|
Name |
Accession |
Description |
Interval |
E-value |
| SH3_MIA2 |
cd11892 |
Src Homology 3 domain of Melanoma Inhibitory Activity 2 protein; MIA2 is expressed ... |
31-103 |
1.70e-45 |
|
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: 157.69 E-value: 1.70e-45
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370465047 31 KCGDLECEALINRVSAMRDYRGPDCRYLNFTKGEEISVYVKLAGEREDLWAGSKGKEFGYFPRDAVQIEEVFI 103
Cdd:cd11892 1 KCGDPECERLMSRVQAIRDYRGPDCRYLSFKKGDEIIVYYKLSGKREDLWAGSTGKEFGYFPKDAVKVEEVYI 73
|
|
| SH3_MIA_like |
cd11760 |
Src Homology 3 domain of Melanoma Inhibitory Activity protein and similar proteins; MIA is a ... |
31-103 |
3.76e-36 |
|
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: 131.06 E-value: 3.76e-36
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370465047 31 KCGDLECEALINRVSAMRDYRGPDCRYLNFTKGEEISVYVKLAGEREDLWAGSKG---KEFGYFPRDAVQIEEVFI 103
Cdd:cd11760 1 LCADAECSNPISRARALEDYHGPDCRFLNFKKGDTIYVYSKLAGERQDLWAGSVGgdaGLFGYFPKNLVQELKVYE 76
|
|
| SH3_MIA3 |
cd11893 |
Src Homology 3 domain of Melanoma Inhibitory Activity 3 protein; MIA3, also called TANGO or ... |
31-102 |
6.10e-25 |
|
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: 99.15 E-value: 6.10e-25
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370465047 31 KCGDLECEALINRVSAMRDYRGPDCRYLNFTKGEEISVYVKLAGEREDLWAGSKGKEFGYFPRDAVQIEEVF 102
Cdd:cd11893 1 RCADEECSMLLCRGKAVKDFTGPDCRFLSFKKGETIYVYYKLSGRRTDLWAGSVGFDFGYFPKDLLDVNHLY 72
|
|
| MIA |
cd11890 |
Melanoma Inhibitory Activity protein; MIA is a single domain protein that adopts a Src ... |
30-118 |
9.42e-15 |
|
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: 71.06 E-value: 9.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465047 30 KKCGDLECEALINRVSAMRDYRGPDCRYLNFTKGEEISVYVKLAGEREDLWAGS--------KGKEFGYFPRDAVQIEEV 101
Cdd:cd11890 2 KLCADQECSHPISIAVALQDYMAPDCRFIPIQRGQVVYVFSKLKGRGRLFWGGSvqgdyygeQAARLGYFPSSIVQEDQY 81
|
90
....*....|....*..
gi 1370465047 102 FISEEIQMSTKESDFLC 118
Cdd:cd11890 82 LKPGKVEVKTDKWDFYC 98
|
|
| MIAL |
cd11891 |
Melanoma Inhibitory Activity-Like protein; MIAL is specifically expressed in the cochlea and ... |
32-102 |
3.25e-11 |
|
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: 60.64 E-value: 3.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465047 32 CGDLECEALINRVSAMRDYRGPDCRYLNFTKGEEISVYVKLAGERE--DLWAGSKGKE--------FGYFPRDAVQIEEV 101
Cdd:cd11891 2 CADEECVYAISLARAEDDYNAPDCRFINIKKGQLIYVYSKLVKENGagEFWSGSVYSEryvdqmgiVGYFPSNLVKEQTV 81
|
.
gi 1370465047 102 F 102
Cdd:cd11891 82 Y 82
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
736-1066 |
7.90e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 66.62 E-value: 7.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465047 736 EVENQMFVEGSQISEATCE--KLNRSNSELEDEILCLEKELKEEKSKHSEQDELMADISKRIQSLEDESKSLKSQVAEAK 813
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKAlaELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELE 760
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465047 814 MTFKIFQMNEERLKIAIKDALNENSQLQESQKQLLQEAEVWKEQVSELNKQkvtfedskvhaeqvLNDKESHIKTLTERL 893
Cdd:TIGR02168 761 AEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAE--------------LTLLNEEAANLRERL 826
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465047 894 LKMKDWAAMLGEDITDDDNlELEMNSEsengayldnppkgalkkliHAAKLNASLKTLEGERNQIYIQLSEVDKTKEELT 973
Cdd:TIGR02168 827 ESLERRIAATERRLEDLEE-QIEELSE-------------------DIESLAAEIEELEELIEELESELEALLNERASLE 886
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465047 974 EHIKNLQTEQASLQSENTHFENENQKLQQKLKVMTEL-------YQENEMKLHRKL-TVEENYRLEKEEklskVDEKISH 1045
Cdd:TIGR02168 887 EALALLRSELEELSEELRELESKRSELRRELEELREKlaqlelrLEGLEVRIDNLQeRLSEEYSLTLEE----AEALENK 962
|
330 340
....*....|....*....|.
gi 1370465047 1046 ATEELETYRKRAKDLEEELER 1066
Cdd:TIGR02168 963 IEDDEEEARRRLKRLENKIKE 983
|
|
| SH3_2 |
pfam07653 |
Variant SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in ... |
46-99 |
5.65e-10 |
|
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: 56.07 E-value: 5.65e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1370465047 46 AMRDYRGPDCRYLNFTKGEEISVYVKlagEREDLWAGSKGKEFGYFPRDAVQIE 99
Cdd:pfam07653 4 VIFDYVGTDKNGLTLKKGDVVKVLGK---DNDGWWEGETGGRVGLVPSTAVEEI 54
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
682-989 |
2.56e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 62.01 E-value: 2.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465047 682 REKKLALMLSGLIEEKSKL------LEKFSLVQK---EYEGYEVESSLKDASFEKEATEAQSLEVENQMfvegsqiseat 752
Cdd:TIGR02169 185 NIERLDLIIDEKRQQLERLrrerekAERYQALLKekrEYEGYELLKEKEALERQKEAIERQLASLEEEL----------- 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465047 753 cEKLNRSNSELEDEIlclekelkeekskhSEQDELMADISKRIQSL-EDESKSLKSQVAEAKMTFKIFQMNEERLKIAIK 831
Cdd:TIGR02169 254 -EKLTEEISELEKRL--------------EEIEQLLEELNKKIKDLgEEEQLRVKEKIGELEAEIASLERSIAEKERELE 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465047 832 DALNENSQLQESQKQLLQEAEVWKEQVSELNKQKVTFEDSKVHAEQVLNDKESHI-------KTLTERLLKMKDWAAMLG 904
Cdd:TIGR02169 319 DAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELeevdkefAETRDELKDYREKLEKLK 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465047 905 EDI----TDDDNLELEMNSESENGAYLDNPPKGA---LKKLIHAAK-LNASLKTLEGERNQIYIQLSEVDKTKEELTEHI 976
Cdd:TIGR02169 399 REInelkRELDRLQEELQRLSEELADLNAAIAGIeakINELEEEKEdKALEIKKQEWKLEQLAADLSKYEQELYDLKEEY 478
|
330
....*....|...
