|
Name |
Accession |
Description |
Interval |
E-value |
| SH3_MIA2 |
cd11892 |
Src Homology 3 domain of Melanoma Inhibitory Activity 2 protein; MIA2 is expressed ... |
31-103 |
1.02e-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: 158.46 E-value: 1.02e-45
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462540304 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 |
4.97e-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: 4.97e-36
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462540304 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 |
7.25e-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: 7.25e-25
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462540304 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 |
1.36e-14 |
|
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: 70.68 E-value: 1.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 30 KKCGDLECEALINRVSAMRDYRGPDCRYLNFTKGEEISVYVKLAGEREDLWAGS--------KGKEFGYFPRDAVQIEEV 101
Cdd:cd11890 2 KLCADQECSHPISIAVALQDYMAPDCRFIPIQRGQVVYVFSKLKGRGRLFWGGSvqgdyygeQAARLGYFPSSIVQEDQY 81
|
90
....*....|....*..
gi 2462540304 102 FISEEIQMSTKESDFLC 118
Cdd:cd11890 82 LKPGKVEVKTDKWDFYC 98
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
736-1066 |
1.68e-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: 69.32 E-value: 1.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 736 EVENQMFVEGSQISEATCE--KLNRSNSELEDEILCLEKELKEEKSKHSEQDELMADISKRIQSLEDESKSLKSQVAEAK 813
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKAlaELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELE 760
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 814 MTFKIFQMNEERLKIAIKDALNENSQLQESQKQLLQEAEVWKEQVSELNKQkvtfedskvhaeqvLNDKESHIKTLTERL 893
Cdd:TIGR02168 761 AEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAE--------------LTLLNEEAANLRERL 826
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 894 LKMKDWAAMLGEDITDDDNlELEMNSEsengayldnppkgalkkliHAAKLNASLKTLEGERNQIYIQLSEVDKTKEELT 973
Cdd:TIGR02168 827 ESLERRIAATERRLEDLEE-QIEELSE-------------------DIESLAAEIEELEELIEELESELEALLNERASLE 886
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 974 EHIKNLQTQQASLQSENTHFENENQKLQQKLKVMTEL-------YQENEMKLHRKL-TVEENYRLEKEEklskVDEKISH 1045
Cdd:TIGR02168 887 EALALLRSELEELSEELRELESKRSELRRELEELREKlaqlelrLEGLEVRIDNLQeRLSEEYSLTLEE----AEALENK 962
|
330 340
....*....|....*....|.
gi 2462540304 1046 ATEELETYRKRAKDLEEELER 1066
Cdd:TIGR02168 963 IEDDEEEARRRLKRLENKIKE 983
|
|
| MIAL |
cd11891 |
Melanoma Inhibitory Activity-Like protein; MIAL is specifically expressed in the cochlea and ... |
32-102 |
2.47e-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: 61.02 E-value: 2.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 32 CGDLECEALINRVSAMRDYRGPDCRYLNFTKGEEISVYVKLAGERE--DLWAGSKGKE--------FGYFPRDAVQIEEV 101
Cdd:cd11891 2 CADEECVYAISLARAEDDYNAPDCRFINIKKGQLIYVYSKLVKENGagEFWSGSVYSEryvdqmgiVGYFPSNLVKEQTV 81
|
.
gi 2462540304 102 F 102
Cdd:cd11891 82 Y 82
|
|
| SH3_2 |
pfam07653 |
Variant SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in ... |
46-99 |
6.52e-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: 6.52e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 2462540304 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 |
1.19e-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: 63.16 E-value: 1.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 682 REKKLALMLSGLIEEKSKL------LEKFSLVQK---EYEGYEVESSLKDASFEKEATEAQSLEVENQMfvegsqiseat 752
Cdd:TIGR02169 185 NIERLDLIIDEKRQQLERLrrerekAERYQALLKekrEYEGYELLKEKEALERQKEAIERQLASLEEEL----------- 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 753 cEKLNRSNSELEDEIlclekelkeekskhSEQDELMADISKRIQSL-EDESKSLKSQVAEAKMTFKIFQMNEERLKIAIK 831
Cdd:TIGR02169 254 -EKLTEEISELEKRL--------------EEIEQLLEELNKKIKDLgEEEQLRVKEKIGELEAEIASLERSIAEKERELE 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 832 DALNENSQLQESQKQLLQEAEVWKEQVSELNKQKVTFEDSKVHAEQVLNDKESHI-------KTLTERLLKMKDWAAMLG 904
Cdd:TIGR02169 319 DAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELeevdkefAETRDELKDYREKLEKLK 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 905 EDI----TDDDNLELEMNSESENGAYLDNPPKGA---LKKLIHAAK-LNASLKTLEGERNQIYIQLSEVDKTKEELTEHI 976
Cdd:TIGR02169 399 REInelkRELDRLQEELQRLSEELADLNAAIAGIeakINELEEEKEdKALEIKKQEWKLEQLAADLSKYEQELYDLKEEY 478
|
330
....*....|...
gi 2462540304 977 KNLQTQQASLQSE 989
Cdd:TIGR02169 479 DRVEKELSKLQRE 491
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
795-1123 |
4.99e-09 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 60.80 E-value: 4.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 795 IQSLEDESKSLKSQVAEAKMTFKIFQMNEERLKIAIKDALNENSQLQESQKQLLQEAEVWKEQVSELNKQKVTfedskvh 874
Cdd:TIGR04523 206 LKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQ------- 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 875 AEQVLNDKESHIKTLTERLLKMK-----DWAAMLGEDITDDDNLELEMNSE-SENGAYLDNppkgaLKKLIhaAKLNASL 948
Cdd:TIGR04523 279 NNKKIKELEKQLNQLKSEISDLNnqkeqDWNKELKSELKNQEKKLEEIQNQiSQNNKIISQ-----LNEQI--SQLKKEL 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 949 KTLEGERNQIYIQLSE-------VDKTKEELTEHIKNLQTQQASLQSENTHFENENQKLQQKLKVMTELYQ--ENEMKLH 1019
Cdd:TIGR04523 352 TNSESENSEKQRELEEkqneiekLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKEllEKEIERL 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 1020 RKLTVEENYRL--------EKEEKLSKVDEKISHATEELETYRKRAKDLEEELERTihsyQGQIISHEKKAHDNWLAARN 1091
Cdd:TIGR04523 432 KETIIKNNSEIkdltnqdsVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQK----QKELKSKEKELKKLNEEKKE 507
|
330 340 350
....*....|....*....|....*....|..
gi 2462540304 1092 AERNLNDLRKENAhnRQKLTETELKFELLEKD 1123
Cdd:TIGR04523 508 LEEKVKDLTKKIS--SLKEKIEKLESEKKEKE 537
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
695-1064 |
1.84e-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: 58.88 E-value: 1.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 695 EEKSKLLEKFS--LVQKEYEGYEVESSLKDASFEKEATEAQSL-----EVENQMFVEGSQIS--EATCEKLNRSNSELED 765
Cdd:TIGR04523 270 SEKQKELEQNNkkIKELEKQLNQLKSEISDLNNQKEQDWNKELkselkNQEKKLEEIQNQISqnNKIISQLNEQISQLKK 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 766 EILCLEKELKEEKSKHSEQDELMADISKRIQSLEDESKSLKSQVAEAKMTFKIFQMNEERLKIAIKDALNENSQLQESQK 845
Cdd:TIGR04523 350 ELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIE 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 846 QLLQEAEVWKEQVSELNKQKVTFEDSKVHAEQVLNDKESHIKTLTERLLKMKDWAAMLGEDITDDDNLELEMNSESENga 925
Cdd:TIGR04523 430 RLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKE-- 507
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 926 yLDNPPKgALKKLIhaAKLNASLKTLEGERNQIYIQLSEV---------DKTKEELTEHIKNLQTQQASLQSENTHFENE 996
Cdd:TIGR04523 508 -LEEKVK-DLTKKI--SSLKEKIEKLESEKKEKESKISDLedelnkddfELKKENLEKEIDEKNKEIEELKQTQKSLKKK 583
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462540304 997 NQKLQQKLKVMTElyqenemklhrkltveENYRLEKEekLSKVDEKISHATEELETYRKRAKDLEEEL 1064
Cdd:TIGR04523 584 QEEKQELIDQKEK----------------EKKDLIKE--IEEKEKKISSLEKELEKAKKENEKLSSII 633
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
698-1068 |
7.48e-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: 56.95 E-value: 7.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 698 SKLLEKFSLVQKEYEGYEVESSLKDASFEKEATEAQSLEVENQMFVEG-----SQIS--EATCEKLNRSNSELEDEIlcl 770
Cdd:TIGR04523 338 SQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEiknleSQINdlESKIQNQEKLNQQKDEQI--- 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 771 EKELKEEKSKHSEQDELMADISKR---IQSLEDESKSLKSQVAEAKMTFKIFQMNEERLKIAIKdalNENSQLQESQKQL 847
Cdd:TIGR04523 415 KKLQQEKELLEKEIERLKETIIKNnseIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSIN---KIKQNLEQKQKEL 491
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 848 LQ----------EAEVWKEQVSELNKQKVTFEDSKVHAEQVLNDKESHIKTLTERLLKMKD---WAAMLGEDITDDDNLE 914
Cdd:TIGR04523 492 KSkekelkklneEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFelkKENLEKEIDEKNKEIE 571
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 915 -LEMNSES-------------ENGAYLDNPPKGALKKLIHAAKLNASLKTLEGERNQIYIQLSEVDKTKEELTEHIKNLQ 980
Cdd:TIGR04523 572 eLKQTQKSlkkkqeekqelidQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIK 651
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 981 TQQASLQSENTHFENENQKLQQKLKVMTELYQ--ENEMKLHRKLTVEENYRLEKEEKLSKVDEKISHATEELETYRKRAK 1058
Cdd:TIGR04523 652 ETIKEIRNKWPEIIKKIKESKTKIDDIIELMKdwLKELSLHYKKYITRMIRIKDLPKLEEKYKEIEKELKKLDEFSKELE 731
|
410
....*....|
