|
Name |
Accession |
Description |
Interval |
E-value |
| SH3_MIA2 |
cd11892 |
Src Homology 3 domain of Melanoma Inhibitory Activity 2 protein; MIA2 is expressed ... |
31-103 |
7.79e-46 |
|
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: 158.85 E-value: 7.79e-46
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 694955909 31 KCGDLECETLINRVSAMRDYRGPDCRYLNFTKGEEISVYVKLAGEREDLWAGSKGKEFGYFPRDAVQIEEVFI 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 |
1.17e-35 |
|
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: 129.91 E-value: 1.17e-35
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 694955909 31 KCGDLECETLINRVSAMRDYRGPDCRYLNFTKGEEISVYVKLAGEREDLWAGSKG---KEFGYFPRDAVQIEEVFI 103
Cdd:cd11760 1 LCADAECSNPISRARALEDYHGPDCRFLNFKKGDTIYVYSKLAGERQDLWAGSVGgdaGLFGYFPKNLVQELKVYE 76
|
|
| SH3_MIA3 |
cd11893 |
Src Homology 3 domain of Melanoma Inhibitory Activity 3 protein; MIA3, also called TANGO or ... |
31-102 |
6.85e-25 |
|
Src Homology 3 domain of Melanoma Inhibitory Activity 3 protein; MIA3, also called TANGO or TANGO1, acts as a tumor suppressor of malignant melanoma. It is downregulated or lost in melanoma cells lines. Unlike other MIA family members, MIA3 is widely expressed except in hematopoietic cells. MIA3 is an ER resident transmembrane protein that is required for the loading of collagen VII into transport vesicles. SNPs in the MIA3 gene have been associated with coronary arterial disease and myocardial infarction. MIA3 contains an N-terminal SH3-like domain, similar to MIA. It is a member of the recently identified family that also includes MIA, MIAL, and MIA2. MIA is a single domain protein that adopts a SH3 domain-like fold; it contains an additional antiparallel beta sheet and two disulfide bonds compared to classical SH3 domains. Unlike classical SH3 domains, MIA does not bind proline-rich ligands.
Pssm-ID: 212826 Cd Length: 73 Bit Score: 99.15 E-value: 6.85e-25
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 694955909 31 KCGDLECETLINRVSAMRDYRGPDCRYLNFTKGEEISVYVKLAGEREDLWAGSKGKEFGYFPRDAVQIEEVF 102
Cdd:cd11893 1 RCADEECSMLLCRGKAVKDFTGPDCRFLSFKKGETIYVYYKLSGRRTDLWAGSVGFDFGYFPKDLLDVNHLY 72
|
|
| MIA |
cd11890 |
Melanoma Inhibitory Activity protein; MIA is a single domain protein that adopts a Src ... |
30-118 |
1.42e-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: 1.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 30 KKCGDLECETLINRVSAMRDYRGPDCRYLNFTKGEEISVYVKLAGEREDLWAGS--------KGKEFGYFPRDAVQIEEV 101
Cdd:cd11890 2 KLCADQECSHPISIAVALQDYMAPDCRFIPIQRGQVVYVFSKLKGRGRLFWGGSvqgdyygeQAARLGYFPSSIVQEDQY 81
|
90
....*....|....*..
gi 694955909 102 FISEEIQMSTKESDFLC 118
Cdd:cd11890 82 LKPGKVEVKTDKWDFYC 98
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
682-975 |
1.34e-12 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 72.79 E-value: 1.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 682 REKKLALMLSGLIEEKSKL------LEKFSLVQK---EYEGYEVESSLKDASFEKEATEAQ--SLEATCEKLNRSNSELE 750
Cdd:TIGR02169 185 NIERLDLIIDEKRQQLERLrrerekAERYQALLKekrEYEGYELLKEKEALERQKEAIERQlaSLEEELEKLTEEISELE 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 751 DEIlclekelkeekskhSERDELMADISKRIQSL-EDESKSLKSQVAEAKMTFKIFQMNEERLKIAIKDALNENSQLQES 829
Cdd:TIGR02169 265 KRL--------------EEIEQLLEELNKKIKDLgEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAE 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 830 QKQLLQEAEVWKEQVSELNKQKVTFEDSEVHAEQVLNDKESHI-------KTLTERLLKMKDWAAMLGEDI----TDDDN 898
Cdd:TIGR02169 331 IDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELeevdkefAETRDELKDYREKLEKLKREInelkRELDR 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 899 LELEMNSESENGAYLDNPPKGA---LKKLIHAAK-LNASLKTLEGERNQIYIQLSEVDKTKEELTEHIKNLQTEQASLQS 974
Cdd:TIGR02169 411 LQEELQRLSEELADLNAAIAGIeakINELEEEKEdKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQR 490
|
.
gi 694955909 975 E 975
Cdd:TIGR02169 491 E 491
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
715-1052 |
1.69e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 72.40 E-value: 1.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 715 EVESSLKDASFEKEATEAQ--SLEATCEKLNRSNSELEDEILCLEKELKEEKSKHSERDELMADISKRIQSLEDESKSLK 792
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKiaELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLS 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 793 SQVAEAKMTFKIFQMNEERLKIAIKDALNENSQLQESQKQLLQEAEVWKEQVSELNKQkvtfedsevhaeqvLNDKESHI 872
Cdd:TIGR02168 754 KELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAE--------------LTLLNEEA 819
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 873 KTLTERLLKMKDWAAMLGEDITDDDNlELEMNSEsengayldnppkgalkkliHAAKLNASLKTLEGERNQIYIQLSEVD 952
Cdd:TIGR02168 820 ANLRERLESLERRIAATERRLEDLEE-QIEELSE-------------------DIESLAAEIEELEELIEELESELEALL 879
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 953 KTKEELTEHIKNLQTEQASLQSENTHFENENQKLQQKLKVMTEL-------YQENEMKLHRKL-TVEENYRLEKEEklsk 1024
Cdd:TIGR02168 880 NERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKlaqlelrLEGLEVRIDNLQeRLSEEYSLTLEE---- 955
|
330 340
....*....|....*....|....*...
gi 694955909 1025 VDEKISHATEELETYRKRAKDLEEELER 1052
Cdd:TIGR02168 956 AEALENKIEDDEEEARRRLKRLENKIKE 983
|
|
| MIAL |
cd11891 |
Melanoma Inhibitory Activity-Like protein; MIAL is specifically expressed in the cochlea and ... |
32-102 |
2.12e-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: 2.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 32 CGDLECETLINRVSAMRDYRGPDCRYLNFTKGEEISVYVKLAGERE--DLWAGSKGKE--------FGYFPRDAVQIEEV 101
Cdd:cd11891 2 CADEECVYAISLARAEDDYNAPDCRFINIKKGQLIYVYSKLVKENGagEFWSGSVYSEryvdqmgiVGYFPSNLVKEQTV 81
|
.
gi 694955909 102 F 102
Cdd:cd11891 82 Y 82
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
733-1061 |
2.60e-10 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 65.04 E-value: 2.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 733 QSLEATCEKLNRSNSELEDEIlclekelkeekskhSERDELMADISKRIQSLEDESKSLKSQVAEAKMTFKIFQMNEERL 812
Cdd:TIGR04523 345 SQLKKELTNSESENSEKQREL--------------EEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQK 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 813 KIAIKDALNENSQLQESQKQLLQEAEVWKEQVSELNKQKVTFEDSEVHAEQVLNDKESHIKTLTERLLKMKDWAAMLGED 892
Cdd:TIGR04523 411 DEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKE 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 893 ITDDDNLELEMNSESENgayLDNPPKgALKKLIhaAKLNASLKTLEGERNQIYIQLSEV---------DKTKEELTEHIK 963
Cdd:TIGR04523 491 LKSKEKELKKLNEEKKE---LEEKVK-DLTKKI--SSLKEKIEKLESEKKEKESKISDLedelnkddfELKKENLEKEID 564
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 964 NLQTEQASLQSENTHFENENQKLQQKLKVmtelYQENEMKLHRKLTveenyrlEKEEKLSKVDEKISHATEE---LETYR 1040
Cdd:TIGR04523 565 EKNKEIEELKQTQKSLKKKQEEKQELIDQ----KEKEKKDLIKEIE-------EKEKKISSLEKELEKAKKEnekLSSII 633
|
330 340
....*....|....*....|.
gi 694955909 1041 KRAKDLEEELERTIHSYQGQI 1061
Cdd:TIGR04523 634 KNIKSKKNKLKQEVKQIKETI 654
|
|
| SH3_2 |
pfam07653 |
Variant SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in ... |
46-99 |
6.65e-10 |
|
Variant SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in signal transduction related to cytoskeletal organization. First described in the Src cytoplasmic tyrosine kinase. The structure is a partly opened beta barrel.
Pssm-ID: 429575 [Multi-domain] Cd Length: 54 Bit Score: 56.07 E-value: 6.65e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 694955909 46 AMRDYRGPDCRYLNFTKGEEISVYVKlagEREDLWAGSKGKEFGYFPRDAVQIE 99
Cdd:pfam07653 4 VIFDYVGTDKNGLTLKKGDVVKVLGK---DNDGWWEGETGGRVGLVPSTAVEEI 54
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
694-1054 |
5.89e-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: 57.34 E-value: 5.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 694 IEEKSKLLEKfslVQKEYEGYEVESslkdasfEKEATEAQSLEATCEKLNRSNSELEDEILCLEKELKEEKSKHSERDEL 773
Cdd:TIGR04523 365 LEEKQNEIEK---LKKENQSYKQEI-------KNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKET 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 774 MADISKRIQSLEDESKSLKSQVAEAKMTFKIFQMNEERLKIAIKdalNENSQLQESQKQLLQ----------EAEVWKEQ 843
Cdd:TIGR04523 435 IIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSIN---KIKQNLEQKQKELKSkekelkklneEKKELEEK 511
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 844 VSELNKQKVTFEDSEVHAEQVLNDKESHIKTLTERLLKMKD---WAAMLGEDITDDDNLE-LEMNSES------------ 907
Cdd:TIGR04523 512 VKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFelkKENLEKEIDEKNKEIEeLKQTQKSlkkkqeekqeli 591
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 908 -ENGAYLDNPPKGALKKLIHAAKLNASLKTLEGERNQIYIQLSEVDKTKEELTEHIKNLQTEQASLQSENTHFENENQKL 986
Cdd:TIGR04523 592 dQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKES 671
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 987 QQKLKVMTELYQ--ENEMKLHRKLTVEENYRLEKEEKLSKVDEKISHATEELETYRKRAKDLEEELERTI 1054
Cdd:TIGR04523 672 KTKIDDIIELMKdwLKELSLHYKKYITRMIRIKDLPKLEEKYKEIEKELKKLDEFSKELENIIKNFNKKF 741
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
682-1112 |
1.11e-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: 56.65 E-value: 1.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 682 REKKLALMLSGLIEEKSKLLE-KFSLVQKEYEGYEVEsslkdasfEKEATEAQSLEATCEKLNRSNSELEDeilclekel 760
Cdd:pfam05483 238 KEKQVSLLLIQITEKENKMKDlTFLLEESRDKANQLE--------EKTKLQDENLKELIEKKDHLTKELED--------- 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 761 keekskhserdelmadISKRIQSLEDESKSLKSQVAEAKMTfkIFQMNEERlkiaikdalneNSQLQESQKQLLQEAEVw 840
Cdd:pfam05483 301 ----------------IKMSLQRSMSTQKALEEDLQIATKT--ICQLTEEK-----------EAQMEELNKAKAAHSFV- 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 841 keqVSELNKQKVTFEDSEVHAEQVLNDKESHIKTLTERLLKMkdwAAMLGEDITDDDNLELEMNSE----SENGAYLDNp 916
Cdd:pfam05483 351 ---VTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKK---SSELEEMTKFKNNKEVELEELkkilAEDEKLLDE- 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 917 pKGALKKLIHAAK-----LNASLKTLEGERNQIYIQLSEVDKTKEELTEHIKNLQTEQASLQSENTHFENENQKLQQKLK 991
Cdd:pfam05483 424 -KKQFEKIAEELKgkeqeLIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENK 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 992 VMTElyQENEMKLHRKLTVEENYRLEKEE-----KLSKVDEKISHATEELETYRKRAKDLEEELERTIHSYQGQIISHEK 1066
Cdd:pfam05483 503 ELTQ--EASDMTLELKKHQEDIINCKKQEermlkQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEY 580
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 694955909 1067 KAHDNWLAARNAERNLNDLRKENAHNRQKLTETELKFELLEKDPYA 1112
Cdd:pfam05483 581 EVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSA 626
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
682-1109 |
1.15e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 56.61 E-value: 1.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 682 REKKLALMLSGLIEEKSKLLEKfSLVQKEYEGYEVESSLKDASFEKEATEA--QSLEATCEKLNRSNSELEDEilcleke 759
Cdd:PRK03918 179 ERLEKFIKRTENIEELIKEKEK-ELEEVLREINEISSELPELREELEKLEKevKELEELKEEIEELEKELESL------- 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 760 lkeeKSKHSERDELMADISKRIQSLEDESKSLKSQVAEAKmtfKIFQMNEE--RLKIAIKDALNENSQLQESQKQLLQEA 837
Cdd:PRK03918 251 ----EGSKRKLEEKIRELEERIEELKKEIEELEEKVKELK---ELKEKAEEyiKLSEFYEEYLDELREIEKRLSRLEEEI 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 838 EVWKEQVSELNKqkvtfedsevhaeqvlndKESHIKTLTERLLKMKDWAAMLGEDITDDDNLELEMNSESENGAYLDNPP 917
Cdd:PRK03918 324 NGIEERIKELEE------------------KEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLT 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 918 KGALKKLIHAA------------KLNASLKTLEGERNQIYIQLSEVDKTK-------EELTEH-----IKNLQTEQASLQ 973
Cdd:PRK03918 386 PEKLEKELEELekakeeieeeisKITARIGELKKEIKELKKAIEELKKAKgkcpvcgRELTEEhrkelLEEYTAELKRIE 465
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 974 SENTHFENENQKLQQKLKVMtELYQENEMKLHRKLTVEENYRlEKEEKLSKVD-EKISHATEELETYRKRA-------KD 1045
Cdd:PRK03918 466 KELKEIEEKERKLRKELREL-EKVLKKESELIKLKELAEQLK-ELEEKLKKYNlEELEKKAEEYEKLKEKLiklkgeiKS 543
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 1046 LEEELERtIHSYQGQIISHEKK-----------------------------------AHDNWLAARNAERNLNDLRKENA 1090
Cdd:PRK03918 544 LKKELEK-LEELKKKLAELEKKldeleeelaellkeleelgfesveeleerlkelepFYNEYLELKDAEKELEREEKELK 622
|
490
....*....|....*....