gi 1370465047 977 KNLQTEQASLQSE 989
Cdd:TIGR02169 479 DRVEKELSKLQRE 491
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
691-1064 |
5.87e-07 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 53.87 E-value: 5.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465047 691 SGLIEEKSKLLEKFSLVQKEYEGYEVESSLKDASFEKEATEAQSLEVENQMFVEGSQISEatcekLNRSNSELEDEILCL 770
Cdd:TIGR04523 280 NKKIKELEKQLNQLKSEISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQ-----LNEQISQLKKELTNS 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465047 771 EKELKEEKSKHSEQDELMADISKRIQSLEDESKSLKSQVAEAKMTFKIFQMNEERLKIAIKDALNENSQLQESQKQLLQE 850
Cdd:TIGR04523 355 ESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKET 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465047 851 AEVWKEQVSELNKQKVTFEDSKVHAEQVLNDKESHIKTLTERLLKMKDWAAMLGEDITDDDNLELEMNSESENgayLDNP 930
Cdd:TIGR04523 435 IIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKE---LEEK 511
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465047 931 PKgALKKLIhaAKLNASLKTLEGERNQIYIQLSEV---------DKTKEELTEHIKNLQTEQASLQSENTHFENENQKLQ 1001
Cdd:TIGR04523 512 VK-DLTKKI--SSLKEKIEKLESEKKEKESKISDLedelnkddfELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQ 588
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370465047 1002 QKLKVMTElyqenemklhrkltveENYRLEKEekLSKVDEKISHATEELETYRKRAKDLEEEL 1064
Cdd:TIGR04523 589 ELIDQKEK----------------EKKDLIKE--IEEKEKKISSLEKELEKAKKENEKLSSII 633
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
941-1123 |
7.66e-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: 53.91 E-value: 7.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465047 941 AAKLNASLKTLEGERNQIYIQLSEVDKTKEELTEHIKNLQTEQASLQSENthfENENQKLQQKLKVMTELyQENEMKLHR 1020
Cdd:TIGR02168 693 IAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEV---EQLEERIAQLSKELTEL-EAEIEELEE 768
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465047 1021 KLTVEENYRLEKEEKLSKVDEKISHATEELETYRKRAKDLEEELERT---IHSYQGQIISHEKKAHDNWLAARNAERNLN 1097
Cdd:TIGR02168 769 RLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLneeAANLRERLESLERRIAATERRLEDLEEQIE 848
|
170 180
....*....|....*....|....*.
gi 1370465047 1098 DLRKENAHNRQKLTETELKFELLEKD 1123
Cdd:TIGR02168 849 ELSEDIESLAAEIEELEELIEELESE 874
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
795-1122 |
1.23e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 52.72 E-value: 1.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465047 795 IQSLEDESKSLKSQVAEAKMTFKIFQMNEERLKIAIKDALNENSQLQESQKQLLQEAEVWKEQVSELNKQKVTfedskvh 874
Cdd:TIGR04523 206 LKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQ------- 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465047 875 AEQVLNDKESHIKTLTERLLKMK-----DWAAMLGEDITDDDNLELEMNSESENgaylDNPPKGALKKLIhaAKLNASLK 949
Cdd:TIGR04523 279 NNKKIKELEKQLNQLKSEISDLNnqkeqDWNKELKSELKNQEKKLEEIQNQISQ----NNKIISQLNEQI--SQLKKELT 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465047 950 TLEGERNQIYIQLSE-------VDKTKEELTEHIKNLQTEQASLQSENTHFENENQKLQQKLKVMTELYQENEmKLHRKL 1022
Cdd:TIGR04523 353 NSESENSEKQRELEEkqneiekLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLE-KEIERL 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465047 1023 TVEenyRLEKEEKLSKVDEKIShateELETYRKRAKDLEEELERTIHSYQGQIISHEKKAHDNWLAARNAERNLNDLRKE 1102
Cdd:TIGR04523 432 KET---IIKNNSEIKDLTNQDS----VKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEE 504
|
330 340
....*....|....*....|
gi 1370465047 1103 NAHNRQKLTETELKFELLEK 1122
Cdd:TIGR04523 505 KKELEEKVKDLTKKISSLKE 524
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
783-1102 |
1.27e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.02 E-value: 1.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465047 783 EQDELMADISKRIQSLEDESKSLKSQVAEAKMTFKIFQMNEERLKIAIKDALNENSQLQESQKQLLQEAEVWKEQVSELN 862
Cdd:COG1196 257 ELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELE 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465047 863 KQKVTFEDSKVHAEQVLNDKESHIKTLTERLLKMKdwAAMLGEDITDDDNLELEMNSESEngayldnppkgALKKLIHAA 942
Cdd:COG1196 337 EELEELEEELEEAEEELEEAEAELAEAEEALLEAE--AELAEAEEELEELAEELLEALRA-----------AAELAAQLE 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465047 943 KLNASLKTLEGERNQIYIQLSEVDKTKEELTEHIKNLQTEQASLQSENTHFENENQKLQQKLKVMTELYQENEMKLHRkl 1022
Cdd:COG1196 404 ELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAE-- 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465047 1023 tveenyRLEKEEKLSKVDEKISHATEELETYRKRAKDLEEELERTIHSYQGQIISHEKKAHDNWLAARNAERNLNDLRKE 1102
Cdd:COG1196 482 ------LLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVED 555
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
694-1126 |
2.08e-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: 52.03 E-value: 2.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465047 694 IEEKSKLLEKFSLVQKEYEGYEVEssLKDASFEKEATEAQSLEVENQMfVEGSQISEATCEKLNR--SNSELEDEILcle 771
Cdd:pfam05483 211 LEMHFKLKEDHEKIQHLEEEYKKE--INDKEKQVSLLLIQITEKENKM-KDLTFLLEESRDKANQleEKTKLQDENL--- 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465047 772 keLKEEKSKHSEQDELmADISKRIQSLEDESKSLKSQVAEAKMTfkIFQMNEERlkiaikdalneNSQLQESQKQLLQEA 851
Cdd:pfam05483 285 --KELIEKKDHLTKEL-EDIKMSLQRSMSTQKALEEDLQIATKT--ICQLTEEK-----------EAQMEELNKAKAAHS 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465047 852 EVwkeqVSELNKQKVTFEDSKVHAEQVLNDKESHIKTLTERLLKMkdwAAMLGEDITDDDNLELEMNSE----SENGAYL 927
Cdd:pfam05483 349 FV----VTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKK---SSELEEMTKFKNNKEVELEELkkilAEDEKLL 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465047 928 DNppKGALKKLIHAAK-----LNASLKTLEGERNQIYIQLSEVDKTKEELTEHIKNLQTEQASLQSENTHFENENQKLQQ 1002
Cdd:pfam05483 422 DE--KKQFEKIAEELKgkeqeLIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLL 499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465047 1003 KLKVMTElyQENEMKLHRKLTVEENYRLEKEE-----KLSKVDEKISHATEELETYRKRAKDLEEELERTIHSYQGQIIS 1077
Cdd:pfam05483 500 ENKELTQ--EASDMTLELKKHQEDIINCKKQEermlkQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARS 577
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1370465047 1078 HEKKAHDNWLAARNAERNLNDLRKENAHNRQKLTETELKFELLEKDPYA 1126
Cdd:pfam05483 578 IEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSA 626
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
791-1127 |
2.70e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 51.98 E-value: 2.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465047 791 ISKRIQSLEDESKS------LKSQVAEAKMTFKIFQMNEERLKI-AIKDALNENSQLQESQKQLLQEAEvwkEQVSELNK 863
Cdd:TIGR02168 198 LERQLKSLERQAEKaerykeLKAELRELELALLVLRLEELREELeELQEELKEAEEELEELTAELQELE---EKLEELRL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465047 864 QKVTFEDSKVHAEQVLNDKESHIKTLTERLLKMKDwaamlgeditdddNLELEMNSESENGAYLDNPPKGALKKLIHAAK 943
Cdd:TIGR02168 275 EVSELEEEIEELQKELYALANEISRLEQQKQILRE-------------RLANLERQLEELEAQLEELESKLDELAEELAE 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465047 944 LNASLKTLEGERNQIYIQLSEVDKTKEELTEHIKNLQTEQASLQSENTHFENENQKLQQKLKVM-TELYQENEMKLHRKL 1022