gi 2462540304 1059 DLEEELERTI 1068
Cdd:TIGR04523 732 NIIKNFNKKF 741
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
694-1126 |
1.86e-07 |
|
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: 55.88 E-value: 1.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 694 IEEKSKLLEKFSLVQKEYEGYEVEssLKDASFEKEATEAQSLEVENQMfVEGSQISEATCEKLNR--SNSELEDEILcle 771
Cdd:pfam05483 211 LEMHFKLKEDHEKIQHLEEEYKKE--INDKEKQVSLLLIQITEKENKM-KDLTFLLEESRDKANQleEKTKLQDENL--- 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 772 keLKEEKSKHSEQDELmADISKRIQSLEDESKSLKSQVAEAKMTfkIFQMNEERlkiaikdalneNSQLQESQKQLLQEA 851
Cdd:pfam05483 285 --KELIEKKDHLTKEL-EDIKMSLQRSMSTQKALEEDLQIATKT--ICQLTEEK-----------EAQMEELNKAKAAHS 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 852 EVwkeqVSELNKQKVTFEDSKVHAEQVLNDKESHIKTLTERLLKMkdwAAMLGEDITDDDNLELEMNSE----SENGAYL 927
Cdd:pfam05483 349 FV----VTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKK---SSELEEMTKFKNNKEVELEELkkilAEDEKLL 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 928 DNppKGALKKLIHAAK-----LNASLKTLEGERNQIYIQLSEVDKTKEELTEHIKNLQTQQASLQSENTHFENENQKLQQ 1002
Cdd:pfam05483 422 DE--KKQFEKIAEELKgkeqeLIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLL 499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 1003 KLKVMTElyQENEMKLHRKLTVEENYRLEKEE-----KLSKVDEKISHATEELETYRKRAKDLEEELERTIHSYQGQIIS 1077
Cdd:pfam05483 500 ENKELTQ--EASDMTLELKKHQEDIINCKKQEermlkQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARS 577
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 2462540304 1078 HEKKAHDNWLAARNAERNLNDLRKENAHNRQKLTETELKFELLEKDPYA 1126
Cdd:pfam05483 578 IEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSA 626
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
669-1066 |
1.89e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 55.84 E-value: 1.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 669 RSFRSVRSRLYVGREKKLALMLSGLIEEKSKLLEKFSLVQKEYEgyEVESSLKDASFEKEAteaqsLEVENQMFVEGSQI 748
Cdd:TIGR02169 662 PRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLD--ELSQELSDASRKIGE-----IEKEIEQLEQEEEK 734
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 749 SEATCEKLNRSNSELEDEILclekelkeekskhsEQDELMADISKRIQSLEDESKSLKSQVAEakmtfkifqmneerlki 828
Cdd:TIGR02169 735 LKERLEELEEDLSSLEQEIE--------------NVKSELKELEARIEELEEDLHKLEEALND----------------- 783
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 829 aIKDALNEnSQLQESQKQLlqeaevwkeqvSELNKQKVTFEDSKVHAEQVLNDK-------ESHIKTLTERLLKMKDWAA 901
Cdd:TIGR02169 784 -LEARLSH-SRIPEIQAEL-----------SKLEEEVSRIEARLREIEQKLNRLtlekeylEKEIQELQEQRIDLKEQIK 850
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 902 MLGEDItDDDNLEL-EMNSESENgayldnpPKGALKKLIhaaklnASLKTLEGERNQIYIQLSEVDKTKEELT------- 973
Cdd:TIGR02169 851 SIEKEI-ENLNGKKeELEEELEE-------LEAALRDLE------SRLGDLKKERDELEAQLRELERKIEELEaqiekkr 916
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 974 EHIKNLQTQQASLQSENTHFENENQKLQQklkvmtelYQENEMKLHrklTVEENyRLEKEEKLSKVDEKISHATEELETY 1053
Cdd:TIGR02169 917 KRLSELKAKLEALEEELSEIEDPKGEDEE--------IPEEELSLE---DVQAE-LQRVEEEIRALEPVNMLAIQEYEEV 984
|
410
....*....|...
gi 2462540304 1054 RKRAKDLEEELER 1066
Cdd:TIGR02169 985 LKRLDELKEKRAK 997
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
941-1123 |
2.08e-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: 2.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 941 AAKLNASLKTLEGERNQIYIQLSEVDKTKEELTEHIKNLQTQQASLQSENthfENENQKLQQKLKVMTELyQENEMKLHR 1020
Cdd:TIGR02168 693 IAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEV---EQLEERIAQLSKELTEL-EAEIEELEE 768
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 1021 KLTVEENYRLEKEEKLSKVDEKISHATEELETYRKRAKDLEEELERT---IHSYQGQIISHEKKAHDNWLAARNAERNLN 1097
Cdd:TIGR02168 769 RLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLneeAANLRERLESLERRIAATERRLEDLEEQIE 848
|
170 180
....*....|....*....|....*.
gi 2462540304 1098 DLRKENAHNRQKLTETELKFELLEKD 1123
Cdd:TIGR02168 849 ELSEDIESLAAEIEELEELIEELESE 874
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
791-1127 |
4.42e-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: 54.68 E-value: 4.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 791 ISKRIQSLEDESKS------LKSQVAEAKMTFKIFQMNEERLKI-AIKDALNENSQLQESQKQLLQEAEvwkEQVSELNK 863
Cdd:TIGR02168 198 LERQLKSLERQAEKaerykeLKAELRELELALLVLRLEELREELeELQEELKEAEEELEELTAELQELE---EKLEELRL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 864 QKVTFEDSKVHAEQVLNDKESHIKTLTERLLKMKDwaamlgeditdddNLELEMNSESENGAYLDNPPKGALKKLIHAAK 943
Cdd:TIGR02168 275 EVSELEEEIEELQKELYALANEISRLEQQKQILRE-------------RLANLERQLEELEAQLEELESKLDELAEELAE 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 944 LNASLKTLEGERNQIYIQLSEVDKTKEELTEHIKNLQTQQASLQSENTHFENENQKLQQKLKVM-TELYQENEMKLHRKL 1022
Cdd:TIGR02168 342 LEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLeARLERLEDRRERLQQ 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 1023 TVEENYRLEKEEKLSKVDEKISHATEELETYRKRAKDLEEELERTihsyQGQIishekkahdnwlaaRNAERNLNDLRKE 1102
Cdd:TIGR02168 422 EIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEEL----REEL--------------EEAEQALDAAERE 483
|
330 340
....*....|....*....|....*
gi 2462540304 1103 NAHNRQKLTETELKFELLEKDPYAL 1127
Cdd:TIGR02168 484 LAQLQARLDSLERLQENLEGFSEGV 508
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
783-1102 |
7.12e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.17 E-value: 7.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 783 EQDELMADISKRIQSLEDESKSLKSQVAEAKMTFKIFQMNEERLKIAIKDALNENSQLQESQKQLLQEAEVWKEQVSELN 862
Cdd:COG1196 257 ELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELE 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 863 KQKVTFEDSKVHAEQVLNDKESHIKTLTERLLKMKdwAAMLGEDITDDDNLELEMNSESEngayldnppkgALKKLIHAA 942
Cdd:COG1196 337 EELEELEEELEEAEEELEEAEAELAEAEEALLEAE--AELAEAEEELEELAEELLEALRA-----------AAELAAQLE 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 943 KLNASLKTLEGERNQIYIQLSEVDKTKEELTEHIKNLQTQQASLQSENTHFENENQKLQQKLKVMTELYQENEMKLHRkl 1022
Cdd:COG1196 404 ELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAE-- 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 1023 tveenyRLEKEEKLSKVDEKISHATEELETYRKRAKDLEEELERTIHSYQGQIISHEKKAHDNWLAARNAERNLNDLRKE 1102
Cdd:COG1196 482 ------LLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVED 555
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
824-1068 |
1.16e-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: 52.46 E-value: 1.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 824 ERLKIAIKDALNENSQLQESQKQLLQEAEVWKEQVSELNKQKVTFEDSKVHAEQVLNDKESHIKTLTERLLKMKDW-AAM 902
Cdd:COG4942 30 EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEElAEL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 903 LGEditdddnleLEMNSESENGAYLDNP--PKGALKKLIHAAKLNASLKTlegernqiyiQLSEVDKTKEELTEHIKNLQ 980
Cdd:COG4942 110 LRA---------LYRLGRQPPLALLLSPedFLDAVRRLQYLKYLAPARRE----------QAEELRADLAELAALRAELE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 981 TQQASLQSENTHFENENQKLQQKLKvmtelyqenemklhrkltveenyrlEKEEKLSKVDEKISHATEELETYRKRAKDL 1060
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKA-------------------------ERQKLLARLEKELAELAAELAELQQEAEEL 225
|
....*...
gi 2462540304 1061 EEELERTI 1068
Cdd:COG4942 226 EALIARLE 233
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
942-1066 |
1.31e-06 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 52.94 E-value: 1.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 942 AKLNASLKTLEGERNQIYIQLSEVDKTKEEltEHIKNLQTQQASLQSENTHFENENQKLQQKLKVMtelyqENEMKLHRK 1021
Cdd:COG2433 383 EELIEKELPEEEPEAEREKEHEERELTEEE--EEIRRLEEQVERLEAEVEELEAELEEKDERIERL-----ERELSEARS 455
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 2462540304 1022 ltvEENYRLEKEEKLSKVDEKISHATEELETYRKRAKDLEEELER 1066
Cdd:COG2433 456 ---EERREIRKDREISRLDREIERLERELEEERERIEELKRKLER 497
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
830-1021 |
2.47e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 51.37 E-value: 2.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 830 IKDALNENSQLQESQKQLLQEAEVWKEQVSELNKQKVTFEDSKVHAEQVLNDKESHIKTLTERLlkmKDWAAMLGEDITD 909
Cdd:COG3883 25 LSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREEL---GERARALYRSGGS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 910 DDNLELEMNSESeNGAYLDNppKGALKKLIHAAK-----LNASLKTLEGERNQIYIQLSEVDKTKEELTEHIKNLQTQQA 984
Cdd:COG3883 102 VSYLDVLLGSES-FSDFLDR--LSALSKIADADAdlleeLKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQA 178
|
170 180 190
....*....|....*....|....*....|....*..
