|
Name |
Accession |
Description |
Interval |
E-value |
| SH3_MIA3 |
cd11893 |
Src Homology 3 domain of Melanoma Inhibitory Activity 3 protein; MIA3, also called TANGO or ... |
38-109 |
2.60e-39 |
|
Src Homology 3 domain of Melanoma Inhibitory Activity 3 protein; MIA3, also called TANGO or TANGO1, acts as a tumor suppressor of malignant melanoma. It is downregulated or lost in melanoma cells lines. Unlike other MIA family members, MIA3 is widely expressed except in hematopoietic cells. MIA3 is an ER resident transmembrane protein that is required for the loading of collagen VII into transport vesicles. SNPs in the MIA3 gene have been associated with coronary arterial disease and myocardial infarction. MIA3 contains an N-terminal SH3-like domain, similar to MIA. It is a member of the recently identified family that also includes MIA, MIAL, and MIA2. MIA is a single domain protein that adopts a SH3 domain-like fold; it contains an additional antiparallel beta sheet and two disulfide bonds compared to classical SH3 domains. Unlike classical SH3 domains, MIA does not bind proline-rich ligands.
Pssm-ID: 212826 Cd Length: 73 Bit Score: 140.75 E-value: 2.60e-39
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907069526 38 CGDEECSMLMYRGKALEDFTGPDCRFVNFKKGDDVYVYYKLAGGSLELWAGSVEHSFGYFPKDLIKVLHKYT 109
Cdd:cd11893 2 CADEECSMLLCRGKAVKDFTGPDCRFLSFKKGETIYVYYKLSGRRTDLWAGSVGFDFGYFPKDLLDVNHLYT 73
|
|
| SH3_MIA_like |
cd11760 |
Src Homology 3 domain of Melanoma Inhibitory Activity protein and similar proteins; MIA is a ... |
38-109 |
1.66e-32 |
|
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: 121.43 E-value: 1.66e-32
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907069526 38 CGDEECSMLMYRGKALEDFTGPDCRFVNFKKGDDVYVYYKLAGGSLELWAGSVEHS---FGYFPKDLIKVLHKYT 109
Cdd:cd11760 2 CADAECSNPISRARALEDYHGPDCRFLNFKKGDTIYVYSKLAGERQDLWAGSVGGDaglFGYFPKNLVQELKVYE 76
|
|
| SH3_MIA2 |
cd11892 |
Src Homology 3 domain of Melanoma Inhibitory Activity 2 protein; MIA2 is expressed ... |
38-115 |
4.88e-27 |
|
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: 105.69 E-value: 4.88e-27
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907069526 38 CGDEECSMLMYRGKALEDFTGPDCRFVNFKKGDDVYVYYKLAGGSLELWAGSVEHSFGYFPKDLIKVlhkyteEELHI 115
Cdd:cd11892 2 CGDPECERLMSRVQAIRDYRGPDCRYLSFKKGDEIIVYYKLSGKREDLWAGSTGKEFGYFPKDAVKV------EEVYI 73
|
|
| MIAL |
cd11891 |
Melanoma Inhibitory Activity-Like protein; MIAL is specifically expressed in the cochlea and ... |
37-108 |
5.62e-19 |
|
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: 82.98 E-value: 5.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 37 VCGDEECSMLMYRGKALEDFTGPDCRFVNFKKGDDVYVYYKLA--GGSLELWAGSV--EH------SFGYFPKDLIKVLH 106
Cdd:cd11891 1 LCADEECVYAISLARAEDDYNAPDCRFINIKKGQLIYVYSKLVkeNGAGEFWSGSVysERyvdqmgIVGYFPSNLVKEQT 80
|
..
gi 1907069526 107 KY 108
Cdd:cd11891 81 VY 82
|
|
| MIA |
cd11890 |
Melanoma Inhibitory Activity protein; MIA is a single domain protein that adopts a Src ... |
36-124 |
3.61e-18 |
|
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: 81.46 E-value: 3.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 36 KVCGDEECSMLMYRGKALEDFTGPDCRFVNFKKGDDVYVYYKLAGGSLELWAGSVEHSF--------GYFPKDLIKVLHK 107
Cdd:cd11890 2 KLCADQECSHPISIAVALQDYMAPDCRFIPIQRGQVVYVFSKLKGRGRLFWGGSVQGDYygeqaarlGYFPSSIVQEDQY 81
|
90
....*....|....*..
gi 1907069526 108 YTEEELHIPADETDFVC 124
Cdd:cd11890 82 LKPGKVEVKTDKWDFYC 98
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1241-1606 |
1.91e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 76.25 E-value: 1.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1241 KQISEKLENIKKENAELMQKLSSYEQKIKESKKYVQETKKQNMILSDEAVKYKDKIKILEETNVSLGDKAKSLRLQLESE 1320
Cdd:TIGR02168 687 EELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEEL 766
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1321 REQNVKNQDLILENKKSIEKLKDVISMNASELSEVQVALNEAKLSEENVKSECHRVQEENARLKKKKEQLQQQVEEWSKS 1400
Cdd:TIGR02168 767 EERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQ 846
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1401 HAELTEQIKSFEKSQEDLEialthkddnisaltnciTQLNRLECELESEdpdkggnesddlangetggdrsEKIRNRIkq 1480
Cdd:TIGR02168 847 IEELSEDIESLAAEIEELE-----------------ELIEELESELEAL----------------------LNERASL-- 885
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1481 mmdvsrtqtavsivEEDLKLLQLKLRASMSTKCNLEDQIKKLEDDRSSLQTAKAGLEDECKTLRQKV----EILNELYQQ 1556
Cdd:TIGR02168 886 --------------EEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIdnlqERLSEEYSL 951
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1907069526 1557 KEMALQKKLSQEEYERQDREQRLTAADEK------VVLAA-EEVKTYKRRIEEMEEE 1606
Cdd:TIGR02168 952 TLEEAEALENKIEDDEEEARRRLKRLENKikelgpVNLAAiEEYEELKERYDFLTAQ 1008
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1239-1625 |
4.37e-13 |
|
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: 74.67 E-value: 4.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1239 TEKQISEKLENIKKENAELMQK------LSSYEQKIKESKKYVQETKKQNMILSDEAVK--------------------- 1291
Cdd:TIGR04523 178 LEKEKLNIQKNIDKIKNKLLKLelllsnLKKKIQKNKSLESQISELKKQNNQLKDNIEKkqqeinektteisntqtqlnq 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1292 -----------YKDKIKILEETNVSLGDKAKSLRlQLESERE--QNVKNQDLILENKKSIEKLKDVISMNASELSEVQVA 1358
Cdd:TIGR04523 258 lkdeqnkikkqLSEKQKELEQNNKKIKELEKQLN-QLKSEISdlNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKI 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1359 LNEAKLSEENVKSECHRVQEENARLKKKKEQLQQQVEEWSKSHAELTEQIKSFEKSQEDLEIALTH-------KDDNISA 1431
Cdd:TIGR04523 337 ISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNqeklnqqKDEQIKK 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1432 LTnciTQLNRLECELE--SEDPDKGGNESDDLANGETggdRSEKIRNRIKQMMDVSRTQtaVSIVEEDLKLLQLKLRASM 1509