Cdd:TIGR02168 342 LEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLeARLERLEDRRERLQQ 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465047 1023 TVEENYRLEKEEKLSKVDEKISHATEELETYRKRAKDLEEELERTihsyQGQIishekkahdnwlaaRNAERNLNDLRKE 1102
Cdd:TIGR02168 422 EIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEEL----REEL--------------EEAEQALDAAERE 483
|
330 340
....*....|....*....|....*
gi 1370465047 1103 NAHNRQKLTETELKFELLEKDPYAL 1127
Cdd:TIGR02168 484 LAQLQARLDSLERLQENLEGFSEGV 508
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
942-1066 |
2.93e-06 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 51.40 E-value: 2.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465047 942 AKLNASLKTLEGERNQIYIQLSEVDKTKEEltEHIKNLQTEQASLQSENTHFENENQKLQQKLKVMtelyqENEMKLHRK 1021
Cdd:COG2433 383 EELIEKELPEEEPEAEREKEHEERELTEEE--EEIRRLEEQVERLEAEVEELEAELEEKDERIERL-----ERELSEARS 455
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1370465047 1022 ltvEENYRLEKEEKLSKVDEKISHATEELETYRKRAKDLEEELER 1066
Cdd:COG2433 456 ---EERREIRKDREISRLDREIERLERELEEERERIEELKRKLER 497
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
694-1068 |
2.96e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 51.56 E-value: 2.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465047 694 IEEKSKLLEKfslVQKEYEGYEVESslkdasfEKEATEAQSLEVENQMFVEGSQISEATCEKLNRSNSELEDEILCLEKE 773
Cdd:TIGR04523 365 LEEKQNEIEK---LKKENQSYKQEI-------KNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKET 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465047 774 LKEEKSKHSEQDELMADISKRIQSLEDESKSLKSQVAEAKMTFKIFQMNEERLKIAIKDALNENSQLQESQKQLLQEAEV 853
Cdd:TIGR04523 435 IIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKD 514
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465047 854 WKEQVSELNKQKVTFEDSKVHAEQVLNDKESHIKTLTERLLKMKDWAAMLGEDIT------DDDNLELEmNSESEN---- 923
Cdd:TIGR04523 515 LTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEKEIDEKNKEieelkqTQKSLKKK-QEEKQElidq 593
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465047 924 -GAYLDNPPKGALKKLIHAAKLNASLKTLEGERNQIYIQLSEVDKTKEELTEHIKNLQTEQASLQSENTHFENENQKLQQ 1002
Cdd:TIGR04523 594 kEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKT 673
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370465047 1003 KLKVMTELYQ--ENEMKLHRKLTVEENYRLEKEEKLSKVDEKISHATEELETYRKRAKDLEEELERTI 1068
Cdd:TIGR04523 674 KIDDIIELMKdwLKELSLHYKKYITRMIRIKDLPKLEEKYKEIEKELKKLDEFSKELENIIKNFNKKF 741
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
824-1068 |
3.28e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.92 E-value: 3.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465047 824 ERLKIAIKDALNENSQLQESQKQLLQEAEVWKEQVSELNKQKVTFEDSKVHAEQVLNDKESHIKTLTERLLKMKDW-AAM 902
Cdd:COG4942 30 EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEElAEL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465047 903 LGEditdddnleLEMNSESENGAYLDNP--PKGALKKLIHAAKLNASLKTlegernqiyiQLSEVDKTKEELTEHIKNLQ 980
Cdd:COG4942 110 LRA---------LYRLGRQPPLALLLSPedFLDAVRRLQYLKYLAPARRE----------QAEELRADLAELAALRAELE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465047 981 TEQASLQSENTHFENENQKLQQKLKvmtelyqenemklhrkltveenyrlEKEEKLSKVDEKISHATEELETYRKRAKDL 1060
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKA-------------------------ERQKLLARLEKELAELAAELAELQQEAEEL 225
|
....*...
gi 1370465047 1061 EEELERTI 1068
Cdd:COG4942 226 EALIARLE 233
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
669-1066 |
5.22e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 50.84 E-value: 5.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465047 669 RSFRSVRSRLYVGREKKLALMLSGLIEEKSKLLEKFSLVQKEYEgyEVESSLKDASFEKEAteaqsLEVENQMFVEGSQI 748
Cdd:TIGR02169 662 PRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLD--ELSQELSDASRKIGE-----IEKEIEQLEQEEEK 734
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465047 749 SEATCEKLNRSNSELEDEILclekelkeekskhsEQDELMADISKRIQSLEDESKSLKSQVAEakmtfkifqmneerlki 828
Cdd:TIGR02169 735 LKERLEELEEDLSSLEQEIE--------------NVKSELKELEARIEELEEDLHKLEEALND----------------- 783
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465047 829 aIKDALNEnSQLQESQKQLlqeaevwkeqvSELNKQKVTFEDSKVHAEQVLNDK-------ESHIKTLTERLLKMKDWAA 901
Cdd:TIGR02169 784 -LEARLSH-SRIPEIQAEL-----------SKLEEEVSRIEARLREIEQKLNRLtlekeylEKEIQELQEQRIDLKEQIK 850
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465047 902 MLGEDItDDDNLEL-EMNSESENgayldnpPKGALKKLIhaaklnASLKTLEGERNQIYIQLSEVDKTKEELT------- 973
Cdd:TIGR02169 851 SIEKEI-ENLNGKKeELEEELEE-------LEAALRDLE------SRLGDLKKERDELEAQLRELERKIEELEaqiekkr 916
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465047 974 EHIKNLQTEQASLQSENTHFENENQKLQQklkvmtelYQENEMKLHrklTVEENyRLEKEEKLSKVDEKISHATEELETY 1053
Cdd:TIGR02169 917 KRLSELKAKLEALEEELSEIEDPKGEDEE--------IPEEELSLE---DVQAE-LQRVEEEIRALEPVNMLAIQEYEEV 984
|
410
....*....|...
gi 1370465047 1054 RKRAKDLEEELER 1066
Cdd:TIGR02169 985 LKRLDELKEKRAK 997
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
715-1081 |
8.62e-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: 50.12 E-value: 8.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465047 715 EVESSLKDAsfeKEATEAQSLEVENQMFVEGSQISEATCEK--LNRSNSELEDEIlclekelkeekskhseqDELMADIS 792
Cdd:pfam15921 328 QLRSELREA---KRMYEDKIEELEKQLVLANSELTEARTERdqFSQESGNLDDQL-----------------QKLLADLH 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465047 793 KRIQSL---EDESKSLKSQVAEAKMTFKIFQ-------MNEERLKIAIKDALNENSQLQESQKQLLQEAEVWKEQVSELN 862
Cdd:pfam15921 388 KREKELsleKEQNKRLWDRDTGNSITIDHLRrelddrnMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLT 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465047 863 KQkvtFEDSKVHAEQVLNDKESHIKTLTERLLKMKDWAAMLGEDitdddnlELEMNSESENGAYLDNPPKGALKKLIHAA 942
Cdd:pfam15921 468 AQ---LESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEK-------ERAIEATNAEITKLRSRVDLKLQELQHLK 537
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465047 943 KLNASLKTLEGERNQIYIQLSEVDKTKEELTEHIKNL--------------QTEQASLQSENTHFENENQKLQ------- 1001
Cdd:pfam15921 538 NEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMtqlvgqhgrtagamQVEKAQLEKEINDRRLELQEFKilkdkkd 617
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465047 1002 ---QKLKVMTELYQENEMKL----HRKLTVEENYRLEKEEKLSKVD---EKISHATEELETYRKRAKDLEEELERTIHSY 1071
Cdd:pfam15921 618 akiRELEARVSDLELEKVKLvnagSERLRAVKDIKQERDQLLNEVKtsrNELNSLSEDYEVLKRNFRNKSEEMETTTNKL 697
|
410
....*....|
gi 1370465047 1072 QGQIISHEKK 1081
Cdd:pfam15921 698 KMQLKSAQSE 707
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
830-1015 |
1.28e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.06 E-value: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465047 830 IKDALNENSQLQESQKQLLQEAEVWKEQVSELNKQKVTFEDSKVHAEQVLNDKESHIKTLTERLlkmKDWAAMLGEDITD 909
Cdd:COG3883 25 LSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREEL---GERARALYRSGGS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465047 910 DDNLELEMNSESeNGAYLDNppKGALKKLIHAAklNASLKTLEGERNQIYIQLSEVDKTKEELTEHIKNLQTEQASLQSE 989
Cdd:COG3883 102 VSYLDVLLGSES-FSDFLDR--LSALSKIADAD--ADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQ 176
|
170 180
....*....|....*....|....*.
