQ-EEYERQEKEQKLSAADEKAVLaiEEVKVYKQRIQDME------EELQKTERSYK 1724
Cdd:PRK03918 657 SEEEYEELREEYLELSRELAGLRAElEELEKRREEIKKTLEKLKEEL--EEREKAKKELEKLEkalervEELREKVKKYK 734
|
....*.
gi 2024390606 1725 NQIAAH 1730
Cdd:PRK03918 735 ALLKER 740
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1326-1762 |
1.29e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 57.25 E-value: 1.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1326 ATLAIIFWRTcLSVKSRMYQVTEKQLAEKIQNLLQEKTEMLDKFSECDEKIKQAKESMKVAQEQKSILSDEIAGLKDTVK 1405
Cdd:COG1196 227 AELLLLKLRE-LEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIA 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1406 ELEETNHQLDDKIKSLRTMLDTERKQNAKKQKKLSETQKSLEKFEEafsmhsaELSEVQIALNESKLSEEKVKAELQHVQ 1485
Cdd:COG1196 306 RLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEE-------ELEEAEAELAEAEEALLEAEAELAEAE 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1486 EENARLKKSKEQLLKEAEgwserhtELTEQIKLYRKSQKDIEEALAYKENEIEVLTNcimQLKQLDTDSASEAKdgegle 1565
Cdd:COG1196 379 EELEELAEELLEALRAAA-------ELAAQLEELEEAEEALLERLERLEEELEELEE---ALAELEEEEEEEEE------ 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1566 wsTKDDLANGELPDNEKMKTQIKQMMDASRVktmLSLVEEDRNSLQSKLSDEVAARHELEEQIKKLEHDSSSLQSAKArl 1645
Cdd:COG1196 443 --ALEEAAEEEAELEEEEEALLELLAELLEE---AALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALL-- 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1646 enecKTLQQKVEILGELYQQKEMALQKKLtqEEYERQEKEQKLSAADEKAVLAIEEVKvykqriqdmEEELQKTERSYKN 1725
Cdd:COG1196 516 ----LAGLRGLAGAVAVLIGVEAAYEAAL--EAALAAALQNIVVEDDEVAAAAIEYLK---------AAKAGRATFLPLD 580
|
410 420 430
....*....|....*....|....*....|....*..
gi 2024390606 1726 QIAAHEKKAHDNWLIARSAERALAEEKREAANLRQKL 1762
Cdd:COG1196 581 KIRARAALAAALARGAIGAAVDLVASDLREADARYYV 617
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1342-1770 |
1.83e-07 |
|
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: 56.59 E-value: 1.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1342 RMYQV--TEKQLAEKIQNLLQEKTEMLDKFSECDEKIKQAKESMKVAQEQKSILSDEIAGLKDTVKELEETN---HQLDD 1416
Cdd:TIGR00606 190 TLRQVrqTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSYENELDPLKNRLKEIEHNLskiMKLDN 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1417 KIKSlrtmLDTERKQNAKKQKKLSetqkslEKFEEAFSMHSAELSEVqialnesklsEEKVKAELQHVQEENARLKKSKE 1496
Cdd:TIGR00606 270 EIKA----LKSRKKQMEKDNSELE------LKMEKVFQGTDEQLNDL----------YHNHQRTVREKERELVDCQRELE 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1497 QLLKEAEGWSERHTEL-TEQIKLYRKSQKDIEEALAYKENEIEVLTNCIMQLKQLDTDSASEAKDGEGLEWSTKDDLAN- 1574
Cdd:TIGR00606 330 KLNKERRLLNQEKTELlVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVIERQEDEAKt 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1575 -----GELPDNEKMKTQikqmmdasrvktMLSLVEEDRNSLQSKLSDEvaaRHELEEQIKKLEHDSSSLQSAKARLENEC 1649
Cdd:TIGR00606 410 aaqlcADLQSKERLKQE------------QADEIRDEKKGLGRTIELK---KEILEKKQEELKFVIKELQQLEGSSDRIL 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1650 KTLQQKVEILGELYQQKEMAL-QKKLTQEEYERQEK---EQKLSAADEKAVLAIEEVKVYKQRIQDMEEELQKTERSYKN 1725
Cdd:TIGR00606 475 ELDQELRKAERELSKAEKNSLtETLKKEVKSLQNEKadlDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKI 554
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 2024390606 1726 QIAAHE-----------KKAHDNWLIARSAERALAEEKREAANLRQKLMEVNQKTI 1770
Cdd:TIGR00606 555 KSRHSDeltsllgyfpnKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHI 610
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1343-1595 |
1.95e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 56.60 E-value: 1.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1343 MYQVTEKQLAEKIQNLLQEKTEMLDKFSECDEKIKQAKESMKVAQEqksilsdEIAGLKDTVKELEETNHQLDDKIKSLR 1422
Cdd:TIGR02168 250 EAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALAN-------EISRLEQQKQILRERLANLERQLEELE 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1423 TMLDTERKQNAKKQKKLSETQKSLEKFEEAFSMHSAELSEVQIALNESKLSEEKVKAELQHVQEENARLKKSKEQllkea 1502
Cdd:TIGR02168 323 AQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIAS----- 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1503 egwserhteLTEQIKLYRKSQKDIEEALAYKENEIEVLTNCIMQLKQLDTDSASEAKDGEGLEWSTKDDLANGELPDNEK 1582
Cdd:TIGR02168 398 ---------LNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELRE 468
|
250
....*....|...
gi 2024390606 1583 MKTQIKQMMDASR 1595
Cdd:TIGR02168 469 ELEEAEQALDAAE 481
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1335-1721 |
2.25e-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: 56.52 E-value: 2.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1335 TCLSVKSRMYQVTEKQLAEKIQnLLQEKTEMLDKFSECDEKIKQAKESMKVAQ----------EQKSILSDEIAGLKDTV 1404
Cdd:TIGR00618 452 QCEKLEKIHLQESAQSLKEREQ-QLQTKEQIHLQETRKKAVVLARLLELQEEPcplcgscihpNPARQDIDNPGPLTRRM 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1405 KELEETNHQLDDKIKSLRTMLDTERKQNAKKQKKLSETQKSLEKFEEAFSMHSAELSEVQ------IALNESKLSEEKVK 1478
Cdd:TIGR00618 531 QRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQnitvrlQDLTEKLSEAEDML 610
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1479 AELQHVQEENARLKKSKEQLLKEAEGWSERHTELT---EQIKLYRKSQKDIEEALAYKENEIEVLTNCIMQLKQLDTDSA 1555
Cdd:TIGR00618 611 ACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLtalHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKE 690
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1556 SEAKDGEGLEWstKDDLANGELPDNEKMKTQIKQMMDA-----SRVKTMLSLVEEDRNSLQ----SKLSDEVAARHELEE 1626
Cdd:TIGR00618 691 QLTYWKEMLAQ--CQTLLRELETHIEEYDREFNEIENAssslgSDLAAREDALNQSLKELMhqarTVLKARTEAHFNNNE 768
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1627 QIKKLEHDSSSLQSAKARLENECKTLQQKVEILGELYQQKEMAL----QKKLTQEEYERQEKEQKLSAADEKAVLAIE-- 1700
Cdd:TIGR00618 769 EVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIpsdeDILNLQCETLVQEEEQFLSRLEEKSATLGEit 848
|
410 420
....*....|....*....|..
gi 2024390606 1701 -EVKVYKQRIQDMEEELQKTER 1721
Cdd:TIGR00618 849 hQLLKYEECSKQLAQLTQEQAK 870
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1603-1764 |
3.38e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 55.83 E-value: 3.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1603 VEEDRNSLQSKLSDEVAARHELEEQIKKLEHDSSSLQSAKARLENECKTLQQKVEILG---ELYQQKEMALQKKLTQEEY 1679
Cdd:TIGR02168 244 LQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEqqkQILRERLANLERQLEELEA 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1680 ERQEKEQKLSAADEKAVLAIEEVKVYKQRIQDMEEELQKTERSYKNQIAAHEKKahDNWLIARSAERALAEEKREAANLR 1759
Cdd:TIGR02168 324 QLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEEL--EEQLETLRSKVAQLELQIASLNNE 401
|
....*
gi 2024390606 1760 QKLME 1764
Cdd:TIGR02168 402 IERLE 406
|
|
| SH3_2 |
pfam07653 |
Variant SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in ... |
108-163 |
6.40e-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: 6.40e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2024390606 108 RGKAMKDFQGPDCRFVNFKKGETVYVYYKLIGmstELWAGSIGSDFGYFPKDLLEI 163
Cdd:pfam07653 1 YGRVIFDYVGTDKNGLTLKKGDVVKVLGKDND---GWWEGETGGRVGLVPSTAVEE 53
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1780-1981 |
1.05e-06 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 54.56 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1780 PTPGRPDRQVPPRRVPLSRD-GSFGPSPVSGGNPSPTQMMEVPSRPLSAPQREGSRAEFGTVVDGPP-APRRPPELPGRM 1857
Cdd:PHA03247 2614 PSPLPPDTHAPDPPPPSPSPaANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPqRPRRRAARPTVG 2693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1858 SVPDLG----------PAVASLISSGPRTSSPATAKDRAPSPKEPEAPRVTTDSPSSiePATVN-----VGPKGPPS--F 1920
Cdd:PHA03247 2694 SLTSLAdpppppptpePAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPAT--PGGPArparpPTTAGPPApaP 2771
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024390606 1921 PGTPVMT-SPVLGPPPPPPVNYGPPPAPFPghygPGPRPLPVPLVCGAPLPPPAARDFLPGP 1981
Cdd:PHA03247 2772 PAAPAAGpPRRLTRPAVASLSESRESLPSP----WDPADPPAAVLAPAAALPPAASPAGPLP 2829
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1373-1760 |
1.39e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.77 E-value: 1.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1373 DEKIKQAKESMKVAQEQKSILSDEIAGLKDTVKELEETNHQLD-DKIKSLRTMLDTERKQNAKKQKKLSETQKSLEKFEE 1451
Cdd:COG4913 294 EAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEALLAALGL 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1452 AFSMHSAELSEVQIALNESKlseEKVKAELQHVQEENARLKKSKEQLLKEAEGWSERHTELTEQIKLYRKSQ----KDIE 1527
Cdd:COG4913 374 PLPASAEEFAALRAEAAALL---EALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLlalrDALA 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1528 EALAYKENEIEVLtnC-IMQLKQLD------------------------TDSASEA----KDGEGLEW----STKDDLAN 1574
Cdd:COG4913 451 EALGLDEAELPFV--GeLIEVRPEEerwrgaiervlggfaltllvppehYAAALRWvnrlHLRGRLVYervrTGLPDPER 528
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1575 GELPDN---EKMKT-----------QIKQMMDASRVKTmlslVEE------------------------DRNSLQSKL-- 1614
Cdd:COG4913 529 PRLDPDslaGKLDFkphpfrawleaELGRRFDYVCVDS----PEElrrhpraitragqvkgngtrhekdDRRRIRSRYvl 604
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1615 -SDEVAARHELEEQIKKLEHDSSSLQSAKARLENECKTLQQKVEILGELYQQKEMALQKKLTQEEYERQEKE-QKLSAAD 1692
Cdd:COG4913 605 gFDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAElERLDASS 684
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024390606 1693 EKAVLAIEEVKVYKQRIQDMEEELQKTERSY---KNQIAAHEK-------KAHDNWLIARSAERALAEEKREAANLRQ 1760
Cdd:COG4913 685 DDLAALEEQLEELEAELEELEEELDELKGEIgrlEKELEQAEEeldelqdRLEAAEDLARLELRALLEERFAAALGDA 762
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1401-1768 |
1.47e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.77 E-value: 1.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1401 KDTVKELEETNHQLDDkIKSLRTMLDTERKQnakkQKKLSETQKSLEKFEEAF---SMHSAELSEVQIALNESKLseEKV 1477
Cdd:COG4913 221 PDTFEAADALVEHFDD-LERAHEALEDAREQ----IELLEPIRELAERYAAARerlAELEYLRAALRLWFAQRRL--ELL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1478 KAELQHVQEENARLKKSKEQLLKEAEGWSERHTELTEQIklyRKSQKDIEEALaykENEIEVLTNcimQLKQLDTDSASE 1557
Cdd:COG4913 294 EAELEELRAELARLEAELERLEARLDALREELDELEAQI---RGNGGDRLEQL---EREIERLER---ELEERERRRARL 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1558 AKDGEGLEWSTKDDLAngelpDNEKMKTQIKQMMDAsrVKTMLSLVEEDRNSLQSKLSDEVAARHELEEQIKKLEHDSSS 1637
Cdd:COG4913 365 EALLAALGLPLPASAE-----EFAALRAEAAALLEA--LEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSN 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1638 ----LQSAKARLENECKTLQQKVEILGELYQQKE------------------------------------MALQKKLTQE 1677
Cdd:COG4913 438 iparLLALRDALAEALGLDEAELPFVGELIEVRPeeerwrgaiervlggfaltllvppehyaaalrwvnrLHLRGRLVYE 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1678 EYERQEKEQKLSAADEKAV---LAIEEVKVY---KQRIQ--------DMEEELQKTERS------YKNQIAAHEKKAHD- 1736
Cdd:COG4913 518 RVRTGLPDPERPRLDPDSLagkLDFKPHPFRawlEAELGrrfdyvcvDSPEELRRHPRAitragqVKGNGTRHEKDDRRr 597
|
410 420 430
....*....|....*....|....*....|....*
gi 2024390606 1737 ---NWLIARSAERALAEEKREAANLRQKLMEVNQK 1768
Cdd:COG4913 598 irsRYVLGFDNRAKLAALEAELAELEEELAEAEER 632
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1356-1768 |
1.80e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 53.61 E-value: 1.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1356 QNLLQEKTEMLDKFSECDEKIKQA------KESMKVAQEQKSILSDEIAGLKDTVKELEET---NHQLDDKIKSLRTMLD 1426
Cdd:PTZ00121 1022 QNFNIEKIEELTEYGNNDDVLKEKdiidedIDGNHEGKAEAKAHVGQDEGLKPSYKDFDFDakeDNRADEATEEAFGKAE 1101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1427 TERKQNAKKQKKLSETQKSLEKFEEAFSMHSAELSEVQIALNESKLSEEKVKAELQHVQEENARLKKS-KEQLLKEAEgw 1505
Cdd:PTZ00121 1102 EAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEArKAEDAKKAE-- 1179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1506 SERHTELTEQIKLYRKSQ--KDIEEALAYKE-NEIEVLTncimqlKQLDTDSASEAKDGEGLEWSTKDDLANGELPDNEK 1582
Cdd:PTZ00121 1180 AARKAEEVRKAEELRKAEdaRKAEAARKAEEeRKAEEAR------KAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEE 1253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1583 MKTQIKQMMDASRVKTMLSLVEEDRNSLQSKLSDEVAARHELEEQIKKLEHDSSSLQSAKARLENECKTLQQKVEILGEL 1662
Cdd:PTZ00121 1254 IRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADA 1333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1663 YQQKEMALQKKLTQEEYERQEKEQKLSAADEKA---VLAIEEVKVYKQRIQDMEEELQKTERSYKNqiaAHEKKAHDNWL 1739
Cdd:PTZ00121 1334 AKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAeaaEKKKEEAKKKADAAKKKAEEKKKADEAKKK---AEEDKKKADEL 1410
|
410 420
....*....|....*....|....*....