gi 694955909 1091 HNRQKLTETELKFELLEKD 1109
Cdd:PRK03918 623 KLEEELDKAFEELAETEKR 641
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
708-1088 |
1.64e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.10 E-value: 1.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 708 QKEYEGYEVESSLK-----DASFEKEATEAQSLEATCEKLNRSNSELEDEIlclekelkeekskhserdelmADISKRIQ 782
Cdd:COG1196 219 KEELKELEAELLLLklrelEAELEELEAELEELEAELEELEAELAELEAEL---------------------EELRLELE 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 783 SLEDESKSLKSQVAEAKMTfkifqmnEERLKIAIKDALNENSQLQESQKQLLQEAEVWKEQVSELNKQKVTFEDSEVHAE 862
Cdd:COG1196 278 ELELELEEAQAEEYELLAE-------LARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAE 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 863 QVLNDKESHIKTLTERLLKMKdwAAMLGEDITDDDNLELEMNSESEngayldnppkgALKKLIHAAKLNASLKTLEGERN 942
Cdd:COG1196 351 EELEEAEAELAEAEEALLEAE--AELAEAEEELEELAEELLEALRA-----------AAELAAQLEELEEAEEALLERLE 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 943 QIYIQLSEVDKTKEELTEHIKNLQTEQASLQSENTHFENENQKLQQKLKVMTELYQENEMKLHRkltveenyRLEKEEKL 1022
Cdd:COG1196 418 RLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAE--------LLEELAEA 489
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 694955909 1023 SKVDEKISHATEELETYRKRAKDLEEELERTIHSYQGQIISHEKKAHDNWLAARNAERNLNDLRKE 1088
Cdd:COG1196 490 AARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVED 555
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
669-990 |
2.25e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 55.71 E-value: 2.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 669 RSFRSVRSRLyvgREKKLALMLSglieeksklleKFSLVQKEYEGYEVESSLKDASFEKEATEAQSLEATCEKLNRSNSE 748
Cdd:COG1196 213 ERYRELKEEL---KELEAELLLL-----------KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEE 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 749 LEDEIlclekelkeekskhSERDELMADISKRIQSLEDESKSLKSQVAEAkmtfkifQMNEERLKIAIKDALNENSQLQE 828
Cdd:COG1196 279 LELEL--------------EEAQAEEYELLAELARLEQDIARLEERRREL-------EERLEELEEELAELEEELEELEE 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 829 SQKQLLQEAEVWKEQVSELNKQKVTFEDSEVHAEQVLNDKESHIKTLTERLLKMKDWAAMLGEDITDDDNLELEMNSESE 908
Cdd:COG1196 338 ELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLE 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 909 ngayldnppkgalKKLIHAAKLNASLKTLEGERNQIYIQLSEVDKTKEELTEHIKNLQTEQASLQSENTHFENENQKLQQ 988
Cdd:COG1196 418 -------------RLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLE 484
|
..
gi 694955909 989 KL 990
Cdd:COG1196 485 EL 486
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
927-1109 |
2.40e-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: 2.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 927 AAKLNASLKTLEGERNQIYIQLSEVDKTKEELTEHIKNLQTEQASLQSENthfENENQKLQQKLKVMTELyQENEMKLHR 1006
Cdd:TIGR02168 693 IAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEV---EQLEERIAQLSKELTEL-EAEIEELEE 768
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 1007 KLTVEENYRLEKEEKLSKVDEKISHATEELETYRKRAKDLEEELERT---IHSYQGQIISHEKKAHDNWLAARNAERNLN 1083
Cdd:TIGR02168 769 RLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLneeAANLRERLESLERRIAATERRLEDLEEQIE 848
|
170 180
....*....|....*....|....*.
gi 694955909 1084 DLRKENAHNRQKLTETELKFELLEKD 1109
Cdd:TIGR02168 849 ELSEDIESLAAEIEELEELIEELESE 874
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
927-1109 |
2.95e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 55.33 E-value: 2.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 927 AAKLNASLKTLEGERNQIYIQLSEVDKTKEELTEHIKNLQTEQASLQSENTHFENENQKLQQKLKVMTEL---YQENEMK 1003
Cdd:COG1196 241 LEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERrreLEERLEE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 1004 LHRKLTVEENYRLEKEEKLSKVDEKISHATEELETYRKRAKDLEEELERTihsyQGQIISHEKKAHDNWLAARNAERNLN 1083
Cdd:COG1196 321 LEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEA----EAELAEAEEELEELAEELLEALRAAA 396
|
170 180
....*....|....*....|....*.
gi 694955909 1084 DLRKENAHNRQKLTETELKFELLEKD 1109
Cdd:COG1196 397 ELAAQLEELEEAEEALLERLERLEEE 422
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
669-1052 |
3.54e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 55.07 E-value: 3.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 669 RSFRSVRSRLYVGREKKLALMLSGLIEEKSKLLEKFSLVQKEYEgyEVESSLKDAS-----FEKEATEAQSLEAT----C 739
Cdd:TIGR02169 662 PRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLD--ELSQELSDASrkigeIEKEIEQLEQEEEKlkerL 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 740 EKLNRSNSELEDEILclekelkeekskhsERDELMADISKRIQSLEDESKSLKSQVAEakmtfkifqmneerlkiaIKDA 819
Cdd:TIGR02169 740 EELEEDLSSLEQEIE--------------NVKSELKELEARIEELEEDLHKLEEALND------------------LEAR 787
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 820 LNEnSQLQESQKQLlqeaevwkeqvSELNKQKVTFEDSEVHAEQVLNDK-------ESHIKTLTERLLKMKDWAAMLGED 892
Cdd:TIGR02169 788 LSH-SRIPEIQAEL-----------SKLEEEVSRIEARLREIEQKLNRLtlekeylEKEIQELQEQRIDLKEQIKSIEKE 855
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 893 ItDDDNLEL-EMNSESENgayldnpPKGALKKLIhaaklnASLKTLEGERNQIYIQLSEVDKTKEELT-------EHIKN 964
Cdd:TIGR02169 856 I-ENLNGKKeELEEELEE-------LEAALRDLE------SRLGDLKKERDELEAQLRELERKIEELEaqiekkrKRLSE 921
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 965 LQTEQASLQSENTHFENENQKLQQklkvmtelYQENEMKLHrklTVEENyRLEKEEKLSKVDEKISHATEELETYRKRAK 1044
Cdd:TIGR02169 922 LKAKLEALEEELSEIEDPKGEDEE--------IPEEELSLE---DVQAE-LQRVEEEIRALEPVNMLAIQEYEEVLKRLD 989
|
....*...
gi 694955909 1045 DLEEELER 1052
Cdd:TIGR02169 990 ELKEKRAK 997
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
777-1113 |
7.34e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 53.91 E-value: 7.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 777 ISKRIQSLEDESKS------LKSQVAEAKMTFKIFQMNEERLKI-AIKDALNENSQLQESQKQLLQEAEvwkEQVSELNK 849
Cdd:TIGR02168 198 LERQLKSLERQAEKaerykeLKAELRELELALLVLRLEELREELeELQEELKEAEEELEELTAELQELE---EKLEELRL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 850 QKVTFEDSEVHAEQVLNDKESHIKTLTERLLKMKDwaamlgeditdddNLELEMNSESENGAYLDNPPKGALKKLIHAAK 929
Cdd:TIGR02168 275 EVSELEEEIEELQKELYALANEISRLEQQKQILRE-------------RLANLERQLEELEAQLEELESKLDELAEELAE 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 930 LNASLKTLEGERNQIYIQLSEVDKTKEELTEHIKNLQTEQASLQSENTHFENENQKLQQKLKVM-TELYQENEMKLHRKL 1008
Cdd:TIGR02168 342 LEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLeARLERLEDRRERLQQ 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 1009 TVEENYRLEKEEKLSKVDEKISHATEELETYRKRAKDLEEELERTihsyQGQIishekkahdnwlaaRNAERNLNDLRKE 1088
Cdd:TIGR02168 422 EIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEEL----REEL--------------EEAEQALDAAERE 483
|
330 340
....*....|....*....|....*
gi 694955909 1089 NAHNRQKLTETELKFELLEKDPYAL 1113
Cdd:TIGR02168 484 LAQLQARLDSLERLQENLEGFSEGV 508
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
810-1054 |
9.21e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.84 E-value: 9.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 810 ERLKIAIKDALNENSQLQESQKQLLQEAEVWKEQVSELNKQKVTFEDSEVHAEQVLNDKESHIKTLTERLLKMKDW-AAM 888
Cdd:COG4942 30 EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEElAEL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 889 LGEditdddnleLEMNSESENGAYLDNP--PKGALKKLIHAAKLNASLKTlegernqiyiQLSEVDKTKEELTEHIKNLQ 966
Cdd:COG4942 110 LRA---------LYRLGRQPPLALLLSPedFLDAVRRLQYLKYLAPARRE----------QAEELRADLAELAALRAELE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 967 TEQASLQSENTHFENENQKLQQKLKvmtelyqenemklhrkltveenyrlEKEEKLSKVDEKISHATEELETYRKRAKDL 1046
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKA-------------------------ERQKLLARLEKELAELAAELAELQQEAEEL 225
|
....*...