gi 1370465047 990 NTHFENENQKLQQKLKVMTELYQENE 1015
Cdd:COG3883 177 QAEQEALLAQLSAEEAAAEAQLAELE 202
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
783-1065 |
1.93e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.91 E-value: 1.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465047 783 EQDELMADISKRIQSLED------ESKSLKSQVAEAKMTFKIFQMNEERLKIAIKDA-------LNENSQLQESQKQLLQ 849
Cdd:PRK03918 142 ESDESREKVVRQILGLDDyenaykNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKekeleevLREINEISSELPELRE 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465047 850 EAEVWKEQVSELNKQKVTFEDSKVHAEQVLNDK---ESHIKTLTERLLKMKDWAAMLGEDITDDDNLELEMNSESENGAY 926
Cdd:PRK03918 222 ELEKLEKEVKELEELKEEIEELEKELESLEGSKrklEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEF 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465047 927 LDNppkgALKKLihaAKLNASLKTLEGERNQIYIQLSEVDKTK---EELTEHIKNLQTEQASLQSENTHFENENQKLQQK 1003
Cdd:PRK03918 302 YEE----YLDEL---REIEKRLSRLEEEINGIEERIKELEEKEerlEELKKKLKELEKRLEELEERHELYEEAKAKKEEL 374
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370465047 1004 LKVMTELYQENEMKLHRKLTVEENYRLEKEEKLSKVDEKIShateELETYRKRAKDLEEELE 1065
Cdd:PRK03918 375 ERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIG----ELKKEIKELKKAIEELK 432
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
695-987 |
1.97e-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: 48.91 E-value: 1.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465047 695 EEKSKLLEKFSLVQKEYEgyEVESSLKDASFEKEATEAQSLEVENQMFVEGSQISEATCEKLNRSNSELEDEilclekel 774
Cdd:TIGR02169 737 ERLEELEEDLSSLEQEIE--NVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEE-------- 806
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465047 775 keekskHSEQDELMADISKRIQS-------LEDESKSLKSQVAEAKMTFKIFQMNEERLKIAIKDALNENSQLQESQKQL 847
Cdd:TIGR02169 807 ------VSRIEARLREIEQKLNRltlekeyLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDL 880
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465047 848 LQEAEVWKEQVSELNKQKVTFEDSKVHAEQVLNDKESHIKTLTERLlkmkdwaAMLGEDITDDDNLELEMNSESENgayl 927
Cdd:TIGR02169 881 ESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKL-------EALEEELSEIEDPKGEDEEIPEE---- 949
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465047 928 dNPPKGALKKLIHaaKLNASLKTLEGERNQIYIQLSEVDKTKEELTEHIKNLQTEQASLQ 987
Cdd:TIGR02169 950 -ELSLEDVQAELQ--RVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAIL 1006
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
683-1122 |
2.64e-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: 48.63 E-value: 2.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465047 683 EKKLALMLSGLI--EEKSKLLEKFSLVQkEYEGYEVESSLK-------DASFEKEATEAQSLEVENQMFVEGSQISEATC 753
Cdd:pfam01576 158 EERISEFTSNLAeeEEKAKSLSKLKNKH-EAMISDLEERLKkeekgrqELEKAKRKLEGESTDLQEQIAELQAQIAELRA 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465047 754 EkLNRSNSELEDEILCLEKELKEEKSKHSEQDELMADISKRIQSLEDEskslKSQVAEAKMTFKIFQMNEERLKIAIKDA 833
Cdd:pfam01576 237 Q-LAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESE----RAARNKAEKQRRDLGEELEALKTELEDT 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465047 834 LNENSQLQESQKQLLQEaevwkeqVSELnkQKVTFEDSKVHAEQVLNDKESH---IKTLTERLLKMKDWAAML--GEDIT 908
Cdd:pfam01576 312 LDTTAAQQELRSKREQE-------VTEL--KKALEEETRSHEAQLQEMRQKHtqaLEELTEQLEQAKRNKANLekAKQAL 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465047 909 DDDNLELEMNSESENGAYLDNPPKGalkklihaaklnaslKTLEGERNQIYIQLSEVDKTKEELTEHIKNLQTEQASLQS 988
Cdd:pfam01576 383 ESENAELQAELRTLQQAKQDSEHKR---------------KKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSS 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465047 989 ENTHFENENQKLQQKLKVMtelyqenEMKLHrklTVEENYRLEKEEKLSkVDEKISHATEELETYRKRAKDLEE---ELE 1065
Cdd:pfam01576 448 LLNEAEGKNIKLSKDVSSL-------ESQLQ---DTQELLQEETRQKLN-LSTRLRQLEDERNSLQEQLEEEEEakrNVE 516
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1370465047 1066 RTIHSYQGQIISHEKKAHDNWLAARNAERNLNDLRKENAHNRQKLTETELKFELLEK 1122
Cdd:pfam01576 517 RQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEK 573
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
708-1004 |
2.66e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.78 E-value: 2.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465047 708 QKEYEGYEVESSL-----KDASFEKEATEAQSLEVENQMFVEGSQISEATCEKLNRSNSELEDEIlclekelkeekskhS 782
Cdd:COG1196 219 KEELKELEAELLLlklreLEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELEL--------------E 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465047 783 EQDELMADISKRIQSLEDESKSLKSQVAEAkmtfkifQMNEERLKIAIKDALNENSQLQESQKQLLQEAEVWKEQVSELN 862
Cdd:COG1196 285 EAQAEEYELLAELARLEQDIARLEERRREL-------EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAE 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465047 863 KQKVTFEDSKVHAEQVLNDKESHIKTLTERLLKMKDWAAMLGEDITDDDNLELEMNSESEngayldnppkgalKKLIHAA 942
Cdd:COG1196 358 AELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLE-------------RLEEELE 424
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370465047 943 KLNASLKTLEGERNQIYIQLSEVDKTKEELTEHIKNLQTEQASLQSENTHFENENQKLQQKL 1004
Cdd:COG1196 425 ELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEEL 486
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
935-1081 |
3.64e-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: 3.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465047 935 LKKLIHAAKLNASLKTLEGERNQIYIQLSEVDKTKEELTEHIKNLQTEQASLQSENTHFENENQKLQQKLKVMTEL---- 1010
Cdd:COG1579 6 LRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQlgnv 85
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370465047 1011 -----YQ--ENEM-KLHRKLTVEENYRLEKEEKLSKVDEKISHATEELETYRKRAKDLEEELERTIHSYQGQIISHEKK 1081
Cdd:COG1579 86 rnnkeYEalQKEIeSLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAE 164
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
694-1037 |
6.85e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 47.36 E-value: 6.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465047 694 IEEKSKLLEKFSLVQKEYEGYEVESSLKDASF---EKEATEAQSLEVENQMFVEGSQISEATcEKLNRSNS---ELEDEI 767
Cdd:TIGR02168 205 LERQAEKAERYKELKAELRELELALLVLRLEElreELEELQEELKEAEEELEELTAELQELE-EKLEELRLevsELEEEI 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465047 768 LCLEKELKEEKSKHSEQDELMADISKRIQSLEDESKSLKSQVAEakmtfkifqmNEERLKIAIKDAlnenSQLQESQKQL 847
Cdd:TIGR02168 284 EELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEE----------LESKLDELAEEL----AELEEKLEEL 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465047 848 LQEAEVWKEQVSELNKQKVTFEDSKVHAEQVLNDKESHIKTLTERLLKMKDWAAMLGEDITD-DDNLElemNSESENGAY 926
Cdd:TIGR02168 350 KEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERlEDRRE---RLQQEIEEL 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465047 927 LDNPPKGALKKLIHA-AKLNASLKTLEGERNQIYIQLSEVDKTKEELTEHIKNLQTEQASLQSENTHFENENQKLQQKLK 1005
Cdd:TIGR02168 427 LKKLEEAELKELQAElEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSE 506
|
330 340 350
....*....|....*....|....*....|....*...