Cdd:TIGR04523 417 LQ---QEKELLEKEIErlKETIIKNNSEIKDLTNQDS---VKELIIKNLDNTRESLETQ--LKVLSRSINKIKQNLEQKQ 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1510 STKCNLEDQIKKLEDDRSSLQTAKAGLEDECKTLRQKVEILNELYQQKEmalqKKLSQEEYERQDREQRLTAA------- 1582
Cdd:TIGR04523 489 KELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKE----SKISDLEDELNKDDFELKKEnlekeid 564
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1907069526 1583 --DEKVVLAAEEVKTYKRRIEEMEEELQKTERSFKN---QIAAHEKKA 1625
Cdd:TIGR04523 565 ekNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDlikEIEEKEKKI 612
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1331-1608 |
6.35e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 71.24 E-value: 6.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1331 ILENKKSIEKLKDVISMNASELSEVQVALNEAKLSEENVKSECHRVQEEnarlkkkkeqlqqqVEEWSKSHAELTEQIKS 1410
Cdd:TIGR02168 672 ILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKE--------------LEELSRQISALRKDLAR 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1411 FEKSQEDLEIALTHKDDNISALTNCITQLNRLECELES---EDPDKGGNESDDLANGEtggDRSEKIRNRIKQM-MDVSR 1486
Cdd:TIGR02168 738 LEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEelaEAEAEIEELEAQIEQLK---EELKALREALDELrAELTL 814
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1487 TQTAVSIVEEDLKLLQLKLRASMSTKCNLEDQIKKLEDDRSSLQTAKAGLEDECKTLRQKVEILNELYQQKE---MALQK 1563
Cdd:TIGR02168 815 LNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEealALLRS 894
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1907069526 1564 KLSQEEYERQDREQRLTAADEKVVLAAEEVKTYKRRIEEMEEELQ 1608
Cdd:TIGR02168 895 ELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRID 939
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1289-1620 |
1.37e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 66.62 E-value: 1.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1289 AVKYKDKIKILEETNVSLGDKAKSLRLQLESEREQnvknQDLILENKKSIEKLKDVISmnaSELSEVQVALNEAKLSEEN 1368
Cdd:TIGR02168 672 ILERRREIEELEEKIEELEEKIAELEKALAELRKE----LEELEEELEQLRKELEELS---RQISALRKDLARLEAEVEQ 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1369 VKSECHRVQEENARLKKKKEQLQQQVEEWSKSHAELTEQIKSFEKSQEDLEIALTHKDDNISALTNCITQLNRleceles 1448
Cdd:TIGR02168 745 LEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNE------- 817
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1449 edpdkggnesdDLANGETGGDRSEKIRNRIKQMMDVSRTQTAVsiVEEDLKLLQLKLRASMSTKCNLEDQIKKLEDDRSS 1528
Cdd:TIGR02168 818 -----------EAANLRERLESLERRIAATERRLEDLEEQIEE--LSEDIESLAAEIEELEELIEELESELEALLNERAS 884
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1529 LQTAKAGLEDECKTLRQKVEILN----ELYQQKEmALQKKLSQEEYE----RQDREQRLTAADEKVVLAAEEVKTYKRRI 1600
Cdd:TIGR02168 885 LEEALALLRSELEELSEELRELEskrsELRRELE-ELREKLAQLELRleglEVRIDNLQERLSEEYSLTLEEAEALENKI 963
|
330 340
....*....|....*....|
gi 1907069526 1601 EEMEEELQKTERSFKNQIAA 1620
Cdd:TIGR02168 964 EDDEEEARRRLKRLENKIKE 983
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1251-1608 |
2.81e-10 |
|
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: 65.86 E-value: 2.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1251 KKENAelMQKLSSYEQKIKESKKYVQETKKQNMILSDE---AVKYKDKIKILEETNVSLgdkaksLRLQLESEREQNVKN 1327
Cdd:TIGR02169 171 KKEKA--LEELEEVEENIERLDLIIDEKRQQLERLRRErekAERYQALLKEKREYEGYE------LLKEKEALERQKEAI 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1328 QDLILENKKSIEKLKDVISMNASELSEVQVALNEA-----KLSEEN---VKSECHRVQEENARLKKKKEQLQQQVEEWSK 1399
Cdd:TIGR02169 243 ERQLASLEEELEKLTEEISELEKRLEEIEQLLEELnkkikDLGEEEqlrVKEKIGELEAEIASLERSIAEKERELEDAEE 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1400 SHAELTEQIKSFEKSQEDLEIALTHKDDNISALTNCI----TQLNRLECELESEDPDkggnesddlaNGETgGDRSEKIR 1475
Cdd:TIGR02169 323 RLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYaelkEELEDLRAELEEVDKE----------FAET-RDELKDYR 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1476 NRIKQMmdvsrTQTAVSIVEEDLKLLQLKLRASMSTKcNLEDQIKKLEDDRSSLQTAKAGLEDECKTLRQKVEILNEL-- 1553
Cdd:TIGR02169 392 EKLEKL-----KREINELKRELDRLQEELQRLSEELA-DLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADls 465
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907069526 1554 -YQQKEMALQKKLSQEEYERQDREQRLTAADEKVVLAAEEVKTYKRRIEEMEEELQ 1608
Cdd:TIGR02169 466 kYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQ 521
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1241-1614 |
2.90e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 65.47 E-value: 2.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1241 KQISEKLENIKKENAELMQKLSSYEQKIKESKKYVQETKKqnmiLSDEAVKYKDKIKILEEtNVSLGDKAKSLRLQLESE 1320
Cdd:PRK03918 303 EEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEE----LKKKLKELEKRLEELEE-RHELYEEAKAKKEELERL 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1321 RE-------QNVKNQDLILENKKS-----IEKLKDVISMNASELSEVQVALNEAKlSEENVKSECHRVQEENARLKKKKE 1388
Cdd:PRK03918 378 KKrltgltpEKLEKELEELEKAKEeieeeISKITARIGELKKEIKELKKAIEELK-KAKGKCPVCGRELTEEHRKELLEE 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1389 QLQQqVEEWSKSHAELTEQIKSFEKSQEDLEIALThKDDNISALTNCITQLNRLECELESEDPDKGGNESDDLangETGG 1468
Cdd:PRK03918 457 YTAE-LKRIEKELKEIEEKERKLRKELRELEKVLK-KESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEY---EKLK 531
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1469 DRSEKIRNRIKqmmdvsrtqtavsIVEEDLKllqlKLRASMSTKCNLEDQIKKLEDDRSSL--QTAKAGLEDEcKTLRQK 1546
Cdd:PRK03918 532 EKLIKLKGEIK-------------SLKKELE----KLEELKKKLAELEKKLDELEEELAELlkELEELGFESV-EELEER 593
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907069526 1547 VEILNELYQQkemalQKKLSQEEYERQDREQRLTAADEKVVLAAEEVKTYKRRIEEMEEELQKTERSF 1614