gi 694955909 1047 EEELERTI 1054
Cdd:COG4942 226 EALIARLE 233
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
769-1051 |
1.68e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 52.76 E-value: 1.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 769 ERDELMADISKRIQSLED------ESKSLKSQVAEAKMTFKIFQMNEERLKIAIKDA-------LNENSQLQESQKQLLQ 835
Cdd:PRK03918 142 ESDESREKVVRQILGLDDyenaykNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKekeleevLREINEISSELPELRE 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 836 EAEVWKEQVSELNKQKVTFEDSEVHAEQVLNDK---ESHIKTLTERLLKMKDWAAMLGEDITDDDNLELEMNSESENGAY 912
Cdd:PRK03918 222 ELEKLEKEVKELEELKEEIEELEKELESLEGSKrklEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEF 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 913 LDNppkgALKKLihaAKLNASLKTLEGERNQIYIQLSEVDKTK---EELTEHIKNLQTEQASLQSENTHFENENQKLQQK 989
Cdd:PRK03918 302 YEE----YLDEL---REIEKRLSRLEEEINGIEERIKELEEKEerlEELKKKLKELEKRLEELEERHELYEEAKAKKEEL 374
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 694955909 990 LKVMTELYQENEMKLHRKLTVEENYRLEKEEKLSKVDEKIShateELETYRKRAKDLEEELE 1051
Cdd:PRK03918 375 ERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIG----ELKKEIKELKKAIEELK 432
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
928-1052 |
2.38e-06 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 52.17 E-value: 2.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 928 AKLNASLKTLEGERNQIYIQLSEVDKTKEEltEHIKNLQTEQASLQSENTHFENENQKLQQKLKVMtelyqENEMKLHRK 1007
Cdd:COG2433 383 EELIEKELPEEEPEAEREKEHEERELTEEE--EEIRRLEEQVERLEAEVEELEAELEEKDERIERL-----ERELSEARS 455
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 694955909 1008 ltvEENYRLEKEEKLSKVDEKISHATEELETYRKRAKDLEEELER 1052
Cdd:COG2433 456 ---EERREIRKDREISRLDREIERLERELEEERERIEELKRKLER 497
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
694-1023 |
3.06e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 51.98 E-value: 3.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 694 IEEKSKLLEKFSLVQKEYEGYEVESSLKDAS--FEKEATEAQSLEATCEKLNRSNSELEDEILCLEKELKEEKSKHSERD 771
Cdd:TIGR02168 222 LRELELALLVLRLEELREELEELQEELKEAEeeLEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLE 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 772 ELMADISKRIQSLEDESKSLKSQVAEakmtfkifqmNEERLKIAIKDAlnenSQLQESQKQLLQEAEVWKEQVSELNKQK 851
Cdd:TIGR02168 302 QQKQILRERLANLERQLEELEAQLEE----------LESKLDELAEEL----AELEEKLEELKEELESLEAELEELEAEL 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 852 VTFEDSEVHAEQVLNDKESHIKTLTERLLKMKDWAAMLGEDITD-DDNLElemNSESENGAYLDNPPKGALKKLIHA-AK 929
Cdd:TIGR02168 368 EELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERlEDRRE---RLQQEIEELLKKLEEAELKELQAElEE 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 930 LNASLKTLEGERNQIYIQLSEVDKTKEELTEHIKNLQTEQASLQSENTHFENENQKLQQKLKVMTELYQENEMK------ 1003
Cdd:TIGR02168 445 LEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLsgilgv 524
|
330 340
....*....|....*....|
gi 694955909 1004 LHRKLTVEENYRLEKEEKLS 1023
Cdd:TIGR02168 525 LSELISVDEGYEAAIEAALG 544
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
717-1109 |
3.52e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 51.56 E-value: 3.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 717 ESSLKDASFEKEATEAQSLEATCEKLNRSNSELEDEILCLEKELKEEKSKHSerdelmaDISKRIQSLEDESKSLKSQVA 796
Cdd:TIGR04523 111 EIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYN-------DLKKQKEELENELNLLEKEKL 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 797 EAKMT---------------FKIFQMNEE--RLKIAIKDALNENSQLQESQKQLLQEAEVWKEQVSELNKQKVTFEDSEV 859
Cdd:TIGR04523 184 NIQKNidkiknkllklelllSNLKKKIQKnkSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQN 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 860 HAEQVLNDKESH-------IKTLTERLLKMK------------DWAAMLGEDITDDDNLELEMNSE-SENGAYLDNppkg 919
Cdd:TIGR04523 264 KIKKQLSEKQKEleqnnkkIKELEKQLNQLKseisdlnnqkeqDWNKELKSELKNQEKKLEEIQNQiSQNNKIISQ---- 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 920 aLKKLIhaAKLNASLKTLEGERNQIYIQLSE-------VDKTKEELTEHIKNLQTEQASLQSENTHFENENQKLQQKLKV 992
Cdd:TIGR04523 340 -LNEQI--SQLKKELTNSESENSEKQRELEEkqneiekLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKK 416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 993 MTELYQ--ENEMKLHRKLTVEENYRL--------EKEEKLSKVDEKISHATEELETYRKRAKDLEEELERTihsyQGQII 1062
Cdd:TIGR04523 417 LQQEKEllEKEIERLKETIIKNNSEIkdltnqdsVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQK----QKELK 492
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 694955909 1063 SHEKKAHDNWLAARNAERNLNDLRKENAhnRQKLTETELKFELLEKD 1109
Cdd:TIGR04523 493 SKEKELKKLNEEKKELEEKVKDLTKKIS--SLKEKIEKLESEKKEKE 537
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
686-1109 |
4.50e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 51.31 E-value: 4.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 686 LALMLSGLIEEKSKLL----EKFSLVQKEYEgyEVESSLKDA-----SFEKEATEAQSLEATCEKLNRSNSELEDEI--L 754
Cdd:COG4717 44 RAMLLERLEKEADELFkpqgRKPELNLKELK--ELEEELKEAeekeeEYAELQEELEELEEELEELEAELEELREELekL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 755 CLEKELKEEKSKHSERDELMADISKRIQSLEDESKSLKSQVAEAKMTFKIFQMNEERLKIA-----------IKDALNEN 823
Cdd:COG4717 122 EKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELleqlslateeeLQDLAEEL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 824 SQLQESQKQLLQEAEVWKEQVSELNKQKVTFEDSEVHAEQVlndkeshiktltERLLKMKDWAAMLGEditdddNLELEM 903
Cdd:COG4717 202 EELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE------------ERLKEARLLLLIAAA------LLALLG 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 904 NSESENGAYLDNPPKGALKK---LIHAAKLNASLKTLEGERNQIYIQLSEVDKTKEELTEHIKNLQTEQASLQSENTHFE 980
Cdd:COG4717 264 LGGSLLSLILTIAGVLFLVLgllALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELL 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 981 NENQKLQQKLKVMTELyqENEMKLhrkltveENYRLEKEEKLSKVDekishaTEELETYRKRAKDLEE--ELERTIHSYQ 1058
Cdd:COG4717 344 DRIEELQELLREAEEL--EEELQL-------EELEQEIAALLAEAG------VEDEEELRAALEQAEEyqELKEELEELE 408
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 1059 GQIISHEKKAHDNWLAA---------RNAERNLNDLRKENAHNRQKLTETELKFELLEKD 1109
Cdd:COG4717 409 EQLEELLGELEELLEALdeeeleeelEELEEELEELEEELEELREELAELEAELEQLEED 468
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
816-1001 |
5.04e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.60 E-value: 5.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 816 IKDALNENSQLQESQKQLLQEAEVWKEQVSELNKQKVTFEDSEVHAEQVLNDKESHIKTLTERLlkmKDWAAMLGEDITD 895
Cdd:COG3883 25 LSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREEL---GERARALYRSGGS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 896 DDNLELEMNSESeNGAYLDNppKGALKKLIHAAklNASLKTLEGERNQIYIQLSEVDKTKEELTEHIKNLQTEQASLQSE 975
Cdd:COG3883 102 VSYLDVLLGSES-FSDFLDR--LSALSKIADAD--ADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQ 176
|
170 180
....*....|....*....|....*.
gi 694955909 976 NTHFENENQKLQQKLKVMTELYQENE 1001
Cdd:COG3883 177 QAEQEALLAQLSAEEAAAEAQLAELE 202
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
921-1067 |
6.34e-06 |
|
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: 49.15 E-value: 6.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 921 LKKLIHAAKLNASLKTLEGERNQIYIQLSEVDKTKEELTEHIKNLQTEQASLQSENTHFENENQKLQQKLKVMTEL---- 996
Cdd:COG1579 6 LRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQlgnv 85
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 694955909 997 -----YQ--ENEM-KLHRKLTVEENYRLEKEEKLSKVDEKISHATEELETYRKRAKDLEEELERTIHSYQGQIISHEKK 1067
Cdd:COG1579 86 rnnkeYEalQKEIeSLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAE 164
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
683-1108 |
8.03e-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: 8.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 683 EKKLALMLSGLI--EEKSKLLEKFSLVQkEYEGYEVESSLKdasfeKEATEAQSLEATCEKLNRSNSELEDEILCLEKEL 760
Cdd:pfam01576 158 EERISEFTSNLAeeEEKAKSLSKLKNKH-EAMISDLEERLK-----KEEKGRQELEKAKRKLEGESTDLQEQIAELQAQI 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 761 KEEKSKHSERDELMADISKRiqsLEDES----------KSLKSQVAEAKMTFKIFQMNEER--------------LKIAI 816
Cdd:pfam01576 232 AELRAQLAKKEEELQAALAR---LEEETaqknnalkkiRELEAQISELQEDLESERAARNKaekqrrdlgeeleaLKTEL 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 817 KDALNENSQLQESQKQLLQEaevwkeqVSELnkQKVTFEDSEVHAEQVLNDKESH---IKTLTERLLKMKDWAAML--GE 891
Cdd:pfam01576 309 EDTLDTTAAQQELRSKREQE-------VTEL--KKALEEETRSHEAQLQEMRQKHtqaLEELTEQLEQAKRNKANLekAK 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 892 DITDDDNLELEMNSESENGAYLDNPPKGalkklihaaklnaslKTLEGERNQIYIQLSEVDKTKEELTEHIKNLQTEQAS 971
Cdd:pfam01576 380 QALESENAELQAELRTLQQAKQDSEHKR---------------KKLEGQLQELQARLSESERQRAELAEKLSKLQSELES 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 972 LQSENTHFENENQKLQQKLKVMtelyqenEMKLHrklTVEENYRLEKEEKLSkVDEKISHATEELETYRKRAKDLEE--- 1048
Cdd:pfam01576 445 VSSLLNEAEGKNIKLSKDVSSL-------ESQLQ---DTQELLQEETRQKLN-LSTRLRQLEDERNSLQEQLEEEEEakr 513
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 1049 ELERTIHSYQGQIISHEKKAHDNWLAARNAERNLNDLRKENAHNRQKLTETELKFELLEK 1108
Cdd:pfam01576 514 NVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEK 573
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
696-1108 |
8.64e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 50.45 E-value: 8.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 696 EKSKLLEKFSLVQKEYEGYEVESSLKDASFEKEATEAQSLEATCEKLNRSNSELEDEIlclekelKEEKSKHSERDELMA 775
Cdd:TIGR02169 351 RRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKREL-------DRLQEELQRLSEELA 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 776 DISKRIQSLEDESKSLKSQVAEAKMTFKIFQMNEERLKIAIKDALNENSQLQESQKQLLQEAEVWKEQVSELNKQKVTFE 855
Cdd:TIGR02169 424 DLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASE 503
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 856 DSE---VHAEQVLNDKESHIKTLTERLLKMKDWAAM---------LGEDITDDDNLE-----------------LEMNSE 906
Cdd:TIGR02169 504 ERVrggRAVEEVLKASIQGVHGTVAQLGSVGERYATaievaagnrLNNVVVEDDAVAkeaiellkrrkagratfLPLNKM 583
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 907 SENGAYLDNP-PKGALKKL--------------------------IHAAK---LNASLKTLEGE---------------R 941
Cdd:TIGR02169 584 RDERRDLSILsEDGVIGFAvdlvefdpkyepafkyvfgdtlvvedIEAARrlmGKYRMVTLEGElfeksgamtggsrapR 663
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 942 NQIYIQLSEVDKTkEELTEHIKNLQTEQASLQSENTHFENENQKLQQKLKVMT----------ELYQENEMKLHRKLTve 1011
Cdd:TIGR02169 664 GGILFSRSEPAEL-QRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASrkigeiekeiEQLEQEEEKLKERLE-- 740
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 1012 enyrlEKEEKLSKVDEKISHATEELETYRKRAkdleEELERTIHSYQGQIisHEKKAHDNWLAARNAERNLNDLRKENAH 1091
Cdd:TIGR02169 741 -----ELEEDLSSLEQEIENVKSELKELEARI----EELEEDLHKLEEAL--NDLEARLSHSRIPEIQAELSKLEEEVSR 809
|
490 500
....*....|....*....|....