gi 2024390606 1740 IARSAERALAEEKREAANLRQKLMEVNQK 1768
Cdd:PTZ00121 1411 KKAAAAKKKADEAKKKAEEKKKADEAKKK 1439
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1780-2072 |
2.12e-06 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 53.40 E-value: 2.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1780 PTPGRPDRQVPPRRVPLSRDGSFGPSPVSggnpsptqmmevPSRPLSAPQREGSRAEFGTVVD--GPPAPRRPPELPGRM 1857
Cdd:PHA03247 2647 PPPERPRDDPAPGRVSRPRRARRLGRAAQ------------ASSPPQRPRRRAARPTVGSLTSlaDPPPPPPTPEPAPHA 2714
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1858 SVPDLGpavASLISSGPRTSSPATAKDRAP-----------SPKEPEAPRVTTDSPSSIEPATVNVGPkgPPSFPGTPVM 1926
Cdd:PHA03247 2715 LVSATP---LPPGPAAARQASPALPAAPAPpavpagpatpgGPARPARPPTTAGPPAPAPPAAPAAGP--PRRLTRPAVA 2789
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1927 TSPVLGPPPPPPVNYGPPPAPFPG-----HYGPGPRPLPVPLVCGAPLPPPAARDFLPgPSLGIrdlppgplpplpdPRS 2001
Cdd:PHA03247 2790 SLSESRESLPSPWDPADPPAAVLApaaalPPAASPAGPLPPPTSAQPTAPPPPPGPPP-PSLPL-------------GGS 2855
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024390606 2002 YRRGHPhFRPPGPPGPRDYPPGPPLPPPASRDYAPSRSRD-----LPPAGPRDYP--AGPAPPPAGSKDYAQPPVQKP 2072
Cdd:PHA03247 2856 VAPGGD-VRRRPPSRSPAAKPAAPARPPVRRLARPAVSRStesfaLPPDQPERPPqpQAPPPPQPQPQPPPPPQPQPP 2932
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1343-1767 |
2.23e-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: 52.80 E-value: 2.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1343 MYQVTEKQlaEKIQNLLQEKTEMLDKFSECDEKIKQAKESMKVAQEQKSILSDEIAGLKDTVKELEETNHQLDDKIK-SL 1421
Cdd:pfam05483 246 LIQITEKE--NKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQiAT 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1422 RTMLD-TERKqnakkqkklsETQksLEKFEEAFSMHSAELSEVQIALNESklsEEKVKAELQhvqeenaRLKKSKEQLLK 1500
Cdd:pfam05483 324 KTICQlTEEK----------EAQ--MEELNKAKAAHSFVVTEFEATTCSL---EELLRTEQQ-------RLEKNEDQLKI 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1501 EAEGWSERHTELTEQIKLYRKSQKDIEEaLAYKENEIEVLTNCIMQLKQLDTDSASEAKDGEGLEWSTKDDLANGEL--- 1577
Cdd:pfam05483 382 ITMELQKKSSELEEMTKFKNNKEVELEE-LKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIqlt 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1578 ---PDNEKMKTQIKQM---MDASRVKTMLSLVEEDRNSLQSKLSDEVAARHELEeqIKKLEHDSSSLQSAKARLENECKT 1651
Cdd:pfam05483 461 aikTSEEHYLKEVEDLkteLEKEKLKNIELTAHCDKLLLENKELTQEASDMTLE--LKKHQEDIINCKKQEERMLKQIEN 538
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1652 LQQK-------VEILGELYQQKEMALQKKLTQEEYERQEKEQKLSAADEKAVLAIEEVKVYKQRIQDME---EELQKTER 1721
Cdd:pfam05483 539 LEEKemnlrdeLESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNkniEELHQENK 618
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 2024390606 1722 SYKNQIAAHEKKAHDNWLIARSAERALAEEKR---EAANLRQKLMEVNQ 1767
Cdd:pfam05483 619 ALKKKGSAENKQLNAYEIKVNKLELELASAKQkfeEIIDNYQKEIEDKK 667
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
1375-1792 |
2.93e-06 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 52.77 E-value: 2.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1375 KIKQAKESMKVAQEQksilsdeIAGLKdTVKELE-ETNHQLDDKIK-SLRTMLDTER-----KQNAKKQKKLSETQKSLE 1447
Cdd:COG5022 763 RYLQALKRIKKIQVI-------QHGFR-LRRLVDyELKWRLFIKLQpLLSLLGSRKEyrsylACIIKLQKTIKREKKLRE 834
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1448 KFEEAFSMHSAELSE--VQIALNESKLSEEKVKAELQHVQEENARLKKSKEQLLKEAEGWSERHTELTEQIKLYRKSQKD 1525
Cdd:COG5022 835 TEEVEFSLKAEVLIQkfGRSLKAKKRFSLLKKETIYLQSAQRVELAERQLQELKIDVKSISSLKLVNLELESEIIELKKS 914
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1526 IEEALAykeNEIEVLTNCIMQLKQLdtDSASEAKDGEGLEWSTKDDLaNGELPDNEKMKTQIKQMMDA--------SRVK 1597
Cdd:COG5022 915 LSSDLI---ENLEFKTELIARLKKL--LNNIDLEEGPSIEYVKLPEL-NKLHEVESKLKETSEEYEDLlkkstilvREGN 988
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1598 TMLSLVEEDRNSLQSkLSDEVAARHELEEQIKKLEHDSSSLQSAKARLENECKTLQ-----QKVEILGELyqqKEMALQK 1672
Cdd:COG5022 989 KANSELKNFKKELAE-LSKQYGALQESTKQLKELPVEVAELQSASKIISSESTELSilkplQKLKGLLLL---ENNQLQA 1064
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1673 KLTQEEYERqekeqKLSAADEKAVLAIEEVKVYKQRIQDMEEELQKT----ERSYKNQIAAHEKKAHDNWLIARSAERAL 1748
Cdd:COG5022 1065 RYKALKLRR-----ENSLLDDKQLYQLESTENLLKTINVKDLEVTNRnlvkPANVLQFIVAQMIKLNLLQEISKFLSQLV 1139
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 2024390606 1749 AEEKREAANLRQKLMEVnqKTIMLQRPLIVKPTPGRPDRQVPPR 1792
Cdd:COG5022 1140 NTLEPVFQKLSVLQLEL--DGLFWEANLEALPSPPPFAALSEKR 1181
|
|
| Taxilin |
pfam09728 |
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain ... |
1341-1654 |
3.04e-06 |
|
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: 51.49 E-value: 3.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1341 SRMYQVTEKQLAEKIQNLLQEKTEMLDKFSE-----------CDEKIKQAK----ESMKVAQEQKSILSDEIAGLKDTVK 1405
Cdd:pfam09728 34 MKRLQKDLKKLKKKQDQLQKEKDQLQSELSKailakskleklCRELQKQNKklkeESKKLAKEEEEKRKELSEKFQSTLK 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1406 ELEET-NHQLDDKIKSlrtmldteRKQNAKKQKKLSETQKSLEKFEEAF-SMHsaELSEVQIALNESKLSEEKVKAELQH 1483
Cdd:pfam09728 114 DIQDKmEEKSEKNNKL--------REENEELREKLKSLIEQYELRELHFeKLL--KTKELEVQLAEAKLQQATEEEEKKA 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1484 VQEENARLKKSKEQLlkeaEGWSERHTELTEQIKLYRKSQKDIEEALA--------YKeNEIEVLTNCIMQLKQldtdsa 1555
Cdd:pfam09728 184 QEKEVAKARELKAQV----QTLSETEKELREQLNLYVEKFEEFQDTLNksnevfttFK-KEMEKMSKKIKKLEK------ 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1556 seakdgEGLEWSTKDDLANgelpdnekmktqikqmmdasrvKTMLSLVEEDRNSLQsklsdevaarhELEEQIKKLEhds 1635
Cdd:pfam09728 253 ------ENLTWKRKWEKSN----------------------KALLEMAEERQKLKE-----------ELEKLQKKLE--- 290
|
330
....*....|....*....
gi 2024390606 1636 sslqsakaRLENECKTLQQ 1654
Cdd:pfam09728 291 --------KLENLCRALQA 301
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1441-1784 |
3.30e-06 |
|
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: 52.67 E-value: 3.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1441 ETQKSLEKFEEAfsmhsAELSEVQIALNESKLSEEKVKAelqhvQEENARLKKSKEQLLKEAEGW---------SERHTE 1511
Cdd:pfam02463 171 KKEALKKLIEET-----ENLAELIIDLEELKLQELKLKE-----QAKKALEYYQLKEKLELEEEYllyldylklNEERID 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1512 LTEQIKLYRKSQKDIEEALAYKENEIEVLTNCIM------------QLKQLDTDSASEAKDGEGLEWSTKDDLANGELPD 1579
Cdd:pfam02463 241 LLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENkeeekekklqeeELKLLAKEEEELKSELLKLERRKVDDEEKLKESE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1580 NEKMKTQIKQMMDasrvktmLSLVEEDRNSLQSKLSDEVAARHELEEQIKKLEHDSSSLQSAKARLENECKTLQQKVEIL 1659
Cdd:pfam02463 321 KEKKKAEKELKKE-------KEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLK 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1660 GELYQQKEMALQKKLTQEEYERQEKEQKLSAADEKAVLAIEEVKV--YKQRIQDMEEELQKTERSYKNQIAAHEKKAHDN 1737
Cdd:pfam02463 394 EEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESieLKQGKLTEEKEELEKQELKLLKDELELKKSEDL 473
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 2024390606 1738 WLIARSAERalaEEKREAANLRQKLMEVNQKTIMLQRPLIVKPTPGR 1784
Cdd:pfam02463 474 LKETQLVKL---QEQLELLLSRQKLEERSQKESKARSGLKVLLALIK 517
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1349-1752 |
3.99e-06 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 52.43 E-value: 3.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1349 KQLAEKIQNLLQEK----TEMLDKFSECDEKIKQAKESMKVAQEQ----KSILSDEIAGLKDTVK----ELEETNHQLDD 1416
Cdd:pfam15921 263 QQHQDRIEQLISEHeveiTGLTEKASSARSQANSIQSQLEIIQEQarnqNSMYMRQLSDLESTVSqlrsELREAKRMYED 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1417 KIKSLRTML----------DTERKQNAKKQKKLSET-QK---SLEKFEEAFSMHSAELSEVQIALNESKLSEEKVKAELQ 1482
Cdd:pfam15921 343 KIEELEKQLvlanselteaRTERDQFSQESGNLDDQlQKllaDLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELD 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1483 HVQEENARLKKSKEQLLKEAEGWSERH--------------TELTEQIKLYRKSQKDIEEALAYKENEIEVLTNCIMQLK 1548
Cdd:pfam15921 423 DRNMEVQRLEALLKAMKSECQGQMERQmaaiqgkneslekvSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLT 502
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1549 Q--LDTDSASEAKDGEGLEWSTKDDLANGELpdnEKMKTQIKQMMDASRVKTMLSLVEEDRNSLQSKLSDEVAARHELEE 1626
Cdd:pfam15921 503 AslQEKERAIEATNAEITKLRSRVDLKLQEL---QHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVG 579
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1627 QIKKlehDSSSLQSAKARLENECKTLQ---QKVEILGELYQQKEMALQKKLTQEEYER-------QEKEQKLSAADEKAV 1696
Cdd:pfam15921 580 QHGR---TAGAMQVEKAQLEKEINDRRlelQEFKILKDKKDAKIRELEARVSDLELEKvklvnagSERLRAVKDIKQERD 656
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 2024390606 1697 LAIEEVKVYKQRIQDMEEELQKTERSYKNQIAAHEKKAHDNWLIARSAERALAEEK 1752
Cdd:pfam15921 657 QLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTR 712
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1345-1756 |
4.25e-06 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 52.28 E-value: 4.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1345 QVTEKQLAEKIQNLLQEKtEMLDKFSECDEKIKQAKESMKVAQEQKSilsdEIAGLKDTVKELEETNHQLDDKIKSLRTM 1424
Cdd:TIGR00618 222 QVLEKELKHLREALQQTQ-QSHAYLTQKREAQEEQLKKQQLLKQLRA----RIEELRAQEAVLEETQERINRARKAAPLA 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1425 LDTER--KQNAKKQKKLSETQKSLEKFEEAFsMHSAELSEVQIALNESKLSEEKVKAELQHVQEENARLKKSKEQLLKEA 1502
Cdd:TIGR00618 297 AHIKAvtQIEQQAQRIHTELQSKMRSRAKLL-MKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQH 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1503 E------GWSERHTELTEQIKLYRK-----------------SQKDIEEALAYKENEIEVLTNCIMQLKQLDTDSASEAK 1559
Cdd:TIGR00618 376 TltqhihTLQQQKTTLTQKLQSLCKeldilqreqatidtrtsAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEK 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1560 DGEGLEWSTKDDLAngELPDNEKMKTQIKQMMD---ASRVKTMLSLVEEDRNSLQSKLSDEVAA---------------- 1620
Cdd:TIGR00618 456 LEKIHLQESAQSLK--EREQQLQTKEQIHLQETrkkAVVLARLLELQEEPCPLCGSCIHPNPARqdidnpgpltrrmqrg 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1621 ---RHELEEQIKKLEHDSSSLQSAKARLENECKTLQQKVEILGELYQQKEMALQkKLTQEEYERQEKEQKLSAADEKAVL 1697
Cdd:TIGR00618 534 eqtYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIP-NLQNITVRLQDLTEKLSEAEDMLAC 612
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 2024390606 1698 AIEEVKVYKQRIQDMEEELQktersYKNQIAAHEKKAHDNwlIARSAERALAEEKREAA 1756
Cdd:TIGR00618 613 EQHALLRKLQPEQDLQDVRL-----HLQQCSQELALKLTA--LHALQLTLTQERVREHA 664
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1452-1695 |
7.28e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.60 E-value: 7.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1452 AFSMHSAELSEVQIALNESKLSEekVKAELQHVQEENARLKKSKEQLLKEAEGWSERHTELTEQIKlyrKSQKDIEEAla 1531
Cdd:COG3883 5 ALAAPTPAFADPQIQAKQKELSE--LQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEID---KLQAEIAEA-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1532 ykENEIEVLTncimqlKQLDTDSASEAKDGEGLewSTKDDLANGELPDN--EKMkTQIKQMMDASR-----VKTMLSLVE 1604
Cdd:COG3883 78 --EAEIEERR------EELGERARALYRSGGSV--SYLDVLLGSESFSDflDRL-SALSKIADADAdlleeLKADKAELE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1605 EDRNSLQSKLSDEVAARHELEEQIKKLEHDSSSLQSAKARLENECKTLQQKVEILGELYQQKEMALQKKLTQEEYERQEK 1684
Cdd:COG3883 147 AKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAA 226
|
250
....*....|.
gi 2024390606 1685 EQKLSAADEKA 1695
Cdd:COG3883 227 AAAAAAAAAAA 237
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1341-1733 |
7.90e-06 |
|
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: 51.20 E-value: 7.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1341 SRMYQVTEKQLAEKIQNLLQEKTEMLdkfsECDEKIKQAKESM--KVAQEQKSI---------LSDEIAGLKDTVKELEE 1409
Cdd:TIGR00606 208 ELKYLKQYKEKACEIRDQITSKEAQL----ESSREIVKSYENEldPLKNRLKEIehnlskimkLDNEIKALKSRKKQMEK 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1410 TNHQLDDKI--------KSLRTMLDTERKQNAKKQKKLSETQKSLEKFEEAFSMHSAELSEVqialnESKLSEEKVKAEL 1481
Cdd:TIGR00606 284 DNSELELKMekvfqgtdEQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTEL-----LVEQGRLQLQADR 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1482 QHVQEENARLKKSKEQLLKEAEGWsERHTELTEQIKLYRKSQKDIEEALAYKENEIEVLTNCIMQLKQLDTDSASEAKDG 1561
Cdd:TIGR00606 359 HQEHIRARDSLIQSLATRLELDGF-ERGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKG 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1562 EGLEWSTKDDLANGELPDNEKMKTQIKQMMDASrvKTMLSLVEEDRNSLQS-KLSDEVAARHELEEQIKKLEHDSSSLQS 1640
Cdd:TIGR00606 438 LGRTIELKKEILEKKQEELKFVIKELQQLEGSS--DRILELDQELRKAERElSKAEKNSLTETLKKEVKSLQNEKADLDR 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1641 AKARLENECKTLQQKVEILgelyQQKEMALQKKLTQEEYERQEKEQklsAADEKAVLA----------------IEEVKV 1704
Cdd:TIGR00606 516 KLRKLDQEMEQLNHHTTTR----TQMEMLTKDKMDKDEQIRKIKSR---HSDELTSLLgyfpnkkqledwlhskSKEINQ 588
|
410 420
....*....|....*....|....*....
gi 2024390606 1705 YKQRIQDMEEELQKTERSyKNQIAAHEKK 1733
Cdd:TIGR00606 589 TRDRLAKLNKELASLEQN-KNHINNELES 616
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1352-1631 |
8.81e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.07 E-value: 8.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1352 AEKIQNLLQEKTEMLDKFSECDEKIKQAKESMKVAQEQKSILS----------------DEIAGLKDTVKELEETNH--- 1412
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQrlaeyswdeidvasaeREIAELEAELERLDASSDdla 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1413 QLDDKIKSLRTMLDTERKQNAKKQKKLSETQKSLEKFEEafsmhsaELSEVQIALNEsklseekvkAELQHVQEENARLK 1492
Cdd:COG4913 689 ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEE-------ELDELQDRLEA---------AEDLARLELRALLE 752
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1493 KSKEQLLKEaegwsERHTELTEQIklyRKSQKDIEEALAYKENEIEvltNCIMQLKQLDTDSASEAKDG-----EGLEWS 1567
Cdd:COG4913 753 ERFAAALGD-----AVERELRENL---EERIDALRARLNRAEEELE---RAMRAFNREWPAETADLDADleslpEYLALL 821
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024390606 1568 TKddLANGELPDNE-KMKTQIKQMMdasrvktmlslvEEDRNSLQSKLSDEvaaRHELEEQIKKL 1631
Cdd:COG4913 822 DR--LEEDGLPEYEeRFKELLNENS------------IEFVADLLSKLRRA---IREIKERIDPL 869
|
|
| Drf_FH1 |
pfam06346 |
Formin Homology Region 1; This region is found in some of the Diaphanous related formins (Drfs) ... |
1790-1981 |
8.83e-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: 47.94 E-value: 8.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1790 PPrrvPLSRDGSFGPSPVSGGNPSPTQMMEVPSRPlSAPQREGSRAEfgtvvdgPPaprrPPELPGRMSVPdlgpavasl 1869
Cdd:pfam06346 3 PP---PLPGDSSTIPLPPGACIPTPPPLPGGGGPP-PPPPLPGSAAI-------PP----PPPLPGGTSIP--------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1870 issgprtsSPATAKDRAPSPKEPEAPRVTTDSPSSIEPATVNVGPKgPPSFPGTPVMTSPVlgppppppvnygpppAPFP 1949
Cdd:pfam06346 59 --------PPPPLPGAASIPPPPPLPGSTGIPPPPPLPGGAGIPPP-PPPLPGGAGVPPPP---------------PPLP 114
|
170 180 190
....*....|....*....|....*....|...