Cdd:PRK03918 594 LKELEPFYNE-----YLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKY 656
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1244-1553 |
7.23e-10 |
|
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: 64.32 E-value: 7.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1244 SEKLENIKKENAELMQKLSSYEQKIKESKKYVQEtkkqnmiLSDEAVKYKDKIKILEETNVSLGDKAKSLRLQLES-ERE 1322
Cdd:TIGR02169 715 SRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSS-------LEQEIENVKSELKELEARIEELEEDLHKLEEALNDlEAR 787
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1323 QNvknQDLILENKKSIEKLKDVISMNASELSEVQVALNEAKLSEENVKSECHRVQEENARLKKKKEQLQQQVEEWSKSHA 1402
Cdd:TIGR02169 788 LS---HSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKE 864
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1403 ELTEQIKSFEKSQEDLEIALTHKDDNISALTNCITQLNRLECELESEDPDKGGNESDDLANGETGGDRSEKIRNRIKQMM 1482
Cdd:TIGR02169 865 ELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDE 944
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907069526 1483 DVSRTQTAVSIVEEDLKLLQLKLRASMSTKCNLEDQIKKLEDDRSSLQTAKAGLEDECKTLRQKVEILNEL 1553
Cdd:TIGR02169 945 EIPEEELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKK 1015
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1242-1624 |
1.36e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 63.62 E-value: 1.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1242 QISEKLENIKKEnAELMQKLSSYEQKIKESKKYVQETKKqnmilSDEAVKYKDKIKILEETNVSLGDKAKSLRLQLESER 1321
Cdd:PTZ00121 1395 EAKKKAEEDKKK-ADELKKAAAAKKKADEAKKKAEEKKK-----ADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEE 1468
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1322 EQNVKNQDLILENKKSIEKLKDVISMNASELSEVQVALNEAKLSEENVKSECHRVQEEnARLKKKKEQLQQQVEEWSKSH 1401
Cdd:PTZ00121 1469 AKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADE-AKKAEEAKKADEAKKAEEKKK 1547
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1402 AELTEQIKSFEKSQEDLEIALTHKDDNISALTNCITQLNRLECELESEDPDKGGNESDDLANGETGGDRSEKIR-NRIKQ 1480
Cdd:PTZ00121 1548 ADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKaEELKK 1627
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1481 MMDVSRT--QTAVSIVEEDLKLLQLKlRASMSTKCNLEDQIKKLEDDRSSLQTAKAGLEDEcktlRQKVEILNELYQQKE 1558
Cdd:PTZ00121 1628 AEEEKKKveQLKKKEAEEKKKAEELK-KAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDE----KKAAEALKKEAEEAK 1702
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907069526 1559 MALQKKLSQEEYERQDREQRltAADEKVVLAAEEVKTYKRRIEEMEEELQKTERSfKNQIAAHEKK 1624
Cdd:PTZ00121 1703 KAEELKKKEAEEKKKAEELK--KAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEE-KKKIAHLKKE 1765
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1241-1628 |
2.11e-09 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 62.73 E-value: 2.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1241 KQISEKLENIKKENAELMQKLSSYEQKIKESKKYVQETKKQNMILSDEAVKYKDKIKILEETNVSLGDKAKSLRLQLeSE 1320
Cdd:TIGR04523 317 KNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQI-ND 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1321 REQNVKNQDLILENK---------------KSIEKLKDVISMNASELSEV---------------------QVALNEAKL 1364
Cdd:TIGR04523 396 LESKIQNQEKLNQQKdeqikklqqekelleKEIERLKETIIKNNSEIKDLtnqdsvkeliiknldntreslETQLKVLSR 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1365 SEENVKSECHRVQEENARLKKKKEQLQQQVEEWSKSHAELTEQIKSFEKSQEDLEIALTHKDDNISALTNCITQLN---- 1440
Cdd:TIGR04523 476 SINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDfelk 555
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1441 --RLECELESEDP--DKGGNESDDLANGETGGD-----RSEKIRNRIKQ----MMDVSRTQTAVSIVEEDLKLLQLKLRA 1507
Cdd:TIGR04523 556 keNLEKEIDEKNKeiEELKQTQKSLKKKQEEKQelidqKEKEKKDLIKEieekEKKISSLEKELEKAKKENEKLSSIIKN 635
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1508 SMSTKCNLEDQIKKLEDDRSSLQTAKAGLEDECKTLRQKVEILNELYQQ--KEMALQKKlsqEEYERQDREQRLTAADEK 1585
Cdd:TIGR04523 636 IKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKIDDIIELMKDwlKELSLHYK---KYITRMIRIKDLPKLEEK 712
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1907069526 1586 vvlaaeevktYKrRIEEMEEELQKTERSFKNQIAAHEKKAHDN 1628
Cdd:TIGR04523 713 ----------YK-EIEKELKKLDEFSKELENIIKNFNKKFDDA 744
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1240-1624 |
2.89e-09 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 62.35 E-value: 2.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1240 EKQISEKLENIKKE--NAELMQK-----LSSYEQKIKESKKYVQETKKQNMILSDEAVKYKDKIKILEETNVSLGDKAKS 1312
Cdd:TIGR04523 35 EKQLEKKLKTIKNElkNKEKELKnldknLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKN 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1313 LRLQ----------LESEREQNVKNQDLILENKKSIEKLKDVISMNASElsevqvaLNEAKLSEENVK----SECHRVQE 1378
Cdd:TIGR04523 115 DKEQknklevelnkLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYND-------LKKQKEELENELnlleKEKLNIQK 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1379 ENARLKKKKEQLQ---QQVEEWSKSHAELTEQIKSFEKSQEDLEIALTHKDDNISALTNCI----TQLNRLECELEsEDP 1451
Cdd:TIGR04523 188 NIDKIKNKLLKLElllSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEIsntqTQLNQLKDEQN-KIK 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1452 DKGGNESDDLANGETGGDRSEKIRNRIKQMMDVSRTQTAVSI----------VEEDLKLLQLKLRASMSTKCNLEDQIKK 1521
Cdd:TIGR04523 267 KQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWnkelkselknQEKKLEEIQNQISQNNKIISQLNEQISQ 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1522 LEDDRSSLQTAKAGLEDECKTLRQKVEILNELYQQKEMALQKKLSQeeyeRQDREQRLTAADEKVVLAAEEVKTYKRRIE 1601
Cdd:TIGR04523 347 LKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQ----INDLESKIQNQEKLNQQKDEQIKKLQQEKE 422
|
410 420 430
....*....|....*....|....*....|...