gi 2462540304 985 SLQSENTHFENENQKLQQKLKVMTELYQENEMKLHRK 1021
Cdd:COG3883 179 EQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAA 215
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
783-1065 |
3.53e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.60 E-value: 3.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 783 EQDELMADISKRIQSLED------ESKSLKSQVAEAKMTFKIFQMNEERLKIAIKDA-------LNENSQLQESQKQLLQ 849
Cdd:PRK03918 142 ESDESREKVVRQILGLDDyenaykNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKekeleevLREINEISSELPELRE 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 850 EAEVWKEQVSELNKQKVTFEDSKVHAEQVLNDK---ESHIKTLTERLLKMKDWAAMLGEDITDDDNLELEMNSESENGAY 926
Cdd:PRK03918 222 ELEKLEKEVKELEELKEEIEELEKELESLEGSKrklEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEF 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 927 LDNppkgALKKLihaAKLNASLKTLEGERNQIYIQLSEVDKTK---EELTEHIKNLQTQQASLQSENTHFENENQKLQQK 1003
Cdd:PRK03918 302 YEE----YLDEL---REIEKRLSRLEEEINGIEERIKELEEKEerlEELKKKLKELEKRLEELEERHELYEEAKAKKEEL 374
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462540304 1004 LKVMTELYQENEMKLHRKLTVEENYRLEKEEKLSKVDEKIShateELETYRKRAKDLEEELE 1065
Cdd:PRK03918 375 ERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIG----ELKKEIKELKKAIEELK 432
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
690-1123 |
3.97e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.60 E-value: 3.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 690 LSGLIEEKSKLLEKFSLVQKEYEGYEVESSLKDASFEKEATEAQSLEVENQMFVEGSQISEATCEKLNRSNSELEdEILC 769
Cdd:PRK03918 212 ISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELK-ELKE 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 770 LEKELKEEKSKHSEQDELMADISKRIQSLEDESKSLKSQVAEA-KMTFKIfqmneERLKIAIKDALNENSQLQESQKqLL 848
Cdd:PRK03918 291 KAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELeEKEERL-----EELKKKLKELEKRLEELEERHE-LY 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 849 QEAEVWKEQVSELNKQKVTFEDSKVHAEqvLNDKESHIKTLTERLLKMKDWAAMLgEDITDDDNLELEMNSESEN----- 923
Cdd:PRK03918 365 EEAKAKKEELERLKKRLTGLTPEKLEKE--LEELEKAKEEIEEEISKITARIGEL-KKEIKELKKAIEELKKAKGkcpvc 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 924 GAYLDNPPKGALKKLIHA--AKLNASLKTLEGERNQIYIQLSEVDKTKEELTEHIKNLQT--QQASLQSENTHFENEnqK 999
Cdd:PRK03918 442 GRELTEEHRKELLEEYTAelKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELaeQLKELEEKLKKYNLE--E 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 1000 LQQKLKVMTELYQE-NEMKLHRKLTVEENYRLEK-EEKLSKVDEKISHATEELETYRKRAKDL----EEELERTIHSYqg 1073
Cdd:PRK03918 520 LEKKAEEYEKLKEKlIKLKGEIKSLKKELEKLEElKKKLAELEKKLDELEEELAELLKELEELgfesVEELEERLKEL-- 597
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 2462540304 1074 qiisheKKAHDNWLAARNAERNLNDLRKENAHNRQKLTETELKFELLEKD 1123
Cdd:PRK03918 598 ------EPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKR 641
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
715-1122 |
4.01e-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: 51.66 E-value: 4.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 715 EVESSLKDAsfeKEATEAQSLEVENQMFVEGSQISEATCEK--LNRSNSELEDEIlclekelkeekskhseqDELMADIS 792
Cdd:pfam15921 328 QLRSELREA---KRMYEDKIEELEKQLVLANSELTEARTERdqFSQESGNLDDQL-----------------QKLLADLH 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 793 KRIQ--SLEDE-SKSLKSQVAEAKMTFKIFQ-------MNEERLKIAIKDALNENSQLQESQKQLLQEAEVWKEQVSELN 862
Cdd:pfam15921 388 KREKelSLEKEqNKRLWDRDTGNSITIDHLRrelddrnMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLT 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 863 KQkvtFEDSKVHAEQVLNDKESHIKTLTERLLKMKDWAAMLGEDitdddnlELEMNSESENGAYLDNPPKGALKKLIHAA 942
Cdd:pfam15921 468 AQ---LESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEK-------ERAIEATNAEITKLRSRVDLKLQELQHLK 537
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 943 KLNASLKTLEGERNQIYIQLSEVDKTKEELTEHIKNLQT-------QQASLQSENTHFENE--NQKLQ-QKLKVMTE--- 1009
Cdd:pfam15921 538 NEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQlvgqhgrTAGAMQVEKAQLEKEinDRRLElQEFKILKDkkd 617
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 1010 -LYQENEMKL--------------HRKLTVEENYRLEKEEKLSKVD---EKISHATEELETYRKRAKDLEEELERTIHSY 1071
Cdd:pfam15921 618 aKIRELEARVsdlelekvklvnagSERLRAVKDIKQERDQLLNEVKtsrNELNSLSEDYEVLKRNFRNKSEEMETTTNKL 697
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462540304 1072 QGQIisheKKAHDNWLAARNAERNLN-----------DLRKENAHNRQKLTETELKFELLEK 1122
Cdd:pfam15921 698 KMQL----KSAQSELEQTRNTLKSMEgsdghamkvamGMQKQITAKRGQIDALQSKIQFLEE 755
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
683-1122 |
7.51e-06 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 50.56 E-value: 7.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 683 EKKLALMLSGLI--EEKSKLLEKFSLVQkEYEGYEVESSLK-------DASFEKEATEAQSLEVENQMFVEGSQISEATC 753
Cdd:pfam01576 158 EERISEFTSNLAeeEEKAKSLSKLKNKH-EAMISDLEERLKkeekgrqELEKAKRKLEGESTDLQEQIAELQAQIAELRA 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 754 EkLNRSNSELEDEILCLEKELKEEKSKHSEQDELMADISKRIQSLEDEskslKSQVAEAKMTFKIFQMNEERLKIAIKDA 833
Cdd:pfam01576 237 Q-LAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESE----RAARNKAEKQRRDLGEELEALKTELEDT 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 834 LNENSQLQESQKQLLQEaevwkeqVSELnkQKVTFEDSKVHAEQVLNDKESH---IKTLTERLLKMKDWAAML--GEDIT 908
Cdd:pfam01576 312 LDTTAAQQELRSKREQE-------VTEL--KKALEEETRSHEAQLQEMRQKHtqaLEELTEQLEQAKRNKANLekAKQAL 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 909 DDDNLELEMNSESENGAYLDNPPKGalkklihaaklnaslKTLEGERNQIYIQLSEVDKTKEELTEHIKNLQTQQASLQS 988
Cdd:pfam01576 383 ESENAELQAELRTLQQAKQDSEHKR---------------KKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSS 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 989 ENTHFENENQKLQQKLKVMtelyqenEMKLHrklTVEENYRLEKEEKLSkVDEKISHATEELETYRKRAKDLEE---ELE 1065
Cdd:pfam01576 448 LLNEAEGKNIKLSKDVSSL-------ESQLQ---DTQELLQEETRQKLN-LSTRLRQLEDERNSLQEQLEEEEEakrNVE 516
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 2462540304 1066 RTIHSYQGQIISHEKKAHDNWLAARNAERNLNDLRKENAHNRQKLTETELKFELLEK 1122
Cdd:pfam01576 517 RQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEK 573
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
708-1004 |
8.03e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 50.71 E-value: 8.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 708 QKEYEGYEVESSLK-----DASFEKEATEAQSLEVENQMFVEGSQISEATCEKLNRSNSELEDEIlclekelkeekskhS 782
Cdd:COG1196 219 KEELKELEAELLLLklrelEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELEL--------------E 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 783 EQDELMADISKRIQSLEDESKSLKSQVAEAkmtfkifQMNEERLKIAIKDALNENSQLQESQKQLLQEAEVWKEQVSELN 862
Cdd:COG1196 285 EAQAEEYELLAELARLEQDIARLEERRREL-------EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAE 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 863 KQKVTFEDSKVHAEQVLNDKESHIKTLTERLLKMKDWAAMLGEDITDDDNLELEMNSESEngayldnppkgalKKLIHAA 942
Cdd:COG1196 358 AELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLE-------------RLEEELE 424
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462540304 943 KLNASLKTLEGERNQIYIQLSEVDKTKEELTEHIKNLQTQQASLQSENTHFENENQKLQQKL 1004
Cdd:COG1196 425 ELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEEL 486
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
935-1081 |
1.56e-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: 48.00 E-value: 1.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 935 LKKLIHAAKLNASLKTLEGERNQIYIQLSEVDKTKEELTEHIKNLQTQQASLQSENTHFENENQKLQQKLKVMTEL---- 1010
Cdd:COG1579 6 LRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQlgnv 85
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462540304 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 |
1.71e-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: 49.67 E-value: 1.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 694 IEEKSKLLEKFSLVQKEYEGYEVESSLKDASF---EKEATEAQSLEVENQMFVEGSQISEATcEKLNRSNS---ELEDEI 767
Cdd:TIGR02168 205 LERQAEKAERYKELKAELRELELALLVLRLEElreELEELQEELKEAEEELEELTAELQELE-EKLEELRLevsELEEEI 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 768 LCLEKELKEEKSKHSEQDELMADISKRIQSLEDESKSLKSQVAEakmtfkifqmNEERLKIAIKDAlnenSQLQESQKQL 847
Cdd:TIGR02168 284 EELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEE----------LESKLDELAEEL----AELEEKLEEL 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 848 LQEAEVWKEQVSELNKQKVTFEDSKVHAEQVLNDKESHIKTLTERLLKMKDWAAMLGEDITD-DDNLElemNSESENGAY 926
Cdd:TIGR02168 350 KEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERlEDRRE---RLQQEIEEL 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 927 LDNPPKGALKKLIHA-AKLNASLKTLEGERNQIYIQLSEVDKTKEELTEHIKNLQTQQASLQSENTHFENENQKLQQKLK 1005
Cdd:TIGR02168 427 LKKLEEAELKELQAElEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSE 506
|
330 340 350
....*....|....*....|....*....|....*...