gi 694955909 1092 NR-------QKLTETELKFELLEK 1108
Cdd:TIGR02169 810 IEarlreieQKLNRLTLEKEYLEK 833
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
779-1109 |
1.45e-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: 49.97 E-value: 1.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 779 KRIQSLEDESKSLKSQVAEAKMTFKIFQMNEERLKIAIKDALNENsQLQESQKQLLQEAEVWKEQV-SELNKQKVTFEDS 857
Cdd:pfam02463 153 ERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKL-QELKLKEQAKKALEYYQLKEkLELEEEYLLYLDY 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 858 EVHAEQVLNDKESHIKTLTERLLKMKdwaamlGEDITDDDNLELEMNSESENGAYLDNPPKGALKKLIHAAKLNASLKTL 937
Cdd:pfam02463 232 LKLNEERIDLLQELLRDEQEEIESSK------QEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKL 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 938 EGERNQIYIQLSEVDKTKEELTEHIKNLQTEQASLQSENTHFENENQKLQQKLKVMTELYQENEMKLHRKLTV------- 1010
Cdd:pfam02463 306 ERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKkkleser 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 1011 -------EENYRLEKEEKLSKVDEKISHATEELETYRKRAKDL---EEELERTIHSYQGQIIshEKKAHDNWLAARNAER 1080
Cdd:pfam02463 386 lssaaklKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEEleiLEEEEESIELKQGKLT--EEKEELEKQELKLLKD 463
|
330 340
....*....|....*....|....*....
gi 694955909 1081 NLNDLRKENAHNRQKLTETELKFELLEKD 1109
Cdd:pfam02463 464 ELELKKSEDLLKETQLVKLQEQLELLLSR 492
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
694-1099 |
2.11e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 49.20 E-value: 2.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 694 IEEKSKLLEKFSLVQKEYEGYEVESSLKDASFEKEATE-------AQSLEATCEKLNRSNSELEDEilclEKELKEEKSK 766
Cdd:TIGR00618 340 IEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLtqhihtlQQQKTTLTQKLQSLCKELDIL----QREQATIDTR 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 767 HSERDELMADISKRIQSLEDESKSLKSQVAEAKMTFKIFQMNEERLKIAIKDALNENSQLQESQKQLLQEAEVWKEQVSE 846
Cdd:TIGR00618 416 TSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLAR 495
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 847 LNKQKVT---FEDSEVHAEQVLNDKEShIKTLTERLLKMKDWAAMLGEDItddDNLELEMNSESENGAYLDNPPKGALKK 923
Cdd:TIGR00618 496 LLELQEEpcpLCGSCIHPNPARQDIDN-PGPLTRRMQRGEQTYAQLETSE---EDVYHQLTSERKQRASLKEQMQEIQQS 571
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 924 L-IHAAKLNASLKTLEGERN-----QIYIQ--LSEVDKTKEELTEHIKNLQtEQASLQSENTHFENENQKLQQKL----K 991
Cdd:TIGR00618 572 FsILTQCDNRSKEDIPNLQNitvrlQDLTEklSEAEDMLACEQHALLRKLQ-PEQDLQDVRLHLQQCSQELALKLtalhA 650
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 992 VMTELYQENE------MKLHRKLTVEENYRLEKE-----EKLSKVDEKISHATE---ELETYRKRAKDLEEELERTIHSy 1057
Cdd:TIGR00618 651 LQLTLTQERVrehalsIRVLPKELLASRQLALQKmqsekEQLTYWKEMLAQCQTllrELETHIEEYDREFNEIENASSS- 729
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 694955909 1058 QGQIISHEKKAHDNWLAARNAERNLNDLRKENAHNRQKLTET 1099
Cdd:TIGR00618 730 LGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVT 771
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
690-973 |
2.36e-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: 49.30 E-value: 2.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 690 LSGLIEEKSKLLEKFSLVQKEYEGYEVESSLKDASFEKEATEAQSLEATCEKLNRSNSELEDEILCLE-----KELKEEK 764
Cdd:TIGR02169 725 IEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRipeiqAELSKLE 804
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 765 SKHSERDELMADISKRIQS-------LEDESKSLKSQVAEAKMTFKIFQMNEERLKIAIKDALNENSQLQESQKQLLQEA 837
Cdd:TIGR02169 805 EEVSRIEARLREIEQKLNRltlekeyLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRL 884
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 838 EVWKEQVSELNKQKVTFEDSEVHAEQVLNDKESHIKTLTERLlkmkdwaAMLGEDITDDDNLELEMNSESENgayldNPP 917
Cdd:TIGR02169 885 GDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKL-------EALEEELSEIEDPKGEDEEIPEE-----ELS 952
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 694955909 918 KGALKKLIHaaKLNASLKTLEGERNQIYIQLSEVDKTKEELTEHIKNLQTEQASLQ 973
Cdd:TIGR02169 953 LEDVQAELQ--RVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAIL 1006
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
768-1130 |
2.97e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 48.91 E-value: 2.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 768 SERDELmADISKRIQSLEDESKSLKSQVAEAKMtfkifQMNEerLKIAIKDALNENSQLQESQKQLLQEAEVWKEQVSEL 847
Cdd:TIGR02169 671 SEPAEL-QRLRERLEGLKRELSSLQSELRRIEN-----RLDE--LSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEEL 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 848 nkqkvtfEDSEVHAEQVLNDKESHIKTLTERLlkmkdwaAMLGEDITdddNLELEMNSesengayldnppkgalkklIHA 927
Cdd:TIGR02169 743 -------EEDLSSLEQEIENVKSELKELEARI-------EELEEDLH---KLEEALND-------------------LEA 786
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 928 AKLNASLKTLEGERNQIYIQLSEVDKTKEELTEHIKNLQTEQASLQSENTHFENENQKLQQKLKvmtELYQEnemklhrk 1007
Cdd:TIGR02169 787 RLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIK---SIEKE-------- 855
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 1008 ltvEENYRLEKEEKLskvdekishatEELETYRKRAKDLEEELErtihSYQGQIISHEKKahdnwlaARNAERNLNDLRK 1087
Cdd:TIGR02169 856 ---IENLNGKKEELE-----------EELEELEAALRDLESRLG----DLKKERDELEAQ-------LRELERKIEELEA 910
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 694955909 1088 ENAHNRQKLTETELKFELLEKDPYALDvPNTAFGREHSPYGPS 1130
Cdd:TIGR02169 911 QIEKKRKRLSELKAKLEALEEELSEIE-DPKGEDEEIPEEELS 952
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
684-1109 |
5.63e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.75 E-value: 5.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 684 KKLALMLSGLIEEKSKLLEKFSLVQKEYEGYEVESSlkdaSFEKEATEAQSLEATCEKLNRSNSELEDEIlclekelKEE 763
Cdd:PRK03918 289 KEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEIN----GIEERIKELEEKEERLEELKKKLKELEKRL-------EEL 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 764 KSKHSERDELMAdISKRIQSLEDESKSLKSQVAEAKMTfkifqmNEERLKIAIKDALNEnsqLQESQKQLLQEAEVWKEQ 843
Cdd:PRK03918 358 EERHELYEEAKA-KKEELERLKKRLTGLTPEKLEKELE------ELEKAKEEIEEEISK---ITARIGELKKEIKELKKA 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 844 VSELNKQKVTF-----EDSEVHAEQV-------LNDKESHIKTLTERLLKMKDWAAMLGEDITDDDNL-----------E 900
Cdd:PRK03918 428 IEELKKAKGKCpvcgrELTEEHRKELleeytaeLKRIEKELKEIEEKERKLRKELRELEKVLKKESELiklkelaeqlkE 507
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 901 LEMNSESENGAYLDNPPKGALKKLIHAAKLNASLKTLEGERNQiyiqLSEVDKTKEELTEHIKNLQTEQASL--QSENTH 978
Cdd:PRK03918 508 LEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEK----LEELKKKLAELEKKLDELEEELAELlkELEELG 583
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 979 FENEnQKLQQKLKVMTELYQE-NEMKLHRKltveenyRLE-KEEKLSKVDEKISHATEELETYRKRAKDLEEELERTIHS 1056
Cdd:PRK03918 584 FESV-EELEERLKELEPFYNEyLELKDAEK-------ELErEEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKK 655
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 694955909 1057 YqgqiiSHEKKahdnwlaaRNAERNLNDLRKENAHNRQKLTETELKFELLEKD 1109
Cdd:PRK03918 656 Y-----SEEEY--------EELREEYLELSRELAGLRAELEELEKRREEIKKT 695
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
715-1001 |
8.81e-05 |
|
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: 47.14 E-value: 8.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 715 EVESSLKD----ASFEKEATEAQSLEATCEKLNRSNSELEDEILCLEKELKEEKSKHSERDELMADISKRIQSLEDESKS 790
Cdd:pfam12128 222 QVEHWIRDiqaiAGIMKIRPEFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKE 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 791 LKSQVAEAKMTFK-IFQMNEERLKIAIKDALNENSQLQESQKQLLQEAEVWKEQVSELNKQKVTFEDSEVHAEQVLNDKE 869
Cdd:pfam12128 302 KRDELNGELSAADaAVAKDRSELEALEDQHGAFLDADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRR 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 870 SHIKT--------LTERLLKMKDWAAMLGEDITDD-DNLELEMNSESENGAYLDNPPKGALKKLIHAAK--LNASLKTLE 938
Cdd:pfam12128 382 SKIKEqnnrdiagIKDKLAKIREARDRQLAVAEDDlQALESELREQLEAGKLEFNEEEYRLKSRLGELKlrLNQATATPE 461
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 694955909 939 gERNQIYIQLSEVDKTKEELTEHIKNLQTEQASLQSENTHFENENQKLQQKLKVMTELYQENE 1001
Cdd:pfam12128 462 -LLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALD 523
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
779-1108 |
1.28e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 46.55 E-value: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 779 KRIQSLEDESKSLKSQVAEAKMTF-----KIFQMNEERLKIAI-----KDALNEN-SQLQESQKQLLQ------------ 835
Cdd:TIGR04523 68 EKINNSNNKIKILEQQIKDLNDKLkknkdKINKLNSDLSKINSeikndKEQKNKLeVELNKLEKQKKEnkknidkfltei 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 836 -----EAEVWKEQVSELNKQKVTFEDSEVHAEQVLNDKESHIKTLTERLLKMKDWAAMLGEDITDDDNLELEMN-SESEN 909
Cdd:TIGR04523 148 kkkekELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISeLKKQN 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 910 gayldnppkgalkklihaAKLNASLKTLEGERNQIYIQLSEVDK----TKEELTEHIKNLQTEQASLQSENT---HFENE 982
Cdd:TIGR04523 228 ------------------NQLKDNIEKKQQEINEKTTEISNTQTqlnqLKDEQNKIKKQLSEKQKELEQNNKkikELEKQ 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 983 NQKLQQKLKVMTELYQENEMK-LHRKLTVEENYRLEKEEKLSKVDEKISHATEELETYRKRAKDLE---EELERTIHSYQ 1058
Cdd:TIGR04523 290 LNQLKSEISDLNNQKEQDWNKeLKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSEsenSEKQRELEEKQ 369
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 694955909 1059 GQIISHEKKAHDNWLAARNAERNLNDLR-------KENAHNRQKLTETELKFELLEK 1108
Cdd:TIGR04523 370 NEIEKLKKENQSYKQEIKNLESQINDLEskiqnqeKLNQQKDEQIKKLQQEKELLEK 426
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
920-1116 |
2.30e-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: 2.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 920 ALKKLIhaAKLNASLKTLEGERNQIYIQLSEVDKTKEELTEHIKNLQTEQASLQSENTHFENENQKLQQKLKVMTELY-- 997
Cdd:COG4942 31 QLQQEI--AELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELae 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 998 -------------------QENEMKLHRKLTVEE---NYRLEKEEKLSKVDEKISHATEELETYRKRAKDLEEELERTIH 1055