gi 1907069526 1602 EMEEELQ----------KTERSFKNQIAAHEKK 1624
Cdd:TIGR04523 423 LLEKEIErlketiiknnSEIKDLTNQDSVKELI 455
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1241-1631 |
1.56e-08 |
|
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: 60.13 E-value: 1.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1241 KQISEKLENIKKENAELMQKLSSYEQKIKESKKYV-------QETKKQNMILSDEAVKYKDKIKILeetnvsLGDKAKSL 1313
Cdd:pfam15921 317 RQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLvlanselTEARTERDQFSQESGNLDDQLQKL------LADLHKRE 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1314 RlQLESEREQNVKNQDLILENKKSIEKLKDVISMNASELSEVQVALneaklseENVKSECHRVQEENARLKKKKEQLQQQ 1393
Cdd:pfam15921 391 K-ELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALL-------KAMKSECQGQMERQMAAIQGKNESLEK 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1394 V-----------EEWSKSHAELTEQ---IKSFEKSQEDLEIALTHKDDNISALTNCITQLnRLECELESEDPDKGGNESD 1459
Cdd:pfam15921 463 VssltaqlestkEMLRKVVEELTAKkmtLESSERTVSDLTASLQEKERAIEATNAEITKL-RSRVDLKLQELQHLKNEGD 541
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1460 DLANGET----------GGDRS-EKIRNRIKQMMDV----SRTQTAVSI----VEEDLKLLQLKLRASMSTKCNLEDQIK 1520
Cdd:pfam15921 542 HLRNVQTecealklqmaEKDKViEILRQQIENMTQLvgqhGRTAGAMQVekaqLEKEINDRRLELQEFKILKDKKDAKIR 621
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1521 KLEDDRSSLQTakagledecktlrQKVEILNelyqqkemALQKKLSQEEYERQDREQRLTaadekvvlaaeEVKTYKRRI 1600
Cdd:pfam15921 622 ELEARVSDLEL-------------EKVKLVN--------AGSERLRAVKDIKQERDQLLN-----------EVKTSRNEL 669
|
410 420 430
....*....|....*....|....*....|.
gi 1907069526 1601 EEMEEELQKTERSFKNQiaAHEKKAHDNWLK 1631
Cdd:pfam15921 670 NSLSEDYEVLKRNFRNK--SEEMETTTNKLK 698
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1237-1625 |
1.95e-08 |
|
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: 59.69 E-value: 1.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1237 QVTEKQISEKLENikkenaelMQKLssyEQKIKESKKYVQETKKQnmilSDEAVKYKDKIKILEETNVSLgdkaksLRLQ 1316
Cdd:TIGR02168 175 KETERKLERTREN--------LDRL---EDILNELERQLKSLERQ----AEKAERYKELKAELRELELAL------LVLR 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1317 LESEREQNVKNQDLILENKKSIEKLKDVISMNASELSEVQVALNEAKLSEENVKSECHRVQEENARLKKKKEQLQQQVEE 1396
Cdd:TIGR02168 234 LEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLAN 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1397 WSKSHAELTEQIKSFEKSQEDLEIALTHKDDNISALTNCITQLNRLECELESEDPD-KGGNESDDlangetggDRSEKIR 1475
Cdd:TIGR02168 314 LERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEElESRLEELE--------EQLETLR 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1476 NRIKQMmdvsrtqtavsivEEDLKLLQLKLRasmstkcNLEDQIKKLEDDRSSLQTAKAGLEDEcKTLRQKVEILNELYQ 1555
Cdd:TIGR02168 386 SKVAQL-------------ELQIASLNNEIE-------RLEARLERLEDRRERLQQEIEELLKK-LEEAELKELQAELEE 444
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907069526 1556 QKEMALQKKLSQEEYERQDR--EQRLTAADEKVVLAAEEVKTYKRRI---EEMEEELQKTERSFKNQIAAHEKKA 1625
Cdd:TIGR02168 445 LEEELEELQEELERLEEALEelREELEEAEQALDAAERELAQLQARLdslERLQENLEGFSEGVKALLKNQSGLS 519
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1232-1650 |
6.19e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 58.23 E-value: 6.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1232 KSRVYQVTEKQISEKLENIKKENAELMQKLSSYEQKIKESKKYVQETKKqnmilSDEAVKYKDKIKI-LEETNVSLGDKA 1310
Cdd:PTZ00121 1344 AAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKK-----ADEAKKKAEEDKKkADELKKAAAAKK 1418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1311 KSLRLQLESEREQNVKNQDLILENKKSIEKLKdvismnaSELSEVQVALNEAKLSEENVKSECHRVQEENARLKKKKEQL 1390
Cdd:PTZ00121 1419 KADEAKKKAEEKKKADEAKKKAEEAKKADEAK-------KKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKK 1491
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1391 qqqVEEWSKSHAELTEQIKSFEKSQEDLEIALTHKDDNISAltnciTQLNRLECELESEDPDKGGNE---SDDLANGETG 1467
Cdd:PTZ00121 1492 ---AEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKK-----AEEAKKADEAKKAEEKKKADElkkAEELKKAEEK 1563
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1468 GDRSEKIRNRIKQMMDVSRTQTAVSI----VEEDLKLLQ--LKLRASMSTKCNLE----DQIKKLEDDRSSLQTAKAGLE 1537
Cdd:PTZ00121 1564 KKAEEAKKAEEDKNMALRKAEEAKKAeearIEEVMKLYEeeKKMKAEEAKKAEEAkikaEELKKAEEEKKKVEQLKKKEA 1643
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1538 DEcktLRQKVEILNELYQQKEMALQKKLSQEEYERQDREQRLTAADEKvvlAAEEVKTYKRRIEEMEEELQKTERSFKNQ 1617
Cdd:PTZ00121 1644 EE---KKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEK---KAAEALKKEAEEAKKAEELKKKEAEEKKK 1717
|
410 420 430
....*....|....*....|....*....|...