gi 2462540304 1006 VMTELYQENEMK------LHRKLTVEENYRLEKEEKLS 1037
Cdd:TIGR02168 507 GVKALLKNQSGLsgilgvLSELISVDEGYEAAIEAALG 544
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
695-987 |
2.64e-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: 2.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 695 EEKSKLLEKFSLVQKEYEgyEVESSLKDASFEKEATEAQSLEVENQMFVEGSQISEATCEKLNRSNSELEDEilclekel 774
Cdd:TIGR02169 737 ERLEELEEDLSSLEQEIE--NVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEE-------- 806
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 775 keekskHSEQDELMADISKRIQS-------LEDESKSLKSQVAEAKMTFKIFQMNEERLKIAIKDALNENSQLQESQKQL 847
Cdd:TIGR02169 807 ------VSRIEARLREIEQKLNRltlekeyLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDL 880
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 848 LQEAEVWKEQVSELNKQKVTFEDSKVHAEQVLNDKESHIKTLTERLlkmkdwaAMLGEDITDDDNLELEMNSESENgayl 927
Cdd:TIGR02169 881 ESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKL-------EALEEELSEIEDPKGEDEEIPEE---- 949
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 928 dNPPKGALKKLIHaaKLNASLKTLEGERNQIYIQLSEVDKTKEELTEHIKNLQTQQASLQ 987
Cdd:TIGR02169 950 -ELSLEDVQAELQ--RVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAIL 1006
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
782-1121 |
3.00e-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: 3.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 782 SEQDELmADISKRIQSLEDESKSLKSQVAEAKMtfkifQMNEerLKIAIKDALNENSQLQESQKQLLQEAEVWKEQVSEL 861
Cdd:TIGR02169 671 SEPAEL-QRLRERLEGLKRELSSLQSELRRIEN-----RLDE--LSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEEL 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 862 NKQKVTFEDSKVHAEQVLNDKESHIKTLTERLLKMKDWAamlgEDITDDDNLELEMNSESEngayldnppkgalkklihA 941
Cdd:TIGR02169 743 EEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEAL----NDLEARLSHSRIPEIQAE------------------L 800
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 942 AKLNASLKTLEGERNQIYIQLSEVDKTKEELTEHIKNLQTQQASLQSENTHFENEnqklqqklkvmtelyqenemklhrk 1021
Cdd:TIGR02169 801 SKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKE------------------------- 855
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 1022 ltvEENYRLEKEEKLskvdekishatEELETYRKRAKDLEEELErtihSYQGQIISHEKKahdnwlaARNAERNLNDLRK 1101
Cdd:TIGR02169 856 ---IENLNGKKEELE-----------EELEELEAALRDLESRLG----DLKKERDELEAQ-------LRELERKIEELEA 910
|
330 340
....*....|....*....|
gi 2462540304 1102 ENAHNRQKLTETELKFELLE 1121
Cdd:TIGR02169 911 QIEKKRKRLSELKAKLEALE 930
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
793-1123 |
3.22e-05 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 48.81 E-value: 3.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 793 KRIQSLEDESKSLKSQVAEAKMTFKIFQMNEERLKIAIKDALNENsQLQESQKQLLQEAEVWKEQV-SELNKQKVTFEDS 871
Cdd:pfam02463 153 ERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKL-QELKLKEQAKKALEYYQLKEkLELEEEYLLYLDY 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 872 KVHAEQVLNDKESHIKTLTERLLKMKdwaamlGEDITDDDNLELEMNSESENGAYLDNPPKGALKKLIHAAKLNASLKTL 951
Cdd:pfam02463 232 LKLNEERIDLLQELLRDEQEEIESSK------QEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKL 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 952 EGERNQIYIQLSEVDKTKEELTEHIKNLQTQQASLQSENTHFENENQKLQQKLKVMTELYQENEMKLHRKLTV------- 1024
Cdd:pfam02463 306 ERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKkkleser 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 1025 -------EENYRLEKEEKLSKVDEKISHATEELETYRKRAKDL---EEELERTIHSYQGQIIshEKKAHDNWLAARNAER 1094
Cdd:pfam02463 386 lssaaklKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEEleiLEEEEESIELKQGKLT--EEKEELEKQELKLLKD 463
|
330 340
....*....|....*....|....*....
gi 2462540304 1095 NLNDLRKENAHNRQKLTETELKFELLEKD 1123
Cdd:pfam02463 464 ELELKKSEDLLKETQLVKLQEQLELLLSR 492
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
948-1122 |
5.33e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.84 E-value: 5.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 948 LKTLEGERNQIYIQLSEVdktkEELTEHIKNLQTQQASLQSENTHFENENQKLQQKLKVMtELYQENEmKLHRKLTvEEN 1027
Cdd:COG4717 73 LKELEEELKEAEEKEEEY----AELQEELEELEEELEELEAELEELREELEKLEKLLQLL-PLYQELE-ALEAELA-ELP 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 1028 YRLE----KEEKLSKVDEKISHATEELETYRKrakDLEEELERTIHSYQGQIISHEKKAHDNWLAARNAERNLNDLRKEN 1103
Cdd:COG4717 146 ERLEeleeRLEELRELEEELEELEAELAELQE---ELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEEL 222
|
170
....*....|....*....
gi 2462540304 1104 AHNRQKLTETELKFELLEK 1122
Cdd:COG4717 223 EELEEELEQLENELEAAAL 241
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
715-1091 |
6.53e-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: 47.41 E-value: 6.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 715 EVESSLKDASFEKEATEAQSLEVENQMFVEGSQISEATcEKLNRSNSELEDeilclekELKEEKSKHSEQDELMADI--- 791
Cdd:pfam05483 251 EKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELI-EKKDHLTKELED-------IKMSLQRSMSTQKALEEDLqia 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 792 SKRIQSLEDESKSLKSQVAEAKMTFKI----------------------FQMNEERLKIAIKDALNENSQLQESQKqLLQ 849
Cdd:pfam05483 323 TKTICQLTEEKEAQMEELNKAKAAHSFvvtefeattcsleellrteqqrLEKNEDQLKIITMELQKKSSELEEMTK-FKN 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 850 EAEVWKEQVSEL--NKQKVTFEDSKVH--AEQVLNDKESHIKTLTERLLKMKDWAAMLGEDITDDDNLELEMnseSENGA 925
Cdd:pfam05483 402 NKEVELEELKKIlaEDEKLLDEKKQFEkiAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEV---EDLKT 478
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 926 YLDNPPKGALKKLIHAAKLNASLKTLEGERNQIYIQLSE-------VDKTKEELTEHIKNLQTQQASLQSENTHFENENQ 998
Cdd:pfam05483 479 ELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKhqediinCKKQEERMLKQIENLEEKEMNLRDELESVREEFI 558
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 999 KLQQKLKVMTELYQENEMKLHRKLTVEE-----------NYRLEKEEKLSKVDE----------KISHATEELETYRKRA 1057
Cdd:pfam05483 559 QKGDEVKCKLDKSEENARSIEYEVLKKEkqmkilenkcnNLKKQIENKNKNIEElhqenkalkkKGSAENKQLNAYEIKV 638
|
410 420 430
....*....|....*....|....*....|....
gi 2462540304 1058 KDLEEELERTIHSYQGQIISHEKKAHDNWLAARN 1091
Cdd:pfam05483 639 NKLELELASAKQKFEEIIDNYQKEIEDKKISEEK 672
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
793-1122 |
8.90e-05 |
|
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: 46.94 E-value: 8.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 793 KRIQSLEDESKSLKSQVAEAKMTFKIfqmNEERLKIAIKDALNENSQLQESQKQ---LLQEAEVWKEQVSELNKQKVTFE 869
Cdd:TIGR04523 68 EKINNSNNKIKILEQQIKDLNDKLKK---NKDKINKLNSDLSKINSEIKNDKEQknkLEVELNKLEKQKKENKKNIDKFL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 870 DSKVHAEQVLNDKESHIKTLTERLLKMKDWAAMLGEDITDDDNLELEMNSESENGAYLdnppKGALKKLIHAAK-LNASL 948
Cdd:TIGR04523 145 TEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELL----LSNLKKKIQKNKsLESQI 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 949 KTLEGERNQIYIQLSEVDKTKEELTEHIKNLQTQQASLQSENTH---------------------FENENQKLQQKLKVM 1007
Cdd:TIGR04523 221 SELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKikkqlsekqkeleqnnkkikeLEKQLNQLKSEISDL 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 1008 TELYQENEMK-LHRKLTVEENYRLEKEEKLSKVDEKISHATEELETYRKRAKDLE---EELERTIHSYQGQIISHEKKAH 1083
Cdd:TIGR04523 301 NNQKEQDWNKeLKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSEsenSEKQRELEEKQNEIEKLKKENQ 380
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 2462540304 1084 DNWLAARNAERNLNDLR-------KENAHNRQKLTETELKFELLEK 1122
Cdd:TIGR04523 381 SYKQEIKNLESQINDLEskiqnqeKLNQQKDEQIKKLQQEKELLEK 426
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
694-1113 |
1.71e-04 |
|
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: 46.12 E-value: 1.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 694 IEEKSKLLEKFSLVQKEYEGYEVESSLKDASFEKEATEAQSLEVEnqmfvegSQISEATCEKLNRSNSELEDEilclEKE 773
Cdd:TIGR00618 340 IEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTL-------QQQKTTLTQKLQSLCKELDIL----QRE 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 774 LKEEKSKHSEQDELMADISKRIQSLEDESKSLKSQVAEAKMTFKIFQMNEERLKIAIKDALNENSQLQESQKQLLQEAEV 853
Cdd:TIGR00618 409 QATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRK 488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 854 WKEQVSELNKQKVT---FEDSKVHAEQVLNDKEShIKTLTERLLKMKDWAAMLGEDItddDNLELEMNSESENGAYLDNP 930
Cdd:TIGR00618 489 KAVVLARLLELQEEpcpLCGSCIHPNPARQDIDN-PGPLTRRMQRGEQTYAQLETSE---EDVYHQLTSERKQRASLKEQ 564
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 931 PKGALKKL-IHAAKLNASLKTLEGERN-----QIYIQ--LSEVDKTKEELTEHIKNLQTQQAsLQSENTHFENENQKLQQ 1002
Cdd:TIGR00618 565 MQEIQQSFsILTQCDNRSKEDIPNLQNitvrlQDLTEklSEAEDMLACEQHALLRKLQPEQD-LQDVRLHLQQCSQELAL 643
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 1003 KL----KVMTELYQENE------MKLHRKLTVEENYRLEKE-----EKLSKVDEKISHATE---ELETYRKRAKDLEEEL 1064
Cdd:TIGR00618 644 KLtalhALQLTLTQERVrehalsIRVLPKELLASRQLALQKmqsekEQLTYWKEMLAQCQTllrELETHIEEYDREFNEI 723
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 2462540304 1065 ERTIHSyQGQIISHEKKAHDNWLAARNAERNLNDLRKENAHNRQKLTET 1113
Cdd:TIGR00618 724 ENASSS-LGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVT 771
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