Cdd:COG4942 109 llralyrlgrqpplalllsPEDFLDAVRRLQYLKylaPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERA 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 694955909 1056 SYQGQIISHEKKAHDNWLAARNAERNLNDLRKENAHNRQKLTETELKFELLEKDPYALDVP 1116
Cdd:COG4942 189 ALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFA 249
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
694-1052 |
3.20e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.44 E-value: 3.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 694 IEEKSKLLEKFSLVQKEYEGYEVEssLKDASFEKEATEAQSLEATCEKLNRSNSELEDEILCLEKELKEEKSKHSE---- 769
Cdd:PRK03918 357 LEERHELYEEAKAKKEELERLKKR--LTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEElkka 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 770 ---------------RDELMADISKRIQSLEDESKSLKSQVAEAKMTFKIFQM--NEERLKIAIKDALNENSQLQESQKQ 832
Cdd:PRK03918 435 kgkcpvcgrelteehRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKvlKKESELIKLKELAEQLKELEEKLKK 514
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 833 L--------LQEAEVWKEQVSELNKQKVTFEDsEVHAEQVLNDK----ESHIKTLTERLLKMKDWAAMLGEDITDDDNLE 900
Cdd:PRK03918 515 YnleelekkAEEYEKLKEKLIKLKGEIKSLKK-ELEKLEELKKKlaelEKKLDELEEELAELLKELEELGFESVEELEER 593
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 901 LEmNSESENGAYLDnpPKGALKKLihaAKLNASLKTLEGERNQIYIQLSEVDKTKEELTEHIKNLQT-----EQASLQSE 975
Cdd:PRK03918 594 LK-ELEPFYNEYLE--LKDAEKEL---EREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKkyseeEYEELREE 667
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 694955909 976 NTHFENENQKLQQKLKVMTELYQENEMKLhRKLTVEENYRLEKEEKLskvdEKISHATEELETYRKRAKDLEEELER 1052
Cdd:PRK03918 668 YLELSRELAGLRAELEELEKRREEIKKTL-EKLKEELEEREKAKKEL----EKLEKALERVEELREKVKKYKALLKE 739
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
770-1108 |
4.02e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 45.11 E-value: 4.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 770 RDELmADISKRIQSLEDESKSLKSQVaeakmtfkifQMNEERLKIAIKDALNENSQLQESQKQLLQEAEVWKEQVSELNK 849
Cdd:pfam15921 418 RREL-DDRNMEVQRLEALLKAMKSEC----------QGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTA 486
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 850 QKVTFEDSEVHAEQV---LNDKESHIKTLTERLLKMKDwaamlgeditdddNLELEmnsesengayldnppkgaLKKLIH 926
Cdd:pfam15921 487 KKMTLESSERTVSDLtasLQEKERAIEATNAEITKLRS-------------RVDLK------------------LQELQH 535
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 927 AAKLNASLKTLEGERNQIYIQLSEVDKTKEELTEHIKNL--------------QTEQASLQSENTHFENENQKLQ----- 987
Cdd:pfam15921 536 LKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMtqlvgqhgrtagamQVEKAQLEKEINDRRLELQEFKilkdk 615
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 988 -----QKLKVMTELYQENEMKL----HRKLTVEENYRLEKEEKLSKVD---EKISHATEELETYRKRAKDLEEELERTIH 1055
Cdd:pfam15921 616 kdakiRELEARVSDLELEKVKLvnagSERLRAVKDIKQERDQLLNEVKtsrNELNSLSEDYEVLKRNFRNKSEEMETTTN 695
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 694955909 1056 SYQGQIisheKKAHDNWLAARNAERNLN-----------DLRKENAHNRQKLTETELKFELLEK 1108
Cdd:pfam15921 696 KLKMQL----KSAQSELEQTRNTLKSMEgsdghamkvamGMQKQITAKRGQIDALQSKIQFLEE 755
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
774-999 |
5.02e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.62 E-value: 5.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 774 MADISKRIQSLEDESKSLKSQVAEAkmtfkifqmnEERLKiAIKDAlNENSQLQESQKQLLQeaevwkeQVSELNKQKVT 853
Cdd:COG3206 170 REEARKALEFLEEQLPELRKELEEA----------EAALE-EFRQK-NGLVDLSEEAKLLLQ-------QLSELESQLAE 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 854 fedsevhAEQVLNDKESHIKTLTERLLKMKDWAAMLGED------ITDDDNLELEMNSESENgaYLDNPPKgalkklihA 927
Cdd:COG3206 231 -------ARAELAEAEARLAALRAQLGSGPDALPELLQSpviqqlRAQLAELEAELAELSAR--YTPNHPD--------V 293
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 694955909 928 AKLNASLKTLEGERNQiyiqlsEVDKTKEELTEHIKNLQTEQASLQSENTHFENENQKLQQKLKVMTELYQE 999
Cdd:COG3206 294 IALRAQIAALRAQLQQ------EAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLERE 359
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
841-1052 |
7.10e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 43.85 E-value: 7.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 841 KEQVSELNKQKVTFEDSEVHAEQVLNDKESHIKTL-------TERLLKMKDWAAMLGEDI------TDDDNLELEMNSES 907
Cdd:PHA02562 173 KDKIRELNQQIQTLDMKIDHIQQQIKTYNKNIEEQrkkngenIARKQNKYDELVEEAKTIkaeieeLTDELLNLVMDIED 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 908 engayldnpPKGALKKLIHA-AKLNASLKTLEGERN------------QiyiQLSEVDKTKEELTEHIKNLQTeqaSLQS 974
Cdd:PHA02562 253 ---------PSAALNKLNTAaAKIKSKIEQFQKVIKmyekggvcptctQ---QISEGPDRITKIKDKLKELQH---SLEK 317
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 694955909 975 ENTHFENENQKLQQklkvmtelYQENEMKLHrkltveenyrlEKEEKLSKVDEKIShateeleTYRKRAKDLEEELER 1052
Cdd:PHA02562 318 LDTAIDELEEIMDE--------FNEQSKKLL-----------ELKNKISTNKQSLI-------TLVDKAKKVKAAIEE 369
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
771-883 |
9.92e-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: 9.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 771 DELMADISKRIQSLEDESKSLKSQVAEAKmtfKIFQMNEERLKIAIKDALNENSQLQESQKQLLQEAEVWKEQVSELNKQ 850
Cdd:smart00787 171 NSIKPKLRDRKDALEEELRQLKQLEDELE---DCDPTELDRAKEKLKKLLQEIMIKVKKLEELEEELQELESKIEDLTNK 247
|
90 100 110
....*....|....*....|....*....|....*..
gi 694955909 851 KVTFEDSEVHAEQVLND----KESHIKTLTERLLKMK 883
Cdd:smart00787 248 KSELNTEIAEAEKKLEQcrgfTFKEIEKLKEQLKLLQ 284
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
748-1060 |
1.20e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 43.35 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 748 ELEDEILCLEKELKEEKSKHSERDELMADIS------KRIQSLEDESKSLKSQVAEAKMTFKIFQMNEERLKIAIKDALN 821
Cdd:PRK01156 153 KILDEILEINSLERNYDKLKDVIDMLRAEISnidyleEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMD 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 822 ENSQLQESQKQLLQEAEVWKEQVSELNKQkvtfeDSEVHAEQVLNDKeshIKTLTERLLKMKDWAAMLG-EDITDDDNLE 900
Cdd:PRK01156 233 DYNNLKSALNELSSLEDMKNRYESEIKTA-----ESDLSMELEKNNY---YKELEERHMKIINDPVYKNrNYINDYFKYK 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 901 LEMNSESENGAYLDnppkGALKKLIHAAKlnaSLKTLEGERNQIYIQLSEVDKTKEELTEhiknLQTEQASLQSENTHFE 980
Cdd:PRK01156 305 NDIENKKQILSNID----AEINKYHAIIK---KLSVLQKDYNDYIKKKSRYDDLNNQILE----LEGYEMDYNSYLKSIE 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 981 NENQKLQQKLKVMTELYQENEMKLHRKLTVEENYRLEKEEKLSKVDEkISHATEELETYRKRAKDLEEELERTIHSYQGQ 1060
Cdd:PRK01156 374 SLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQD-ISSKVSSLNQRIRALRENLDELSRNMEMLNGQ 452
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
779-1105 |
1.23e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 43.57 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 779 KRIQSLEDESKSLKSQVAEAKMTF--KIFQMnEERLKIA---IKDALNENSQL-QES-------QKQLL------QEAEV 839
Cdd:pfam15921 317 RQLSDLESTVSQLRSELREAKRMYedKIEEL-EKQLVLAnseLTEARTERDQFsQESgnlddqlQKLLAdlhkreKELSL 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 840 WKEQVSELNKQKVTFEDSEVHAEQVLNDKESHIKTLTERLLKMKD---------WAAMLGEDITDDDNLELEMNSESENG 910
Cdd:pfam15921 396 EKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSecqgqmerqMAAIQGKNESLEKVSSLTAQLESTKE 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 911 AYLDNPPKGALKKLI------HAAKLNASL----KTLEGERNQIYIQLSEVDKTKEELT------EHIKNLQTEQASLQS 974
Cdd:pfam15921 476 MLRKVVEELTAKKMTlesserTVSDLTASLqekeRAIEATNAEITKLRSRVDLKLQELQhlknegDHLRNVQTECEALKL 555
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 975 ENTHFENENQKLQQKLKVMTELYQEN-----EMKLHR-KLTVEENYRLEKEEKLSKVDEKISHATEELETyrkRAKDLEE 1048
Cdd:pfam15921 556 QMAEKDKVIEILRQQIENMTQLVGQHgrtagAMQVEKaQLEKEINDRRLELQEFKILKDKKDAKIRELEA---RVSDLEL 632
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 694955909 1049 ELERTIH--SYQGQIISHEKKAHDNWL-AARNAERNLNDLR------KENAHNRQKLTET---ELKFEL 1105
Cdd:pfam15921 633 EKVKLVNagSERLRAVKDIKQERDQLLnEVKTSRNELNSLSedyevlKRNFRNKSEEMETttnKLKMQL 701
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
934-1058 |
1.27e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.37 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 934 LKTLEGERNQIYIQLSEVDKTK---EELTEHIKNLQTEQASLQSENTHFENENQKLQQKLKVMTELYQENEMKLHR---K 1007
Cdd:COG4913 663 VASAEREIAELEAELERLDASSddlAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAaedL 742
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 694955909 1008 LTVEENYRLEK---EEKLSKVDEKISHA-TEELETYRKRAKDLEEELERTIHSYQ 1058
Cdd:COG4913 743 ARLELRALLEErfaAALGDAVERELRENlEERIDALRARLNRAEEELERAMRAFN 797
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
690-1108 |
1.27e-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: 43.50 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 690 LSGLIEEKSKLLEK--FSLVQKEYEGYEVESSLKDA-SFEKEATEAQSLEATCEKlNRSNSELEDEILCLEKELKEEKSK 766
Cdd:TIGR00606 438 LGRTIELKKEILEKkqEELKFVIKELQQLEGSSDRIlELDQELRKAERELSKAEK-NSLTETLKKEVKSLQNEKADLDRK 516
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 767 HSERDELMADISKRIQSLEDESKSLKSQVAEAKMTFKIFQMNEERLKIAIKDALNEnSQLQESQKQLLQEAEVWKEQVSE 846
Cdd:TIGR00606 517 LRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYFPNK-KQLEDWLHSKSKEINQTRDRLAK 595
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 847 LNKQKVTFEDSEVHAEQVLNDKESHIKTLTERLLKmkdwaAMLGEDITDD-DNLELEMNSESENGAYLDNppkgalkkli 925
Cdd:TIGR00606 596 LNKELASLEQNKNHINNELESKEEQLSSYEDKLFD-----VCGSQDEESDlERLKEEIEKSSKQRAMLAG---------- 660
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 926 hAAKLNASLKTLEGERNQIYIQLSEVD-KTKEELTEHIKNLQTEQASLQSENTHFENENQKLQQKLKVMTELY--QENEM 1002
Cdd:TIGR00606 661 -ATAVYSQFITQLTDENQSCCPVCQRVfQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLApgRQSII 739
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 1003 KLHRKLTVEENYRLEK-EEKLSKVDEKISHATEELETY---RKRAKDLEEELErTIHSYQGQIISHEKKAHD--NWLAAR 1076
Cdd:TIGR00606 740 DLKEKEIPELRNKLQKvNRDIQRLKNDIEEQETLLGTImpeEESAKVCLTDVT-IMERFQMELKDVERKIAQqaAKLQGS 818
|
410 420 430
....*....|....*....|....*....|..