gi 2024390606 1950 GhyGPG-PRPLPVPLVCGAPlPPPaardflPGP 1981
Cdd:pfam06346 115 G--GPGiPPPPPFPGGPGIP-PPP------PGM 138
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1364-1767 |
1.05e-05 |
|
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: 50.91 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1364 EMLDKFSEcDEKIKQAKESMKVAQEQKSILSDeiaGLKDTVKELEETNHQLDDKIKSLRTMLDTERKQNAKKQK------ 1437
Cdd:pfam07111 128 EMVRKNLE-EGSQRELEEIQRLHQEQLSSLTQ---AHEEALSSLTSKAEGLEKSLNSLETKRAGEAKQLAEAQKeaellr 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1438 -KLSETQKSLE---KFEEAFSMHSAELSEVQIALNESKLSEEKVKAELQHVQEENARLKKSKEQLLKEAEGWSE----RH 1509
Cdd:pfam07111 204 kQLSKTQEELEaqvTLVESLRKYVGEQVPPEVHSQTWELERQELLDTMQHLQEDRADLQATVELLQVRVQSLTHmlalQE 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1510 TELTEQIK----------------LYRKSQKDIEEALAYKENEIE---VLTNCIMQLKQLDTDSASEAKDGEGLEWSTKD 1570
Cdd:pfam07111 284 EELTRKIQpsdslepefpkkcrslLNRWREKVFALMVQLKAQDLEhrdSVKQLRGQVAELQEQVTSQSQEQAILQRALQD 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1571 DLANGELpdnEKMKTQIKQMmDASRVKTMLSLVEEDRNSLQSKLSDEVAA----RHELEEQIKKLEHDSSSLQSAKARLE 1646
Cdd:pfam07111 364 KAAEVEV---ERMSAKGLQM-ELSRAQEARRRQQQQTASAEEQLKFVVNAmsstQIWLETTMTRVEQAVARIPSLSNRLS 439
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1647 ------NECKTLQQKVEILGELYQQK------------EMALQKKLTQEEYERQEKEQKLSA--ADEKAVLAIEEVKVYK 1706
Cdd:pfam07111 440 yavrkvHTIKGLMARKVALAQLRQEScpppppappvdaDLSLELEQLREERNRLDAELQLSAhlIQQEVGRAREQGEAER 519
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024390606 1707 QRI----QDMEEELQKTERSYKNQIAAHEkkahdnwliarSAERALAEEKREAANLRQKLMEVNQ 1767
Cdd:pfam07111 520 QQLsevaQQLEQELQRAQESLASVGQQLE-----------VARQGQQESTEEAASLRQELTQQQE 573
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1351-1764 |
1.05e-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: 50.94 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1351 LAEKIQNLLQEKTEMLDKFSECDEKIKQAKESMKVAQEQKSILSDEIAGLKDTVKELEETNHQLDDKIKSLRTMLDTERK 1430
Cdd:pfam01576 143 LEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQE 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1431 QNAKKQKKLSETQKSLEKFEEAFSMHSAELSEVQIALNESKLSEEKVKAELQHVQEE-------NARLKKSKEQLLKEAE 1503
Cdd:pfam01576 223 QIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDleseraaRNKAEKQRRDLGEELE 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1504 GW------------------SERHTELTEQIKLYRKSQKDIEEALA-YKENEIEVLTNCIMQLKQLDTDSASEAKDGEGL 1564
Cdd:pfam01576 303 ALkteledtldttaaqqelrSKREQEVTELKKALEEETRSHEAQLQeMRQKHTQALEELTEQLEQAKRNKANLEKAKQAL 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1565 EWStkddlaNGELPDNEKMKTQIKQMMDASRVKtmlslVEEDRNSLQSKLSDEVAARHELEEQIKKLEHDSSSLQSAKAR 1644
Cdd:pfam01576 383 ESE------NAELQAELRTLQQAKQDSEHKRKK-----LEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNE 451
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1645 LENECKTLQQKVEILGELYQQKEMALQkkltqeeyerQEKEQKLSAADEkaVLAIEEVKVYKQRIQDMEEE----LQKTE 1720
Cdd:pfam01576 452 AEGKNIKLSKDVSSLESQLQDTQELLQ----------EETRQKLNLSTR--LRQLEDERNSLQEQLEEEEEakrnVERQL 519
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 2024390606 1721 RSYKNQIAAHEKKAHDNWLIARSAERALAEEKREAANLRQKLME 1764
Cdd:pfam01576 520 STLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEE 563
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1573-1809 |
1.09e-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: 50.15 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1573 ANGELPDNEKMKTQIKQMMDASRVKtmLSLVEEDRNSLQSKLSDEVAARHELEEQIKKLEHDSSSLQSAKARLENECKTL 1652
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKE--LAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1653 QQKVEILGELYQQKEMALQKK---------LTQEE----YERQEKEQKLSAADEKavlAIEEVKVYKQRIQDMEEELQKT 1719
Cdd:COG4942 96 RAELEAQKEELAELLRALYRLgrqpplallLSPEDfldaVRRLQYLKYLAPARRE---QAEELRADLAELAALRAELEAE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1720 ERSYKNQIAAHEKKAHDNWLIARSAERALAEEKREAANLRQKLMEVNQKTIMLQRpLIVKPTPGRPDRQVPPRRVPLSRD 1799
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEA-LIARLEAEAAAAAERTPAAGFAAL 251
|
250
....*....|
gi 2024390606 1800 GSFGPSPVSG 1809
Cdd:COG4942 252 KGKLPWPVSG 261
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1373-1562 |
1.17e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.83 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1373 DEKIKQAKESMKVAQEQKSILSDEIAGLKDTVKELEETNHQLDDKIKSLRTMLDTERKQNAKKQKKLSETQKSLEKFEEA 1452
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1453 FSMHSAELSEVQIALNESKLSE------------EKVKAELQHVQEENARLKKSKEQLLKEAEgwserhtELTEQIKLYR 1520
Cdd:COG3883 95 LYRSGGSVSYLDVLLGSESFSDfldrlsalskiaDADADLLEELKADKAELEAKKAELEAKLA-------ELEALKAELE 167
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2024390606 1521 KSQKDIEEALAYKENEIEVLTNCIMQLKQLDTDSASEAKDGE 1562
Cdd:COG3883 168 AAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAE 209
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1393-1756 |
1.22e-05 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 50.07 E-value: 1.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1393 LSDEIAGLKDTVKELEETNHQLDDKIKSLRTMLDTERKQNAKKQKKLSETQKSLEKFEEAFSMHSAELSEVQIALNESKL 1472
Cdd:pfam19220 39 ILRELPQAKSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVARLAKLEAALREAEAAKEELRIELRDKTA 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1473 SEEKVKAEL-------QHVQEENARLK---KSKEQLLKEAEGwsERhTELTEQIKLY----RKSQKDIEEALAykenEIE 1538
Cdd:pfam19220 119 QAEALERQLaaeteqnRALEEENKALReeaQAAEKALQRAEG--EL-ATARERLALLeqenRRLQALSEEQAA----ELA 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1539 VLTNCIMQLKQLDTDSASEAKDGEGlewstkdDLANgELPDNEKMKTQIKQMMDASRVktmlslveeDRNSLQSKLsDEV 1618
Cdd:pfam19220 192 ELTRRLAELETQLDATRARLRALEG-------QLAA-EQAERERAEAQLEEAVEAHRA---------ERASLRMKL-EAL 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1619 AARH---------------ELEEQIKKLEHDSSSLQSAKARLENECKTLQQkveilgELYQQKEMALQ-KKLTQEEYERQ 1682
Cdd:pfam19220 254 TARAaateqllaearnqlrDRDEAIRAAERRLKEASIERDTLERRLAGLEA------DLERRTQQFQEmQRARAELEERA 327
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024390606 1683 EKEQKLSAADEKAVLAIEEvkvykqRIQDMEEELQKTERSYKNQIAAHEKKAHD--NWLIARSAERALAEEKREAA 1756
Cdd:pfam19220 328 EMLTKALAAKDAALERAEE------RIASLSDRIAELTKRFEVERAALEQANRRlkEELQRERAERALAQGALEIA 397
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1352-1530 |
1.45e-05 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 50.22 E-value: 1.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1352 AEKIQNLLQEKTEMLDK---FSECD-EKIKQAKESMKVAQEQKSILSDEIAG-------LKDTVKELEETNHQLDDKIKS 1420
Cdd:PRK04778 322 AKEQNKELKEEIDRVKQsytLNESElESVRQLEKQLESLEKQYDEITERIAEqeiayseLQEELEEILKQLEEIEKEQEK 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1421 LRTMLDTERK--QNAKK-----QKKLSETQKSLEK---------FEEAFSMHSAELSEVQIALNESKLSEEKVKAELQHV 1484
Cdd:PRK04778 402 LSEMLQGLRKdeLEAREkleryRNKLHEIKRYLEKsnlpglpedYLEMFFEVSDEIEALAEELEEKPINMEAVNRLLEEA 481
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1485 QEENARLKKSKEQLLKEAegwserhtELTEQI----KLYRKSQKDIEEAL 1530
Cdd:PRK04778 482 TEDVETLEEETEELVENA--------TLTEQLiqyaNRYRSDNEEVAEAL 523
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1344-1762 |
1.76e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 50.07 E-value: 1.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1344 YQVTEKQLAEKIQNLLQEKTEMLDKFSECDEKIKQAKESMKVAQEQKSILSDEIAGLKDTVKELEETNHQLD-------- 1415
Cdd:TIGR02169 348 ERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSeeladlna 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1416 ------DKIKSLRTMLDTERKQNAKKQKKLSETQKSLEKFEEAFSMHSAELSEVQIALNESKLSEEKVKAELQHVQEENA 1489
Cdd:TIGR02169 428 aiagieAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVR 507
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1490 RLKKSKEQLLKEAEGwseRHTELTEQIKLYRKSQKDIEEALAYKENEIEVLTN-----CIMQLKQLDTDSA--------- 1555
Cdd:TIGR02169 508 GGRAVEEVLKASIQG---VHGTVAQLGSVGERYATAIEVAAGNRLNNVVVEDDavakeAIELLKRRKAGRAtflplnkmr 584
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1556 SEAKDGEGL-------------EWSTK---------------DDLANG-ELPDNEKMKTQIKQMMDASRVKTMLSLVEED 1606
Cdd:TIGR02169 585 DERRDLSILsedgvigfavdlvEFDPKyepafkyvfgdtlvvEDIEAArRLMGKYRMVTLEGELFEKSGAMTGGSRAPRG 664
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1607 RNSLQSKLSDEVAarhELEEQIKKLEHDSSSLQSAKARLENECKTLQQKVEIL----------GELYQQKEMALQKKLTQ 1676
Cdd:TIGR02169 665 GILFSRSEPAELQ---RLRERLEGLKRELSSLQSELRRIENRLDELSQELSDAsrkigeiekeIEQLEQEEEKLKERLEE 741
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1677 EEYERQEKEQKLSAADEK--------------------------AVLAIEEVKVYKQRIQDMEEELQKTE---------- 1720
Cdd:TIGR02169 742 LEEDLSSLEQEIENVKSElkelearieeleedlhkleealndleARLSHSRIPEIQAELSKLEEEVSRIEarlreieqkl 821
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024390606 1721 ---------------------RSYKNQIAAHEKKAHDNWLIARSAERALAEEKREAANLRQKL 1762
Cdd:TIGR02169 822 nrltlekeylekeiqelqeqrIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRL 884
|
|
| PHA03379 |
PHA03379 |
EBNA-3A; Provisional |
1779-1917 |
1.92e-05 |
|
EBNA-3A; Provisional
Pssm-ID: 223066 [Multi-domain] Cd Length: 935 Bit Score: 50.06 E-value: 1.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1779 KPTPG--RPDRQVPPRRVPLSRDGSFGPSPVSGGNPSPTQMMEvpsrplSAPQREGSRAEFGTVVDGPPAPRRPPE---- 1852
Cdd:PHA03379 410 EPTYGtpRPPVEKPRPEVPQSLETATSHGSAQVPEPPPVHDLE------PGPLHDQHSMAPCPVAQLPPGPLQDLEpgdq 483
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024390606 1853 LPGRMSVPDLGPAVASLISSG---PRTSSPATAKDRAPSPKEPE------APRVTTDSPSSIEPATVNVGPKGP 1917
Cdd:PHA03379 484 LPGVVQDGRPACAPVPAPAGPivrPWEASLSQVPGVAFAPVMPQpmpvepVPVPTVALERPVCPAPPLIAMQGP 557
|
|
| ADIP |
pfam11559 |
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ... |
1608-1718 |
2.21e-05 |
|
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: 46.54 E-value: 2.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1608 NSLQSKLSDEVAARHELEEQIKKLEHDSSSLQSAKARLENECKTLQQKVeilgELYQQKEMALQKKL-TQEEYERQEKE- 1685
Cdd:pfam11559 41 YELLQQRDRDLEFRESLNETIRTLEAEIERLQSKIERLKTQLEDLEREL----ALLQAKERQLEKKLkTLEQKLKNEKEe 116
|
90 100 110
....*....|....*....|....*....|....*
gi 2024390606 1686 -QKL-SAADEKAVLAIEEVKVYKQRIQDMEEELQK 1718
Cdd:pfam11559 117 lQRLkNALQQIKTQFAHEVKKRDREIEKLKERLAQ 151
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1376-1528 |
2.86e-05 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 49.44 E-value: 2.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1376 IKQAKESMkvaQEQKSILSDEIAGLKDTVKELEETNHQLDDKIKslrtmlDTERKQNAKKQKKlsetqkslEKFEEAF-- 1453
Cdd:PRK00409 504 IEEAKKLI---GEDKEKLNELIASLEELERELEQKAEEAEALLK------EAEKLKEELEEKK--------EKLQEEEdk 566
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024390606 1454 SMHSAElSEVQIALNESKLSEEKVKAELQHVQEENARLKKSKEqlLKEAegwserHTELTEQIKLYRKSQKDIEE 1528
Cdd:PRK00409 567 LLEEAE-KEAQQAIKEAKKEADEIIKELRQLQKGGYASVKAHE--LIEA------RKRLNKANEKKEKKKKKQKE 632
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
1625-1768 |
2.99e-05 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 48.92 E-value: 2.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1625 EEQIKKLEHDSSSLQSAKARLENecKTLQQKvEILGELYQQkemalQKKLTQEEYERQEKEQKLSAADEKAvlaieevkv 1704
Cdd:PRK11637 169 QETIAELKQTREELAAQKAELEE--KQSQQK-TLLYEQQAQ-----QQKLEQARNERKKTLTGLESSLQKD--------- 231
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024390606 1705 ykqriQDMEEELQKTERSYKNQIAAHEKKAHdnwliARsAERalaeEKREAANLRQKLMEVNQK 1768
Cdd:PRK11637 232 -----QQQLSELRANESRLRDSIARAEREAK-----AR-AER----EAREAARVRDKQKQAKRK 280
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1351-1667 |
3.11e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 49.27 E-value: 3.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1351 LAEKIQNLLQEKTEMLDKFSECDEKIKQAKESMKVAQEQKSILSDEIA--------------GLKDTVKELEETNHQLDD 1416
Cdd:PRK02224 347 LREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEelrerfgdapvdlgNAEDFLEELREERDELRE 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1417 KIKSLRTMLDTERKQNAKKQKKL--------------SETQKSLEKFEEAFSMHSAELSEVQIALNE------------- 1469
Cdd:PRK02224 427 REAELEATLRTARERVEEAEALLeagkcpecgqpvegSPHVETIEEDRERVEELEAELEDLEEEVEEveerleraedlve 506
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1470 -----------SKLSEEKV---KAELQHVQEENARLKKSKEQLLKEAEGWSERHTELTEQIKLYRKSQKDIEEALAYKEN 1535
Cdd:PRK02224 507 aedrierleerREDLEELIaerRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKE 586
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1536 EIEvltncimQLKQLDTDSASEAKDGEGLEWSTKDDLANGELPDNEKMKTQIKQmmdaSRVKTMLSLVEEDR-NSLQSKL 1614
Cdd:PRK02224 587 RIE-------SLERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKR----ERKRELEAEFDEARiEEAREDK 655
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024390606 1615 SDEVAARHELEEQIKKLEHDSSSLQSAKARLENECK----------TLQQKVEILGELYQQKE 1667
Cdd:PRK02224 656 ERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEeleelrerreALENRVEALEALYDEAE 718
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1782-1982 |
3.30e-05 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 49.55 E-value: 3.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1782 PGRPDRQVPPR-RVPLSRDGsfGPSPVSGGNPSPtQMMEVPSRPLSA-----PQREGSRAEFGTVVDG------------ 1843
Cdd:PHA03247 2475 PGAPVYRRPAEaRFPFAAGA--APDPGGGGPPDP-DAPPAPSRLAPAilpdePVGEPVHPRMLTWIRGleelasddagdp 2551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1844 -PPAPRRPPELPGRMSVPDLGPAvaslissgPRTSSPA-TAKDRAPS-PKEPEAPRVTtdspssiepatvnVGPKGPPsf 1920
Cdd:PHA03247 2552 pPPLPPAAPPAAPDRSVPPPRPA--------PRPSEPAvTSRARRPDaPPQSARPRAP-------------VDDRGDP-- 2608
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024390606 1921 PGTPVMTSPVLGPPPPPPvnygpppaPFPghyGPGPRPLPVPLVCGAPLPPPAARDFLPGPS 1982
Cdd:PHA03247 2609 RGPAPPSPLPPDTHAPDP--------PPP---SPSPAANEPDPHPPPTVPPPERPRDDPAPG 2659
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1349-1713 |
3.89e-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: 48.89 E-value: 3.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1349 KQLAEKIQNLLQEKTEMLDKFSECD---EKIKQAKESMKVAQEQKSILSDEIAGLKDTVKELEE------------TNHQ 1413
Cdd:TIGR00606 747 PELRNKLQKVNRDIQRLKNDIEEQEtllGTIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQqaaklqgsdldrTVQQ 826
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1414 LDDKIKSLRTMLDTERKQNAKKQKKLSETQKSLEKFEEAFSMHSAELSEVQIALNESKLSEEKVKAELQHVQEENARLKK 1493
Cdd:TIGR00606 827 VNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKD 906
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1494 SKEQLLKEAEGWSERHTELTEQIKLYRKSQKDIEEALAYKENEIEvltNCIMQLKQLDtDSASEAKDGEGLEWSTKDDLA 1573
Cdd:TIGR00606 907 AKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVK---NIHGYMKDIE-NKIQDGKDDYLKQKETELNTV 982
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1574 NGELPDNEKMKTQIKQMMDASRVKTmlslveeDRNSLQSKLSDEVAARHELEEQIKKLE-----HDSSSLQSAKARLENE 1648
Cdd:TIGR00606 983 NAQLEECEKHQEKINEDMRLMRQDI-------DTQKIQERWLQDNLTLRKRENELKEVEeelkqHLKEMGQMQVLQMKQE 1055
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1649 CKTLQQKVEILGE-----LYQQKEMALQKKLtqeeYERQEKEQKLSAADEKAVLAIEEVKVYKQRIQDME 1713
Cdd:TIGR00606 1056 HQKLEENIDLIKRnhvlaLGRQKGYEKEIKH----FKKELREPQFRDAEEKYREMMIVMRTTELVNKDLD 1121
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1360-1549 |
4.44e-05 |
|
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: 48.89 E-value: 4.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1360 QEKTEMLDKFSECDEKIKQAKesmkvAQEQKSILSDEIAGLKDTVKELEETNHQLDDKIKSLRTMLDTERKQNAKKQKKL 1439
Cdd:TIGR01612 1521 KDVTELLNKYSALAIKNKFAK-----TKKDSEIIIKEIKDAHKKFILEAEKSEQKIKEIKKEKFRIEDDAAKNDKSNKAA 1595
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1440 SETQKSLEKFEEAFsmhsAELSEVQIALNESKLSEEKVKAELQHVQEEnarlkkSKEQLLKEAEGWSERHTELTEQIKLY 1519
Cdd:TIGR01612 1596 IDIQLSLENFENKF----LKISDIKKKINDCLKETESIEKKISSFSID------SQDTELKENGDNLNSLQEFLESLKDQ 1665
|
170 180 190
....*....|....*....|....*....|
gi 2024390606 1520 RKSQKDIEEALAYKENEIEVLTNCIMQLKQ 1549
Cdd:TIGR01612 1666 KKNIEDKKKELDELDSEIEKIEIDVDQHKK 1695
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1337-1755 |
4.84e-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: 48.89 E-value: 4.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1337 LSVKSRMYQVTEKQLAEKIQNLLQEKTEMLDKF----SECDEKIKQAKEsmkvAQEQKSILSDEIAGLKDTVKELEETNH 1412
Cdd:TIGR00606 700 LQSKLRLAPDKLKSTESELKKKEKRRDEMLGLApgrqSIIDLKEKEIPE----LRNKLQKVNRDIQRLKNDIEEQETLLG 775
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1413 QLDDKIKSLRTMLdterkqnaKKQKKLSETQKSLEKFEEAFSMHSAELSEVQIALNESKLSEEKvkaelQHVQEENARLK 1492
Cdd:TIGR00606 776 TIMPEEESAKVCL--------TDVTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEK-----QEKQHELDTVV 842
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1493 KSKEQLLKEAEGWSERHTELTEQIKLYRKSQKDIEEALAYKENEIEVLTNCIMQLKQLDTDSASEAKDGEGLEWSTKDDL 1572
Cdd:TIGR00606 843 SKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQ 922
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1573 ANGELPDNEKMKTQIKQMMDASRVKTMLSLVEEDRNSLQSKLSD-EVAARHELEEQIKKLEHDSSSLQSAKARLENECKT 1651
Cdd:TIGR00606 923 QEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDgKDDYLKQKETELNTVNAQLEECEKHQEKINEDMRL 1002
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1652 LQQKVEIlgelYQQKEMALQKKLTQEEYERQEKEQKLSAADEKAVLAIEEVKVYKQRIQDMEEELQKTERSYkNQIAAHE 1731
Cdd:TIGR00606 1003 MRQDIDT----QKIQERWLQDNLTLRKRENELKEVEEELKQHLKEMGQMQVLQMKQEHQKLEENIDLIKRNH-VLALGRQ 1077
|
410 420
....*....|....*....|....*....