855-1066 |
2.06e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 45.78 E-value: 2.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 855 KEQVSELNKQKVTFEDSKVHAEQVLNDKESHIKTL-------TERLLKMKDWAAMLGEDI------TDDDNLELEMNSES 921
Cdd:PHA02562 173 KDKIRELNQQIQTLDMKIDHIQQQIKTYNKNIEEQrkkngenIARKQNKYDELVEEAKTIkaeieeLTDELLNLVMDIED 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 922 engayldnpPKGALKKLIHA-AKLNASLKTLEGERN------------QiyiQLSEVDKTKEELTEHIKNLQTQqasLQS 988
Cdd:PHA02562 253 ---------PSAALNKLNTAaAKIKSKIEQFQKVIKmyekggvcptctQ---QISEGPDRITKIKDKLKELQHS---LEK 317
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462540304 989 ENTHFENENQKLQQklkvmtelYQENEMKLHrkltveenyrlEKEEKLSKVDEKIShateeleTYRKRAKDLEEELER 1066
Cdd:PHA02562 318 LDTAIDELEEIMDE--------FNEQSKKLL-----------ELKNKISTNKQSLI-------TLVDKAKKVKAAIEE 369
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
788-1013 |
2.11e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.78 E-value: 2.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 788 MADISKRIQSLEDESKSLKSQVAEAkmtfkifqmnEERLKiAIKDAlNENSQLQESQKQLLQeaevwkeQVSELNKQKVT 867
Cdd:COG3206 170 REEARKALEFLEEQLPELRKELEEA----------EAALE-EFRQK-NGLVDLSEEAKLLLQ-------QLSELESQLAE 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 868 fedskvhAEQVLNDKESHIKTLTERLLKMKDWAAMLGED------ITDDDNLELEMNSESENgaYLDNPPKgalkklihA 941
Cdd:COG3206 231 -------ARAELAEAEARLAALRAQLGSGPDALPELLQSpviqqlRAQLAELEAELAELSAR--YTPNHPD--------V 293
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462540304 942 AKLNASLKTLEGERNQiyiqlsEVDKTKEELTEHIKNLQTQQASLQSENTHFENENQKLQQKLKVMTELYQE 1013
Cdd:COG3206 294 IALRAQIAALRAQLQQ------EAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLERE 359
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
934-1130 |
2.21e-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: 45.14 E-value: 2.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 934 ALKKLIhaAKLNASLKTLEGERNQIYIQLSEVDKTKEELTEHIKNLQTQQASLQSENTHFENENQKLQQKLKVMTELY-- 1011
Cdd:COG4942 31 QLQQEI--AELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELae 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 1012 -------------------QENEMKLHRKLTVEE---NYRLEKEEKLSKVDEKISHATEELETYRKRAKDLEEELERTIH 1069
Cdd:COG4942 109 llralyrlgrqpplalllsPEDFLDAVRRLQYLKylaPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERA 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462540304 1070 SYQGQIISHEKKAHDNWLAARNAERNLNDLRKENAHNRQKLTETELKFELLEKDPYALDVP 1130
Cdd:COG4942 189 ALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFA 249
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
942-1067 |
2.45e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.53 E-value: 2.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 942 AKLNASLKTLEGERNQI--YIQLSEVDKTKEELTEHIKNLQTQQASLQSENTHFENENQKLQQKLKVMTELYQENEMKLH 1019
Cdd:COG4717 105 EELEAELEELREELEKLekLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLE 184
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 2462540304 1020 RKLTVEENYRLEKEEKLSKVDEKISHATEELETYRKRAKDLEEELERT 1067
Cdd:COG4717 185 QLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQL 232
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
731-1112 |
2.54e-04 |
|
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: 45.55 E-value: 2.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 731 EAQSLEVENQMFVEGSQISEATCEKLNRSNSELEDEILCLEKELKEEKSKHSEQDELMADISKRIQSLEDESKSLKSQVA 810
Cdd:pfam01576 6 EMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHELESRLE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 811 EakmtfkifqmNEERlkiaikdalneNSQLQESQKQLLQEAEVWKEQVSELN--KQKVTFEdsKVHAEQVLNDKESHIKT 888
Cdd:pfam01576 86 E----------EEER-----------SQQLQNEKKKMQQHIQDLEEQLDEEEaaRQKLQLE--KVTTEAKIKKLEEDILL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 889 LTERLLKMKDWAAMLGEDITDddnLELEMNSESENGAYLDnppKGALKKLIHAAKLNASLKTLEGERNQIYIQLSEVDKT 968
Cdd:pfam01576 143 LEDQNSKLSKERKLLEERISE---FTSNLAEEEEKAKSLS---KLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGE 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 969 KEELTEHIKNLQTQQASLQSENTHFENENQKLQQKLKvmTELYQENE-MKLHRKLtveENYRLEKEEKLSKvdEKISHAT 1047
Cdd:pfam01576 217 STDLQEQIAELQAQIAELRAQLAKKEEELQAALARLE--EETAQKNNaLKKIREL---EAQISELQEDLES--ERAARNK 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 1048 EEletyrKRAKDLEEELE----------------RTIHSYQGQIISHEKKAHDNwlAARNAERNLNDLRKENAHNRQKLT 1111
Cdd:pfam01576 290 AE-----KQRRDLGEELEalkteledtldttaaqQELRSKREQEVTELKKALEE--ETRSHEAQLQEMRQKHTQALEELT 362
|
.
gi 2462540304 1112 E 1112
Cdd:pfam01576 363 E 363
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
759-1108 |
3.06e-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: 45.60 E-value: 3.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 759 SNSELEDEILCLEKELKEEKSKHSEQDELMADISKRIQSLEDESKSLKSQVAEAKMTFKIF--QMNEERLKI------AI 830
Cdd:pfam12128 598 SEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLfdEKQSEKDKKnkalaeRK 677
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 831 KDALNENSQLQESQKQLLQEAEVWKEQVSElnkQKVTFEDSKVHAEQVL-NDKESHIKTLTERLLKMKDWAAMLGEDITD 909
Cdd:pfam12128 678 DSANERLNSLEAQLKQLDKKHQAWLEEQKE---QKREARTEKQAYWQVVeGALDAQLALLKAAIAARRSGAKAELKALET 754
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 910 DDNLELE-MNSESENGAYLDNPPKGALKKLIHAAKLNASL--------KTLEGERNQIYIQLSEVDKTKEELTEhikNLQ 980
Cdd:pfam12128 755 WYKRDLAsLGVDPDVIAKLKREIRTLERKIERIAVRRQEVlryfdwyqETWLQRRPRLATQLSNIERAISELQQ---QLA 831
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 981 TQQASLQSENTHFENENQKLQQKLKVMTElyqenemkLHRKLTVEENY--RLEKEEKLSKVDEKISHATEELETYRKRAK 1058
Cdd:pfam12128 832 RLIADTKLRRAKLEMERKASEKQQVRLSE--------NLRGLRCEMSKlaTLKEDANSEQAQGSIGERLAQLEDLKLKRD 903
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 2462540304 1059 DLEEELERTIHSYQGQIISHEKKAHD-NWLAARNAERNLNDLRKENAHNRQ 1108
Cdd:pfam12128 904 YLSESVKKYVEHFKNVIADHSGSGLAeTWESLREEDHYQNDKGIRLLDYRK 954
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
823-1128 |
4.65e-04 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 45.07 E-value: 4.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 823 EERLKIAIKDALNENSQ--LQESQKQLLQEaevwKEQVSELNKQKVTF-EDSKVHAEQVLNDKESHIKTLTERLLKMKDW 899
Cdd:COG5022 858 KKRFSLLKKETIYLQSAqrVELAERQLQEL----KIDVKSISSLKLVNlELESEIIELKKSLSSDLIENLEFKTELIARL 933
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 900 AAMLgEDITDDDNLELEMNSESENGAYLDNppKGALKKLihAAKLNASLKTLEGERNQIYIQLSEVDKTKEELTEHIKNL 979
Cdd:COG5022 934 KKLL-NNIDLEEGPSIEYVKLPELNKLHEV--ESKLKET--SEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQY 1008
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 980 QTQQASLQS--ENTHFENENQKLQQKLKVM-TELYQENEM-KLHRKLTVEENYrLEKEEKLSKVDEKISHATEELETYRK 1055
Cdd:COG5022 1009 GALQESTKQlkELPVEVAELQSASKIISSEsTELSILKPLqKLKGLLLLENNQ-LQARYKALKLRRENSLLDDKQLYQLE 1087
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462540304 1056 RAKDLEEELERTIHSYQGQIISHEKKAHDNwlaARNAERNLNDLRKENAHNRQKLTETELKFELLEKDPYALD 1128
Cdd:COG5022 1088 STENLLKTINVKDLEVTNRNLVKPANVLQF---IVAQMIKLNLLQEISKFLSQLVNTLEPVFQKLSVLQLELD 1157
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
783-1015 |
4.70e-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: 44.83 E-value: 4.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 783 EQDELMADISKRIQSLEDESKSLKSQVAEAKMTFK-IFQMNEERLKIAIKDALNENSQLQESQKQLLQEAEVWKEQVSEL 861
Cdd:pfam12128 280 ERQETSAELNQLLRTLDDQWKEKRDELNGELSAADaAVAKDRSELEALEDQHGAFLDADIETAAADQEQLPSWQSELENL 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 862 NKQKVTFEDSKVHAEQVLNDKESHIKT--------LTERLLKMKDWAAMLGEDITDD-DNLELEMNSESENGAYLDNPPK 932
Cdd:pfam12128 360 EERLKALTGKHQDVTAKYNRRRSKIKEqnnrdiagIKDKLAKIREARDRQLAVAEDDlQALESELREQLEAGKLEFNEEE 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 933 GALKKLIHAAK--LNASLKTLEgERNQIYIQLSEVDKTKEELTEHIKNLQTQQASLQSENTHFENENQKLQQKLKVMTEL 1010
Cdd:pfam12128 440 YRLKSRLGELKlrLNQATATPE-LLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEER 518
|
....*
gi 2462540304 1011 YQENE 1015
Cdd:pfam12128 519 QSALD 523
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
785-1121 |
5.38e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 44.44 E-value: 5.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 785 DELMADISKRIQSLEDESKSLKSQvaeakmtfkifqmnEERLKIAIKDALNensQLQESQKQLLQEAEVWKEQVSELNKQ 864
Cdd:PRK04778 111 ESLLDLIEEDIEQILEELQELLES--------------EEKNREEVEQLKD---LYRELRKSLLANRFSFGPALDELEKQ 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 865 KVTFEDSKVHAEQvLNDKESHIKTlTERLLKMKDWAAMLGEDITDddnlelemnsesengayldnppkgaLKKLIHAAKl 944
Cdd:PRK04778 174 LENLEEEFSQFVE-LTESGDYVEA-REILDQLEEELAALEQIMEE-------------------------IPELLKELQ- 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 945 naslKTLEGERNQI---YIQLSE---------VDKTKEELTEHIKNLQTQQASLQSENThfENENQKLQQKLKVMTELYq 1012
Cdd:PRK04778 226 ----TELPDQLQELkagYRELVEegyhldhldIEKEIQDLKEQIDENLALLEELDLDEA--EEKNEEIQERIDQLYDIL- 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 1013 ENEMKLHRKLtveenyrlekEEKLSKVDEKISHATEEletyrkrAKDLEEELERTIHSYQgqiISHEKKAHdnwlaARNA 1092
Cdd:PRK04778 299 EREVKARKYV----------EKNSDTLPDFLEHAKEQ-------NKELKEEIDRVKQSYT---LNESELES-----VRQL 353
|
330 340
....*....|....*....|....*....