gi 1370465047 1006 VMTELYQENEMK------LHRKLTVEENYRLEKEEKLS 1037
Cdd:TIGR02168 507 GVKALLKNQSGLsgilgvLSELISVDEGYEAAIEAALG 544
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
690-1123 |
8.52e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.98 E-value: 8.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465047 690 LSGLIEEKSKLLEKFSLVQKEYEGYEVESSLKDASFEKEATEAQSLEVENQMFVEGSQISEATCEKLNRSNSELEdEILC 769
Cdd:PRK03918 212 ISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELK-ELKE 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465047 770 LEKELKEEKSKHSEQDELMADISKRIQSLEDESKSLKSQVAEA-KMTFKIFQMNEERLKIAIK-DALNENSQLQESQKQL 847
Cdd:PRK03918 291 KAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELeEKEERLEELKKKLKELEKRlEELEERHELYEEAKAK 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465047 848 LQEAEVWKEQVSELN--------------KQKVTFEDSKVHAEQV-LNDKESHIKTLTERLLKMKDWAAMLGEDITDDDN 912
Cdd:PRK03918 371 KEELERLKKRLTGLTpeklekeleelekaKEEIEEEISKITARIGeLKKEIKELKKAIEELKKAKGKCPVCGRELTEEHR 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465047 913 LELeMNSESENGAYLDNPPKGALKKLihaAKLNASLKTLEGERNQI--YIQLSEVDKTKEELTEHIKNLQTEQasLQSEN 990
Cdd:PRK03918 451 KEL-LEEYTAELKRIEKELKEIEEKE---RKLRKELRELEKVLKKEseLIKLKELAEQLKELEEKLKKYNLEE--LEKKA 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465047 991 THFENENQKL----QQKLKVMTELYQENEMKlhRKLTVEENYRLEKEEKLSKVDEKIshateeletyRKRAKDLEEELER 1066
Cdd:PRK03918 525 EEYEKLKEKLiklkGEIKSLKKELEKLEELK--KKLAELEKKLDELEEELAELLKEL----------EELGFESVEELEE 592
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1370465047 1067 TIHSYqgqiisheKKAHDNWLAARNAERNLNDLRKENAHNRQKLTETELKFELLEKD 1123
Cdd:PRK03918 593 RLKEL--------EPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKR 641
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
942-1128 |
1.49e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 46.20 E-value: 1.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465047 942 AKLNASLKTLEGERNQIYIQLSEVDKTKEELTEHIKNLQTEQASLqsenthfENENQKLQQKLKvmtELYQENEMkLHRK 1021
Cdd:TIGR02168 256 EELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRL-------EQQKQILRERLA---NLERQLEE-LEAQ 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465047 1022 LTVEENYRLEKEEKLSKVDEKISHATEELETYR---KRAKDLEEELERTIHSYQGQIISHEKKAHD--NWLAARNAERNL 1096
Cdd:TIGR02168 325 LEELESKLDELAEELAELEEKLEELKEELESLEaelEELEAELEELESRLEELEEQLETLRSKVAQleLQIASLNNEIER 404
|
170 180 190
....*....|....*....|....*....|..
gi 1370465047 1097 NDLRKENAHNRQKLTETELKFELLEKDPYALD 1128
Cdd:TIGR02168 405 LEARLERLEDRRERLQQEIEELLKKLEEAELK 436
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
682-1066 |
1.92e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.83 E-value: 1.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465047 682 REKKLALMLSGLIEEKSKLLEKfSLVQKEYEGYEVESSLKDASFEKEATEAQSLEVEnqmfvegsqiseATCEKLNRSNS 761
Cdd:PRK03918 179 ERLEKFIKRTENIEELIKEKEK-ELEEVLREINEISSELPELREELEKLEKEVKELE------------ELKEEIEELEK 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465047 762 ELEdeilclekelkEEKSKHSEQDELMADISKRIQSLEDESKSLKSQVAEAKmTFKIFQMNEERLKIAIKDALNENSQLQ 841
Cdd:PRK03918 246 ELE-----------SLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELK-ELKEKAEEYIKLSEFYEEYLDELREIE 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465047 842 ESQKQLLQEAEVWKEQVSELNKqkvtfedskvhaeqvlndKESHIKTLTERLLKMKDWAAMLGEDITDDDNLELEMNSES 921
Cdd:PRK03918 314 KRLSRLEEEINGIEERIKELEE------------------KEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELE 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465047 922 ENGAYLDNPPKGALKKLIHAA------------KLNASLKTLEGERNQIYIQLSEVDKTK-------EELTEH-----IK 977
Cdd:PRK03918 376 RLKKRLTGLTPEKLEKELEELekakeeieeeisKITARIGELKKEIKELKKAIEELKKAKgkcpvcgRELTEEhrkelLE 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465047 978 NLQTEQASLQSENTHFENENQKLQQKLKVMtELYQENEMKLHRKLTVEENYRlEKEEKLSKVD-EKISHATEELETYRKR 1056
Cdd:PRK03918 456 EYTAELKRIEKELKEIEEKERKLRKELREL-EKVLKKESELIKLKELAEQLK-ELEEKLKKYNlEELEKKAEEYEKLKEK 533
|
410
....*....|
gi 1370465047 1057 AKDLEEELER 1066
Cdd:PRK03918 534 LIKLKGEIKS 543
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
948-1122 |
2.08e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.53 E-value: 2.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465047 948 LKTLEGERNQIYIQLSEVdktkEELTEHIKNLQTEQASLQSENTHFENENQKLQQKLKVMtELYQENEMKLHRKLTVEEN 1027
Cdd:COG4717 73 LKELEEELKEAEEKEEEY----AELQEELEELEEELEELEAELEELREELEKLEKLLQLL-PLYQELEALEAELAELPER 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465047 1028 YR--LEKEEKLSKVDEKISHATEELETYRKrakDLEEELERTIHSYQGQIISHEKKAHDNWLAARNAERNLNDLRKENAH 1105
Cdd:COG4717 148 LEelEERLEELRELEEELEELEAELAELQE---ELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEE 224
|
170
....*....|....*..