gi 694955909 1077 NAERNLNDLRKENAHNRQKLTETELKFELLEK 1108
Cdd:TIGR00606 819 DLDRTVQQVNQEKQEKQHELDTVVSKIELNRK 850
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
824-1102 |
1.38e-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: 43.50 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 824 SQLQESQKQLLQEAEVWKEQVSELNKQKVTFEDSEVHAeqvlndkESHIKTLTERLLKMKDwaamlgeDITDDDNLELEM 903
Cdd:TIGR01612 540 KEIEAGLKESYELAKNWKKLIHEIKKELEEENEDSIHL-------EKEIKDLFDKYLEIDD-------EIIYINKLKLEL 605
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 904 NSESENGAYLDNPPKGA--LKKLIhaaklnaslktlegERNQIYIqlSEVDKTKE-ELTEHIKNLQTEQASLQSENTH-F 979
Cdd:TIGR01612 606 KEKIKNISDKNEYIKKAidLKKII--------------ENNNAYI--DELAKISPyQVPEHLKNKDKIYSTIKSELSKiY 669
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 980 ENENQKLQQKLkvmTELYQENEMKlhrklTVEENYRLEK-EEKLSKVDEKISHATEE--------LETYRKRAKDLEEEL 1050
Cdd:TIGR01612 670 EDDIDALYNEL---SSIVKENAID-----NTEDKAKLDDlKSKIDKEYDKIQNMETAtvelhlsnIENKKNELLDIIVEI 741
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 694955909 1051 ERTIHSYqgqiISHE--KKAHDNWLAARNAERNLNDLRKENAH-NRQKLTETELK 1102
Cdd:TIGR01612 742 KKHIHGE----INKDlnKILEDFKNKEKELSNKINDYAKEKDElNKYKSKISEIK 792
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
771-1071 |
1.42e-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: 43.50 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 771 DELMADISKRiQSLEDESKSLKSQVAEAKMTFKIFQMNEERL-----KIAIKDALNEN--------SQLQESQKQLLQEA 837
Cdd:TIGR01612 1486 NELKEHIDKS-KGCKDEADKNAKAIEKNKELFEQYKKDVTELlnkysALAIKNKFAKTkkdseiiiKEIKDAHKKFILEA 1564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 838 EVWKEQVSELNKQKVTFEDSEVH---AEQVLNDKESHIKTLTERLLKMKDWAAMLGEDITDDDNLE-----LEMNSE--- 906
Cdd:TIGR01612 1565 EKSEQKIKEIKKEKFRIEDDAAKndkSNKAAIDIQLSLENFENKFLKISDIKKKINDCLKETESIEkkissFSIDSQdte 1644
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 907 -SENGAYLD----------NPPKGALKKLIHAAKLNASLKTLEGERNQ--------IYIQLSEVDKTKEELTEHIKNL-- 965
Cdd:TIGR01612 1645 lKENGDNLNslqefleslkDQKKNIEDKKKELDELDSEIEKIEIDVDQhkknyeigIIEKIKEIAIANKEEIESIKELie 1724
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 966 QTEQASLQSENTH-FE--NENQKLQQKLKVMTELYQENeMKLHRKLTveeNYRlekeEKLSKvdEKISHatEELETYRKR 1042
Cdd:TIGR01612 1725 PTIENLISSFNTNdLEgiDPNEKLEEYNTEIGDIYEEF-IELYNIIA---GCL----ETVSK--EPITY--DEIKNTRIN 1792
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 694955909 1043 AKD--LEE-ELERTIHSYQ--------GQIISHEKKAHDN 1071
Cdd:TIGR01612 1793 AQNefLKIiEIEKKSKSYLddieakefDRIINHFKKKLDH 1832
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
715-1098 |
1.64e-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: 43.24 E-value: 1.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 715 EVESSLKDASFEKEATEAQSLEATCEKLNRSNSELEDEILCLEKELKEEKSKHSERDELMADISKRIQSLEDESKSLKSQ 794
Cdd:pfam01576 4 EEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHELESR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 795 VAEakmtfkifqmNEERlkiaikdalneNSQLQESQKQLLQEAEVWKEQVSELN--KQKVTFEdsEVHAEQVLNDKESHI 872
Cdd:pfam01576 84 LEE----------EEER-----------SQQLQNEKKKMQQHIQDLEEQLDEEEaaRQKLQLE--KVTTEAKIKKLEEDI 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 873 KTLTERLLKMKDWAAMLGEDITDddnLELEMNSESENGAYLDnppKGALKKLIHAAKLNASLKTLEGERNQIYIQLSEVD 952
Cdd:pfam01576 141 LLLEDQNSKLSKERKLLEERISE---FTSNLAEEEEKAKSLS---KLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLE 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 953 KTKEELTEHIKNLQTEQASLQSENTHFENENQKLQQKLKvmTELYQENE-MKLHRKLtveENYRLEKEEKLSKvdEKISH 1031
Cdd:pfam01576 215 GESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLE--EETAQKNNaLKKIREL---EAQISELQEDLES--ERAAR 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 1032 ATEEletyrKRAKDLEEELE--RT--------------IHSYQGQIISHEKKAHDNwlAARNAERNLNDLRKENAHNRQK 1095
Cdd:pfam01576 288 NKAE-----KQRRDLGEELEalKTeledtldttaaqqeLRSKREQEVTELKKALEE--ETRSHEAQLQEMRQKHTQALEE 360
|
...
gi 694955909 1096 LTE 1098
Cdd:pfam01576 361 LTE 363
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
696-1108 |
1.97e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 42.74 E-value: 1.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 696 EKSKLLEKFSLVQKEYEGYEVESSLKDASFEKEATEAQSLEatceklnRSNSELEDEILclekelkeekSKHSERDEL-- 773
Cdd:TIGR02168 331 KLDELAEELAELEEKLEELKEELESLEAELEELEAELEELE-------SRLEELEEQLE----------TLRSKVAQLel 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 774 -MADISKRIQSLEDESKSL-------KSQVAEAKMTFKIFQMNEERLKIAIKDALNEnsQLQESQKQLLQEAEVWKEQVS 845
Cdd:TIGR02168 394 qIASLNNEIERLEARLERLedrrerlQQEIEELLKKLEEAELKELQAELEELEEELE--ELQEELERLEEALEELREELE 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 846 ELNKQKVTFEDSEVHA-------EQVLNDKES---HIKTLTERLLKMKDWAAMLGEDITDDDNLELEMN----------- 904
Cdd:TIGR02168 472 EAEQALDAAERELAQLqarldslERLQENLEGfseGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEaalggrlqavv 551
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 905 SESENGA-----YLDNPPKG-----ALKKLIHAAKLNASLKTLEGERNQIYIqLSEVDKTKEELTEHIKNL--------Q 966
Cdd:TIGR02168 552 VENLNAAkkaiaFLKQNELGrvtflPLDSIKGTEIQGNDREILKNIEGFLGV-AKDLVKFDPKLRKALSYLlggvlvvdD 630
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 967 TEQASLQSENTHFENENQKLQQKL-------------KVMTELYQENEMKLHRKlTVEEnyRLEKEEKLSKVDEKISHAT 1033
Cdd:TIGR02168 631 LDNALELAKKLRPGYRIVTLDGDLvrpggvitggsakTNSSILERRREIEELEE-KIEE--LEEKIAELEKALAELRKEL 707
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 694955909 1034 EELETYRKRAKDLEEELERTIHSYQGQIISHEKKAHDNWLAARNAERNLNDLRKENAHNRQKLTETELKFELLEK 1108
Cdd:TIGR02168 708 EELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEA 782
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
690-974 |
2.05e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 42.74 E-value: 2.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 690 LSGLIEEKSKLLEKFSLVQKEYEGYEVESSLKDASFEKEATEA-------QSLEATCEKLNRSNSELEDEILCLEKELKE 762
Cdd:TIGR02168 735 LARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELaeaeaeiEELEAQIEQLKEELKALREALDELRAELTL 814
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 763 -EKSKHSERDEL------MADISKRIQSLEDESKSLKSQVAEAKMTFKIFQMNEERLKIAIKDALNENSQLQESQKQLLQ 835
Cdd:TIGR02168 815 lNEEAANLRERLeslerrIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRS 894
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 836 EAEVWKEQVSELNKQKVTFEDSevhaeqvLNDKESHIKTLTERLLKMKDWAAMLGEDITDDDNLELEMNSESENGayLDN 915
Cdd:TIGR02168 895 ELEELSEELRELESKRSELRRE-------LEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENK--IED 965
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 916 PPKGALKKLIhaaKLNASLKTLeGERNQIYIQ-LSEVDKTKEELTEHIKNLQTEQASLQS 974
Cdd:TIGR02168 966 DEEEARRRLK---RLENKIKEL-GPVNLAAIEeYEELKERYDFLTAQKEDLTEAKETLEE 1021
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
791-1070 |
2.28e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 42.40 E-value: 2.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 791 LKSQVAEAKMTFKIFQMNEERLKIAIKDALNENSQLQESQKQLLQEAEVWK-EQVSELNKQKVTFEDSEVHAEQVLNDKE 869
Cdd:pfam05483 160 LKETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARlEMHFKLKEDHEKIQHLEEEYKKEINDKE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 870 SHIKTL----TERLLKMKDWAAMLGEDITDDDNLELEMNSESENGAYLdNPPKGALKKLIHAAKLN-----ASLKTLEgE 940
Cdd:pfam05483 240 KQVSLLliqiTEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKEL-IEKKDHLTKELEDIKMSlqrsmSTQKALE-E 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 941 RNQIYI------------QLSEVDKTKEELTEHIKNLQTEQASLQ----SENTHFENENQKLqqKLKVMTELYQENEMKL 1004
Cdd:pfam05483 318 DLQIATkticqlteekeaQMEELNKAKAAHSFVVTEFEATTCSLEellrTEQQRLEKNEDQL--KIITMELQKKSSELEE 395
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 694955909 1005 HRKLTVEENYRLEKEEKLSKVDEKISHATEELETyrkrakdLEEELERTIHSYQGQIISHEKKAHD 1070
Cdd:pfam05483 396 MTKFKNNKEVELEELKKILAEDEKLLDEKKQFEK-------IAEELKGKEQELIFLLQAREKEIHD 454
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
681-1046 |
2.30e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.20 E-value: 2.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 681 GREKKLALMLSGLIEEKSKLLEKFSLVQKEYEgyEVESSLKDASFEKEATEAQ------SLEATCEKLNRSNSELEDEIL 754
Cdd:COG4372 17 GLRPKTGILIAALSEQLRKALFELDKLQEELE--QLREELEQAREELEQLEEEleqarsELEQLEEELEELNEQLQAAQA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 755 CLEKELKEEKSKHSERDEL---MADISKRIQSLEDESKSLKSQVAEakmtfkifqmneerLKIAIKDALNENSQLQESQK 831
Cdd:COG4372 95 ELAQAQEELESLQEEAEELqeeLEELQKERQDLEQQRKQLEAQIAE--------------LQSEIAEREEELKELEEQLE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 832 QLLQEAEVWKEQVSELNKQKVTFEDSEVHAEqvLNDKESHIKTLTERLLKMKDWAAMLGEDITDDDNLELEMNSESENGA 911
Cdd:COG4372 161 SLQEELAALEQELQALSEAEAEQALDELLKE--ANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSAL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 912 YLDNPPKGALKKLIHAAKLNASLKTLEGERNQIYIQLSEVDKTKEELTEHIKNLQTEQASLQSENTHFENENQKLQQKLK 991
Cdd:COG4372 239 LDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALL 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 694955909 992 vmtELYQENEMKLHRKLTVEENYRLEKEEKLSKVDEKISHATEELETYRKRAKDL 1046
Cdd:COG4372 319 ---AALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGVADG 370
|
|
| YabA |
COG4467 |
Regulator of replication initiation timing YabA [Replication, recombination and repair]; |
940-1007 |
2.30e-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: 2.30e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 694955909 940 ERNQIYIQLSEVDKTKEELTEHIKNLQTEQASLQSENTHFENENQKLQQKLKVMTELYQENEMKLHRK 1007
Cdd:COG4467 2 DKKELFDRLSELEEQLGELLKELGELKDEVAELLEENARLRIENEHLRERLEELEKKKEKKAEKDIGE 69
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
769-1109 |
2.47e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 42.50 E-value: 2.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 769 ERDELMADISKRIQSLEDESKSlkSQVAEAKMtfkifqmnEERL--KIAIKDALNEnsQLQESQKQLLQEAEVWKEQVSE 846
Cdd:pfam10174 412 DKDKQLAGLKERVKSLQTDSSN--TDTALTTL--------EEALseKERIIERLKE--QREREDRERLEELESLKKENKD 479
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 847 LnKQKVTFEDSEV-HAEQVLNDKESHIKTLTERLLKmkdwaamlgediTDDDNLELEMNSEsengayldnppkgalKKLI 925
Cdd:pfam10174 480 L-KEKVSALQPELtEKESSLIDLKEHASSLASSGLK------------KDSKLKSLEIAVE---------------QKKE 531
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 926 HAAKLNASLKTLEgernqiyiQLSEVDKTKEELTEHIKNLQTEQASLQSENTHFENENQKLQQKLKVMtelyqenemklh 1005
Cdd:pfam10174 532 ECSKLENQLKKAH--------NAEEAVRTNPEINDRIRLLEQEVARYKEESGKAQAEVERLLGILREV------------ 591
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 1006 rkltveENYRLEKEEKLSKVDEKISHATEELETYRKRAKDLEEELERTihsyQGQIISHEKKAHDNwLAARNAERNLNDL 1085
Cdd:pfam10174 592 ------ENEKNDKDKKIAELESLTLRQMKEQNKKVANIKHGQQEMKKK----GAQLLEEARRREDN-LADNSQQLQLEEL 660
|
330 340
....*....|....*....|....*....