gi 2462540304 1093 ERNLNDLRKENAHNRQKLTETELKFELLE 1121
Cdd:PRK04778 354 EKQLESLEKQYDEITERIAEQEIAYSELQ 382
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
934-1123 |
6.13e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.54 E-value: 6.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 934 ALKKLIHAAKLNASLKTLEGERNQIYIQLSEVDKTKEELTEHIKNLQTQQASLQSENTHFENENQK---LQQKL-KVMTE 1009
Cdd:COG1196 217 ELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELEleeAQAEEyELLAE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 1010 LYQENEMKLHRKLTVEENY--RLEKEEKLSKVDEKISHATEELETYRKRAKDLEEEL----------ERTIHSYQGQIIS 1077
Cdd:COG1196 297 LARLEQDIARLEERRRELEerLEELEEELAELEEELEELEEELEELEEELEEAEEELeeaeaelaeaEEALLEAEAELAE 376
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2462540304 1078 HEKKAHDNWLAARNAERNLNDLRKENAHNRQKLTETELKFELLEKD 1123
Cdd:COG1196 377 AEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEE 422
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
669-890 |
7.15e-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: 44.28 E-value: 7.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 669 RSFRSVRSRLY-----VGREKKLALMLSGLIEEKSKLLEKFSLVQKEYE--GYEVESSLKDASFEKEATEAQSLEVENQM 741
Cdd:TIGR02168 817 EEAANLRERLEslerrIAATERRLEDLEEQIEELSEDIESLAAEIEELEelIEELESELEALLNERASLEEALALLRSEL 896
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 742 FVEGSQIseatcEKLNRSNSELEDEilclekelkeekskHSEQDELMADISKRIQSLEDESKSLKSQVAE-AKMTFKIFQ 820
Cdd:TIGR02168 897 EELSEEL-----RELESKRSELRRE--------------LEELREKLAQLELRLEGLEVRIDNLQERLSEeYSLTLEEAE 957
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462540304 821 MNEERLKIAIKDALNENSQLQESQKQL-------LQEAEVWKEQVSELNKQKVTFEDSKVHAEQVLN--DKESHIKTLT 890
Cdd:TIGR02168 958 ALENKIEDDEEEARRRLKRLENKIKELgpvnlaaIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEeiDREARERFKD 1036
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
762-1074 |
8.52e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 43.74 E-value: 8.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 762 ELEDEILCLEKELKEEKSKHSEQDELMADIS------KRIQSLEDESKSLKSQVAEAKMTFKIFQMNEERLKIAIKDALN 835
Cdd:PRK01156 153 KILDEILEINSLERNYDKLKDVIDMLRAEISnidyleEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMD 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 836 ENSQLQESQKQLLQEAEVWKEQVSELNKQkvtfeDSKVHAEQVLNDKeshIKTLTERLLKMKDWAAMLG-EDITDDDNLE 914
Cdd:PRK01156 233 DYNNLKSALNELSSLEDMKNRYESEIKTA-----ESDLSMELEKNNY---YKELEERHMKIINDPVYKNrNYINDYFKYK 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 915 LEMNSESENGAYLDnppkGALKKLIHAAKlnaSLKTLEGERNQIYIQLSEVDKTKEELTEhiknLQTQQASLQSENTHFE 994
Cdd:PRK01156 305 NDIENKKQILSNID----AEINKYHAIIK---KLSVLQKDYNDYIKKKSRYDDLNNQILE----LEGYEMDYNSYLKSIE 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 995 NENQKLQQKLKVMTELYQENEMKLHRKLTVEENYRLEKEEKLSKVDEkISHATEELETYRKRAKDLEEELERTIHSYQGQ 1074
Cdd:PRK01156 374 SLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQD-ISSKVSSLNQRIRALRENLDELSRNMEMLNGQ 452
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
785-897 |
9.52e-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: 43.08 E-value: 9.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 785 DELMADISKRIQSLEDESKSLKSQVAEAKmtfKIFQMNEERLKIAIKDALNENSQLQESQKQLLQEAEVWKEQVSELNKQ 864
Cdd:smart00787 171 NSIKPKLRDRKDALEEELRQLKQLEDELE---DCDPTELDRAKEKLKKLLQEIMIKVKKLEELEEELQELESKIEDLTNK 247
|
90 100 110
....*....|....*....|....*....|....*..
gi 2462540304 865 KVTFEDSKVHAEQVLND----KESHIKTLTERLLKMK 897
Cdd:smart00787 248 KSELNTEIAEAEKKLEQcrgfTFKEIEKLKEQLKLLQ 284
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
790-1121 |
1.51e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.11 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 790 DISKRIQSLEDESKSLKSQVAEAKMTFKIFQMNEERLKIAIKDALNENSQLQESQKQLLQEAEVWKEQVSElnkqkvtfe 869
Cdd:PRK02224 311 AVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVED--------- 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 870 dskvhAEQVLNDKESHIKTLTERLlkmkdwaamlgEDITDD-DNLELEMNSESENgayldnppKGALKKLIhaAKLNASL 948
Cdd:PRK02224 382 -----RREEIEELEEEIEELRERF-----------GDAPVDlGNAEDFLEELREE--------RDELRERE--AELEATL 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 949 KTLEG--ERNQiyiQLSEVDKTKE-----ELTEHIKNL---QTQQASLQSENTHFENENQKLQQKLKVMTELyQENEMKL 1018
Cdd:PRK02224 436 RTARErvEEAE---ALLEAGKCPEcgqpvEGSPHVETIeedRERVEELEAELEDLEEEVEEVEERLERAEDL-VEAEDRI 511
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 1019 HRKLTVEENYRLEKEEKLSKVDEKishaTEELETYRKRAKDLEEELERTIHSYQgqiishekKAHDNWLAARNAERNLND 1098
Cdd:PRK02224 512 ERLEERREDLEELIAERRETIEEK----RERAEELRERAAELEAEAEEKREAAA--------EAEEEAEEAREEVAELNS 579
|
330 340
....*....|....*....|...
gi 2462540304 1099 LRKENAHNRQKLTETELKFELLE 1121
Cdd:PRK02224 580 KLAELKERIESLERIRTLLAAIA 602
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
781-1116 |
1.75e-03 |
|
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: 43.12 E-value: 1.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 781 HSEQDELMADISKRIQSLEDESKSLKS-QVAEAKMTFKIFQMNEERLKIAIKdalnenSQLQESQKQLLQEAEVWKEQVS 859
Cdd:TIGR01612 488 NSKQDNTVKLILMRMKDFKDIIDFMELyKPDEVPSKNIIGFDIDQNIKAKLY------KEIEAGLKESYELAKNWKKLIH 561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 860 ELNKQKVTFEDSKVHAeqvlndkESHIKTLTERLLKMKDwaamlgeDITDDDNLELEMNSESENGAYLDNPPKGA--LKK 937
Cdd:TIGR01612 562 EIKKELEEENEDSIHL-------EKEIKDLFDKYLEIDD-------EIIYINKLKLELKEKIKNISDKNEYIKKAidLKK 627
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 938 LIhaaklnaslktlegERNQIYIqlSEVDKTKE-ELTEHIKNLQTQQASLQSENTH-FENENQKLQQKLkvmTELYQENE 1015
Cdd:TIGR01612 628 II--------------ENNNAYI--DELAKISPyQVPEHLKNKDKIYSTIKSELSKiYEDDIDALYNEL---SSIVKENA 688
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 1016 MKlhrklTVEENYRLEK-EEKLSKVDEKISHATEE--------LETYRKRAKDLEEELERTIHSYqgqiISHE--KKAHD 1084
Cdd:TIGR01612 689 ID-----NTEDKAKLDDlKSKIDKEYDKIQNMETAtvelhlsnIENKKNELLDIIVEIKKHIHGE----INKDlnKILED 759
|
330 340 350
....*....|....*....|....*....|...