gi 2024390606 1732 KKAHDNWLIA----RSAERALAEEK-REA 1755
Cdd:TIGR00606 1078 KGYEKEIKHFkkelREPQFRDAEEKyREM 1106
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
1395-1511 |
5.52e-05 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 47.77 E-value: 5.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1395 DEIAGLKDTVKELEETNHQLDDKIKSLRTMLDTERKQNAKKQKKLSETQKSLEKFEEAFSMHSAELSEVQiaLNESKLSE 1474
Cdd:PRK11637 170 ETIAELKQTREELAAQKAELEEKQSQQKTLLYEQQAQQQKLEQARNERKKTLTGLESSLQKDQQQLSELR--ANESRLRD 247
|
90 100 110
....*....|....*....|....*....|....*..
gi 2024390606 1475 EKVKAElqhvQEENARlkksKEQLLKEAEGWSERHTE 1511
Cdd:PRK11637 248 SIARAE----REAKAR----AEREAREAARVRDKQKQ 276
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1345-1717 |
5.91e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.39 E-value: 5.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1345 QVTEKQLAEKIQNLLQEKTEMLDKFSECDEKIKQAKESMKVAQEQKSILSDEIAGLKDTVKELEETNHQLDDKIKSLRTM 1424
Cdd:COG1196 357 EAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEE 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1425 LDTERKQNAKKQKKLSETQKSLEKFEEAFS--MHSAELSEVQIALNESKLSEEKVKAELQHVQEENARLKKSKEQLLKEA 1502
Cdd:COG1196 437 EEEEEEALEEAAEEEAELEEEEEALLELLAelLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLL 516
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1503 EGWSERHTELTEQIKLYRKSQKDIEEALAYKENEI-----EVLTNCIMQLKQ----------LDTDSASEAkDGEGLEWS 1567
Cdd:COG1196 517 AGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIvveddEVAAAAIEYLKAakagratflpLDKIRARAA-LAAALARG 595
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1568 TKDDLANGELPDNEKMKTQIKQMMDASRVKTMLSLVEEDRN-----------------------------SLQSKLSDEV 1618
Cdd:COG1196 596 AIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALrravtlagrlrevtlegeggsaggsltggSRRELLAALL 675
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1619 AARHELEEQIKKLEHDSSSLQSAKARLENECKTLQQKVEILGELYQQKEMALQKKLTQ---------------------- 1676
Cdd:COG1196 676 EAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEreelleelleeeelleeealee 755
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1677 --EEYERQEKEQKLSAADEK-----AV--LAIEEVKVYKQRIQDMEEELQ 1717
Cdd:COG1196 756 lpEPPDLEELERELERLEREiealgPVnlLAIEEYEELEERYDFLSEQRE 805
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1603-1733 |
7.31e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 46.46 E-value: 7.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1603 VEEDRNSLQSKLSDEVAARHELEEQIKKLEHDSSSLQSAKARLEN---------ECKTLQQKVEILGELYQQKEmalqKK 1673
Cdd:COG1579 36 LEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEqlgnvrnnkEYEALQKEIESLKRRISDLE----DE 111
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1674 LTQEEYERQEKEQKLSAADEKAVLAIEEVKVYKQRIQDMEEELQKTERSYKNQIAAHEKK 1733
Cdd:COG1579 112 ILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAK 171
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1349-1534 |
7.80e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.52 E-value: 7.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1349 KQLAEKIQNLLQEKTEMLDKFSECDEKIKQAKESMKVAQEQKSILSDEIAGLKdtvKELEETNHQLDDKIKSL------- 1421
Cdd:COG3883 26 SELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAE---AEIEERREELGERARALyrsggsv 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1422 ------------------RTMLDTERKQNAKKQKKLSETQKSLEKFEEAFSMHSAELSEVQIALNESKLSEEKVKAELqh 1483
Cdd:COG3883 103 syldvllgsesfsdfldrLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQ-- 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2024390606 1484 vQEENARLKKSKEQLLKEAEGWSERHTELTEQIKLYRKSQKDIEEALAYKE 1534
Cdd:COG3883 181 -EALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAA 230
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1416-1736 |
8.53e-05 |
|
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: 47.79 E-value: 8.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1416 DKIKSLRTMLDTERKQnakKQKKLSETQKSLEKFEEAfsmhsaelsevqiaLNESKLSEEKVKAELQHVQEENARLKKS- 1494
Cdd:pfam05483 88 EKIKKWKVSIEAELKQ---KENKLQENRKIIEAQRKA--------------IQELQFENEKVSLKLEEEIQENKDLIKEn 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1495 ----------KEQLLKEAEGWSERHTELTEQIKLYRKSQKDIEEA-LAYKE----------------------------- 1534
Cdd:pfam05483 151 natrhlcnllKETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMiLAFEElrvqaenarlemhfklkedhekiqhleee 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1535 --NEIEVLTNCIMQLKQLDTDSASEAKDGEGLEWSTKDDLANGElpdnEKMKTQIKQMMDASRVKTMLSLVEED-RNSLQ 1611
Cdd:pfam05483 231 ykKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLE----EKTKLQDENLKELIEKKDHLTKELEDiKMSLQ 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1612 SKLSDEVAARHELEEQIKKL-----EHDSSSLQSAKAR----------------LENECKTLQQKVEILGELYQQKEMAL 1670
Cdd:pfam05483 307 RSMSTQKALEEDLQIATKTIcqlteEKEAQMEELNKAKaahsfvvtefeattcsLEELLRTEQQRLEKNEDQLKIITMEL 386
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024390606 1671 QKKLTQ-EEYERQEKEQKLSAADEKAVLAIEEVKVY-KQRIQDMEEELQKTERSYKNQIAAHEKKAHD 1736
Cdd:pfam05483 387 QKKSSElEEMTKFKNNKEVELEELKKILAEDEKLLDeKKQFEKIAEELKGKEQELIFLLQAREKEIHD 454
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
1754-1984 |
9.79e-05 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 47.56 E-value: 9.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1754 EAANLRQKLMEVNQKTIMLQRPLIVKPTPGRPDRQVPPRRVPlsrdGSFGPSPVSGGNPSPTQMMEVPSRPLSAPQREGS 1833
Cdd:PRK12323 371 GAGPATAAAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAA----AAAARAVAAAPARRSPAPEALAAARQASARGPGG 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1834 RAEFGTVVDGPPAPRRPPELPGRMSVPDLGPAVaslissgPRTSSPATAkdRAPSPKEPEAPRVTTDSPSSIEPATVNVG 1913
Cdd:PRK12323 447 APAPAPAPAAAPAAAARPAAAGPRPVAAAAAAA-------PARAAPAAA--PAPADDDPPPWEELPPEFASPAPAQPDAA 517
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024390606 1914 PKGPPSFPGTPVMTSPVLGPPPPPPVNYGPPPApfpghygPGPRPLPVPLVcgAPLPPPAARDFLPGPSLG 1984
Cdd:PRK12323 518 PAGWVAESIPDPATADPDDAFETLAPAPAAAPA-------PRAAAATEPVV--APRPPRASASGLPDMFDG 579
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
1569-1768 |
1.00e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 47.61 E-value: 1.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1569 KDDLANGELPDNEKMKTQIKQMMDA-SRVKTMLSLVEEDRNSLQSKLSDEVAARHE-----LEEQIKKLEHDSSSLQSAK 1642
Cdd:PRK05771 37 KEELSNERLRKLRSLLTKLSEALDKlRSYLPKLNPLREEKKKVSVKSLEELIKDVEeelekIEKEIKELEEEISELENEI 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1643 ARLENECKTLqqkvEILGELyqqkEMALQKKLTQE-------EYERQEKEQKLSAADEKAVLAIEEVK--------VYKQ 1707
Cdd:PRK05771 117 KELEQEIERL----EPWGNF----DLDLSLLLGFKyvsvfvgTVPEDKLEELKLESDVENVEYISTDKgyvyvvvvVLKE 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024390606 1708 RIQDMEEELQKTErsYKNQIAAHEKKAHDnwLIARSAERaLAEEKREAANLRQKLMEVNQK 1768
Cdd:PRK05771 189 LSDEVEEELKKLG--FERLELEEEGTPSE--LIREIKEE-LEEIEKERESLLEELKELAKK 244
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1345-1777 |
1.17e-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: 47.35 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1345 QVTEKQLAEKIQNLLQEKTEMLDKfsECDEKIKQAKESMKVAQEQKSILSDEIAGLKDTVKELEETNHQLDDKIKSLRTM 1424
Cdd:TIGR00606 403 QEDEAKTAAQLCADLQSKERLKQE--QADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQEL 480
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1425 LDTERKQNAKKQKKLSETQKSLEKFeeafsmhsaeLSEVQIALNESKLSEEKVKAELQHVQEEN------ARLKKSKEQL 1498
Cdd:TIGR00606 481 RKAERELSKAEKNSLTETLKKEVKS----------LQNEKADLDRKLRKLDQEMEQLNHHTTTRtqmemlTKDKMDKDEQ 550
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1499 LKEAEgwSERHTELTEQIKlYRKSQKDIEEALAYKENEIEV-------LTNCIMQLKQLDTDSASEAKDGEGLEWSTKDD 1571
Cdd:TIGR00606 551 IRKIK--SRHSDELTSLLG-YFPNKKQLEDWLHSKSKEINQtrdrlakLNKELASLEQNKNHINNELESKEEQLSSYEDK 627
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1572 L-----ANGELPDNEKMKTQIKQmmdASRVKTMLSLVEEDRNSLQSKLSDEVAA-----------RHELEEQIKKLEHDS 1635
Cdd:TIGR00606 628 LfdvcgSQDEESDLERLKEEIEK---SSKQRAMLAGATAVYSQFITQLTDENQSccpvcqrvfqtEAELQEFISDLQSKL 704
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1636 SSLQSAKARLENECKTLQQKVEILGELYQQKEMALQKKlTQEEYERQEKEQKLSA--ADEKAVLAIEEVKVYKQR----- 1708
Cdd:TIGR00606 705 RLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLK-EKEIPELRNKLQKVNRdiQRLKNDIEEQETLLGTIMpeees 783
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024390606 1709 ----------IQDMEEELQKTERSYKNQIAahEKKAHDNWLIARSAERALAEEKREAANLRQKLmEVNQKTIMLQRPLI 1777
Cdd:TIGR00606 784 akvcltdvtiMERFQMELKDVERKIAQQAA--KLQGSDLDRTVQQVNQEKQEKQHELDTVVSKI-ELNRKLIQDQQEQI 859
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1349-1677 |
1.19e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.82 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1349 KQLAEKIQNLLQEKTEMLDKFSECDEKIKQAKESMKVAQEQKSILSDEIAGLKDTVKELEETNHQLDDKIKSLRTMLDTE 1428
Cdd:COG4372 41 DKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEEL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1429 RKQNAKKQKKLSETQKSLEKFEEAFSMHSAELSEVQIALNEskLSEEKVKAELQHVQEENARLKKSKEQLLKEAEGWSER 1508
Cdd:COG4372 121 QKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLES--LQEELAALEQELQALSEAEAEQALDELLKEANRNAEK 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1509 HTELTEQIKLYRKSQKDIEEA---LAYKENEIEVLTNCIMQLKQLDTDSASEAKDGEGLEWSTKDDLANGELPDNEKMKT 1585
Cdd:COG4372 199 EEELAEAEKLIESLPRELAEElleAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEEL 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1586 QIKQMMDASRVKTMLSLVEEDRNSLQSKLSDEVAARHELEEQIKKLEHDSSSLQSAKARLENECKTLQQKVEILGELYQQ 1665
Cdd:COG4372 279 EIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLEL 358
|
330
....*....|..
gi 2024390606 1666 KEMALQKKLTQE 1677
Cdd:COG4372 359 LSKGAEAGVADG 370
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1346-1673 |
1.39e-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: 47.35 E-value: 1.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1346 VTEKQLAEKIQNLLQEKTEMLDKFSECDEKIKQAKESMK-VAQEQKSIlsdEIAGLKdtvkeleeTNHQLDDKIKSLRTM 1424
Cdd:TIGR01612 1412 LDDKDIDECIKKIKELKNHILSEESNIDTYFKNADENNEnVLLLFKNI---EMADNK--------SQHILKIKKDNATND 1480
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1425 LD---TERKQNAKKQKKLS----ETQKSLEKFEEAFSMHSAELSEVqiaLNesKLSEEKVKAELqhvqeenARLKKSKEQ 1497
Cdd:TIGR01612 1481 HDfniNELKEHIDKSKGCKdeadKNAKAIEKNKELFEQYKKDVTEL---LN--KYSALAIKNKF-------AKTKKDSEI 1548
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1498 LLKEAEGWSERHT---ELTEQ-IKLYRKSQKDIEEALAYKENEIEVLTNCIMQLKQLDTdsaseakdgEGLEWSTKDDLA 1573
Cdd:TIGR01612 1549 IIKEIKDAHKKFIleaEKSEQkIKEIKKEKFRIEDDAAKNDKSNKAAIDIQLSLENFEN---------KFLKISDIKKKI 1619
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1574 NGELPDNEKMKTQIKQMMDASRvKTMLSLVEEDRNSLQSKLSDEVAARHELEEQIKKLEHDSSSLQSakarLENECKTLQ 1653
Cdd:TIGR01612 1620 NDCLKETESIEKKISSFSIDSQ-DTELKENGDNLNSLQEFLESLKDQKKNIEDKKKELDELDSEIEK----IEIDVDQHK 1694
|
330 340
....*....|....*....|
gi 2024390606 1654 QKVEIlGELYQQKEMALQKK 1673
Cdd:TIGR01612 1695 KNYEI-GIIEKIKEIAIANK 1713
|
|
| Agg_substance |
NF033875 |
LPXTG-anchored aggregation substance; Aggregation substances, as described in Enterococcus, ... |
523-713 |
1.67e-04 |
|
LPXTG-anchored aggregation substance; Aggregation substances, as described in Enterococcus, are LPXTG-anchored large surface proteins that contribute to virulence. Several closely related paralogs may be found in a single strain.
Pssm-ID: 411439 [Multi-domain] Cd Length: 1306 Bit Score: 47.01 E-value: 1.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 523 DPDAKEKTNKTEQFEEQLLTDETVLHPEELKSTAvpdppvlhSPGDGLKFKSFVEGKQDALSPPAGDVNQSPEGVLLAET 602
Cdd:NF033875 61 DPQSGSETPKTAVSEEATVQKDTTSQPTKVEEVA--------SEKNGAEQSSATPNDTTNAQQPTVGAEKSAQEQPVVSP 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 603 EKEEEKFGGDTLKESSENNFKHRKLWEKM-------KEKGKAKYEPSGDVLAKPVEDVQNTSQSDTGDTDLLKDKLEQEM 675
Cdd:NF033875 133 ETTNEPLGQPTEVAPAENEANKSTSIPKEfetpdvdKAVDEAKKDPNITVVEKPAEDLGNVSSKDLAAKEKEVDQLQKEQ 212
|
170 180 190
....*....|....*....|....*....|....*...
gi 2024390606 676 PvveKEILRQEEDLKQTREADHENQRPISVKKEPEIER 713
Cdd:NF033875 213 A---KKIAQQAAELKAKNEKIAKENAEIAAKNKAEKER 247
|
|
| PHA03378 |
PHA03378 |
EBNA-3B; Provisional |
1778-1971 |
1.71e-04 |
|
EBNA-3B; Provisional
Pssm-ID: 223065 [Multi-domain] Cd Length: 991 Bit Score: 46.98 E-value: 1.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1778 VKPTPGRPdrqvpPRRVPLSRDGSFGPSPVSGGNPSPTQmmEVPSRPLS-APQREGSRAEfgtvvdgPPAPRRPPEL-PG 1855
Cdd:PHA03378 647 VFPTPHQP-----PQVEITPYKPTWTQIGHIPYQPSPTG--ANTMLPIQwAPGTMQPPPR-------APTPMRPPAApPG 712
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1856 RMSVPDLGPAVASLISSGP-RTSSPATAKDRAPSPK-EPEAPRVTTDSPSSIEPATVNVG---PKGPPSFPGTPvmtspv 1930
Cdd:PHA03378 713 RAQRPAAATGRARPPAAAPgRARPPAAAPGRARPPAaAPGRARPPAAAPGRARPPAAAPGaptPQPPPQAPPAP------ 786
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2024390606 1931 lgppppppvNYGPPPAPFPghyGPGPRPLPVPLVCGAPLPP 1971
Cdd:PHA03378 787 ---------QQRPRGAPTP---QPPPQAGPTSMQLMPRAAP 815
|
|
| PHA03378 |
PHA03378 |
EBNA-3B; Provisional |
1780-2046 |
1.73e-04 |
|
EBNA-3B; Provisional
Pssm-ID: 223065 [Multi-domain] Cd Length: 991 Bit Score: 46.98 E-value: 1.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1780 PTPGRPDRQVPPRRVPLSRDGSFGPSP-------VSGGNPSPTQMMEVPSRPLSApqregsraefgtvvdGPPAPRRPPE 1852
Cdd:PHA03378 625 PMPLRPIPMRPLRMQPITFNVLVFPTPhqppqveITPYKPTWTQIGHIPYQPSPT---------------GANTMLPIQW 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1853 LPGRMSVPDLGPAVASLISSGP-RTSSPATAKDRAPSPKEpeaprvttdSPSSIEPATVNVGPKGPPSFPGTPVMTSPVL 1931
Cdd:PHA03378 690 APGTMQPPPRAPTPMRPPAAPPgRAQRPAAATGRARPPAA---------APGRARPPAAAPGRARPPAAAPGRARPPAAA 760
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1932 GPPPPPPVNYGPPPAPFPGHYGPgPRPLPVPLVCGAPLPPP----AARDFLPgPSLGIRDLPPGPLPPLPDPRSYRRGHP 2007
Cdd:PHA03378 761 PGRARPPAAAPGAPTPQPPPQAP-PAPQQRPRGAPTPQPPPqagpTSMQLMP-RAAPGQQGPTKQILRQLLTGGVKRGRP 838
|
250 260 270
....*....|....*....|....*....|....*....