gi 1907069526 1618 IAAHEKKAHDNWLKARAAERAMAEEKREAANLR 1650
Cdd:PTZ00121 1718 AEELKKAEEENKIKAEEAKKEAEEDKKKAEEAK 1750
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1227-1609 |
2.15e-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: 56.27 E-value: 2.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1227 TILVVKSR--VYQVTEKQISEKlENIKKENaELMQKLSSYEQKIKESKKYVQETKKQnmILSDEAVKYKDKIKILEE--T 1302
Cdd:pfam05483 260 TFLLEESRdkANQLEEKTKLQD-ENLKELI-EKKDHLTKELEDIKMSLQRSMSTQKA--LEEDLQIATKTICQLTEEkeA 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1303 NVSLGDKAKSLRLQLESEREQNVKN-QDLILENKKSIEKLKD---VISM----NASELSEVQVALNEAKLSEENVKsech 1374
Cdd:pfam05483 336 QMEELNKAKAAHSFVVTEFEATTCSlEELLRTEQQRLEKNEDqlkIITMelqkKSSELEEMTKFKNNKEVELEELK---- 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1375 RVQEENARLKKKKEQLQQQVEEWSKSHAELTEQIKSFEKSQEDLEIALTHKDdniSALTNCITQLNRLECELESE----- 1449
Cdd:pfam05483 412 KILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIK---TSEEHYLKEVEDLKTELEKEklkni 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1450 ----DPDKGGNESDDLAngETGGDRSEKIRNRIKQMMDVSRTQTAVSIVEEDLKLLQLKLRASMST------------KC 1513
Cdd:pfam05483 489 eltaHCDKLLLENKELT--QEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESvreefiqkgdevKC 566
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1514 NL---EDQIKKLEDDRSSLQTAKAGLEDECKTLRQKVEILN---ELYQQKEMALQKKLSQEeyerqdrEQRLTAADEKVV 1587
Cdd:pfam05483 567 KLdksEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNkniEELHQENKALKKKGSAE-------NKQLNAYEIKVN 639
|
410 420
....*....|....*....|..
gi 1907069526 1588 LAAEEVKTYKRRIEEMEEELQK 1609
Cdd:pfam05483 640 KLELELASAKQKFEEIIDNYQK 661
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1229-1610 |
2.26e-07 |
|
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: 56.13 E-value: 2.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1229 LVVKSRVYQVTEKQISEKLENIKKENAELMQKLSSYEQKIKES--KKYVQETKKQNMILSDEAVKYKDKIKILEETNVSL 1306
Cdd:pfam02463 669 SELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEElkKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEE 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1307 gdKAKSLRLQLESEREQNVKNQDLILENKKSIEKLKDVISMNASELSEVQVALNEAKlsEENVKSECHRVQEENARLKKK 1386
Cdd:pfam02463 749 --EEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEEL--RALEEELKEEAELLEEEQLLI 824
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1387 KEQLQQQVEEWSKSHAELTEQIKSFEKSQEDLEIALthKDDNISALTNCITQLNRLECELESEDpdkggnesddlangET 1466
Cdd:pfam02463 825 EQEEKIKEEELEELALELKEEQKLEKLAEEELERLE--EEITKEELLQELLLKEEELEEQKLKD--------------EL 888
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1467 GGDRSEKirNRIKQMMDVSRTQTAVSIVEEDLKLLQLKLRASMSTKCNLEDQIKKLEDDRSSLQTAKAGLEDECKTLRQK 1546
Cdd:pfam02463 889 ESKEEKE--KEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLL 966
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907069526 1547 VEILNELYQQKEMALQKKLSQEEYERQDRE-QRLTAADEKVVLAAEEVKTyKRRIEEMEEELQKT 1610
Cdd:pfam02463 967 LAKEELGKVNLMAIEEFEEKEERYNKDELEkERLEEEKKKLIRAIIEETC-QRLKEFLELFVSIN 1030
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1241-1605 |
3.10e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.46 E-value: 3.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1241 KQISEKLENIKKENAELMQKLSSYEQKIKESKKYVQETKKqnmilsdEAVKYKDKIKILEEtnvsLGDKAKSLRlQLESE 1320
Cdd:PRK03918 234 EELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKK-------EIEELEEKVKELKE----LKEKAEEYI-KLSEF 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1321 REQNVKNQDLILENKKSIEKLKDVISMNASELSEVQVALNEAKLSEENVKSECHRVqEENARLKKKKEQLQQQVEEWSKS 1400
Cdd:PRK03918 302 YEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEEL-EERHELYEEAKAKKEELERLKKR 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1401 HAELT-----EQIKSFEKSQEDLEIALTHKDDNISALTNCITQL----NRLE--------CELESEDPDKGG---NESDD 1460
Cdd:PRK03918 381 LTGLTpekleKELEELEKAKEEIEEEISKITARIGELKKEIKELkkaiEELKkakgkcpvCGRELTEEHRKElleEYTAE 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1461 LANGE----TGGDRSEKIRNRIKQMMDVSRTQTAVSIVEEDLKllQLKLRASMSTKCNLEDQIKKLEDDRsSLQTAKAGL 1536
Cdd:PRK03918 461 LKRIEkelkEIEEKERKLRKELRELEKVLKKESELIKLKELAE--QLKELEEKLKKYNLEELEKKAEEYE-KLKEKLIKL 537
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907069526 1537 EDECKTLRQKVEILNELYQQKEmALQKKLSQEEYERQDREQRLTAadekvvLAAEEVKTYKRRIEEMEE 1605
Cdd:PRK03918 538 KGEIKSLKKELEKLEELKKKLA-ELEKKLDELEEELAELLKELEE------LGFESVEELEERLKELEP 599
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1478-1624 |
8.06e-07 |
|
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: 52.23 E-value: 8.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1478 IKQMMDVSRTQTAVSIVEEDLKLLQLKLRASMSTKCNLEDQIKKLEDDRSSLQTAKAGLEDECKTLRQKVEILNELYQQ- 1556
Cdd:COG1579 6 LRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNv 85
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907069526 1557 ---KEM-ALQKKLSQEEYERQDREQRLTAADEKVVLAAEEVKTYKRRIEEMEEELQKTERSFKNQIAAHEKK 1624
Cdd:COG1579 86 rnnKEYeALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAE 157
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1239-1612 |
8.27e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 54.28 E-value: 8.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1239 TEKQISEKLENIKKENAELMQKLSSYEQKIKESKKYVQETKKQNMILSDEAVKYKDKIKILEETNVSLGDKAkslrlQLE 1318
Cdd:PRK02224 231 QARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEA-----GLD 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1319 SEREQNVKNQDLILENKKsiEKLKDVISmnaSELSEVQVALNEAKLSEENVK---SECHRVQEENARLKKKKEQLQQQVE 1395
Cdd:PRK02224 306 DADAEAVEARREELEDRD--EELRDRLE---ECRVAAQAHNEEAESLREDADdleERAEELREEAAELESELEEAREAVE 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1396 EWSKSHAELTEQI----KSFEKSQEDLEIALTHKDDNISALTNCITQLNRLECELESEDPDKGGNEsDDLANG---ETGg 1468
Cdd:PRK02224 381 DRREEIEELEEEIeelrERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAE-ALLEAGkcpECG- 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1469 drsekirnrikqmMDVSRTQTAVSIVEEDLKLLQLKLRASmstkcNLEDQIKKLEDDRSSLQTAKAgLEDECKTLRQKVE 1548
Cdd:PRK02224 459 -------------QPVEGSPHVETIEEDRERVEELEAELE-----DLEEEVEEVEERLERAEDLVE-AEDRIERLEERRE 519
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907069526 1549 ILNELYQQKEMALQKKLSQ--------EEYERQDREQRLTAAD--EKVVLAAEEVKTYKRRIEEMEEELQKTER 1612
Cdd:PRK02224 520 DLEELIAERRETIEEKRERaeelreraAELEAEAEEKREAAAEaeEEAEEAREEVAELNSKLAELKERIESLER 593
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1288-1630 |
1.02e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.17 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1288 EAVKYKDKIKILEETNVSLGDKAKSLRLQLESEREQNVKNQDLILENKKSIEKLKDvismnasELSEVQVALNEAKLSEE 1367
Cdd:COG1196 226 EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELEL-------ELEEAQAEEYELLAELA 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1368 NVKSECHRVQEENARLKKKKEQLQQQVEEWSKSHAELTEQIKSFEKSQEDLEIALTHKDDNISaltncitQLNRLECELE 1447
Cdd:COG1196 299 RLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELA-------EAEEALLEAE 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1448 SEdpdkggnesddlangetggdRSEKIRNRIKQMMDVSRTQTAVSIVEEDLKLLQLKLRASMSTKCNLEDQIKKLEDDRS 1527
Cdd:COG1196 372 AE--------------------LAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALA 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1528 SLQTAKAGLEDEcktLRQKVEILNELyQQKEMALQKKLSQEEYERQDREQRLTAADEKVVLAAEEVKTYKRRIEEMEEEL 1607
Cdd:COG1196 432 ELEEEEEEEEEA---LEEAAEEEAEL-EEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFL 507
|
330 340
....*....|....*....|...