gi 2462540304 1085 NWLAARNAERNLNDLRKENAH-NRQKLTETELK 1116
Cdd:TIGR01612 760 FKNKEKELSNKINDYAKEKDElNKYKSKISEIK 792
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
785-1013 |
1.86e-03 |
|
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: 43.12 E-value: 1.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 785 DELMADISKRiQSLEDESKSLKSQVAEAKMTFKIFQMNEERL-----KIAIKDALNEN--------SQLQESQKQLLQEA 851
Cdd:TIGR01612 1486 NELKEHIDKS-KGCKDEADKNAKAIEKNKELFEQYKKDVTELlnkysALAIKNKFAKTkkdseiiiKEIKDAHKKFILEA 1564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 852 EVWKEQVSELNKQKVTFEDSKVH---AEQVLNDKESHIKTLTERLLKMKDWAAMLGEDITDDDNLE-----LEMNSE--- 920
Cdd:TIGR01612 1565 EKSEQKIKEIKKEKFRIEDDAAKndkSNKAAIDIQLSLENFENKFLKISDIKKKINDCLKETESIEkkissFSIDSQdte 1644
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 921 -SENGAYLD----------NPPKGALKKLIHAAKLNASLKTLEGERNQ--------IYIQLSEVDKTKEELTEHIKNL-- 979
Cdd:TIGR01612 1645 lKENGDNLNslqefleslkDQKKNIEDKKKELDELDSEIEKIEIDVDQhkknyeigIIEKIKEIAIANKEEIESIKELie 1724
|
250 260 270
....*....|....*....|....*....|....*..
gi 2462540304 980 QTQQASLQSENTH-FE--NENQKLQQKLKVMTELYQE 1013
Cdd:TIGR01612 1725 PTIENLISSFNTNdLEgiDPNEKLEEYNTEIGDIYEE 1761
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
936-1081 |
1.88e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.83 E-value: 1.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 936 KKLIHAAKLNASLKTLEGERNQIYIQLSEVDKTKEELTEHIKNLQTQQA---------SLQSENTHFENENQKLQQKLKV 1006
Cdd:COG4717 78 EELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQllplyqeleALEAELAELPERLEELEERLEE 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 1007 MTELYQENEM------KLHRKL-TVEENYRLEKEEKLSKVDEKISHATEELETYRKRAKDLEEELERT---IHSYQGQII 1076
Cdd:COG4717 158 LRELEEELEEleaelaELQEELeELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELeeeLEQLENELE 237
|
....*
gi 2462540304 1077 SHEKK 1081
Cdd:COG4717 238 AAALE 242
|
|
| YabA |
COG4467 |
Regulator of replication initiation timing YabA [Replication, recombination and repair]; |
954-1021 |
1.95e-03 |
|
Regulator of replication initiation timing YabA [Replication, recombination and repair];
Pssm-ID: 443564 [Multi-domain] Cd Length: 107 Bit Score: 39.08 E-value: 1.95e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462540304 954 ERNQIYIQLSEVDKTKEELTEHIKNLQTQQASLQSENTHFENENQKLQQKLKVMTELYQENEMKLHRK 1021
Cdd:COG4467 2 DKKELFDRLSELEEQLGELLKELGELKDEVAELLEENARLRIENEHLRERLEELEKKKEKKAEKDIGE 69
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
948-1072 |
2.20e-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: 2.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 948 LKTLEGERNQIYIQLSEVDKTK---EELTEHIKNLQTQQASLQSENTHFENENQKLQQKLKVMTELYQENEMKLHR---K 1021
Cdd:COG4913 663 VASAEREIAELEAELERLDASSddlAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAaedL 742
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 2462540304 1022 LTVEENYRLEK---EEKLSKVDEKISHA-TEELETYRKRAKDLEEELERTIHSYQ 1072
Cdd:COG4913 743 ARLELRALLEErfaAALGDAVERELRENlEERIDALRARLNRAEEELERAMRAFN 797
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
940-1123 |
3.23e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.43 E-value: 3.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 940 HAAKLNASLKTLEGERNQIYIQLSEVDKTKEELTEHIKNLQTQQASLQSENTHFENENQKLQQKL-KVMTELYQENE--M 1016
Cdd:COG4372 4 LGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELeQARSELEQLEEelE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 1017 KLHRKLTVEENYRLEKEEKLSKVDEKISHATEELETYRKRAKDLEEELERtihsyqgqiISHEKKAHDNWLAARNAErnL 1096
Cdd:COG4372 84 ELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQ---------LEAQIAELQSEIAEREEE--L 152
|
170 180
....*....|....*....|....*..
gi 2462540304 1097 NDLRKENAHNRQKLTETELKFELLEKD 1123
Cdd:COG4372 153 KELEEQLESLQEELAALEQELQALSEA 179
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
703-1093 |
3.55e-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: 42.08 E-value: 3.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 703 KFSLVQKEYEGYEVESSLKDASFEKEAT-----EAQSLEVENQMFVEGSQISEATCEKLNRsnsELEDEILCLEKELKEE 777
Cdd:pfam01576 235 RAQLAKKEEELQAALARLEEETAQKNNAlkkirELEAQISELQEDLESERAARNKAEKQRR---DLGEELEALKTELEDT 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 778 KSKHSEQDELMadiSKRIQ-------SLEDESKSLKSQVAE--AKMTFKIFQMNEE-----RLKIAI---KDAL-NENSQ 839
Cdd:pfam01576 312 LDTTAAQQELR---SKREQevtelkkALEEETRSHEAQLQEmrQKHTQALEELTEQleqakRNKANLekaKQALeSENAE 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 840 LQESQKQLLQeaevwKEQVSELNKQKVTFEDSKVHAEqvLNDKESHIKTLTERLLKMK----DWAAMLGEdiTDDDNLEL 915
Cdd:pfam01576 389 LQAELRTLQQ-----AKQDSEHKRKKLEGQLQELQAR--LSESERQRAELAEKLSKLQseleSVSSLLNE--AEGKNIKL 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 916 EMNSESENGAYLDNPpkgALKKLIHAAKLNAS--LKTLEGERNQIYIQLSEVDKTKEELTEHIKNLQTQQASLQsenthf 993
Cdd:pfam01576 460 SKDVSSLESQLQDTQ---ELLQEETRQKLNLStrLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMK------ 530
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 994 enenQKLQQKLKVMtELYQENEMKLHRKLtveENYRLEKEEKlskvdekiSHATEELETYRKRakdLEEELERTI--HSY 1071
Cdd:pfam01576 531 ----KKLEEDAGTL-EALEEGKKRLQREL---EALTQQLEEK--------AAAYDKLEKTKNR---LQQELDDLLvdLDH 591
|
410 420 430
....*....|....*....|....*....|.
gi 2462540304 1072 QGQIISH-EKK--------AHDNWLAARNAE 1093
Cdd:pfam01576 592 QRQLVSNlEKKqkkfdqmlAEEKAISARYAE 622
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1031-1114 |
3.99e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 41.29 E-value: 3.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 1031 EKEEKLSKVDEKISHATEELETYRKRAKDLEEELERTihsyQGQIISHEKKAHDNWLAARNAERNLNDLRKENAHNRQKL 1110
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAAL----ERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
....
gi 2462540304 1111 TETE 1114
Cdd:COG4942 100 EAQK 103
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
820-1067 |
4.11e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.05 E-value: 4.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 820 QMNEERLKIAIKDALNENSQLQESQKQLLQEAEVWKEQVSELNKQKvtfedsKVHAEQVLNDKEShIKTLTERLLKMKDW 899
Cdd:COG1340 7 SSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQV------KELREEAQELREK-RDELNEKVKELKEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 900 AAMLGEDITDDDNlELEMNSESENGAYLDNPPKGALKKLIhaAKL-----NASLkTLEGERnQIYIQLSEVD------KT 968
Cdd:COG1340 80 RDELNEKLNELRE-ELDELRKELAELNKAGGSIDKLRKEI--ERLewrqqTEVL-SPEEEK-ELVEKIKELEkelekaKK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 969 KEELTEHIKNLQTQQASLQSE-NTHFENEN---QKLQQKLKVMTELYQE-NEMK-----LHRKLtveenyrLEKEEKLSK 1038
Cdd:COG1340 155 ALEKNEKLKELRAELKELRKEaEEIHKKIKelaEEAQELHEEMIELYKEaDELRkeadeLHKEI-------VEAQEKADE 227
|
250 260
....*....|....*....|....*....
gi 2462540304 1039 VDEKISHATEELETYRKRAKDLEEELERT 1067
Cdd:COG1340 228 LHEEIIELQKELRELRKELKKLRKKQRAL 256
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
937-1113 |
4.21e-03 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 40.90 E-value: 4.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 937 KLIHAAKLNASLKTLEGErNQIYIQLSEVDKTKEELTEHIKNLQTQQASLQSENTHFENenqklQQKLKVMTelYQENEM 1016
Cdd:pfam09787 25 KLIASLKEGSGVEGLDSS-TALTLELEELRQERDLLREEIQKLRGQIQQLRTELQELEA-----QQQEEAES--SREQLQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 1017 KLHRKLTVEENYRLEKEEKLSKVDEKISHateeletyrkrakdLEEELERTIHSYQGQIISHEKKAHDnwLAARNAERNL 1096
Cdd:pfam09787 97 ELEEQLATERSARREAEAELERLQEELRY--------------LEEELRRSKATLQSRIKDREAEIEK--LRNQLTSKSQ 160
|
170
....*....|....*...