gi 2024390606 2008 HFRPpgppgprdyppgpplpppasrdyaPSRSRDLPPAG 2046
Cdd:PHA03378 839 SLKK------------------------PAALERQAAAG 853
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1607-1768 |
1.80e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.55 E-value: 1.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1607 RNSLQSKLSDEVAARHELEEQIKKLEHDsssLQSAKARLENecktLQQKVEIL-----GELYQQKEMALQKKLTQEEYER 1681
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKE---LEEAEAALEE----FRQKNGLVdlseeAKLLLQQLSELESQLAEARAEL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1682 QEKEQKLSAADEK---------AVLAIEEVKVYKQRIQDMEEELQKTERSYKNQ----IAAHEKKAHDNWLIARSAERAL 1748
Cdd:COG3206 236 AEAEARLAALRAQlgsgpdalpELLQSPVIQQLRAQLAELEAELAELSARYTPNhpdvIALRAQIAALRAQLQQEAQRIL 315
|
170 180
....*....|....*....|
gi 2024390606 1749 AEEKREAANLRQKLMEVNQK 1768
Cdd:COG3206 316 ASLEAELEALQAREASLQAQ 335
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1349-1678 |
2.43e-04 |
|
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: 46.10 E-value: 2.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1349 KQLAEKIQNLLQEKTEMLDkfsecdEKIKQAKESMKVAQEQKSILsdeiaglkdtVKELEETNHQLDDKIKSLRTMLDTE 1428
Cdd:COG5185 249 AQTSDKLEKLVEQNTDLRL------EKLGENAESSKRLNENANNL----------IKQFENTKEKIAEYTKSIDIKKATE 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1429 RKQNakkQKKLSETQKSLE-KFEEAFSMHSAELSEVQIALNESKLSEEKVKAELQHVQEENaRLKKSKEQLLKEAEGWSE 1507
Cdd:COG5185 313 SLEE---QLAAAEAEQELEeSKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEV-ELSKSSEELDSFKDTIES 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1508 RHTELTEQIKLYRKSQKDIEEALA--YKENEIEvLTNCIMQLKQLDTDSASEAKDGEGLEWSTkdDLANGELPDNEKMKT 1585
Cdd:COG5185 389 TKESLDEIPQNQRGYAQEILATLEdtLKAADRQ-IEELQRQIEQATSSNEEVSKLLNELISEL--NKVMREADEESQSRL 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1586 QIKQMMDASRVKTMLSLVEEDRNSLQSKLSdevAARHELEEQIKKLEHDSSSLQSAKARLENECKTLQQKVEIlgELYQQ 1665
Cdd:COG5185 466 EEAYDEINRSVRSKKEDLNEELTQIESRVS---TLKATLEKLRAKLERQLEGVRSKLDQVAESLKDFMRARGY--AHILA 540
|
330
....*....|...
gi 2024390606 1666 KEMALQKKLTQEE 1678
Cdd:COG5185 541 LENLIPASELIQA 553
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1354-1530 |
2.78e-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: 44.53 E-value: 2.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1354 KIQNLLQEKTEMLDKFSECDEKIKQAKESMKVAQEQKSILSDEIAGLKDTVKELEETNHQLDDKIKSlrtmlDTERKQNA 1433
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKK-----YEEQLGNV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1434 KKQKKLSETQKSLEKFEEAFSMHSAELSEVQIALNESKLSEEKVKAELQHVQEENARLKKSKEQLLKEAEgwsERHTELT 1513
Cdd:COG1579 86 RNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELE---AELEELE 162
|
170
....*....|....*..
gi 2024390606 1514 EQIKLYRKSqkdIEEAL 1530
Cdd:COG1579 163 AEREELAAK---IPPEL 176
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1380-1729 |
3.40e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 46.06 E-value: 3.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1380 KESMKVAQEQKSILSDEiaglKDTVKELEETNHQLDdKIKSLRTMLDTERKQNAKKQKKLSETQKSLEKFEEAFSMHSAE 1459
Cdd:PRK11281 42 QAQLDALNKQKLLEAED----KLVQQDLEQTLALLD-KIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETRE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1460 -LSEVQIALNESKLSEekVKAELQHVQEE----NARLKKSKEQllkeaegwSERhtelteqiklyrkSQKDIEEALAyke 1534
Cdd:PRK11281 117 tLSTLSLRQLESRLAQ--TLDQLQNAQNDlaeyNSQLVSLQTQ--------PER-------------AQAALYANSQ--- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1535 neievltncimQLKQLDTDSASEAKDGEGLEWSTKDDLaNGELpdnekmktqikQMMDASrvktmlslVEEDRNSLQ--S 1612
Cdd:PRK11281 171 -----------RLQQIRNLLKGGKVGGKALRPSQRVLL-QAEQ-----------ALLNAQ--------NDLQRKSLEgnT 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1613 KLSDEVAARHEL-EEQIKKLEHDSSSLQSA--KARLENECKTLQQ------KVEILGELYQQKEMALQKKLTQEeyerqe 1683
Cdd:PRK11281 220 QLQDLLQKQRDYlTARIQRLEHQLQLLQEAinSKRLTLSEKTVQEaqsqdeAARIQANPLVAQELEINLQLSQR------ 293
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 2024390606 1684 keqKLSAADEKAVLAIEEVKVyKQRIqdmeEELQKTERSYKNQIAA 1729
Cdd:PRK11281 294 ---LLKATEKLNTLTQQNLRV-KNWL----DRLTQSERNIKEQISV 331
|
|
| HlpA |
COG2825 |
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ... |
1639-1727 |
3.49e-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: 43.29 E-value: 3.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1639 QSAKARLENECKTLQQKVEILGELYQQKEMALQKK---LTQEeyERQEKEQKLSAADEKavlaieevkvYKQRIQDMEEE 1715
Cdd:COG2825 42 KAAQKKLEKEFKKRQAELQKLEKELQALQEKLQKEaatLSEE--ERQKKERELQKKQQE----------LQRKQQEAQQD 109
|
90
....*....|..
gi 2024390606 1716 LQKTERSYKNQI 1727
Cdd:COG2825 110 LQKRQQELLQPI 121
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1400-1732 |
3.75e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 45.66 E-value: 3.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1400 LKDTVKELEETNHQLD---DKIKSLRTMLDTERKQNAKKQKKLSETQKSLEKFEEAFSMHSAELSEVQIALNE-SKLSEE 1475
Cdd:PRK01156 171 LKDVIDMLRAEISNIDyleEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNElSSLEDM 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1476 KVKAE---------LQHVQEENARLKKSKEQLLK---------------------EAEGWSERHTELTEQIKLYRKSQKD 1525
Cdd:PRK01156 251 KNRYEseiktaesdLSMELEKNNYYKELEERHMKiindpvyknrnyindyfkyknDIENKKQILSNIDAEINKYHAIIKK 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1526 IEEALAY------KENEIEVLTNCIMQLKQLDTDSASEAKDGEGLEWSTKDDLANGELPDNEKMKTQIKQMMDASRVKTM 1599
Cdd:PRK01156 331 LSVLQKDyndyikKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKE 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1600 LSLVEEDRNSLQSKLSDEVAARHELEEQIKKLEHDSSSLQSakarlENECKTL-----QQKVEILGELYQQKEMALQKKL 1674
Cdd:PRK01156 411 LNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNG-----QSVCPVCgttlgEEKSNHIINHYNEKKSRLEEKI 485
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024390606 1675 TQEEYE----RQEKEQKLSAADEKAVLAIEEVKVYKQRIQDMEEELQKTERSYKNQIAAHEK 1732
Cdd:PRK01156 486 REIEIEvkdiDEKIVDLKKRKEYLESEEINKSINEYNKIESARADLEDIKIKINELKDKHDK 547
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1583-1760 |
3.86e-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: 44.15 E-value: 3.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1583 MKTQIKQMMDASRVKTMLSLVEEDRNSLQSKLSdevaarhELEEQIKKLEHD-------SSSLQSAKARLENECKTLQQK 1655
Cdd:COG1579 2 MPEDLRALLDLQELDSELDRLEHRLKELPAELA-------ELEDELAALEARleaakteLEDLEKEIKRLELEIEEVEAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1656 VEI----LGELYQQKEM-ALQKKLTQEEYERQEKEQKLSAADEKAVLAIEEVKVYKQRIQDMEEELQKTERSYKNQIAAH 1730
Cdd:COG1579 75 IKKyeeqLGNVRNNKEYeALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAEL 154
|
170 180 190
....*....|....*....|....*....|
gi 2024390606 1731 EKKahdnwLIARSAERALAEEKREAANLRQ 1760
Cdd:COG1579 155 EAE-----LEELEAEREELAAKIPPELLAL 179
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1772-2036 |
4.56e-04 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 45.70 E-value: 4.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1772 LQRPLIVKPTPG-RPDRQVPPRRVPLSRDGSFGPSPVSGGNPSPTQMMEVPSRPlSAPQREGSRAefgtVVDGPPA---P 1847
Cdd:PHA03247 2698 LADPPPPPPTPEpAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATP-GGPARPARPP----TTAGPPApapP 2772
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1848 RRPPELPGRMSVPdlgPAVASLISSGPRTSSPATAKDRAPSPKEPEAPRVTTDSPSSIEPATVNVGPKGPPSFPGtPVMT 1927
Cdd:PHA03247 2773 AAPAAGPPRRLTR---PAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPG-PPPP 2848
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1928 SPvlgppppppvnygpppaPFPGHYGPG------PRPLPVPLVCGAPLPPPAARDFLPGPS-----LGIRDLPPGPLPPL 1996
Cdd:PHA03247 2849 SL-----------------PLGGSVAPGgdvrrrPPSRSPAAKPAAPARPPVRRLARPAVSrstesFALPPDQPERPPQP 2911
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 2024390606 1997 PDPRSYRRGHPHFRPPGPPGPRDYPPGPPLPPPASRDYAP 2036
Cdd:PHA03247 2912 QAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAG 2951
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
1780-2048 |
5.21e-04 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 45.16 E-value: 5.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1780 PTPGrPDRQVPPRRVPLSRDGSFGPSPVSGGNPSPTQMMEVPSRPLSAPQREGSRAEFGTVVDGPPAPRRPPELPGrmsv 1859
Cdd:PHA03307 128 PSPA-PDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQAALPLSSPEETARAPSSPPAEPPPSTPPAAA---- 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1860 PDLGPAVASLISSGPRTSSPATAKDRApSPKEPEAPRVTTDSPSSIEPATVNVGPKGPPSFPGTPvmTSPVLGPPPPPPV 1939
Cdd:PHA03307 203 SPRPPRRSSPISASASSPAPAPGRSAA-DDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLP--TRIWEASGWNGPS 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1940 NYGPPPAPFPGHYGPGPRPLP-VPLVCGAPLPPPAARDFLPGPSLGIrdLPPGPLPPLPDPRSYRRGHPHFRPPGPPgpr 2018
Cdd:PHA03307 280 SRPGPASSSSSPRERSPSPSPsSPGSGPAPSSPRASSSSSSSRESSS--SSTSSSSESSRGAAVSPGPSPSRSPSPS--- 354
|
250 260 270
....*....|....*....|....*....|
gi 2024390606 2019 dyppgpplPPPASRDYAPSRSRDLPPAGPR 2048
Cdd:PHA03307 355 --------RPPPPADPSSPRKRPRPSRAPS 376
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1474-1768 |
5.30e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 45.01 E-value: 5.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1474 EEKVKAELQHVQEEnarlKKSKEQLLKEAEGWS----ERHTELTEQIKLYRKSQKDIEEALAYKENeievltncimQLKQ 1549
Cdd:TIGR04523 35 EKQLEKKLKTIKNE----LKNKEKELKNLDKNLnkdeEKINNSNNKIKILEQQIKDLNDKLKKNKD----------KINK 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1550 LDTDS---ASEAKDGEGLEWSTKDDLANGELPDNEKMKTQIKqmmdasrVKTMLSLVEEDRNSLQSKLSDEVAARHELEE 1626
Cdd:TIGR04523 101 LNSDLskiNSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDK-------FLTEIKKKEKELEKLNNKYNDLKKQKEELEN 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1627 QIKKLEHDSSSLQSAKARLENECKTLQQKVEILgELYQQKEMALQKKLT--------------QEEYERQEKEQKLSAAD 1692
Cdd:TIGR04523 174 ELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNL-KKKIQKNKSLESQISelkkqnnqlkdnieKKQQEINEKTTEISNTQ 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1693 EKAVLAIEEVKVYKQRIQDMEEELQKTER----------SYKNQIAAHEKKAHDNWLIARSAEraLAEEKREAANLRQKL 1762
Cdd:TIGR04523 253 TQLNQLKDEQNKIKKQLSEKQKELEQNNKkikelekqlnQLKSEISDLNNQKEQDWNKELKSE--LKNQEKKLEEIQNQI 330
|
....*.
gi 2024390606 1763 MEVNQK 1768
Cdd:TIGR04523 331 SQNNKI 336
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
1801-1974 |
5.67e-04 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 44.87 E-value: 5.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1801 SFGPSPVSGGNPSPT-------QMMEVPSRPLSAPQREGSRAEFGTVVDGPPAPRRPP-ELPGRMSVP--DLGPAVASLI 1870
Cdd:PRK12323 362 AFRPGQSGGGAGPATaaaapvaQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVaAAPARRSPApeALAAARQASA 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1871 SSGPRTSSPATAKDRAPSPKEPEA-------PRVTTDSPSSIEPATVNV-GPKGPPSFPGTPV-MTSPVLGPPPPPPVNY 1941
Cdd:PRK12323 442 RGPGGAPAPAPAPAAAPAAAARPAaagprpvAAAAAAAPARAAPAAAPApADDDPPPWEELPPeFASPAPAQPDAAPAGW 521
|
170 180 190
....*....|....*....|....*....|....
gi 2024390606 1942 GPPPAPFPGHYGP-GPRPLPVPLVCGAPLPPPAA 1974
Cdd:PRK12323 522 VAESIPDPATADPdDAFETLAPAPAAAPAPRAAA 555
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
1638-1761 |
5.91e-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: 44.11 E-value: 5.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1638 LQSAKARLENECKTLQQKVEILGELYQQKEmALQKKLTQEEYERQEKEQKLSAADEKAVLAIEEVKVYKQRIQDMEEELQ 1717
Cdd:cd16269 151 REKLVEKYRQVPRKGVKAEEVLQEFLQSKE-AEAEAILQADQALTEKEKEIEAERAKAEAAEQERKLLEEQQRELEQKLE 229
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 2024390606 1718 KTERSYKNQIAAHEKK-AHDNWLIARSAERALAEEKREAANLRQK 1761
Cdd:cd16269 230 DQERSYEEHLRQLKEKmEEERENLLKEQERALESKLKEQEALLEE 274
|
|
| DUF4200 |
pfam13863 |
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ... |
1337-1423 |
6.42e-04 |
|
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil domain of unknwon function.
Pssm-ID: 464003 [Multi-domain] Cd Length: 119 Bit Score: 41.40 E-value: 6.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1337 LSVKSRMYQVTEKQLAEKIQNL------LQEKTEMLDKFS-ECDEKIKQAKESMKVAQEQKSILSDEIAGLKDTVKELEE 1409
Cdd:pfam13863 15 LDAKREEIERLEELLKQREEELekkeqeLKEDLIKFDKFLkENDAKRRRALKKAEEETKLKKEKEKEIKKLTAQIEELKS 94
|
90
....*....|....
gi 2024390606 1410 TNHQLDDKIKSLRT 1423
Cdd:pfam13863 95 EISKLEEKLEEYKP 108
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
1785-2005 |
6.76e-04 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 45.16 E-value: 6.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1785 PDRQVPPRRVPLSRDGSFGPSPVSGGNPSPTqmmEVPSRPLSAPQREGSRAEFGTVVDGPPAPRrPPELPGRMSVPDLGP 1864
Cdd:PHA03307 61 ACDRFEPPTGPPPGPGTEAPANESRSTPTWS---LSTLAPASPAREGSPTPPGPSSPDPPPPTP-PPASPPPSPAPDLSE 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1865 AVASLISSGPR--TSSPATAKDRAPSPKEPEAPRVTTDsPSSIEPATVNVGPKGPPSFPGT--PVMTSPVLGPPPPPPVN 1940
Cdd:PHA03307 137 MLRPVGSPGPPpaASPPAAGASPAAVASDAASSRQAAL-PLSSPEETARAPSSPPAEPPPStpPAAASPRPPRRSSPISA 215
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024390606 1941 YGPPPAPFPGHYGPGPRP-------LPVPLVCG------APLPPPAARDFLPGPSLGIRDLPPGPLPPLPDPRSYRRG 2005
Cdd:PHA03307 216 SASSPAPAPGRSAADDAGasssdssSSESSGCGwgpeneCPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRE 293
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1359-1694 |
7.74e-04 |
|
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: 44.43 E-value: 7.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1359 LQEKTEMLDKfsecdeKIKQAKEsmkvAQEQKSILSDEIAGLKDTV-----------KELEETNHQLDDK---------- 1417
Cdd:pfam10174 354 LEEKESFLNK------KTKQLQD----LTEEKSTLAGEIRDLKDMLdvkerkinvlqKKIENLQEQLRDKdkqlaglker 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1418 IKSLRTMLDTERKQNAKKQKKLSETQKSLEKFEEAFSMHSAE-LSEVQIALNESKLSEEKVKAELQHVQEENARLKKSKE 1496
Cdd:pfam10174 424 VKSLQTDSSNTDTALTTLEEALSEKERIIERLKEQREREDRErLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKE 503
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1497 Q-------------LLKEAEGWSERHTEltEQIKLYRKSQKDIEEALAYKENE-----IEVLTNCIMQLKQLDTDSASEA 1558
Cdd:pfam10174 504 HasslassglkkdsKLKSLEIAVEQKKE--ECSKLENQLKKAHNAEEAVRTNPeindrIRLLEQEVARYKEESGKAQAEV 581
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1559 -------KDGEGLEWSTKDDLANGELPDNEKMKTQIK-----QMMDASRVKTMLSLVEEDRNSLQSKLSDevAARHELEE 1626
Cdd:pfam10174 582 erllgilREVENEKNDKDKKIAELESLTLRQMKEQNKkvaniKHGQQEMKKKGAQLLEEARRREDNLADN--SQQLQLEE 659
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024390606 1627 QIKKLEHDSSSLQSAKARLENECKTLQQKVEILGELYQQKEMALqkkltqEEYERQEKEQKLSAADEK 1694
Cdd:pfam10174 660 LMGALEKTRQELDATKARLSSTQQSLAEKDGHLTNLRAERRKQL------EEILEMKQEALLAAISEK 721
|
|
| MISS |
pfam15822 |
MAPK-interacting and spindle-stabilising protein-like; MISS is a family of eukaryotic ... |
1780-1981 |
7.86e-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: 43.44 E-value: 7.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1780 PTPGRPDRQVP----------PRRVPLSRDGSFGPSPVSGGnPSPTQMMevPSRPLSAPQregsraefgtvvDGPPAPRR 1849
Cdd:pfam15822 21 PKPGQPPQGWPgsnpwnnpsaPPAVPSGLPPSTAPSTVPFG-PAPTGMY--PSIPLTGPS------------PGPPAPFP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1850 PPELpgrmSVPDLGPAVASLISSGPRTSSPATAkdraPSPKEPEAPRVTTDSPSSIEPATVnvGPKGP-PSFPGTPVMTS 1928
Cdd:pfam15822 86 PSGP----SCPPPGGPYPAPTVPGPGPIGPYPT----PNMPFPELPRPYGAPTDPAAAAPS--GPWGSmSSGPWAPGMGG 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2024390606 1929 PVLGPPPPPPVN---YGPPPAPFPGHYGPGPRPLPVPLVCG--APLPPPAARDFLPGP 1981
Cdd:pfam15822 156 QYPAPNMPYPSPgpyPAVPPPQSPGAAPPVPWGTVPPGPWGppAPYPDPTGSYPMPGL 213
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
1348-1506 |
8.67e-04 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 43.85 E-value: 8.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1348 EKQLAEKIQNLLQEKTEmLDKFSEcdeKIKQAKESMkvaQEQKSILSDEIAGLKDTVKELEETNHQLDDKIKSlrtMLDT 1427
Cdd:smart00787 146 KEGLDENLEGLKEDYKL-LMKELE---LLNSIKPKL---RDRKDALEEELRQLKQLEDELEDCDPTELDRAKE---KLKK 215
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024390606 1428 ERKQNAKKQKKLSETQKSLEKFEEAFSMHSAELSEVQIALNEsklsEEKVKAELQHVQEENARLKKSKEQLLKEAEGWS 1506
Cdd:smart00787 216 LLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAE----AEKKLEQCRGFTFKEIEKLKEQLKLLQSLTGWK 290
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1469-1774 |
9.47e-04 |
|
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: 44.58 E-value: 9.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1469 ESKLSEEKVKAELQHVQEENARLKKSKEQLLKEAEGWSERHTELTEQIKLYRKSQkdiEEALAYKENEIEVLTNCIMQLK 1548
Cdd:pfam02463 633 ELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAES---ELAKEEILRRQLEIKKKEQREK 709
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1549 QLDTDSASEAKDGEGLEWSTKDDLANGELPDNEKMKTQIKQMMDASRVKTMLSLVEEDRNSLQSKLSDEVAARHELEEQI 1628
Cdd:pfam02463 710 EELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVE 789
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1629 KKLEHDssslqsaKARLENECKTLQQKVEILGELYQQKEMALQKKLTQEEYERQEKEQKLSAADEKAVLAIEEVKVYKQR 1708
Cdd:pfam02463 790 EEKEEK-------LKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEE 862
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024390606 1709 IQDMEEELQKTERSYKNQIAAHEKKAHdnwliarsaeraLAEEKreaanlrqklmEVNQKTIMLQR 1774
Cdd:pfam02463 863 ITKEELLQELLLKEEELEEQKLKDELE------------SKEEK-----------EKEEKKELEEE 905
|
|
| OmpH |
pfam03938 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
1639-1727 |
1.02e-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: 41.41 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1639 QSAKARLENECKTLQQKVEILGELYQQKEMALQKKLTQEEYERQEKEQKLSAADEKavlaieevkvYKQRIQDMEEELQK 1718
Cdd:pfam03938 18 KAAQAQLEKKFKKRQAELEAKQKELQKLYEELQKDGALLEEEREEKEQELQKKEQE----------LQQLQQKAQQELQK 87
|
....*....