gi 1370465047 1106 NRQKLTETELKFELLEK 1122
Cdd:COG4717 225 LEEELEQLENELEAAAL 241
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
782-1144 |
2.98e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 45.06 E-value: 2.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465047 782 SEQDELmADISKRIQSLEDESKSLKSQVAEAKMtfkifQMNEerLKIAIKDALNENSQLQESQKQLLQEAEVWKEQVSEL 861
Cdd:TIGR02169 671 SEPAEL-QRLRERLEGLKRELSSLQSELRRIEN-----RLDE--LSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEEL 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465047 862 NKQKVTFEDSKVHAEQVLNDKESHIKTLTERLLKMKDWAamlgEDITDDDNLELEMNSESEngayldnppkgalkklihA 941
Cdd:TIGR02169 743 EEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEAL----NDLEARLSHSRIPEIQAE------------------L 800
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465047 942 AKLNASLKTLEGERNQIYIQLSEVDKTKEELTEHIKNLQTEQASLQSENTHFENEnqklqqklkvmtelyqenemklhrk 1021
Cdd:TIGR02169 801 SKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKE------------------------- 855
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465047 1022 ltvEENYRLEKEEKLskvdekishatEELETYRKRAKDLEEELErtihSYQGQIISHEKKahdnwlaARNAERNLNDLRK 1101
Cdd:TIGR02169 856 ---IENLNGKKEELE-----------EELEELEAALRDLESRLG----DLKKERDELEAQ-------LRELERKIEELEA 910
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1370465047 1102 ENAHNRQKLTETELKFELLEKDPYALDvPNTAFGREHSPYGPS 1144
Cdd:TIGR02169 911 QIEKKRKRLSELKAKLEALEEELSEIE-DPKGEDEEIPEEELS 952
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
942-1130 |
4.97e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.98 E-value: 4.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465047 942 AKLNASLKTLEGERNQIYIQLSEVDKTKEELTEHIKNLQTEQASLQSENTHFENENQKLQQKLKVMTELY---------- 1011
Cdd:COG4942 37 AELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELaellralyrl 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465047 1012 -----------QENEMKLHRKLTVEE---NYRLEKEEKLSKVDEKISHATEELETYRKRAKDLEEELERTIHSYQGQIIS 1077
Cdd:COG4942 117 grqpplalllsPEDFLDAVRRLQYLKylaPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAE 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1370465047 1078 HEKKAHDNWLAARNAERNLNDLRKENAHNRQKLTETELKFELLEKDPYALDVP 1130
Cdd:COG4942 197 RQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFA 249
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
793-1123 |
7.14e-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: 43.81 E-value: 7.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465047 793 KRIQSLEDESKSLKSQVAEAKMTFKIFQMNEERLKIAIKDALNENsQLQESQKQLLQEAEVWKEQV-SELNKQKVTFEDS 871
Cdd:pfam02463 153 ERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKL-QELKLKEQAKKALEYYQLKEkLELEEEYLLYLDY 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465047 872 KVHAEQVLNDKESHIKTLTERLLKMKdwaamlGEDITDDDNLELEMNSESENGAYLDNPPKGALKKLIHAAKLNASLKTL 951
Cdd:pfam02463 232 LKLNEERIDLLQELLRDEQEEIESSK------QEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKL 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465047 952 EGERNQIYIQLSEVDKTKEELTEHIKNLQTEQASLQSENTHFENENQKLQQKLKVMTELYQENEMKLHRKLTV------- 1024
Cdd:pfam02463 306 ERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKkkleser 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465047 1025 -------EENYRLEKEEKLSKVDEKISHATEELETYRKRAKDL---EEELERTIHSYQGQIIshEKKAHDNWLAARNAER 1094
Cdd:pfam02463 386 lssaaklKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEEleiLEEEEESIELKQGKLT--EEKEELEKQELKLLKD 463
|
330 340
....*....|....*....|....*....
gi 1370465047 1095 NLNDLRKENAHNRQKLTETELKFELLEKD 1123
Cdd:pfam02463 464 ELELKKSEDLLKETQLVKLQEQLELLLSR 492
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
783-1015 |
9.00e-04 |
|
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: 43.67 E-value: 9.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465047 783 EQDELMADISKRIQSLEDESKSLKSQVAEAKMTFK-IFQMNEERLKIAIKDALNENSQLQESQKQLLQEAEVWKEQVSEL 861
Cdd:pfam12128 280 ERQETSAELNQLLRTLDDQWKEKRDELNGELSAADaAVAKDRSELEALEDQHGAFLDADIETAAADQEQLPSWQSELENL 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465047 862 NKQKVTFEDSKVHAEQVLNDKESHIKT--------LTERLLKMKDWAAMLGEDITDD-DNLELEMNSESENGAYLDNPPK 932
Cdd:pfam12128 360 EERLKALTGKHQDVTAKYNRRRSKIKEqnnrdiagIKDKLAKIREARDRQLAVAEDDlQALESELREQLEAGKLEFNEEE 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465047 933 GALKKLIHAAK--LNASLKTLEgERNQIYIQLSEVDKTKEELTEHIKNLQTEQASLQSENTHFENENQKLQQKLKVMTEL 1010
Cdd:pfam12128 440 YRLKSRLGELKlrLNQATATPE-LLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEER 518
|
....*
gi 1370465047 1011 YQENE 1015
Cdd:pfam12128 519 QSALD 523
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
855-1066 |
9.05e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 43.46 E-value: 9.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465047 855 KEQVSELNKQKVTFEDSKVHAEQVLNDKESHIKTL-------TERLLKMKDWAAMLGEDI------TDDDNLELEMNSES 921
Cdd:PHA02562 173 KDKIRELNQQIQTLDMKIDHIQQQIKTYNKNIEEQrkkngenIARKQNKYDELVEEAKTIkaeieeLTDELLNLVMDIED 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465047 922 engayldnpPKGALKKLIHA-AKLNASLKTLEGERN------------QiyiQLSEVDKTKEELTEHIKNLQTeqaSLQS 988
Cdd:PHA02562 253 ---------PSAALNKLNTAaAKIKSKIEQFQKVIKmyekggvcptctQ---QISEGPDRITKIKDKLKELQH---SLEK 317
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370465047 989 ENTHFENENQKLQQklkvmtelYQENEMKLHrkltveenyrlEKEEKLSKVDEKIShateeleTYRKRAKDLEEELER 1066
Cdd:PHA02562 318 LDTAIDELEEIMDE--------FNEQSKKLL-----------ELKNKISTNKQSLI-------TLVDKAKKVKAAIEE 369
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
934-1123 |
1.02e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.39 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465047 934 ALKKLIHAAKLNASLKTLEGERNQIYIQLSEVDKTKEELTEHIKNLQTEQASLQSENTHFENENQK---LQQKL-KVMTE 1009
Cdd:COG1196 217 ELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELEleeAQAEEyELLAE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465047 1010 LYQENEMKLHRKLTVEENY--RLEKEEKLSKVDEKISHATEELETYRKRAKDLEEEL----------ERTIHSYQGQIIS 1077
Cdd:COG1196 297 LARLEQDIARLEERRRELEerLEELEEELAELEEELEELEEELEELEEELEEAEEELeeaeaelaeaEEALLEAEAELAE 376
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1370465047 1078 HEKKAHDNWLAARNAERNLNDLRKENAHNRQKLTETELKFELLEKD 1123
Cdd:COG1196 377 AEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEE 422
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
942-1067 |
1.04e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.22 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465047 942 AKLNASLKTLEGERNQI--YIQLSEVDKTKEELTEHIKNLQTEQASLQSENTHFENENQKLQQKLKVMTELYQENEMKLH 1019
Cdd:COG4717 105 EELEAELEELREELEKLekLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLE 184
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1370465047 1020 RKLTVEENYRLEKEEKLSKVDEKISHATEELETYRKRAKDLEEELERT 1067
Cdd:COG4717 185 QLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQL 232
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
788-1013 |
1.21e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.08 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465047 788 MADISKRIQSLEDESKSLKSQVAEAKMTFKIFQMNeerlkiaikdalNENSQLQESQKQLLQeaevwkeQVSELNKQKVT 867
Cdd:COG3206 170 REEARKALEFLEEQLPELRKELEEAEAALEEFRQK------------NGLVDLSEEAKLLLQ-------QLSELESQLAE 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465047 868 fedskvhAEQVLNDKESHIKTLTERLLKMKDWAAMLGED------ITDDDNLELEMNSESENgaYLDNPPKgalkklihA 941
Cdd:COG3206 231 -------ARAELAEAEARLAALRAQLGSGPDALPELLQSpviqqlRAQLAELEAELAELSAR--YTPNHPD--------V 293
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370465047 942 AKLNASLKTLEGERNQiyiqlsEVDKTKEELTEHIKNLQTEQASLQSENTHFENENQKLQQKLKVMTELYQE 1013
Cdd:COG3206 294 IALRAQIAALRAQLQQ------EAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLERE 359
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
715-1091 |
1.60e-03 |
|
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: 42.79 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465047 715 EVESSLKDASFEKEATEAQSLEVENQMFVEGSQISEATcEKLNRSNSELEDeilclekELKEEKSKHSEQDELMADI--- 791
Cdd:pfam05483 251 EKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELI-EKKDHLTKELED-------IKMSLQRSMSTQKALEEDLqia 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465047 792 SKRIQSLEDESKSLKSQVAEAKMTFKI----------------------FQMNEERLKIAIKDALNENSQLQESQKqLLQ 849
Cdd:pfam05483 323 TKTICQLTEEKEAQMEELNKAKAAHSFvvtefeattcsleellrteqqrLEKNEDQLKIITMELQKKSSELEEMTK-FKN 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465047 850 EAEVWKEQVSEL--NKQKVTFEDSKVH--AEQVLNDKESHIKTLTERLLKMKDWAAMLGEDITDDDNLELEMnseSENGA 925
Cdd:pfam05483 402 NKEVELEELKKIlaEDEKLLDEKKQFEkiAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEV---EDLKT 478
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465047 926 YLDNPPKGALKKLIHAAKLNASLKTLEGERNQIYIQLSE-------VDKTKEELTEHIKNLQTEQASLQSENTHFENENQ 998
Cdd:pfam05483 479 ELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKhqediinCKKQEERMLKQIENLEEKEMNLRDELESVREEFI 558
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465047 999 KLQQKLKVMTELYQENEMKLHRKLTVEE-----------NYRLEKEEKLSKVDE----------KISHATEELETYRKRA 1057
Cdd:pfam05483 559 QKGDEVKCKLDKSEENARSIEYEVLKKEkqmkilenkcnNLKKQIENKNKNIEElhqenkalkkKGSAENKQLNAYEIKV 638
|
410 420 430
....*....|....*....|....*....|....