gi 694955909 1086 RKENAHNRQKLTETELKFE-----LLEKD 1109
Cdd:pfam10174 661 MGALEKTRQELDATKARLSstqqsLAEKD 689
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
723-1053 |
2.78e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 42.33 E-value: 2.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 723 ASFEKEATEAQSLEATCEKLN-------RSNSELEDEIlclEKELKEEKSKHSERDELMAD----------ISKRIQSLE 785
Cdd:PRK02224 244 EEHEERREELETLEAEIEDLRetiaeteREREELAEEV---RDLRERLEELEEERDDLLAEaglddadaeaVEARREELE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 786 DESKSLKSQVAEAKMTFKIFQMNEERLKIAIKDALNENSQLQESQKQL---LQEAEV----WKEQVSELNKQKVTFEDSE 858
Cdd:PRK02224 321 DRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELeseLEEAREavedRREEIEELEEEIEELRERF 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 859 VHAEQVLNDKESHIKTLTERLlkmkdwaAMLGEDITdddnlELEMNSESENGAYLDNppkgalKKLIHAAKLNASLKTLE 938
Cdd:PRK02224 401 GDAPVDLGNAEDFLEELREER-------DELREREA-----ELEATLRTARERVEEA------EALLEAGKCPECGQPVE 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 939 GErnQIYIQLSEVDKTKEELTEHIKNLQTEQASLQSENTHF------ENENQKLQQKLKVMTELYQEnemklhRKLTVEE 1012
Cdd:PRK02224 463 GS--PHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAedlveaEDRIERLEERREDLEELIAE------RRETIEE 534
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 694955909 1013 nyrleKEEKLSKVDEKISHATEELETYRKRAKDLEEELERT 1053
Cdd:PRK02224 535 -----KRERAEELRERAAELEAEAEEKREAAAEAEEEAEEA 570
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
782-1079 |
2.87e-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: 2.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 782 QSLEDESKSLKSQVAE--AKMTFKIFQMNEE-----RLKIAI---KDAL-NENSQLQESQKQLLQeaevwKEQVSELNKQ 850
Cdd:pfam01576 334 KALEEETRSHEAQLQEmrQKHTQALEELTEQleqakRNKANLekaKQALeSENAELQAELRTLQQ-----AKQDSEHKRK 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 851 KVTFEDSEVHAEqvLNDKESHIKTLTERLLKMK----DWAAMLGEdiTDDDNLELEMNSESENGAYLDNPpkgALKKLIH 926
Cdd:pfam01576 409 KLEGQLQELQAR--LSESERQRAELAEKLSKLQseleSVSSLLNE--AEGKNIKLSKDVSSLESQLQDTQ---ELLQEET 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 927 AAKLNAS--LKTLEGERNQIYIQLSEVDKTKEELTEHIKNLQTEQASLQsenthfenenQKLQQKLKVMtELYQENEMKL 1004
Cdd:pfam01576 482 RQKLNLStrLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMK----------KKLEEDAGTL-EALEEGKKRL 550
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 1005 HRKLtveENYRLEKEEKlskvdekiSHATEELETYRKRakdLEEELERTI--HSYQGQIISH-EKK--------AHDNWL 1073
Cdd:pfam01576 551 QREL---EALTQQLEEK--------AAAYDKLEKTKNR---LQQELDDLLvdLDHQRQLVSNlEKKqkkfdqmlAEEKAI 616
|
....*.
gi 694955909 1074 AARNAE 1079
Cdd:pfam01576 617 SARYAE 622
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
921-1107 |
2.92e-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: 41.44 E-value: 2.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 921 LKKLIHAAKLNASLKTLEGERNQIYIQLSEVDKTKEELTE--HIKNLQTEQASL-----QSENTHFENENQ---KLQQKL 990
Cdd:pfam13868 11 LNSKLLAAKCNKERDAQIAEKKRIKAEEKEEERRLDEMMEeeRERALEEEEEKEeerkeERKRYRQELEEQieeREQKRQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 991 KVMTELYQENEMKLHRKLTVEENYRLEKEEKLSKVDEK---ISHATEELETYRKRAKDLEEELERTIHSYQGQIISHEKK 1067
Cdd:pfam13868 91 EEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLreeIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEE 170
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 694955909 1068 AHDNWLAARNA-ERNLNDLRKENAHNRQKLTE-TELKFELLE 1107
Cdd:pfam13868 171 REAEREEIEEEkEREIARLRAQQEKAQDEKAErDELRAKLYQ 212
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
806-1053 |
3.17e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.43 E-value: 3.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 806 QMNEERLKIAIKDALNENSQLQESQKQLLQEAEVWKEQVSELNKQKVTFEDsevHAEQVLNDKESHIKTLTERLLKMKDW 885
Cdd:COG1340 7 SSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELRE---EAQELREKRDELNEKVKELKEERDEL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 886 AAMLGEDITDDDNLELEMNSESENGayldnPPKGALKKLIhaAKL-----NASLkTLEGERnQIYIQLSEVD------KT 954
Cdd:COG1340 84 NEKLNELREELDELRKELAELNKAG-----GSIDKLRKEI--ERLewrqqTEVL-SPEEEK-ELVEKIKELEkelekaKK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 955 KEELTEHIKNLQTEQASLQSE-NTHFENEN---QKLQQKLKVMTELYQE-NEMK-----LHRKLtveenyrLEKEEKLSK 1024
Cdd:COG1340 155 ALEKNEKLKELRAELKELRKEaEEIHKKIKelaEEAQELHEEMIELYKEaDELRkeadeLHKEI-------VEAQEKADE 227
|
250 260
....*....|....*....|....*....
gi 694955909 1025 VDEKISHATEELETYRKRAKDLEEELERT 1053
Cdd:COG1340 228 LHEEIIELQKELRELRKELKKLRKKQRAL 256
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1017-1100 |
3.26e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 41.67 E-value: 3.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 1017 EKEEKLSKVDEKISHATEELETYRKRAKDLEEELERTihsyQGQIISHEKKAHDNWLAARNAERNLNDLRKENAHNRQKL 1096
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAAL----ERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
....
gi 694955909 1097 TETE 1100
Cdd:COG4942 100 EAQK 103
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
928-1100 |
4.29e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 41.49 E-value: 4.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 928 AKLNASLKTLEGERNQIYIQLSEVDKTKEELTEHIKNLQTEQASLQSENTHFENENQKLQQKLKVMTELYQ--------E 999
Cdd:TIGR00618 194 GKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQlrarieelR 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 1000 NEMKLHRKLTVEENYRLEKE------EKLSKVDEKISHATEEL-ETYRKRAKDLEeelERTIHSYQGQIISHEKKAHDNW 1072
Cdd:TIGR00618 274 AQEAVLEETQERINRARKAAplaahiKAVTQIEQQAQRIHTELqSKMRSRAKLLM---KRAAHVKQQSSIEEQRRLLQTL 350
|
170 180
....*....|....*....|....*....
gi 694955909 1073 LAARNAERNLNDLRKE-NAHNRQKLTETE 1100
Cdd:TIGR00618 351 HSQEIHIRDAHEVATSiREISCQQHTLTQ 379
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
669-851 |
4.62e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 41.58 E-value: 4.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 669 RSFRSVRSRLY-----VGREKKLALMLSGLIEEKSKLLEKFSLVQKEYE--GYEVESSLKDASFEKEATEAQSleatcEK 741
Cdd:TIGR02168 817 EEAANLRERLEslerrIAATERRLEDLEEQIEELSEDIESLAAEIEELEelIEELESELEALLNERASLEEAL-----AL 891
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 742 LNRSNSELEDEILCLEKELKEEKSKHSERDELMADISKRIQSLEDESKSLKSQVAE-AKMTFKIFQMNEERLKIAIKDAL 820
Cdd:TIGR02168 892 LRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEeYSLTLEEAEALENKIEDDEEEAR 971
|
170 180 190
....*....|....*....|....*....|....*...
gi 694955909 821 NENSQLQESQKQL-------LQEAEVWKEQVSELNKQK 851
Cdd:TIGR02168 972 RRLKRLENKIKELgpvnlaaIEEYEELKERYDFLTAQK 1009
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
929-1114 |
5.23e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.04 E-value: 5.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 929 KLNASLKTLEGERNQIYIQLSEVDKTKEELTEHIKNLQTEQASLQSENTHFENENQKLQQKLKvmtELYQENEmklhrKL 1008
Cdd:COG4372 56 QAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELE---ELQKERQ-----DL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 1009 TVEENyrlEKEEKLSKVDEKISHATEELETYRKRAKDLEEELERTIHSYQGQIISHEKKAHDNWLAARNAERNLNDLRKE 1088
Cdd:COG4372 128 EQQRK---QLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAE 204
|
170 180
....*....|....*....|....*.
gi 694955909 1089 NAHNRQKLTETELKFELLEKDPYALD 1114
Cdd:COG4372 205 AEKLIESLPRELAEELLEAKDSLEAK 230
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
923-1099 |
6.06e-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: 40.51 E-value: 6.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 923 KLIHAAKLNASLKTLEGErNQIYIQLSEVDKTKEELTEHIKNLQTEQASLQSENTHFENenqklQQKLKVMTelYQENEM 1002
Cdd:pfam09787 25 KLIASLKEGSGVEGLDSS-TALTLELEELRQERDLLREEIQKLRGQIQQLRTELQELEA-----QQQEEAES--SREQLQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 1003 KLHRKLTVEENYRLEKEEKLSKVDEKISHateeletyrkrakdLEEELERTIHSYQGQIISHEKKAHDnwLAARNAERNL 1082
Cdd:pfam09787 97 ELEEQLATERSARREAEAELERLQEELRY--------------LEEELRRSKATLQSRIKDREAEIEK--LRNQLTSKSQ 160
|
170
....*....|....*...