gi 2024390606 1719 TERSYKNQI 1727
Cdd:pfam03938 88 KQQELLQPI 96
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1377-1768 |
1.16e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.99 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1377 KQAKESMKVAQEQKSILSDEIAGLKDTVKELEETNHQLDDKIKSLRTmLDTERKQNAKKQKKLSETQKSLEKFEEAFSMH 1456
Cdd:COG4717 53 KEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEE-LEEELEELEAELEELREELEKLEKLLQLLPLY 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1457 SAElsevqialnesklseEKVKAELQHVQEenaRLkkskEQLLKEAEGWSERHTELTEQIKLYRKSQKDIEEALAYKENE 1536
Cdd:COG4717 132 QEL---------------EALEAELAELPE---RL----EELEERLEELRELEEELEELEAELAELQEELEELLEQLSLA 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1537 --------IEVLTNCIMQLKQLDTDSASEAKDGEGLEwSTKDDLANGELPDNEKMKTQIKQMM----------------- 1591
Cdd:COG4717 190 teeelqdlAEELEELQQRLAELEEELEEAQEELEELE-EELEQLENELEAAALEERLKEARLLlliaaallallglggsl 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1592 --DASRVKTMLSLV------------------EEDRNSLQSKLSDEVAARHELEEQIKKLEHDSSslqSAKARLENECKT 1651
Cdd:COG4717 269 lsLILTIAGVLFLVlgllallflllarekaslGKEAEELQALPALEELEEEELEELLAALGLPPD---LSPEELLELLDR 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1652 LQQKVEILGELyqqkeMALQKKLTQEEYErQEKEQKLSAAD-------EKAVLAIEEVKVYKQRIQDMEEELQKTERSYK 1724
Cdd:COG4717 346 IEELQELLREA-----EELEEELQLEELE-QEIAALLAEAGvedeeelRAALEQAEEYQELKEELEELEEQLEELLGELE 419
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 2024390606 1725 NQIAAHEKKAHDNWLiaRSAERALAEEKREAANLRQKLMEVNQK 1768
Cdd:COG4717 420 ELLEALDEEELEEEL--EELEEELEELEEELEELREELAELEAE 461
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1774-1976 |
1.19e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 44.16 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1774 RPLIVKPTPGRPDRQVPPRRVPlsrDGSFGPSpVSGGNPS-PTQMMEVPSRPLSAPQREGSRAEFGTVVDGPPAPRR--P 1850
Cdd:PHA03247 273 RGATGPPPPPEAAAPNGAAAPP---DGVWGAA-LAGAPLAlPAPPDPPPPAPAGDAEEEDDEDGAMEVVSPLPRPRQhyP 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1851 PELPGRMSVPDLGPAVASLISSG---PRTSSPATAKDR-APSPKEP--------EAPRVTTDSPSSIEPATVNVGPKGPP 1918
Cdd:PHA03247 349 LGFPKRRRPTWTPPSSLEDLSAGrhhPKRASLPTRKRRsARHAATPfargpggdDQTRPAAPVPASVPTPAPTPVPASAP 428
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2024390606 1919 SFPGTPVMTSPVlgppppppvnygpppapfPGHYGPGPRPLPVPLVCGAPLPPPAARD 1976
Cdd:PHA03247 429 PPPATPLPSAEP------------------GSDDGPAPPPERQPPAPATEPAPDDPDD 468
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1391-1648 |
1.22e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 43.85 E-value: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1391 SILSDEIAGLKDTVKELEETNHQLDDKIKSLRTMLDTERK----QNAKKQKKLSETQKSLEKFEEAFSMHSAELSEVQIA 1466
Cdd:PHA02562 163 SVLSEMDKLNKDKIRELNQQIQTLDMKIDHIQQQIKTYNKnieeQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDE 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1467 LNESKLSEEKVKAELQHVQEENARLKKSKEQLLKEAEGWSERHT--ELTEQIklyrKSQKDIEEALAYKeneievLTNCI 1544
Cdd:PHA02562 243 LLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKMYEKGGVcpTCTQQI----SEGPDRITKIKDK------LKELQ 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1545 MQLKQLDT--DSASEAKDgeglewstkddlangELPDNEKMKTQIKQmmDASRVKTMLSLVEEDRNSLQSKLSDEVAARH 1622
Cdd:PHA02562 313 HSLEKLDTaiDELEEIMD---------------EFNEQSKKLLELKN--KISTNKQSLITLVDKAKKVKAAIEELQAEFV 375
|
250 260
....*....|....*....|....*.
gi 2024390606 1623 ELEEQIKKLEHDSSSLQSAKARLENE 1648
Cdd:PHA02562 376 DNAEELAKLQDELDKIVKTKSELVKE 401
|
|
| Rab5-bind |
pfam09311 |
Rabaptin-like protein; Members of this family are predominantly found in Rabaptin and allow ... |
1398-1658 |
1.29e-03 |
|
Rabaptin-like protein; Members of this family are predominantly found in Rabaptin and allow for binding to the GTPase Rab5. This interaction is necessary and sufficient for Rab5-dependent recruitment of Rabaptin5 to early endosomal membranes.
Pssm-ID: 462752 [Multi-domain] Cd Length: 307 Bit Score: 43.03 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1398 AGLKDTVKELEETNHQLDDKIKslRTMldTERKQNAKKQKKLS-ETQKSLEKFEEAFSMHSAELSEVQIALNESKLSEEK 1476
Cdd:pfam09311 19 AETRDQVKKLQEMLRQANDQLE--KTM--KDKKELEDKMNQLSeETSNQVSTLAKRNQKSETLLDELQQAFSQAKRNFQD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1477 ----VKAELQHVQEENARLKKSKEQLLkeaeGWSERHTEL--TEQIKLYRKSQKDIEEALAYKENEIEVLTNCIMQLKQL 1550
Cdd:pfam09311 95 qlavLMDSREQVSDELVRLQKDNESLQ----GKHSLHVSLqqAEKFDMPDTVQELQELVLKYREELIEVRTAADHMEEKL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1551 DtDSASEAKDGEGLEWSTKDDLANGELPDNEKMKTQIKQMmdaSRVKTMLSLVEEDRNSLQSKLSDEVAA-------RHE 1623
Cdd:pfam09311 171 K-AEILFLKEQIQAEQCLKENLEETLQAEIENCKEEIASI---SSLKVELERIKAEKEQLENGLTEKIRQledlqttKGS 246
|
250 260 270
....*....|....*....|....*....|....*
gi 2024390606 1624 LEEQIKKLEHDSSSLQSAKARLENECKTLQQKVEI 1658
Cdd:pfam09311 247 LETQLKKETNEKAAVEQLVFEEKNKAQRLQTELDV 281
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1381-1778 |
1.33e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 44.17 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1381 ESMKVAQEQKsilsDEIAGL---------KDTVKELEETNHQLDDKIkSLRTMLDTERKQNAKKQKKLSETQKSLEKFEE 1451
Cdd:COG3096 246 EAIRVTQSDR----DLFKHLiteatnyvaADYMRHANERRELSERAL-ELRRELFGARRQLAEEQYRLVEMARELEELSA 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1452 AFSMHSAE-------LSEVQIALNEsklsEEKVKAELQHVQEENARLKKSKEQlLKEAEgwsERHTELTEQIKLYRKSQK 1524
Cdd:COG3096 321 RESDLEQDyqaasdhLNLVQTALRQ----QEKIERYQEDLEELTERLEEQEEV-VEEAA---EQLAEAEARLEAAEEEVD 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1525 DIEEALAYKENEIEVLTNCIMQLKQldtdsASEAKdGEGLEWSTKDDLAngelPDNekmktqIKQMMDASRVKtmLSLVE 1604
Cdd:COG3096 393 SLKSQLADYQQALDVQQTRAIQYQQ-----AVQAL-EKARALCGLPDLT----PEN------AEDYLAAFRAK--EQQAT 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1605 EDRNSLQSKLSDEVAARHELEEQIKKLE------HDSSSLQSAKARLEN--ECKTLQQKVEILGELYQQKEMALQKkltQ 1676
Cdd:COG3096 455 EEVLELEQKLSVADAARRQFEKAYELVCkiagevERSQAWQTARELLRRyrSQQALAQRLQQLRAQLAELEQRLRQ---Q 531
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1677 EEYERQEKE------QKLSAADEKAVLA------IEEVKVYKQRIQDMEEELQKTERSYKNQIAAHEKKAhDNWLIARSA 1744
Cdd:COG3096 532 QNAERLLEEfcqrigQQLDAAEELEELLaeleaqLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARA-PAWLAAQDA 610
|
410 420 430
....*....|....*....|....*....|....
gi 2024390606 1745 ERALAEEKREAANLRQKLMEVNQKTIMLQRPLIV 1778
Cdd:COG3096 611 LERLREQSGEALADSQEVTAAMQQLLEREREATV 644
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1347-1672 |
1.42e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.60 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1347 TEKQLAEKIQNLLQEKTEMLDKFSECDEKIKQAKEsmkvAQEQKSILSDEIAGLKDTVKELEETNHQLD---DKIKSLRT 1423
Cdd:COG4717 102 EELEELEAELEELREELEKLEKLLQLLPLYQELEA----LEAELAELPERLEELEERLEELRELEEELEeleAELAELQE 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1424 MLDTERKQ-NAKKQKKLSETQKSLEKFEEAFSMHSAELSEVQIALNESKLSEEKVKAELQHVQEEN-------------- 1488
Cdd:COG4717 178 ELEELLEQlSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEErlkearlllliaaa 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1489 ---------------------------------ARLKKSKEQLLKEAEgwseRHTELTEQIKLYRKSQKDIEEALAYKEN 1535
Cdd:COG4717 258 llallglggsllsliltiagvlflvlgllallfLLLAREKASLGKEAE----ELQALPALEELEEEELEELLAALGLPPD 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1536 -EIEVLTNCIMQLKQLDTDSASEAKDGEGLEW----------------STKDDLANG-----ELPDNEKMKTQIKQMMDA 1593
Cdd:COG4717 334 lSPEELLELLDRIEELQELLREAEELEEELQLeeleqeiaallaeagvEDEEELRAAleqaeEYQELKEELEELEEQLEE 413
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024390606 1594 SRVKTMLSLVEEDRNSLQSKLSDEVAARHELEEQIKKLEHDSSSLQSAKARLENEcktlqqkvEILGELYQQKEMALQK 1672
Cdd:COG4717 414 LLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEED--------GELAELLQELEELKAE 484
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1412-1538 |
1.50e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.22 E-value: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1412 HQLDDKIKSLRTMLDTERKQNAKKQKKLSETQKSLEKFEEAFSMHSAELSEVQIALNESKLSEEKVKA---------ELQ 1482
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEqlgnvrnnkEYE 92
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 2024390606 1483 HVQEENARLKKSKEQLLKEAEGWSERHTELTEQIKLYRKSQKDIEEALAYKENEIE 1538
Cdd:COG1579 93 ALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELD 148
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1349-1508 |
1.70e-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: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1349 KQLAEKIQNLLQEKTEMLDKFSECDEKIKQAKESMKVAQEQKSILSDEIAGLKDTVKELEETNHQLDDKIKSLRTMLD-- 1426
Cdd:pfam07888 76 RELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELErm 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1427 TERKQNAKKQKKLSETQKS-----LEKFEEAFSMHSAELSEVQIALNESKLSEEKVK---AELQHVQEENARLKKSKEQL 1498
Cdd:pfam07888 156 KERAKKAGAQRKEEEAERKqlqakLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQdtiTTLTQKLTTAHRKEAENEAL 235
|
170
....*....|
gi 2024390606 1499 LKEAEGWSER 1508
Cdd:pfam07888 236 LEELRSLQER 245
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1338-1776 |
2.03e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 43.36 E-value: 2.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1338 SVKSRMYQVTEKQLAEKIQNLLQ---EKT-EMLDKFSECDEKIKQAKESMKVAQEQKSILSDEIAGLKDT-VKELEETNH 1412
Cdd:PRK11281 40 DVQAQLDALNKQKLLEAEDKLVQqdlEQTlALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDnDEETRETLS 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1413 QLDdkIKSLRTMLDTERKQNAKKQKKLSET-------QKSLEKFEEAFSMHSAELSEVQIALNESKLSEEKVKAELQH-V 1484
Cdd:PRK11281 120 TLS--LRQLESRLAQTLDQLQNAQNDLAEYnsqlvslQTQPERAQAALYANSQRLQQIRNLLKGGKVGGKALRPSQRVlL 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1485 QEENARLKKSKEQLLKEAEG-------WSERHTELTEQIKLYRKSQKDIEEALAYKeneievltncimQLKQLDtDSASE 1557
Cdd:PRK11281 198 QAEQALLNAQNDLQRKSLEGntqlqdlLQKQRDYLTARIQRLEHQLQLLQEAINSK------------RLTLSE-KTVQE 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1558 AKDGEGLEWSTKDDLANGELPDNEKM-KTQIKQ-------MMDASRVKTML-SLVEEDRNslqsklsdevaarheLEEQI 1628
Cdd:PRK11281 265 AQSQDEAARIQANPLVAQELEINLQLsQRLLKAteklntlTQQNLRVKNWLdRLTQSERN---------------IKEQI 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1629 KKLEhdsSSLqsakarlenecktLQQKVeilgeLYQQKEMALQKKLTQEeyerqekeqklsAADEKAVLAIEEVKVYKQR 1708
Cdd:PRK11281 330 SVLK---GSL-------------LLSRI-----LYQQQQALPSADLIEG------------LADRIADLRLEQFEINQQR 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1709 --IQDMEEELQKTERSYKNQIAAHEKKAHDNWLIARSA-----ERALAEEKREAANLrqklmEVNQKTIM-----LQRPL 1776
Cdd:PRK11281 377 daLFQPDAYIDKLEAGHKSEVTDEVRDALLQLLDERRElldqlNKQLNNQLNLAINL-----QLNQQQLLsvsdsLQSTL 451
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
1774-1938 |
2.31e-03 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 43.24 E-value: 2.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1774 RPLIVKPTPGRPDRQVPPRRVPLSRDGSFGPSPvSGGNPSPtqmmEVPSRPLSAPQREGSRAEFGTVVDGPPAPRRPPEL 1853
Cdd:PHA03307 261 APITLPTRIWEASGWNGPSSRPGPASSSSSPRE-RSPSPSP----SSPGSGPAPSSPRASSSSSSSRESSSSSTSSSSES 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1854 PGRMSVPdLGPAVASLISSGpRTSSPATAKDRAPSPKEPEAPRVTTDSPSSIEPATV-------NVGPKGPPSFPGT--- 1923
Cdd:PHA03307 336 SRGAAVS-PGPSPSRSPSPS-RPPPPADPSSPRKRPRPSRAPSSPAASAGRPTRRRAraavagrARRRDATGRFPAGrpr 413
|
170
....*....|....*
gi 2024390606 1924 PVMTSPVLGPPPPPP 1938
Cdd:PHA03307 414 PSPLDAGAASGAFYA 428
|
|
| SepH |
NF040712 |
septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces ... |
1780-1921 |
2.33e-03 |
|
septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces venezuelae, and homologs were identified in Mycobacterium smegmatis. SepH contains a N-terminal DUF3071 domain and a conserved C-terminal region. It binds directly to cell division protein FtsZ to stimulate the assembly of FtsZ protofilaments.