gi 1370465047 1058 KDLEEELERTIHSYQGQIISHEKKAHDNWLAARN 1091
Cdd:pfam05483 639 NKLELELASAKQKFEEIIDNYQKEIEDKKISEEK 672
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
694-1113 |
1.61e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 42.65 E-value: 1.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465047 694 IEEKSKLLEKFSLVQKEYEGYEVESSLKDASFEKEATEAQSLEVEnqmfvegSQISEATCEKLNRSNSELEDEilclEKE 773
Cdd:TIGR00618 340 IEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTL-------QQQKTTLTQKLQSLCKELDIL----QRE 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465047 774 LKEEKSKHSEQDELMADISKRIQSLEDESKSLKSQVAEAKMTFKIFQMNEERLKIAIKDALNENSQLQESQKQLLQEAEV 853
Cdd:TIGR00618 409 QATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRK 488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465047 854 WKEQVSELNKQKVT---FEDSKVHAEQVLNDKEShIKTLTERLLKMKDWAAMLGEDItddDNLELEMNSESENGAYLDNP 930
Cdd:TIGR00618 489 KAVVLARLLELQEEpcpLCGSCIHPNPARQDIDN-PGPLTRRMQRGEQTYAQLETSE---EDVYHQLTSERKQRASLKEQ 564
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465047 931 PKGALKKL-IHAAKLNASLKTLEGERN-----QIYIQ--LSEVDKTKEELTEHIKNLQtEQASLQSENTHFENENQKLQQ 1002
Cdd:TIGR00618 565 MQEIQQSFsILTQCDNRSKEDIPNLQNitvrlQDLTEklSEAEDMLACEQHALLRKLQ-PEQDLQDVRLHLQQCSQELAL 643
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465047 1003 KL----KVMTELYQENE------MKLHRKLTVEENYRLEKE-----EKLSKVDEKISHATE---ELETYRKRAKDLEEEL 1064
Cdd:TIGR00618 644 KLtalhALQLTLTQERVrehalsIRVLPKELLASRQLALQKmqsekEQLTYWKEMLAQCQTllrELETHIEEYDREFNEI 723
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1370465047 1065 ERTIHSyQGQIISHEKKAHDNWLAARNAERNLNDLRKENAHNRQKLTET 1113
Cdd:TIGR00618 724 ENASSS-LGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVT 771
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
948-1072 |
1.75e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.59 E-value: 1.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465047 948 LKTLEGERNQIYIQLSEVDKTK---EELTEHIKNLQTEQASLQSENTHFENENQKLQQKLKVMTELYQENEMKLHR---K 1021
Cdd:COG4913 663 VASAEREIAELEAELERLDASSddlAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAaedL 742
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1370465047 1022 LTVEENYRLEK---EEKLSKVDEKISHA-TEELETYRKRAKDLEEELERTIHSYQ 1072
Cdd:COG4913 743 ARLELRALLEErfaAALGDAVERELRENlEERIDALRARLNRAEEELERAMRAFN 797
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
762-1074 |
2.22e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 42.20 E-value: 2.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465047 762 ELEDEILCLEKELKEEKSKHSEQDELMADIS------KRIQSLEDESKSLKSQVAEAKMTFKIFQMNEERLKIAIKDALN 835
Cdd:PRK01156 153 KILDEILEINSLERNYDKLKDVIDMLRAEISnidyleEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMD 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465047 836 ENSQLQESQKQLLQEAEVWKEQVSELNKQkvtfeDSKVHAEQVLNDKeshIKTLTERLLKMKDWAAMLG-EDITDDDNLE 914
Cdd:PRK01156 233 DYNNLKSALNELSSLEDMKNRYESEIKTA-----ESDLSMELEKNNY---YKELEERHMKIINDPVYKNrNYINDYFKYK 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465047 915 LEMNSESENGAYLDnppkGALKKLIHAAKlnaSLKTLEGERNQIYIQLSEVDKTKEELTEhiknLQTEQASLQSENTHFE 994
Cdd:PRK01156 305 NDIENKKQILSNID----AEINKYHAIIK---KLSVLQKDYNDYIKKKSRYDDLNNQILE----LEGYEMDYNSYLKSIE 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465047 995 NENQKLQQKLKVMTELYQENEMKLHRKLTVEENYRLEKEEKLSKVDEkISHATEELETYRKRAKDLEEELERTIHSYQGQ 1074
Cdd:PRK01156 374 SLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQD-ISSKVSSLNQRIRALRENLDELSRNMEMLNGQ 452
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
759-1108 |
2.42e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 42.13 E-value: 2.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465047 759 SNSELEDEILCLEKELKEEKSKHSEQDELMADISKRIQSLEDESKSLKSQVAEAKMTFKIF--QMNEERLKI------AI 830
Cdd:pfam12128 598 SEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLfdEKQSEKDKKnkalaeRK 677
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465047 831 KDALNENSQLQESQKQLLQEAEVWKEQVSElnkQKVTFEDSKVHAEQVL-NDKESHIKTLTERLLKMKDWAAMLGEDITD 909
Cdd:pfam12128 678 DSANERLNSLEAQLKQLDKKHQAWLEEQKE---QKREARTEKQAYWQVVeGALDAQLALLKAAIAARRSGAKAELKALET 754
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465047 910 DDNLELE-MNSESENGAYLDNPPKGALKKLIHAAKLNASL--------KTLEGERNQIYIQLSEVDKTKEELTEhikNLQ 980
Cdd:pfam12128 755 WYKRDLAsLGVDPDVIAKLKREIRTLERKIERIAVRRQEVlryfdwyqETWLQRRPRLATQLSNIERAISELQQ---QLA 831
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465047 981 TEQASLQSENTHFENENQKLQQKLKVMTElyqenemkLHRKLTVEENY--RLEKEEKLSKVDEKISHATEELETYRKRAK 1058
Cdd:pfam12128 832 RLIADTKLRRAKLEMERKASEKQQVRLSE--------NLRGLRCEMSKlaTLKEDANSEQAQGSIGERLAQLEDLKLKRD 903
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1370465047 1059 DLEEELERTIHSYQGQIISHEKKAHD-NWLAARNAERNLNDLRKENAHNRQ 1108
Cdd:pfam12128 904 YLSESVKKYVEHFKNVIADHSGSGLAeTWESLREEDHYQNDKGIRLLDYRK 954
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
669-890 |
2.58e-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: 2.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465047 669 RSFRSVRSRLY-----VGREKKLALMLSGLIEEKSKLLEKFSLVQKEYE--GYEVESSLKDASFEKEATEAQSLEVENQM 741
Cdd:TIGR02168 817 EEAANLRERLEslerrIAATERRLEDLEEQIEELSEDIESLAAEIEELEelIEELESELEALLNERASLEEALALLRSEL 896
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465047 742 FVEGSQIseatcEKLNRSNSELEDEilclekelkeekskHSEQDELMADISKRIQSLEDESKSLKSQVAE-AKMTFKIFQ 820
Cdd:TIGR02168 897 EELSEEL-----RELESKRSELRRE--------------LEELREKLAQLELRLEGLEVRIDNLQERLSEeYSLTLEEAE 957
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370465047 821 MNEERLKIAIKDALNENSQLQESQKQL-------LQEAEVWKEQVSELNKQKVTFEDSKVHAEQVLN--DKESHIKTLT 890
Cdd:TIGR02168 958 ALENKIEDDEEEARRRLKRLENKIKELgpvnlaaIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEeiDREARERFKD 1036
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
785-897 |
2.70e-03 |
|
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: 41.16 E-value: 2.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465047 785 DELMADISKRIQSLEDESKSLKSQVAEAKmtfKIFQMNEERLKIAIKDALNENSQLQESQKQLLQEAEVWKEQVSELNKQ 864
Cdd:smart00787 171 NSIKPKLRDRKDALEEELRQLKQLEDELE---DCDPTELDRAKEKLKKLLQEIMIKVKKLEELEEELQELESKIEDLTNK 247
|
90 100 110
....*....|....*....|....*....|....*..