gi 2462540304 1097 NDLRKENAHNRQK-LTET 1113
Cdd:pfam09787 161 SSSSQSELENRLHqLTET 178
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
684-1123 |
5.04e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.20 E-value: 5.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 684 KKLALMLSGLIEEKSKLLEKFSLVQKEYEGYE-----VESSLKDA-SFEKEATEAQSLEVENQMFVEGSQISEATCEKLN 757
Cdd:PRK03918 289 KEKAEEYIKLSEFYEEYLDELREIEKRLSRLEeeingIEERIKELeEKEERLEELKKKLKELEKRLEELEERHELYEEAK 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 758 RSNSELEdeilclEKELKEEKSKHSEQDELMADISKRIQSLEDESKSLKSQVAEAKMTFKIFQMNEERLKIAIKDALNEN 837
Cdd:PRK03918 369 AKKEELE------RLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCG 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 838 SQL-QESQKQLLQEaevWKEQVSELNKQKVTFEDSKVHAEQVLNDKESHIKTlTERLLKMKDWAAMLgeditdddnLELE 916
Cdd:PRK03918 443 RELtEEHRKELLEE---YTAELKRIEKELKEIEEKERKLRKELRELEKVLKK-ESELIKLKELAEQL---------KELE 509
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 917 MNSESENGAYLDNPPKGALKKLIHAAKLNASLKTLEGERNQiyiqLSEVDKTKEELTEHIKNLQTQQASL--QSENTHFE 994
Cdd:PRK03918 510 EKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEK----LEELKKKLAELEKKLDELEEELAELlkELEELGFE 585
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 995 NEnQKLQQKLKVMTELYQE-NEMKLHRKltveenyRLE-KEEKLSKVDEKISHATEELETYRKRAKDLEEELERTIHSYq 1072
Cdd:PRK03918 586 SV-EELEERLKELEPFYNEyLELKDAEK-------ELErEEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKY- 656
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 2462540304 1073 gqiiSHEKKahdnwlaaRNAERNLNDLRKENAHNRQKLTETELKFELLEKD 1123
Cdd:PRK03918 657 ----SEEEY--------EELREEYLELSRELAGLRAELEELEKRREEIKKT 695
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
690-1122 |
5.48e-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: 41.19 E-value: 5.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 690 LSGLIEEKSKLLEK--FSLVQKEYEGYEVESSLKDA-SFEKEATEAqslEVENQMFVEGSQISEATCEKLNRSNSELE-D 765
Cdd:TIGR00606 438 LGRTIELKKEILEKkqEELKFVIKELQQLEGSSDRIlELDQELRKA---ERELSKAEKNSLTETLKKEVKSLQNEKADlD 514
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 766 EILCLEKELKEEKSKHSEQDELMADISKRIQSLEDESKSLKSQvaeakmtfkifqmNEERLKIAIKDALNEnSQLQESQK 845
Cdd:TIGR00606 515 RKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSR-------------HSDELTSLLGYFPNK-KQLEDWLH 580
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 846 QLLQEAEVWKEQVSELNKQKVTFEDSKVHAEQVLNDKESHIKTLTERLLKmkdwaAMLGEDITDD-DNLELEMNSESENG 924
Cdd:TIGR00606 581 SKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFD-----VCGSQDEESDlERLKEEIEKSSKQR 655
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 925 AYLDNppkgalkklihAAKLNASLKTLEGERNQIYIQLSEVD-KTKEELTEHIKNLQTQQASLQSENTHFENENQKLQQK 1003
Cdd:TIGR00606 656 AMLAG-----------ATAVYSQFITQLTDENQSCCPVCQRVfQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKR 724
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 1004 LKVMTELY--QENEMKLHRKLTVEENYRLEK-EEKLSKVDEKISHATEELETY---RKRAKDLEEELErTIHSYQGQIIS 1077
Cdd:TIGR00606 725 RDEMLGLApgRQSIIDLKEKEIPELRNKLQKvNRDIQRLKNDIEEQETLLGTImpeEESAKVCLTDVT-IMERFQMELKD 803
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 2462540304 1078 HEKKAHD--NWLAARNAERNLNDLRKENAHNRQKLTETELKFELLEK 1122
Cdd:TIGR00606 804 VERKIAQqaAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRK 850
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
935-1121 |
5.99e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 40.67 E-value: 5.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 935 LKKLIHAAKLNASLKTLEGERNQIYIQLSEVDKTKEELTE--HIKNLQTQQASL-----QSENTHFENENQ---KLQQKL 1004
Cdd:pfam13868 11 LNSKLLAAKCNKERDAQIAEKKRIKAEEKEEERRLDEMMEeeRERALEEEEEKEeerkeERKRYRQELEEQieeREQKRQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 1005 KVMTELYQENEMKLHRKLTVEENYRLEKEEKLSKVDEK---ISHATEELETYRKRAKDLEEELERTIHSYQGQIISHEKK 1081
Cdd:pfam13868 91 EEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLreeIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEE 170
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2462540304 1082 AHDNWLAARNA-ERNLNDLRKENAHNRQKLTE-TELKFELLE 1121
Cdd:pfam13868 171 REAEREEIEEEkEREIARLRAQQEKAQDEKAErDELRAKLYQ 212
|
|
| PRK13169 |
PRK13169 |
DNA replication initiation control protein YabA; |
954-1017 |
6.21e-03 |
|
DNA replication initiation control protein YabA;
Pssm-ID: 183876 Cd Length: 110 Bit Score: 37.92 E-value: 6.21e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462540304 954 ERNQIYIQLSEVDKTKEELTEHIKNLQTQQASLQSENTHFENENQKLQQKLKVMTELYQENEMK 1017
Cdd:PRK13169 2 DKKEIFDALDDLEQNLGVLLKELGALKKQLAELLEENTALRLENDKLRERLEELEAEEPAKEKK 65
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
942-1094 |
7.33e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.58 E-value: 7.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 942 AKLNASLKTLEGERNQIYIQLSEVDKTKEELTEHIKNLQTQQASLQSENTHFENENQKLQQKL-KVMTELYQE------- 1013
Cdd:COG3883 26 SELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELgERARALYRSggsvsyl 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 1014 -------------NEMKLHRKLTVEENYRLEK----EEKLSKVDEKISHATEELETYRKRAKDLEEELERTIHSYQGQI- 1075
Cdd:COG3883 106 dvllgsesfsdflDRLSALSKIADADADLLEElkadKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLa 185
|
170 180
....*....|....*....|
gi 2462540304 1076 -ISHEKKAHDNWLAARNAER 1094
Cdd:COG3883 186 qLSAEEAAAEAQLAELEAEL 205
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
943-1128 |
8.23e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.27 E-value: 8.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 943 KLNASLKTLEGERNQIyiqLSEVDKTKEELTEHIKNLQTQQASLQSENTHFENENQKLQQKLKVMTELYQENEmKLHRKL 1022
Cdd:COG4372 42 KLQEELEQLREELEQA---REELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAE-ELQEEL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 1023 --TVEENYRLEK-----EEKLSKVDEKISHATEELETYRKRAKDLEEELERTIHSYQGQIISHEKKAHDNWLAARNAERN 1095
Cdd:COG4372 118 eeLQKERQDLEQqrkqlEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAE 197
|
170 180 190
....*....|....*....|....*....|...
gi 2462540304 1096 LNDLRKENAHNRQKLTETELKFELLEKDPYALD 1128
Cdd:COG4372 198 KEEELAEAEKLIESLPRELAEELLEAKDSLEAK 230
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
688-1102 |
8.62e-03 |
|
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: 40.49 E-value: 8.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 688 LMLSGLIEEKSKLLEKFSLVQKEYEGYEVESSLKDASfEKEATEA----QSLEVENQMFVEGSQISEATCEKLNRSnSEL 763
Cdd:pfam05557 125 LELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQ-QSSLAEAeqriKELEFEIQSQEQDSEIVKNSKSELARI-PEL 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 764 EDEIlclekelkeekSKHSEQDELMADISKRIQSLEDESKSLKS---QVAEAKMTFKIFQMNEERL--------KIAIKD 832
Cdd:pfam05557 203 EKEL-----------ERLREHNKHLNENIENKLLLKEEVEDLKRkleREEKYREEAATLELEKEKLeqelqswvKLAQDT 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 833 ALNENS--QLQESQKQLLQEAEVWKEQVSELNKQKVTFEDSKVHAEQV----------LNDKESHIKTLTERL------- 893
Cdd:pfam05557 272 GLNLRSpeDLSRRIEQLQQREIVLKEENSSLTSSARQLEKARRELEQElaqylkkiedLNKKLKRHKALVRRLqrrvlll 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 894 -----------------LKMKDWAAMLGEDITDDDNLELEM---NSESENGAYLDNPPKGALKKLihAAKLNASLKTLeg 953
Cdd:pfam05557 352 tkerdgyrailesydkeLTMSNYSPQLLERIEEAEDMTQKMqahNEEMEAQLSVAEEELGGYKQQ--AQTLERELQAL-- 427
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 954 eRNQiyIQLSEVDKTKEELTEHIKNLQTqqasLQSENTHFENENQKLQQKLkVMTELYQENEMKLHRKLTVEENYRLEKE 1033
Cdd:pfam05557 428 -RQQ--ESLADPSYSKEEVDSLRRKLET----LELERQRLREQKNELEMEL-ERRCLQGDYDPKKTKVLHLSMNPAAEAY 499
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462540304 1034 EKLSKVDEKIShatEELETYRKRAKDLEEELertihsyqgqiishEKKAHDNWLAARNAERNLNDLRKE 1102
Cdd:pfam05557 500 QQRKNQLEKLQ---AEIERLKRLLKKLEDDL--------------EQVLRLPETTSTMNFKEVLDLRKE 551
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
788-1066 |
9.59e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.43 E-value: 9.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 788 MADISKRIQSLEDESKSLKSQVAEAKMTFKifqmNEERLkIAIKDALNENSQLQESQKQL--------LQEAEVWKEQVS 859
Cdd:PRK03918 461 LKRIEKELKEIEEKERKLRKELRELEKVLK----KESEL-IKLKELAEQLKELEEKLKKYnleelekkAEEYEKLKEKLI 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 860 ELNKQKVTFEDSKVHAEQVLNDK---ESHIKTLTERLLKMKDWAAMLGEDITDDDNLELEmNSESENGAYLDnpPKGALK 936
Cdd:PRK03918 536 KLKGEIKSLKKELEKLEELKKKLaelEKKLDELEEELAELLKELEELGFESVEELEERLK-ELEPFYNEYLE--LKDAEK 612
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462540304 937 KLihaAKLNASLKTLEGERNQIYIQLSEVDKTKEELTEHIKNLQT-----QQASLQSENTHFENENQKLQQKLKVMTELY 1011
Cdd:PRK03918 613 EL---EREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKkyseeEYEELREEYLELSRELAGLRAELEELEKRR 689
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 2462540304 1012 QENEMKLhRKLTVEENYRLEKEEKLskvdEKISHATEELETYRKRAKDLEEELER 1066
Cdd:PRK03918 690 EEIKKTL-EKLKEELEEREKAKKEL----EKLEKALERVEELREKVKKYKALLKE 739
|
|
| |