gi 1907069526 1608 QKTERSFKNQIAAHEKKAHDNWL 1630
Cdd:COG1196 508 EGVKAALLLAGLRGLAGAVAVLI 530
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1251-1666 |
1.19e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 53.99 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1251 KKENAELMQKLSSYEQKIKESKKYVQETKKQNMILSDEAVKYKDKIKILEETNvslgdKAKSLRLQLESEREQNVKNQdl 1330
Cdd:PTZ00121 1314 AKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKA-----EAAEKKKEEAKKKADAAKKK-- 1386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1331 iLENKKSIEKLKDVISMNASELSEVQVALNEAKLSEENVKSECHRVQEENARLKKKKEQLQqqveEWSKSHAELTEQIKS 1410
Cdd:PTZ00121 1387 -AEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKA----DEAKKKAEEAKKAEE 1461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1411 FEKSQEDLEIALTHKDDNISALTNCITQLNRLECELESEDPDKGGNE---SDDLANGETGGDRSEKIRNRIKQMMDVSRT 1487
Cdd:PTZ00121 1462 AKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAkkkADEAKKAEEAKKADEAKKAEEAKKADEAKK 1541
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1488 QTAVSIVEEDLKLLQLKlRASMSTKCnleDQIKKLEDDRSslqTAKAGLEDECKTLRQKVEILNELYQQKEMALQKKLSQ 1567
Cdd:PTZ00121 1542 AEEKKKADELKKAEELK-KAEEKKKA---EEAKKAEEDKN---MALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKK 1614
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1568 EEYERQDREQRLTAADEKvvlaaEEVKTYKRRIEE---MEEELQKTERSFKNQIAAHEKKAHDNWLKARAAERAMAEEKR 1644
Cdd:PTZ00121 1615 AEEAKIKAEELKKAEEEK-----KKVEQLKKKEAEekkKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKK 1689
|
410 420
....*....|....*....|..
gi 1907069526 1645 EAANLRHKLLEMTQKMAMRQDE 1666
Cdd:PTZ00121 1690 AAEALKKEAEEAKKAEELKKKE 1711
|
|
| SH3_2 |
pfam07653 |
Variant SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in ... |
49-105 |
1.30e-06 |
|
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: 46.82 E-value: 1.30e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1907069526 49 RGKALEDFTGPDCRFVNFKKGDDVYVYYKLAGGSlelWAGSVEHSFGYFPKDLIKVL 105
Cdd:pfam07653 1 YGRVIFDYVGTDKNGLTLKKGDVVKVLGKDNDGW---WEGETGGRVGLVPSTAVEEI 54
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1241-1661 |
1.35e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.53 E-value: 1.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1241 KQISEKLENIKKENAELMQKLSSYEQKIKESKKyVQETKKQNMILSDEAVKYKDKIKILEETNVSLGDKAKSLRLQLEsE 1320
Cdd:PRK03918 255 RKLEEKIRELEERIEELKKEIEELEEKVKELKE-LKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIK-E 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1321 REQNVKNQDLILENKKSIEKLKDVISMNASELSEVQVALNEA-KLSEENVKSECHRVQEEnarlkkkkeqlqqqVEEWSK 1399
Cdd:PRK03918 333 LEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELeRLKKRLTGLTPEKLEKE--------------LEELEK 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1400 SHAELTEQIKSFEKSQEDLEIALTHKDDNISALTN----CITQLNRLECELESEDPDKGGNESDDLANG-ETGGDRSEKI 1474
Cdd:PRK03918 399 AKEEIEEEISKITARIGELKKEIKELKKAIEELKKakgkCPVCGRELTEEHRKELLEEYTAELKRIEKElKEIEEKERKL 478
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1475 RNRIKQMMDVSRTQTAVSIVEEDLKllQLKLRASMSTKCNLEDQIKKLEDDRSsLQTAKAGLEDECKTLRQKVEILNELY 1554
Cdd:PRK03918 479 RKELRELEKVLKKESELIKLKELAE--QLKELEEKLKKYNLEELEKKAEEYEK-LKEKLIKLKGEIKSLKKELEKLEELK 555
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1555 QQKEmALQKKLSQEEYERQDREQRLTAadekvvLAAEEVKTYKRRIEEMEeelqktersfknqiaahekKAHDNWLKARA 1634
Cdd:PRK03918 556 KKLA-ELEKKLDELEEELAELLKELEE------LGFESVEELEERLKELE-------------------PFYNEYLELKD 609
|
410 420
....*....|....*....|....*..