gi 694955909 1083 NDLRKENAHNRQK-LTET 1099
Cdd:pfam09787 161 SSSSQSELENRLHqLTET 178
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
667-1085 |
6.13e-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: 41.19 E-value: 6.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 667 LWRSFRSVRSRLYVGREKKLALMLSGLIEEKskllekfslvqkEYEGYEVESSLKD--ASFEKEATEAQSLEATCEKLNR 744
Cdd:TIGR01612 657 IYSTIKSELSKIYEDDIDALYNELSSIVKEN------------AIDNTEDKAKLDDlkSKIDKEYDKIQNMETATVELHL 724
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 745 SNSEledeilclekelkeekSKHSERDELMADISKRIQSleDESKSLKSQVAEakmtfkiFQMNEERLKIAIKDALNENS 824
Cdd:TIGR01612 725 SNIE----------------NKKNELLDIIVEIKKHIHG--EINKDLNKILED-------FKNKEKELSNKINDYAKEKD 779
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 825 QLQESQKQLLQEAEVWKEQVSELNKQ----KVTFEDSEVHAEQVLNDKESHIKTLTERLLKMKDWAAMLGEDITDDDNLE 900
Cdd:TIGR01612 780 ELNKYKSKISEIKNHYNDQINIDNIKdedaKQNYDKSKEYIKTISIKEDEIFKIINEMKFMKDDFLNKVDKFINFENNCK 859
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 901 LEMNSESENGAYLDNPPKGAL--------KKLIHAAK--LNASLKTLEGERNQIYiQLSEVD---KTKEELTEHIKNLQT 967
Cdd:TIGR01612 860 EKIDSEHEQFAELTNKIKAEIsddklndyEKKFNDSKslINEINKSIEEEYQNIN-TLKKVDeyiKICENTKESIEKFHN 938
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 968 EQASLqsenthfeneNQKLQQKLKVMTE---LYQENEMKLHRKLTVEENyRLEKEEKLSKVDEKISHATEELETYRKRAK 1044
Cdd:TIGR01612 939 KQNIL----------KEILNKNIDTIKEsnlIEKSYKDKFDNTLIDKIN-ELDKAFKDASLNDYEAKNNELIKYFNDLKA 1007
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 694955909 1045 DLEEELERTIhsYQgQIISHEKKAHDNWLAARNAERNLNDL 1085
Cdd:TIGR01612 1008 NLGKNKENML--YH-QFDEKEKATNDIEQKIEDANKNIPNI 1045
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
926-1109 |
6.33e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.66 E-value: 6.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 926 HAAKLNASLKTLEGERNQIYIQLSEVDKTKEELTEHIKNLQTEQASLQSENTHFENENQKLQQKLKVMTELYQENEMKLH 1005
Cdd:COG4372 4 LGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 1006 rkltveenyrlEKEEKLSKVDEKISHATEELETYRKRAKDLEEELERTIHSY-----QGQIISHEKKAHDNWLAARNAEr 1080
Cdd:COG4372 84 -----------ELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERqdleqQRKQLEAQIAELQSEIAEREEE- 151
|
170 180
....*....|....*....|....*....
gi 694955909 1081 nLNDLRKENAHNRQKLTETELKFELLEKD 1109
Cdd:COG4372 152 -LKELEEQLESLQEELAALEQELQALSEA 179
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
715-1052 |
6.76e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.79 E-value: 6.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 715 EVESSLKDAS-----FEKEAT----EAQSLEATCEKLNRSNSELEDEILCLEKELKEEKSKHSERDELMADISKRI---- 781
Cdd:PRK02224 325 ELRDRLEECRvaaqaHNEEAEslreDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFgdap 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 782 ---QSLEDESKSLKSQVAEAKMtfkifQMNEERLKI-AIKDALNENSQLQESQK-----QLLQEA------EVWKEQVSE 846
Cdd:PRK02224 405 vdlGNAEDFLEELREERDELRE-----REAELEATLrTARERVEEAEALLEAGKcpecgQPVEGSphvetiEEDRERVEE 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 847 LNKQKVTFEDSEVHAEQVLNDKESHIKTLT--ERLLKMKDWAAMLGED---ITDDDNLELEmnSESENGAYLDNppkgal 921
Cdd:PRK02224 480 LEAELEDLEEEVEEVEERLERAEDLVEAEDriERLEERREDLEELIAErreTIEEKRERAE--ELRERAAELEA------ 551
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 922 kkliHAAKLNASLKTLEGERNQIYIQLSEVDKTKEELTEHIKNLQTeQASLQSENTHFENENQKLQQKLKVMTELYQENE 1001
Cdd:PRK02224 552 ----EAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLER-IRTLLAAIADAEDEIERLREKREALAELNDERR 626
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 694955909 1002 MKL----HRKLTVEENY---RLEK--------EEKLSKVDEKISHATEELETYRKRAKDLEEELER 1052
Cdd:PRK02224 627 ERLaekrERKRELEAEFdeaRIEEaredkeraEEYLEQVEEKLDELREERDDLQAEIGAVENELEE 692
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
701-1110 |
7.25e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 40.98 E-value: 7.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 701 LEKFSLVQKEYEGYEVESSLKDASFEKEATEAQSLEATCEKLnRSN--SELEDEIlclEKELKEEKSKHSERDELMADIS 778
Cdd:pfam12128 339 IETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRR-RSKikEQNNRDI---AGIKDKLAKIREARDRQLAVAE 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 779 KRIQSLEDEsksLKSQVAEAKMTFKIfqmNEERLKIAIKDALNENSQLQESQKQLLQEAEvwkeQVSELNKQKVTFEDSE 858
Cdd:pfam12128 415 DDLQALESE---LREQLEAGKLEFNE---EEYRLKSRLGELKLRLNQATATPELLLQLEN----FDERIERAREEQEAAN 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 859 VHAEQvLNDKESHIKTLTER-LLKMKDWAAMLGEDITDDDNLELEMNSES---------ENGAYLDNPPKGALKKLIHAA 928
Cdd:pfam12128 485 AEVER-LQSELRQARKRRDQaSEALRQASRRLEERQSALDELELQLFPQAgtllhflrkEAPDWEQSIGKVISPELLHRT 563
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 929 KLNASLK-------------TLEGERNQIYIQLSEVDKTKEELTEHIKNLQTEQASLQSENTHFENENQKLQQKLKVMT- 994
Cdd:pfam12128 564 DLDPEVWdgsvggelnlygvKLDLKRIDVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETf 643
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 995 --ELYQENEMKLHRKLTVEENYRLEKEEKLSkvdEKISHATEELETYRKRAKDLEEELERTIHSYQGQIISHEKKAHDNW 1072
Cdd:pfam12128 644 arTALKNARLDLRRLFDEKQSEKDKKNKALA---ERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYW 720
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 694955909 1073 LAARNAERNLNDL-------RKENAHNRQKLTETELKFELLEKDP 1110
Cdd:pfam12128 721 QVVEGALDAQLALlkaaiaaRRSGAKAELKALETWYKRDLASLGV 765
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
712-1047 |
7.34e-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: 40.80 E-value: 7.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 712 EGYEVESSLKDASFEKEATEAQSLEatcekLNRSNSELEDEILCLEKELKEEKSKHSERDELMADISKRIQSLEDESKSL 791
Cdd:TIGR00606 795 ERFQMELKDVERKIAQQAAKLQGSD-----LDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNEL 869
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 792 KS---QVAEAKMTFKIFQMNEERLKI-------AIKDALNENSQLQESQKQLLQEAEvwkEQVSELNKQKVTFEDSEVHA 861
Cdd:TIGR00606 870 KSeklQIGTNLQRRQQFEEQLVELSTevqslirEIKDAKEQDSPLETFLEKDQQEKE---ELISSKETSNKKAQDKVNDI 946
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 862 EQVLNDKESHIKTLTERLLKMKDWAAMLGEDITDDDNLELEMNSESENGAyldNPPKGALKKLIHAAKLNASLKTLEGER 941
Cdd:TIGR00606 947 KEKVKNIHGYMKDIENKIQDGKDDYLKQKETELNTVNAQLEECEKHQEKI---NEDMRLMRQDIDTQKIQERWLQDNLTL 1023
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 942 NQIYIQLSEVdktKEELTEHIKNLQTEQAslqsenTHFENENQKLQQKLkvmtELYQENEMKLHRKLTVEENYRLEKEEK 1021
Cdd:TIGR00606 1024 RKRENELKEV---EEELKQHLKEMGQMQV------LQMKQEHQKLEENI----DLIKRNHVLALGRQKGYEKEIKHFKKE 1090
|
330 340 350
....*....|....*....|....*....|.
gi 694955909 1022 LSK-----VDEKISHATEELETYRKRAKDLE 1047
Cdd:TIGR00606 1091 LREpqfrdAEEKYREMMIVMRTTELVNKDLD 1121
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
697-989 |
8.72e-03 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 40.18 E-value: 8.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 697 KSKLLEK--FSLVQkeyEGYEVESSLKDASFEKEATEAQSLEATCEK--LNRSNSELEDEILCLEKELKEEKSKHSERDE 772
Cdd:pfam15905 74 DQKELEKeiRALVQ---ERGEQDKRLQALEEELEKVEAKLNAAVREKtsLSASVASLEKQLLELTRVNELLKAKFSEDGT 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 773 lmadiSKRIQSLEDESKSLKSQVaEAKMtfKIFQMNEERLKIaikdalnensQLQESQKQLLQEaevwKEQVSELNKQKV 852
Cdd:pfam15905 151 -----QKKMSSLSMELMKLRNKL-EAKM--KEVMAKQEGMEG----------KLQVTQKNLEHS----KGKVAQLEEKLV 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 853 TFEDSEV----HAEQVLNDKEsHIKTLTERLLKMKDWAAMLGEDI-TDDDNLELEMNSESENgayldnppKGALKKLIHa 927
Cdd:pfam15905 209 STEKEKIeeksETEKLLEYIT-ELSCVSEQVEKYKLDIAQLEELLkEKNDEIESLKQSLEEK--------EQELSKQIK- 278
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 694955909 928 aKLNASLKTLEGERNQIyiqLSEvDKTKEEltehikNLQTEQASLQSENTHFENENQKLQQK 989
Cdd:pfam15905 279 -DLNEKCKLLESEKEEL---LRE-YEEKEQ------TLNAELEELKEKLTLEEQEHQKLQQK 329
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
724-1104 |
9.30e-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: 40.80 E-value: 9.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 724 SFEKEATEAQSLEATCEKLNRSNSELEDEILCLEKELKEEKSKHSERDELM----------------------------- 774
Cdd:TIGR00606 242 SYENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMekvfqgtdeqlndlyhnhqrtvrekerel 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 775 ADISKRIQSLEDESKSLKSQVAEAKMTFKIFQMNEERLK--IAIKDALNENSQLQESQKQLLQEAEVWKEQVSELNKQKV 852
Cdd:TIGR00606 322 VDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQehIRARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVIE 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 853 TFEDSEVHAEQVLNDKESHIKTLTERLLKMKDWAAMLGEDITDDDNLELEMNSESENGAYLDNPPKGALKKLIhaaKLNA 932
Cdd:TIGR00606 402 RQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRIL---ELDQ 478
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 933 SLKTLEGErnqiyIQLSEVDKTKEELTEHIKNLQTEQASLQSENTHFENENQKLQQKlkvmTELYQENEMKLHRKLTVEE 1012
Cdd:TIGR00606 479 ELRKAERE-----LSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHH----TTTRTQMEMLTKDKMDKDE 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 1013 NYRlekEEKLSKVDEKISHATEELETyrkrakdleEELERTIHSYQGQIISHEKKAHDNWLAARNAERNLNDLRKEnahn 1092
Cdd:TIGR00606 550 QIR---KIKSRHSDELTSLLGYFPNK---------KQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNE---- 613
|
410
....*....|..
gi 694955909 1093 RQKLTETELKFE 1104
Cdd:TIGR00606 614 LESKEEQLSSYE 625
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
817-1131 |
9.43e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 40.45 E-value: 9.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 817 KDALNENSQLQESQKQLLQEA-EVWKEQVSELNKQKvtFEDSEVHAEQV--LNDKESHIKTLTERLLKMK---------- 883
Cdd:COG5022 815 YLACIIKLQKTIKREKKLRETeEVEFSLKAEVLIQK--FGRSLKAKKRFslLKKETIYLQSAQRVELAERqlqelkidvk 892
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 884 ------------DWAAM-LGEDITDDDNLELEMNSESE-------NGAYLDNPPKGALKKLIHAAKL---NASLKTLEGE 940
Cdd:COG5022 893 sisslklvnlelESEIIeLKKSLSSDLIENLEFKTELIarlkkllNNIDLEEGPSIEYVKLPELNKLhevESKLKETSEE 972
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 941 RNQIYIQL-----------SEVDKTKEELTEHIKNLQTEQASLQS--ENTHFENENQKLQQKLKVM-TELYQENEM-KLH 1005
Cdd:COG5022 973 YEDLLKKStilvregnkanSELKNFKKELAELSKQYGALQESTKQlkELPVEVAELQSASKIISSEsTELSILKPLqKLK 1052
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694955909 1006 RKLTVEENYrLEKEEKLSKVDEKISHATEELETYRKRAKDLEEELERTIHSYQGQIISHEKKAHDNwlaARNAERNLNDL 1085
Cdd:COG5022 1053 GLLLLENNQ-LQARYKALKLRRENSLLDDKQLYQLESTENLLKTINVKDLEVTNRNLVKPANVLQF---IVAQMIKLNLL 1128
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 694955909 1086 RKENAHNRQKLTETELKFELLEKDPYALDVPNTAFGREHSPYGPSP 1131
Cdd:COG5022 1129 QEISKFLSQLVNTLEPVFQKLSVLQLELDGLFWEANLEALPSPPPF 1174
|
|
| |