gi 1370465047 865 KVTFEDSKVHAEQVLND----KESHIKTLTERLLKMK 897
Cdd:smart00787 248 KSELNTEIAEAEKKLEQcrgfTFKEIEKLKEQLKLLQ 284
|
|
| YabA |
COG4467 |
Regulator of replication initiation timing YabA [Replication, recombination and repair]; |
954-1021 |
4.31e-03 |
|
Regulator of replication initiation timing YabA [Replication, recombination and repair];
Pssm-ID: 443564 [Multi-domain] Cd Length: 107 Bit Score: 37.93 E-value: 4.31e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370465047 954 ERNQIYIQLSEVDKTKEELTEHIKNLQTEQASLQSENTHFENENQKLQQKLKVMTELYQENEMKLHRK 1021
Cdd:COG4467 2 DKKELFDRLSELEEQLGELLKELGELKDEVAELLEENARLRIENEHLRERLEELEKKKEKKAEKDIGE 69
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1031-1114 |
5.44e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.52 E-value: 5.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465047 1031 EKEEKLSKVDEKISHATEELETYRKRAKDLEEELERTihsyQGQIISHEKKAHDNWLAARNAERNLNDLRKENAHNRQKL 1110
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAAL----ERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
....
gi 1370465047 1111 TETE 1114
Cdd:COG4942 100 EAQK 103
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
942-1081 |
6.14e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.91 E-value: 6.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465047 942 AKLNASLKTLEGERNQIYIQLSEVDKTKE--ELTEHIKNLQTEQASLQSENTHFENENQKLQQKLKVMTELYQENEMKLH 1019
Cdd:COG4717 98 EELEEELEELEAELEELREELEKLEKLLQllPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQE 177
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370465047 1020 RKLTVEENYRLEKEEKLSKVDEKISHATEELETYRKRAKDLEEELERT---IHSYQGQIISHEKK 1081
Cdd:COG4717 178 ELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELeeeLEQLENELEAAALE 242
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
790-1065 |
7.38e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.41 E-value: 7.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465047 790 DISKRIQSLEDESKSLKSQVAEAKMTFKIFQMNEERLKIAIKDALNENSQLQESQKQL---LQEAEV----WKEQVSELN 862
Cdd:PRK02224 311 AVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELeseLEEAREavedRREEIEELE 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465047 863 KQKVTFEDSKVHAEQVLNDKESHIKTLTERLlkmkdwaAMLGEDITdddnlELEMNSESENGAYLDNppkgalKKLIHAA 942
Cdd:PRK02224 391 EEIEELRERFGDAPVDLGNAEDFLEELREER-------DELREREA-----ELEATLRTARERVEEA------EALLEAG 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465047 943 KLNASLKTLEGErnQIYIQLSEVDKTKEELTEHIKNLQTEQASLQSENTHF------ENENQKLQQKLKVMTELYQENEM 1016
Cdd:PRK02224 453 KCPECGQPVEGS--PHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAedlveaEDRIERLEERREDLEELIAERRE 530
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1370465047 1017 KLHRKLTVEENYRLEKEEKLSKVDEKISHAT---EELETYRKRAKDLEEELE 1065
Cdd:PRK02224 531 TIEEKRERAEELRERAAELEAEAEEKREAAAeaeEEAEEAREEVAELNSKLA 582
|
|
| SH3_MYO15 |
cd11884 |
Src Homology 3 domain of Myosin XV; This subfamily is composed of proteins with similarity to ... |
44-97 |
9.24e-03 |
|
Src Homology 3 domain of Myosin XV; This subfamily is composed of proteins with similarity to Myosin XVa. Myosin XVa is an unconventional myosin that is critical for the normal growth of mechanosensory stereocilia of inner ear hair cells. Mutations in the myosin XVa gene are associated with nonsyndromic hearing loss. Myosin XVa contains a unique N-terminal extension followed by a motor domain, light chain-binding IQ motifs, and a tail consisting of a pair of MyTH4-FERM tandems separated by a SH3 domain, and a PDZ domain. SH3 domains bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs; they play a role in the regulation of enzymes by intramolecular interactions, changing the subcellular localization of signal pathway components and mediate multiprotein complex assemblies.
Pssm-ID: 212817 [Multi-domain] Cd Length: 56 Bit Score: 35.76 E-value: 9.24e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1370465047 44 VSAMRDYRGPDCRYLNFTKGEEISVyVKLAGEREDLWA-GSKGKEFGYFPRDAVQ 97
Cdd:cd11884 2 VVAVRAYITRDQTLLSFHKGDVIKL-LPKEGPLDPGWLfGTLDGRSGAFPKEYVQ 55
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
731-1065 |
9.55e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 40.16 E-value: 9.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465047 731 EAQSLEVENQMFVEGSQISEATCEKLNRSNSELEDEILCLEKELKEEKSKHSEQDELMADISKRIQSLEDESKSLKSQVA 810
Cdd:pfam01576 6 EMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHELESRLE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465047 811 EakmtfkifqmNEERlkiaikdalneNSQLQESQKQLLQEAEVWKEQVSELN--KQKVTFEdsKVHAEQVLNDKESHIKT 888
Cdd:pfam01576 86 E----------EEER-----------SQQLQNEKKKMQQHIQDLEEQLDEEEaaRQKLQLE--KVTTEAKIKKLEEDILL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465047 889 LTERLLKMKDWAAMLGEDITDDDNLELEMNSESENGAYLDNppkgalKKLIHAAKLNASLKTLEGERNQIYIQLSEVDKT 968
Cdd:pfam01576 143 LEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKN------KHEAMISDLEERLKKEEKGRQELEKAKRKLEGE 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465047 969 KEELTEHIKNLQTEQASLQSENTHFENENQKLQQKLKvmTELYQENE-MKLHRKLtveENYRLEKEEKLSKvdEKISHAT 1047
Cdd:pfam01576 217 STDLQEQIAELQAQIAELRAQLAKKEEELQAALARLE--EETAQKNNaLKKIREL---EAQISELQEDLES--ERAARNK 289
|
330
....*....|....*...
gi 1370465047 1048 EEletyrKRAKDLEEELE 1065
Cdd:pfam01576 290 AE-----KQRRDLGEELE 302
|
|
| |