gi 1907069526 1635 AERAMAEEKREAANLRHKLLEMTQKMA 1661
Cdd:PRK03918 610 AEKELEREEKELKKLEEELDKAFEELA 636
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1014-1144 |
1.84e-06 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 53.40 E-value: 1.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1014 SGVETAPLVTPPPPEE-----GWARPGEE--RQPPQQDSLPQENTGD-------LSVQPPEEPELSDQPVTSVQPPEEPE 1079
Cdd:PHA03247 2833 SAQPTAPPPPPGPPPPslplgGSVAPGGDvrRRPPSRSPAAKPAAPArppvrrlARPAVSRSTESFALPPDQPERPPQPQ 2912
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907069526 1080 LSDQPVTsvQPPEEPELSDQPvtsvqPPEEPELSDQPVTGYTSTSEVSQKPDTKKDIDLGPVMEG 1144
Cdd:PHA03247 2913 APPPPQP--QPQPPPPPQPQP-----PPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPG 2970
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1240-1623 |
3.16e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.08 E-value: 3.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1240 EKQISEkLENIKKENAELMQKLSSYEQKIKESKKYVQETKKQNMILsDEAVKYKDKIKILEETNVSLGDKAKSLRlQLES 1319
Cdd:COG4717 77 EEELKE-AEEKEEEYAELQEELEELEEELEELEAELEELREELEKL-EKLLQLLPLYQELEALEAELAELPERLE-ELEE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1320 EREQNVKNQDLILENKKSIEKLKDVISMNASELS-EVQVALNEAKLSEENVKSECHRVQEEnarlkkkkeqlqqqVEEWS 1398
Cdd:COG4717 154 RLEELRELEEELEELEAELAELQEELEELLEQLSlATEEELQDLAEELEELQQRLAELEEE--------------LEEAQ 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1399 KSHAELTEQIKSFEKSQEDLEI------------------ALTHKDDNISALTNCITQLNRLECEL-------ESEDPDK 1453
Cdd:COG4717 220 EELEELEEELEQLENELEAAALeerlkearlllliaaallALLGLGGSLLSLILTIAGVLFLVLGLlallfllLAREKAS 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1454 GGNESDDLANGETGGDRSEKIRNRIKQMMDVSRTQTAVSIVEEDLKLLQLKLRASMSTKCNLEDQIKKLEDDRSSLQtAK 1533
Cdd:COG4717 300 LGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALL-AE 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1534 AGLEDEcKTLRQKVEILNElYQQKEMALQKKLSQEEYERQDREQRLTAADEKVVlaAEEVKTYKRRIEEMEEE---LQKT 1610
Cdd:COG4717 379 AGVEDE-EELRAALEQAEE-YQELKEELEELEEQLEELLGELEELLEALDEEEL--EEELEELEEELEELEEEleeLREE 454
|
410
....*....|...
gi 1907069526 1611 ERSFKNQIAAHEK 1623
Cdd:COG4717 455 LAELEAELEQLEE 467
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1402-1666 |
6.07e-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: 51.60 E-value: 6.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1402 AELTEQIKSFEKSQEDLEIAL-----THKDDNISALTNCITQLNRLECELESEdpdkggnesddLANGETGGDRSEKIRN 1476
Cdd:TIGR02168 209 AEKAERYKELKAELRELELALlvlrlEELREELEELQEELKEAEEELEELTAE-----------LQELEEKLEELRLEVS 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1477 RIKQMMDVSRT-----QTAVSIVEEDLKLLQLKLRASMSTKCNLEDQIKKLEDDRSSLQTAKAGLEDECKTLRQKVEiln 1551
Cdd:TIGR02168 278 ELEEEIEELQKelyalANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELE--- 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1552 elyqqkemALQKKLSQEEYERQDREQRLTAADE-------KVVLAAEEVKTYKRRIEEMEEELQKTERS---FKNQIAAH 1621
Cdd:TIGR02168 355 --------SLEAELEELEAELEELESRLEELEEqletlrsKVAQLELQIASLNNEIERLEARLERLEDRrerLQQEIEEL 426
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1907069526 1622 EKKAHDNWLKarAAERAMAEEKREAANLRHKLLEMTQKMAMRQDE 1666
Cdd:TIGR02168 427 LKKLEEAELK--ELQAELEELEEELEELQEELERLEEALEELREE 469
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1351-1606 |
1.12e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 50.45 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1351 ELSEVQVALNEAKLSEENVKSECHRVQEENARLKKKKEQLQQQVEEWSKSHAELTEQIKSFEKSQEDLEIALTHKDDnis 1430
Cdd:TIGR02169 675 ELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQ--- 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1431 ALTNCITQLNRLECELESEDPDKgGNESDDLANGET--GGDRSEKIRNRI-KQMMDVSRTQTAVSIVEEDLKLLQLKLRA 1507
Cdd:TIGR02169 752 EIENVKSELKELEARIEELEEDL-HKLEEALNDLEArlSHSRIPEIQAELsKLEEEVSRIEARLREIEQKLNRLTLEKEY 830
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1508 SMSTKCNLEDQIKKLEDDRSS-------LQTAKAGLEDECKTLRQKVEILNELYQ---------QKEM-ALQKKLSQEEY 1570
Cdd:TIGR02169 831 LEKEIQELQEQRIDLKEQIKSiekeienLNGKKEELEEELEELEAALRDLESRLGdlkkerdelEAQLrELERKIEELEA 910
|
250 260 270
....*....|....*....|....*....|....*.
gi 1907069526 1571 ERQDREQRLTAADEKVVLAAEEVKTYKRRIEEMEEE 1606
Cdd:TIGR02169 911 QIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEI 946
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1472-1667 |
1.43e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 49.38 E-value: 1.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1472 EKIRNRIKQMMD-VSRTQTAVSIVEEDLKLLQLKLRAsmstkcnLEDQIKKLEDDRSSLQTAKAGLEDECKTLRQKVEIL 1550
Cdd:COG4942 30 EQLQQEIAELEKeLAALKKEEKALLKQLAALERRIAA-------LARRIRALEQELAALEAELAELEKEIAELRAELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1551 NELYQQKEMALQKK---------LSQEEY---------------ERQDREQRLTAADEKVVLAAEEVKTYKRRIEEMEEE 1606
Cdd:COG4942 103 KEELAELLRALYRLgrqpplallLSPEDFldavrrlqylkylapARREQAEELRADLAELAALRAELEAERAELEALLAE 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907069526 1607 LQKTERSFKNQIAAHEKKAHDNWLKARAAERAMAEEKREAANLRHKLLEMTQKMAMRQDEP 1667
Cdd:COG4942 183 LEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERT 243
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
1247-1627 |
2.41e-05 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 49.30 E-value: 2.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1247 LENIKKENAELMQKLSSYEQKIKESKKYVQETKKQN---MILSDEAVKYKDKIKILEETNvslgDKAKSLRLQLESEREQ 1323
Cdd:pfam05622 68 LEQLQEENFRLETARDDYRIKCEELEKEVLELQHRNeelTSLAEEAQALKDEMDILRESS----DKVKKLEATVETYKKK 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1324 -----NVKNQDLILENKKSI---------EKLKDVISMNAS-ELSEVQVALNEAKLSEENVKSEchRVQEENARLKKKKE 1388
Cdd:pfam05622 144 ledlgDLRRQVKLLEERNAEymqrtlqleEELKKANALRGQlETYKRQVQELHGKLSEESKKAD--KLEFEYKKLEEKLE 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1389 QLQQQVEEWSK---SHAELTEQIKSFEKSQEDLEIALTHKDDNISALTNCITQLNRLE-CE----LESEDP----DKGGN 1456
Cdd:pfam05622 222 ALQKEKERLIIerdTLRETNEELRCAQLQQAELSQADALLSPSSDPGDNLAAEIMPAEiREklirLQHENKmlrlGQEGS 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1457 ESDDLANGETGGDRSEKIRNRIKQMMDVSRTQTAV--SIVEEDLKLLQL---KLRASMSTKCNLEDQIKKLEDDRSSLQT 1531
Cdd:pfam05622 302 YRERLTELQQLLEDANRRKNELETQNRLANQRILElqQQVEELQKALQEqgsKAEDSSLLKQKLEEHLEKLHEAQSELQK 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1532 AKAGLED-ECKTLRQKveilnelyQQKEMALQKKLSQEEYERQDREQRLTAADEKvvlAAEEVKTYKRRIEEMEE-ELQk 1609
Cdd:pfam05622 382 KKEQIEElEPKQDSNL--------AQKIDELQEALRKKDEDMKAMEERYKKYVEK---AKSVIKTLDPKQNPASPpEIQ- 449
|
410
....*....|....*...