Pssm-ID: 468676 [Multi-domain] Cd Length: 346 Bit Score: 42.45 E-value: 2.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1780 PTPGRPDRQVP--PRRVPLSRD-GSFGPSPVSGGNPSPTQMMEVPSRPLSA--PQREGSRAEFGTVVDGPPAPRRPPELP 1854
Cdd:NF040712 190 PDFGRPLRPLAtvPRLAREPADaRPEEVEPAPAAEGAPATDSDPAEAGTPDdlASARRRRAGVEQPEDEPVGPGAAPAAE 269
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024390606 1855 GRMSVPDLGPAVASLISSGPrtSSPATAKDRAPSPKEPEAPRVTTDSPSSIEPATVNVGPKGPPSFP 1921
Cdd:NF040712 270 PDEATRDAGEPPAPGAAETP--EAAEPPAPAPAAPAAPAAPEAEEPARPEPPPAPKPKRRRRRASVP 334
|
|
| Tektin |
pfam03148 |
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular ... |
1403-1725 |
2.57e-03 |
|
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular sites as centrioles, basal bodies, and along ciliary and flagellar doublet microtubules. Tektins form unique protofilaments, organized as longitudinal polymers of tektin heterodimers with axial periodicity matching tubulin. Tektin polypeptides consist of several alpha-helical regions that are predicted to form coiled coils. Indeed, tektins share considerable structural similarities with intermediate filament proteins. Possible functional roles for tektins are: stabilization of tubulin protofilaments; attachment of A and B-tubules in ciliary/flagellar microtubule doublets and C-tubules in centrioles; binding of axonemal components.
Pssm-ID: 460827 [Multi-domain] Cd Length: 383 Bit Score: 42.54 E-value: 2.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1403 TVKELEETNHQLDDKIKSL---RTMLDTERKQNAKKQKKLSETQKSLEKFEEAFsmhsaelsEVQIALNESKLS--EEKV 1477
Cdd:pfam03148 37 TKWDQYDSNRRLGERIQDItfwKSELEKELEELDEEIELLLEEKRRLEKALEAL--------EEPLHIAQECLTlrEKRQ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1478 KAELQH--VQEEnarLKKSKEqLLKEAEGWSERHTE-LTEQIKLYRKSQKDIEEALAYKENEIEVLTNCImqlkQLDTDS 1554
Cdd:pfam03148 109 GIDLVHdeVEKE---LLKEVE-LIEGIQELLQRTLEqAWEQLRLLRAARHKLEKDLSDKKEALEIDEKCL----SLNNTS 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1555 AS----------EAKDGEGLEWS--TKDDLANGElpdNEKMKT-QIKQMMDASRVKT------MLSLVEEdrnSLQSKLS 1615
Cdd:pfam03148 181 PNisykpgptriPPNSSTPEEWEkfTQDNIERAE---KERAASaQLRELIDSILEQTandlraQADAVNF---ALRKRIE 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1616 DEVAARHELEEQIKKLEHDssslqsaKARLENECKTLQQKVeilgelyQQKEMALqkKLTQEEYE-----------RQEK 1684
Cdd:pfam03148 255 ETEDAKNKLEWQLKKTLQE-------IAELEKNIEALEKAI-------RDKEAPL--KLAQTRLEnrtyrpnvelcRDEA 318
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 2024390606 1685 EQKLsaadekavlaIEEVKVYKQRIQDMEEELQKTERSYKN 1725
Cdd:pfam03148 319 QYGL----------VDEVKELEETIEALKQKLAEAEASLQA 349
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1348-1722 |
2.74e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 43.04 E-value: 2.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1348 EKQLAEKIQNLLQEKTEMLDKFSECDEKIKQAKESMKVAQEQKSILSDE------IAGLKDTVKELEETNHQLDDKIKSL 1421
Cdd:pfam02463 249 EQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEElksellKLERRKVDDEEKLKESEKEKKKAEK 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1422 RTMLDTERKQNAKKQKKLSETQKSLEKFEEAFSMHSAELSEVQIALNESKLSEEKVKAELQHVQEENARLKKSKEQLLKE 1501
Cdd:pfam02463 329 ELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQ 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1502 AEgwsERHTELTEQIKLYRKSQKDIEEALAYKENEIEVLTNCIMQLKQLDTDSASEAKDGEGLEwsTKDDLANGELPDNE 1581
Cdd:pfam02463 409 LL---LELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKK--SEDLLKETQLVKLQ 483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1582 KMKTQIKQMMDASRVKTMLSLVEEDRNSLQSKLSDEVAARHELEEQIKKLEHDSSSLQSAKARLENECKTLQQKVEILGE 1661
Cdd:pfam02463 484 EQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEER 563
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024390606 1662 LYQQKEMALQKKLTQEEYERQEKEQKLSAADEKAVLAIEEVKVYKQRIQDMEEELQKTERS 1722
Cdd:pfam02463 564 QKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKV 624
|
|
| PHA03379 |
PHA03379 |
EBNA-3A; Provisional |
1785-1984 |
2.96e-03 |
|
EBNA-3A; Provisional
Pssm-ID: 223066 [Multi-domain] Cd Length: 935 Bit Score: 42.74 E-value: 2.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1785 PDRQVPPRRVPLSRDGSFGPSPVSGGNPSPTqmmEVPS------RPLSAPQREGSRAEFGTVVDgPPAPRRPPELPGRMS 1858
Cdd:PHA03379 466 PVAQLPPGPLQDLEPGDQLPGVVQDGRPACA---PVPApagpivRPWEASLSQVPGVAFAPVMP-QPMPVEPVPVPTVAL 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1859 VPDLGPAVASLISSGP-RTSSPATAKDR------APSPKEPEAPRVTTDSPSSIEP------ATVNVGP----KGPPSFP 1921
Cdd:PHA03379 542 ERPVCPAPPLIAMQGPgETSGIVRVRERwrpapwTPNPPRSPSQMSVRDRLARLRAeaqpyqASVEVQPpqltQVSPQQP 621
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024390606 1922 -GTPVMTSPVLGPPPPPPVNYGPPPAPFPGHYGPGPRPLPV--PLVCGAPLPPPAArDFLPGPSLG 1984
Cdd:PHA03379 622 mEYPLEPEQQMFPGSPFSQVADVMRAGGVPAMQPQYFDLPLqqPISQGAPLAPLRA-SMGPVPPVP 686
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1407-1718 |
3.03e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 42.80 E-value: 3.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1407 LEETNHQLDDKIKSLRTMLDTERKQNAKKQKKLSETQKSLEKfeeafsMHSAELSEVQIALNESKlSEEKVKAELQHVQE 1486
Cdd:pfam15921 80 LEEYSHQVKDLQRRLNESNELHEKQKFYLRQSVIDLQTKLQE------MQMERDAMADIRRRESQ-SQEDLRNQLQNTVH 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1487 ENARLKKSKEQLLKEAEGWSE--RHTELTEQIKLY--RKSQKDIEEALAYKENEIEVLTNCIMQ---------LKQLDTd 1553
Cdd:pfam15921 153 ELEAAKCLKEDMLEDSNTQIEqlRKMMLSHEGVLQeiRSILVDFEEASGKKIYEHDSMSTMHFRslgsaiskiLRELDT- 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1554 sasEAKDGEGLEWSTKDDLANGELPDNEKMKTQIKQMMDasRVKTMLSLVEEDRNSLQSKLSDEVAARHELEEQIKKLEH 1633
Cdd:pfam15921 232 ---EISYLKGRIFPVEDQLEALKSESQNKIELLLQQHQD--RIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQE 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1634 DSSSLQSAKARlenECKTLQQKVEILgelyqQKEMALQKKLTQEEYErqEKEQKLSAADEKAVLAIEEVKVYKQRIQDME 1713
Cdd:pfam15921 307 QARNQNSMYMR---QLSDLESTVSQL-----RSELREAKRMYEDKIE--ELEKQLVLANSELTEARTERDQFSQESGNLD 376
|
....*
gi 2024390606 1714 EELQK 1718
Cdd:pfam15921 377 DQLQK 381
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
600-843 |
3.08e-03 |
|
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273344 [Multi-domain] Cd Length: 1096 Bit Score: 42.68 E-value: 3.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 600 AETEKEEEKFGGDTLKESSENNFKHRKLWEkMKEKGKAKYEPSGDVLAKPVE---DVQNTSQSDTGDTDLLKDKLEQEMP 676
Cdd:TIGR00927 655 AEGENGEESGGEAEQEGETETKGENESEGE-IPAERKGEQEGEGEIEAKEADhkgETEAEEVEHEGETEAEGTEDEGEIE 733
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 677 VVEKEILRQEEDLKQTrEADHENQRPiSVKKEPEIERGSMKETSADErDPSRRGAAEQPRPWENETEYSEADVKEELSRN 756
Cdd:TIGR00927 734 TGEEGEEVEDEGEGEA-EGKHEVETE-GDRKETEHEGETEAEGKEDE-DEGEIQAGEDGEMKGDEGAEGKVEHEGETEAG 810
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 757 LGKMTIFEERIEKSSPEEKSKSAAQNTNAENstqQGTAHTDNEDSDRNLGTSSARETtlrlELQSEEPDAEEDPDLKQEE 836
Cdd:TIGR00927 811 EKDEHEGQSETQADDTEVKDETGEQELNAEN---QGEAKQDEKGVDGGGGSDGGDSE----EEEEEEEEEEEEEEEEEEE 883
|
....*..
gi 2024390606 837 ELLEDEN 843
Cdd:TIGR00927 884 EEEEEEN 890
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1350-1688 |
3.51e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 42.63 E-value: 3.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1350 QLAEKIQNLLQEktemldkFSECDEKIKQAKESMKVAQEQKSilsdeiaglkdtvkELEETNHQLDDKIKSLRTML---- 1425
Cdd:COG3096 344 RQQEKIERYQED-------LEELTERLEEQEEVVEEAAEQLA--------------EAEARLEAAEEEVDSLKSQLadyq 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1426 ---DT------------ERKQNAKKQKKLSE-TQKSLEKFEEAFSMHSAELSEVQIALnESKLSEekvkAELQHVQEENA 1489
Cdd:COG3096 403 qalDVqqtraiqyqqavQALEKARALCGLPDlTPENAEDYLAAFRAKEQQATEEVLEL-EQKLSV----ADAARRQFEKA 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1490 RlkkskeQLLKEAEGWSER---HTELTEQIKLYRkSQKdieeALAYKENEIEvltnciMQLKQLDTDSASEAKDGEGLEw 1566
Cdd:COG3096 478 Y------ELVCKIAGEVERsqaWQTARELLRRYR-SQQ----ALAQRLQQLR------AQLAELEQRLRQQQNAERLLE- 539
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1567 stkddlangelpdnEKMKTQIKQMMDASRVKTMLSLVEEDRNSLQSKLSDEVAARHELEEQIKKLEHDSSSLQS------ 1640
Cdd:COG3096 540 --------------EFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAArapawl 605
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 2024390606 1641 -AKARLENECKTLQQKVEILGELYQQKEMALQK--KLTQEEYERQEKEQKL 1688
Cdd:COG3096 606 aAQDALERLREQSGEALADSQEVTAAMQQLLERerEATVERDELAARKQAL 656
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
1623-1765 |
3.53e-03 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 41.96 E-value: 3.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1623 ELEEQIKKLEhdsSSLQSAKARLENECKTLQQKVEILGELYQQKEMALQKKLTQEEYERQEKEQKLSAADEKAVLAIE-E 1701
Cdd:COG1566 80 DLQAALAQAE---AQLAAAEAQLARLEAELGAEAEIAAAEAQLAAAQAQLDLAQRELERYQALYKKGAVSQQELDEARaA 156
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024390606 1702 VKVYKQRIQDMEEELQKTersyKNQIAAHEKKAhdnwliARSAERALAEEKREAANLRQKLMEV 1765
Cdd:COG1566 157 LDAAQAQLEAAQAQLAQA----QAGLREEEELA------AAQAQVAQAEAALAQAELNLARTTI 210
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1468-1730 |
3.62e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.59 E-value: 3.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1468 NESKLseEKVKAELQHVQEENARLKKSKEQLLKEAEGWSERHTELtEQIKLYRKSQKDIEEAlaykENEIEVLTNcimQL 1547
Cdd:COG4913 608 NRAKL--AALEAELAELEEELAEAEERLEALEAELDALQERREAL-QRLAEYSWDEIDVASA----EREIAELEA---EL 677
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1548 KQLDTDSaseakdgeglewstkDDLAngelpdnekmktqikqmmdasrvktmlslveedrnSLQSKLSDEVAARHELEEQ 1627
Cdd:COG4913 678 ERLDASS---------------DDLA-----------------------------------ALEEQLEELEAELEELEEE 707
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1628 IKKLEHDSSSLQSAKARLENECKTLQQKVEILGELyqqkemalqkkltQEEYERQEKEQKLSAADEKAVLAiEEVKVYKQ 1707
Cdd:COG4913 708 LDELKGEIGRLEKELEQAEEELDELQDRLEAAEDL-------------ARLELRALLEERFAAALGDAVER-ELRENLEE 773
|
250 260
....*....|....*....|...
gi 2024390606 1708 RIQDMEEELQKTERSYKNQIAAH 1730
Cdd:COG4913 774 RIDALRARLNRAEEELERAMRAF 796
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1342-1677 |
3.71e-03 |
|
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: 42.73 E-value: 3.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1342 RMYQVTEKQLAEKIQNLLQEKTEMLDKFSECDEKIKQAKESMKVAQEQKSILSDEIAGLKDTVKELEETNHQLDDKIKSL 1421
Cdd:TIGR00606 294 KVFQGTDEQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSL 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1422 RTMLDT---ERKQNAKKQKKLSETQKsLEKFEEAFSMHSAELSEVQ--IALNESKLSE--EKVKAELQHVQEENARLKKS 1494
Cdd:TIGR00606 374 ATRLELdgfERGPFSERQIKNFHTLV-IERQEDEAKTAAQLCADLQskERLKQEQADEirDEKKGLGRTIELKKEILEKK 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1495 KEQL------LKEAEGWSERHTELTEQIklyRKSQKDIeeALAYKENEIEVLTNCIMQLK--QLDTDSASEAKDGEglew 1566
Cdd:TIGR00606 453 QEELkfvikeLQQLEGSSDRILELDQEL---RKAEREL--SKAEKNSLTETLKKEVKSLQneKADLDRKLRKLDQE---- 523
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1567 stkddlaNGELpdnEKMKTQIKQMMDASRVKTMlslVEEDRNSLQSKLSDEVAARHELEEQIKKLEHDSSSLQSAKARLE 1646
Cdd:TIGR00606 524 -------MEQL---NHHTTTRTQMEMLTKDKMD---KDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTR 590
|
330 340 350
....*....|....*....|....*....|.
gi 2024390606 1647 NECKTLQQKVEILGELYQQKEMALQKKLTQE 1677
Cdd:TIGR00606 591 DRLAKLNKELASLEQNKNHINNELESKEEQL 621
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1347-1758 |
3.71e-03 |
|
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: 42.73 E-value: 3.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1347 TEKQLAEKIQNLLQEKTEMLDKFSECDEKIKQAKESMKVAQEQKSILSDEIAGLKDTvKELEETNHQLDDKIKSLRTMLD 1426
Cdd:TIGR00606 516 KLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYFPNK-KQLEDWLHSKSKEINQTRDRLA 594
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1427 TERKQNAKKQKKLSETQKSLEKFEEAFSMHSAELSEVqialneskLSEEKVKAELQHVQEENARLKKSKEQLLKEAEGWS 1506
Cdd:TIGR00606 595 KLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDV--------CGSQDEESDLERLKEEIEKSSKQRAMLAGATAVYS 666
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1507 ERHTELTEQ-------IKLYRKSQKDIEEALAYKENEIEVLTNCIMQLKQLDTDSASEAKDGEGLEWSTKD--DLANGEL 1577
Cdd:TIGR00606 667 QFITQLTDEnqsccpvCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSiiDLKEKEI 746
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1578 PD----NEKMKTQIKQMM-DASRVKTMLSLVEEDRNSLQSKLSDEVAARH---ELEEQIKKLEHDSSSLQSAKARL---- 1645
Cdd:TIGR00606 747 PElrnkLQKVNRDIQRLKnDIEEQETLLGTIMPEEESAKVCLTDVTIMERfqmELKDVERKIAQQAAKLQGSDLDRtvqq 826
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1646 --------ENECKTLQQKVEILGELYQQKE---MALQKKLTQEEYER---QEKEQKLSAADEKAVLAIEEVKVYKQRIQD 1711
Cdd:TIGR00606 827 vnqekqekQHELDTVVSKIELNRKLIQDQQeqiQHLKSKTNELKSEKlqiGTNLQRRQQFEEQLVELSTEVQSLIREIKD 906
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 2024390606 1712 MEEELQKTERSYKNQIAAHEKKAHDNWLIARSAERALAEEKREAANL 1758
Cdd:TIGR00606 907 AKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNI 953
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1620-1773 |
4.21e-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: 42.35 E-value: 4.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1620 ARHELEEQIKKLEhdsssLQSAKA----RLENECKTLQqkVEILGELYQQKE---MALQKKLTQEEYERQEKEQKLSAAD 1692
Cdd:TIGR02168 194 ILNELERQLKSLE-----RQAEKAerykELKAELRELE--LALLVLRLEELReelEELQEELKEAEEELEELTAELQELE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1693 EKavlaIEEVKVYKQRIQDMEEELQKTERSYKNQIAA--HEKKAHDNWLiaRSAERALAEEKREAANLRQKLMEVNQKTI 1770
Cdd:TIGR02168 267 EK----LEELRLEVSELEEEIEELQKELYALANEISRleQQKQILRERL--ANLERQLEELEAQLEELESKLDELAEELA 340
|
...
gi 2024390606 1771 MLQ 1773
Cdd:TIGR02168 341 ELE 343
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
670-1189 |
4.47e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.44 E-value: 4.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 670 KLEQEMPVVEKEILRQEEDLKQTREADHENQRPISVKKEPEIERGSMKETSADERDPSRRGAAEQPRPWENETEYSEADV 749
Cdd:PTZ00121 1237 KDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKK 1316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 750 KEELSRNLGKMTIFEERIEKSSPEEKSKSAAQNTNAENSTQQGTAHTDNEDSDRnLGTSSARETTLRLELQSEEPDAEED 829
Cdd:PTZ00121 1317 ADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAE-KKKEEAKKKADAAKKKAEEKKKADE 1395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 830 PDLKQEEELLEDENAASAKLLQARLANIQGNAQTTRSTNPDLGVLSEAvsgtvnptyETGEKTNSFSEDTKEISRVQDAH 909
Cdd:PTZ00121 1396 AKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEA---------KKADEAKKKAEEAKKAEEAKKKA 1466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 910 EVGNK--EVDKPVSEDTKLDEIEHVMEDNKESSE-----AEEPSAVEEydFKSPDREDSNDFNQRKGHLPEGLLLGDSEE 982
Cdd:PTZ00121 1467 EEAKKadEAKKKAEEAKKADEAKKKAEEAKKKADeakkaAEAKKKADE--AKKAEEAKKADEAKKAEEAKKADEAKKAEE 1544
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 983 IQNSEDTRNAHQ-HSAHFPSPADMSAATNDtvtDYSESVKRLTITRDfLDEKRVIRLQKYLGLQNVIRIEAM--FQDMKI 1059
Cdd:PTZ00121 1545 KKKADELKKAEElKKAEEKKKAEEAKKAEE---DKNMALRKAEEAKK-AEEARIEEVMKLYEEEKKMKAEEAkkAEEAKI 1620
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1060 EMELARKAsqnnEEIEKALDQILKSSDSSI-----------MDVVGKVLDSRVAENQEEVVKEMDLYDEE-----SALMD 1123
Cdd:PTZ00121 1621 KAEELKKA----EEEKKKVEQLKKKEAEEKkkaeelkkaeeENKIKAAEEAKKAEEDKKKAEEAKKAEEDekkaaEALKK 1696
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024390606 1124 DIQELIYSLRSKYSSASESVPLGSFL-EQEEDQLHVQGAAKEAENDAAPGRNLHGTDESSQKFQQLE 1189
Cdd:PTZ00121 1697 EAEEAKKAEELKKKEAEEKKKAEELKkAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLK 1763
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1447-1763 |
5.52e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 42.03 E-value: 5.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1447 EKFEEAFSMHSAELSEVQIALNESKLSEEKVKAelqHVQEENARLKKSKEQLLKEAEGWSE-RHTELTEQIKLYRKSQKD 1525
Cdd:pfam15921 74 EHIERVLEEYSHQVKDLQRRLNESNELHEKQKF---YLRQSVIDLQTKLQEMQMERDAMADiRRRESQSQEDLRNQLQNT 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1526 IEEALAYKENEIEVLTNCIMQLKQLDTDSASEakdgEGLEWSTKDDLANGELPDNEKMKTQikQMMDASRVKTMLSLVEE 1605
Cdd:pfam15921 151 VHELEAAKCLKEDMLEDSNTQIEQLRKMMLSH----EGVLQEIRSILVDFEEASGKKIYEH--DSMSTMHFRSLGSAISK 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1606 DRNSLQSKLSDEVAARHELEEQIKKLEHDSSS-----LQSAKARLENECKtlQQKVEILGELYQQKEMALQKKLTQEEYE 1680
Cdd:pfam15921 225 ILRELDTEISYLKGRIFPVEDQLEALKSESQNkiellLQQHQDRIEQLIS--EHEVEITGLTEKASSARSQANSIQSQLE 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1681 RQEKEqklsaADEKAVLAIEEVKVYKQRIQDMEEELQKTERSYKNQIAAHEKK---AHDNWLIARSAERALAEEKREAAN 1757
Cdd:pfam15921 303 IIQEQ-----ARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQlvlANSELTEARTERDQFSQESGNLDD 377
|
....*.
gi 2024390606 1758 LRQKLM 1763
Cdd:pfam15921 378 QLQKLL 383
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1349-1448 |
5.55e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 40.68 E-value: 5.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1349 KQLAEKIQNLLQEKTEMLDKFSECDEKIKQAKESMKVAQEQK--SILSDEIAGLKDTVKELEETNHQLDDKIKSLRTMLD 1426
Cdd:COG1579 48 EAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKeyEALQKEIESLKRRISDLEDEILELMERIEELEEELA 127
|
90 100
....*....|....*....|..
gi 2024390606 1427 TERKQNAKKQKKLSETQKSLEK 1448
Cdd:COG1579 128 ELEAELAELEAELEEKKAELDE 149
|
|
| NIP100 |
COG5244 |
Dynactin complex subunit involved in mitotic spindle partitioning in anaphase B [Cell cycle ... |
1331-1768 |
5.63e-03 |
|
Dynactin complex subunit involved in mitotic spindle partitioning in anaphase B [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 227569 [Multi-domain] Cd Length: 669 Bit Score: 41.59 E-value: 5.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1331 IFWRTCLSVKSRMYQVTEKqlaekIQNLLqektEMLDKFSECDEKIKQAKESMKVAQEQKSI--LSDEIAGLKDTVKE-- 1406
Cdd:COG5244 62 IFIRPDDDSLLNGNAAYEK-----IKGGL----VCESKGMDKDGEIKQENHEDRIHFEESKIrrLEETIEALKSTEKEei 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1407 --LEETNHQLDDKIKSLRTMLDTERKQNAKKQKKLSETQ-KSLEKFEEAFSMHSAEL-SEVQIALN------ESKLSEEK 1476
Cdd:COG5244 133 veLRRENEELDKINLSLRERISSEEPELNKDGSKLSYDElKEFVEESRVQVYDMVELvSDISETLNrngsiqRSSVRECE 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1477 VKAELQHVQEENARLKKSKEQLLKEAEGWSERHTEL--TEQIKLYRKS--QKDIEEALAYkENEIEVLTNCIMQLKQLDT 1552
Cdd:COG5244 213 RSNIHDVLFLVNGILDGVIDELNGELERLRRQLVSLmsSHGIEVEENSrlKATLEKFQSL-ELKVNTLQEELYQNKLLKK 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1553 -----DSASEAKDGEGLEWSTK-------DDLANGELPDNEKMKTQIKQMMDASRVKTMLSLVEEDRNS----------L 1610
Cdd:COG5244 292 fyqiyEPFAQAALSSQLQYLAEviesenfGKLENIEIHIILKVLSSISYALHIYTIKNTPDHLETTLQCfvniapismwL 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1611 QSKLSDEVAARHELEEQI-KKLEHDSSSLQSAKARL----ENECKTLQ--------QKVEILGELYQQKEMALQKKLTqe 1677
Cdd:COG5244 372 SEFLQRKFSSKQETAFSIcQFLEDNKDVTLILKILHpileTTVPKLLAflrtnsnfNDNDTLCLIGSLYEIARIDKLI-- 449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1678 eyERQEKEQKLSAADEKAVLAIEEVKVYKQRIQDMEEE-LQKTERSYKNQIAAHEKKahdnwliarSAERALAEEKREAA 1756
Cdd:COG5244 450 --GKEEISKQDNRLFLYPSCDITLSSILTILFSDKLEVfFQGIESLLENITIFPEQP---------SQQTSDSENIKENS 518
|
490
....*....|..
gi 2024390606 1757 NLRQKLMEVNQK 1768
Cdd:COG5244 519 LLSDRLNEENIR 530
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1408-1718 |
6.03e-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: 41.70 E-value: 6.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1408 EETNHQLDDKIKSLRTMLDTERKQNAK---KQKKLS------------------ETQKSLEKFEEAFSMHSAELSEVQIA 1466
Cdd:pfam01576 741 EEKRRQLVKQVRELEAELEDERKQRAQavaAKKKLEldlkeleaqidaankgreEAVKQLKKLQAQMKDLQRELEEARAS 820
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1467 ----LNESKLSEEKVK---AELQHVQEENA---RLKKSKEQLLKE-----AEGWSERHTELTEQIKLYRKSQkDIEEALA 1531
Cdd:pfam01576 821 rdeiLAQSKESEKKLKnleAELLQLQEDLAaseRARRQAQQERDEladeiASGASGKSALQDEKRRLEARIA-QLEEELE 899
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1532 YKENEIEVLTN----CIMQLKQLDTDSASEAKDGEGLEWStkddlangelpdNEKMKTQIKQMmdasrvKTMLSlveEDR 1607
Cdd:pfam01576 900 EEQSNTELLNDrlrkSTLQVEQLTTELAAERSTSQKSESA------------RQQLERQNKEL------KAKLQ---EME 958
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1608 NSLQSKLSDEVAArheLEEQIKKLEHdssslqsakaRLENECKTLQQKveilGELYQQKEMALQKKLTQEEYERQEKEQK 1687
Cdd:pfam01576 959 GTVKSKFKSSIAA---LEAKIAQLEE----------QLEQESRERQAA----NKLVRRTEKKLKEVLLQVEDERRHADQY 1021
|
330 340 350
....*....|....*....|....*....|.
gi 2024390606 1688 LSAADEkavlAIEEVKVYKQRIQDMEEELQK 1718
Cdd:pfam01576 1022 KDQAEK----GNSRMKQLKRQLEEAEEEASR 1048
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1345-1503 |
6.24e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.68 E-value: 6.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1345 QVTEKQLAEKIQNLLQE-KTEMLDKFSEC---DEKIKQAKESMKVAQEQ-KSILSDEIAGLKDTVKE-LEETNHQLDDKI 1418
Cdd:COG4717 362 ELQLEELEQEIAALLAEaGVEDEEELRAAleqAEEYQELKEELEELEEQlEELLGELEELLEALDEEeLEEELEELEEEL 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1419 KSLRTMLDTERKQNAKKQKKLS--ETQKSLEKFEEAFSMHSAELSEVQIALNESKLSEEKVKAELQHVQEENArlkkskE 1496
Cdd:COG4717 442 EELEEELEELREELAELEAELEqlEEDGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREERL------P 515
|
....*..
gi 2024390606 1497 QLLKEAE 1503
Cdd:COG4717 516 PVLERAS 522
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
1351-1559 |
6.25e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 41.99 E-value: 6.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1351 LAEKIQNLLQEKTEMLDKFSECDEK------IKQAKESMKVAQEQKSILSDEIAGLKDTVKELEETNHQLDDKIKSLRTM 1424
Cdd:COG5022 911 LKKSLSSDLIENLEFKTELIARLKKllnnidLEEGPSIEYVKLPELNKLHEVESKLKETSEEYEDLLKKSTILVREGNKA 990
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1425 LDterkQNAKKQKKLSETQKSLEKFEEafsmHSAELSEVQIALNESKLSEEKVKAELQHVQEENaRLKKSKEQLLKEAeg 1504
Cdd:COG5022 991 NS----ELKNFKKELAELSKQYGALQE----STKQLKELPVEVAELQSASKIISSESTELSILK-PLQKLKGLLLLEN-- 1059
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024390606 1505 wsERHTELTEQIKLYRKSQKDIE------EALAYKENEIEVLtncimQLKQLDTDSASEAK 1559
Cdd:COG5022 1060 --NQLQARYKALKLRRENSLLDDkqlyqlESTENLLKTINVK-----DLEVTNRNLVKPAN 1113
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1346-1508 |
6.99e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 41.38 E-value: 6.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1346 VTEKQLAEKIQNLLQEKTEMLDKFSECDEKIKQAKESMKVAQEQKSILSDEIAGLKDTVKELEE----------TNHQLD 1415
Cdd:COG2433 385 LIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERelsearseerREIRKD 464
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1416 DKIKSLRTMLDTERKQNAKKQKKLSETQKSLEKFEEafsMHSAELSEVQIALNE-SKLSEEKVKAelqhvQEENARLKKS 1494
Cdd:COG2433 465 REISRLDREIERLERELEEERERIEELKRKLERLKE---LWKLEHSGELVPVKVvEKFTKEAIRR-----LEEEYGLKEG 536
|
170
....*....|....
gi 2024390606 1495 KEQLLKEAEGWSER 1508
Cdd:COG2433 537 DVVYLRDASGAGRS 550
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1352-1496 |
6.99e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.30 E-value: 6.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1352 AEKIQNLLQEKTEMLDKFSECDEKIKQAKESMKvAQEQKsiLSDEIAGLKDTVKELEETNHQLDDKIKSlrtmLDTERKQ 1431
Cdd:PRK12704 53 AIKKEALLEAKEEIHKLRNEFEKELRERRNELQ-KLEKR--LLQKEENLDRKLELLEKREEELEKKEKE----LEQKQQE 125
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024390606 1432 NAKKQKKLSE-TQKSLEKFEEAFSMHSAELSEVQIALNESKLSEEkvKAELQHVQEENARL---KKSKE 1496
Cdd:PRK12704 126 LEKKEEELEElIEEQLQELERISGLTAEEAKEILLEKVEEEARHE--AAVLIKEIEEEAKEeadKKAKE 192
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1339-1676 |
7.10e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.54 E-value: 7.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1339 VKSRMyqvtekqLAEKIQNLLQEKTEMLDKFSECDEKIKQAKESMKVAQEQKSIL-----SDEIAGL-KDTVKELEET-- 1410
Cdd:COG3206 90 LKSRP-------VLERVVDKLNLDEDPLGEEASREAAIERLRKNLTVEPVKGSNVieisyTSPDPELaAAVANALAEAyl 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1411 NHQLDDKIKSLRTMLDTERKQNAKKQKKLSETQKSLEKFEEAfsmHSAELSEVQIALNESKLSEekVKAELQHVQEENAR 1490
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQK---NGLVDLSEEAKLLLQQLSE--LESQLAEARAELAE 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1491 LKKSKEQLLKEAEGWSERHTELTE--QIKLYRKSQKDIEEALAykeneievltncimQLKQLDTDSASEAKDgeglewst 1568
Cdd:COG3206 238 AEARLAALRAQLGSGPDALPELLQspVIQQLRAQLAELEAELA--------------ELSARYTPNHPDVIA-------- 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1569 kddlANGELpdnEKMKTQIKQmmdasRVKTMLSLVEEDRNSLQSKLSdevaarhELEEQIKKLEHDSSSLQSAKARLENe 1648
Cdd:COG3206 296 ----LRAQI---AALRAQLQQ-----EAQRILASLEAELEALQAREA-------SLQAQLAQLEARLAELPELEAELRR- 355
|
330 340 350
....*....|....*....|....*....|...
gi 2024390606 1649 cktLQQKVEILGELYQQ-----KEMALQKKLTQ 1676
Cdd:COG3206 356 ---LEREVEVARELYESllqrlEEARLAEALTV 385
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1373-1768 |
8.24e-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: 8.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1373 DEKIKQAKESMKVAQEQKSILSDEiaglkdtVKELEETNHQLDDKIKSLRTMLDTER-----------KQNAKKQKK--- 1438
Cdd:pfam01576 4 EEEMQAKEEELQKVKERQQKAESE-------LKELEKKHQQLCEEKNALQEQLQAETelcaeaeemraRLAARKQELeei 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1439 LSETQKSLEKFEEAFSMHSAELSEVQ--IALNESKLSEE---KVKAELQHVQEEnARLKKSKEQLLKEAegwsERHTELT 1513
Cdd:pfam01576 77 LHELESRLEEEEERSQQLQNEKKKMQqhIQDLEEQLDEEeaaRQKLQLEKVTTE-AKIKKLEEDILLLE----DQNSKLS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1514 EQIKLYRKSQKDIEEALAYKENEIEVLTNCIMQLKQLDTDSA----SEAKDGEGLE-WSTKDDLANGELPDN-EKMKTQI 1587
Cdd:pfam01576 152 KERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEerlkKEEKGRQELEkAKRKLEGESTDLQEQiAELQAQI 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1588 KQMmdasrvKTMLSLVEEDRNSLQSKLSDEVAAR-------HELEEQIKKLEHDSSSLQSAKARLENECKTLQQKVEIL- 1659
Cdd:pfam01576 232 AEL------RAQLAKKEEELQAALARLEEETAQKnnalkkiRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALk 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1660 GELyqqkEMALQKKLTQEEYeRQEKEQKLsaADEKAVLAiEEVKVYKQRIQDME-------EELQKTERSYKNQIAAHEK 1732
Cdd:pfam01576 306 TEL----EDTLDTTAAQQEL-RSKREQEV--TELKKALE-EETRSHEAQLQEMRqkhtqalEELTEQLEQAKRNKANLEK 377
|
410 420 430
....*....|....*....|....*....|....*.
gi 2024390606 1733 KAHdnwliarSAERALAEEKREAANLRQKLMEVNQK 1768
Cdd:pfam01576 378 AKQ-------ALESENAELQAELRTLQQAKQDSEHK 406
|
|
| KLF9_13_N-like |
cd21975 |
Kruppel-like factor (KLF) 9, KLF13, KLF14, KLF16, and similar proteins; Kruppel/Krueppel-like ... |
1820-1975 |
8.75e-03 |
|
Kruppel-like factor (KLF) 9, KLF13, KLF14, KLF16, and similar proteins; Kruppel/Krueppel-like transcription factors (KLFs) belong to a family of proteins, called the Specificity Protein (SP)/KLF family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. Members of the KLF family can act as activators or repressors of transcription depending on cell and promoter context. KLFs regulate various cellular functions, such as proliferation, differentiation, and apoptosis, as well as the development and homeostasis of several types of tissue. KLF9, KLF10, KLF11, KLF13, KLF14, and KLF16 share a conserved alpha-helical motif AA/VXXL that mediates their binding to Sin3A and their activities as transcriptional repressors. In addition to the C-terminal DNA-binding domain, each KLF also has a unique N-terminal activation/repression domain that confers specificity and allows it to bind specifically to a certain partner, leading to distinct activities in vivo. This model represents the related N-terminal domains of KLF9, KLF13, KLF14, KLF16, and similar proteins.
Pssm-ID: 409240 [Multi-domain] Cd Length: 163 Bit Score: 39.29 E-value: 8.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024390606 1820 VPSRPLSAPQREGSRAEFGTVVDGPPAPRRPPELPGRMSVPDLGPAVASLISSGPRTSSPATA--KDRAPSPKEPEAPRV 1897
Cdd:cd21975 21 VRPDPEGAGLAAGLDVRATREVAKGPGPPGPAWKPDGADSPGLVTAAPHLLAANVLAPLRGPSveGSSLESGDADMGSDS 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024390606 1898 TTDSPSSIEPATVNVGPKGPPSFPGTPvmtspvlgppppppvnyGPPPAPFPGHYGPGPRPLPVPLVCGAPLPPPAAR 1975
Cdd:cd21975 101 DVAPASGAAASTSPESSSDAASSPSPL-----------------SLLHPGEAGLEPERPRPRVRRGVRRRGVTPAAKR 161
|
|
| DUF6730 |
pfam20503 |
Family of unknown function (DUF6730); This family of proteins is functionally uncharacterized. ... |
1393-1448 |
9.10e-03 |
|
Family of unknown function (DUF6730); This family of proteins is functionally uncharacterized. This family of proteins is found in bacteria. Proteins in this family are typically between 105 and 155 amino acids in length.
Pssm-ID: 466652 Cd Length: 82 Bit Score: 37.11 E-value: 9.10e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024390606 1393 LSDEIAGLKDTVKELEETNHQLDD-KIK--------SLRTMLDTERKQNAKKQKKLSETQKSLEK 1448
Cdd:pfam20503 11 LTEEIEGFNKSVERLEKLSQQLKDtKIKidtseiekLLEEHLKQQKKKLEEQEEFLREIEKKLKK 75
|
|
|