gi 1907069526 1610 terSFKNQIAAHEKKAHD 1627
Cdd:pfam05622 450 ---ALKNQLLEKDKKIEH 464
|
|
| RND_1 |
NF037998 |
protein translocase SecDF, variant type; Members of this family are identified by TCDB as ... |
1209-1372 |
3.90e-05 |
|
protein translocase SecDF, variant type; Members of this family are identified by TCDB as belonging to 2.A.6.4.4, a variant 12-TM type SecDF, as found in Spiroplasma, Mesoplasma, and Acholeplasma.
Pssm-ID: 468306 Cd Length: 1237 Bit Score: 49.01 E-value: 3.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1209 VIITAVLGIVSFAIFSWrtiLVVKSRVYQVTEKQISEKLENIKKENAELMQKLSSYEQKI-------KESKKYVQETKKQ 1281
Cdd:NF037998 580 VIISLVLVIIVARLMIW---LTIKLQWFKKYPWLLPLDTDFANQGVAILNYKISRLENKIekltnkeKLSSKLLLKIKKI 656
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1282 NmilsDEAVKYKDKIKILEET-NVSLGDKAKSLRLQLESEREQNVKNQDLILENKKSIEKLKDVISMNaselsEVQVALN 1360
Cdd:NF037998 657 N----DKIDLLKKKEENKEAKkNAKLIEKVKAKIKKLEQKITKLKLNKKKSNKIIKIRWKKKDWIFFL-----KDNTDVI 727
|
170
....*....|..
gi 1907069526 1361 EAKLSEENVKSE 1372
Cdd:NF037998 728 LAIESEIEIQVI 739
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1242-1665 |
4.06e-05 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 48.89 E-value: 4.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1242 QISEKLENIKKENAElmQKLSSYEQKIKESKKYVQETKK------QNMilsDEAVKYKDKIKILEETNVSLgDKAKSLRL 1315
Cdd:TIGR01612 868 QFAELTNKIKAEISD--DKLNDYEKKFNDSKSLINEINKsieeeyQNI---NTLKKVDEYIKICENTKESI-EKFHNKQN 941
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1316 QLESEREQNVKnqdlILENKKSIEK-LKDVISMN-ASELSEVQVALNEAKLSEENVKSEcHRVQEENARLKKKKEQLQ-- 1391
Cdd:TIGR01612 942 ILKEILNKNID----TIKESNLIEKsYKDKFDNTlIDKINELDKAFKDASLNDYEAKNN-ELIKYFNDLKANLGKNKEnm 1016
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1392 --QQVEEWSKSHAELTEQIKSFEKSQEDLEIALTHKDDNIS---------------------ALTNcITQLNRLECELES 1448
Cdd:TIGR01612 1017 lyHQFDEKEKATNDIEQKIEDANKNIPNIEIAIHTSIYNIIdeiekeigkniellnkeileeAEIN-ITNFNEIKEKLKH 1095
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1449 EDPDKGGNE------------SDDLANGETGGDRS----EKIRNRIKQMMDVSRTQ-------TAVSIVEEDLKLLQLKL 1505
Cdd:TIGR01612 1096 YNFDDFGKEenikyadeinkiKDDIKNLDQKIDHHikalEEIKKKSENYIDEIKAQindledvADKAISNDDPEEIEKKI 1175
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1506 R---ASMSTKCNLEDQIKKLEDDRSSLQTAKAGLEdecktlrqKVEILNELYQQkemALQKKLSQEEYERQDREQRLTAA 1582
Cdd:TIGR01612 1176 EnivTKIDKKKNIYDEIKKLLNEIAEIEKDKTSLE--------EVKGINLSYGK---NLGKLFLEKIDEEKKKSEHMIKA 1244
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1583 DEKVVLAAEEVKTYKRRIE-EMEEELQ-KTERSFKNQIAAHEKKAHdnwlkaraaeRAMAEEKREAANLRHKLLEMTQKM 1660
Cdd:TIGR01612 1245 MEAYIEDLDEIKEKSPEIEnEMGIEMDiKAEMETFNISHDDDKDHH----------IISKKHDENISDIREKSLKIIEDF 1314
|
....*
gi 1907069526 1661 AMRQD 1665
Cdd:TIGR01612 1315 SEESD 1319
|
|
| PRK14949 |
PRK14949 |
DNA polymerase III subunits gamma and tau; Provisional |
716-1119 |
4.33e-05 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 237863 [Multi-domain] Cd Length: 944 Bit Score: 48.57 E-value: 4.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 716 SAQQSRENSPSARDGRSDMNSQVFEKvilgtlnlNTEKTKQPANMILETGQESETTSEEAGDVGKESGHSVVVDSEESHL 795
Cdd:PRK14949 382 PSALAAAVQAPHANEPQFVNAAPAEK--------KTALTEQTTAQQQVQAANAEAVAEADASAEPADTVEQALDDESELL 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 796 ADMRAQRP---SQVHGLRDETAAQTPGSGEAVLSKNPNDlqkdnPEEELVNTLGLEDPgVGEISEGEPEDTKEFGVSESQ 872
Cdd:PRK14949 454 AALNAEQAvilSQAQSQGFEASSSLDADNSAVPEQIDST-----AEQSVVNPSVTDTQ-VDDTSASNNSAADNTVDDNYS 527
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 873 GTDAEDLRDDPSRQATPEIPDivLKSIREDLPIINSFFKDDQQSLHRFLKYFDVRELEGLLEDMSirlrSAHQNSLPYNM 952
Cdd:PRK14949 528 AEDTLESNGLDEGDYAQDSAP--LDAYQDDYVAFSSESYNALSDDEQHSANVQSAQSAAEAQPSS----QSLSPISAVTT 601
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 953 EKV-------LDKVFRASESRILSMAEKMLDTGVAKNRDLGSKESSP---------LEEAEVLDDIQDLIYFVRYQYSGV 1016
Cdd:PRK14949 602 AAAsladddiLDAVLAARDSLLSDLDALSPKEGDGKKSSADRKPKTPpsrappaslSKPASSPDASQTSASFDLDPDFEL 681
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1017 ETAPLV-----------TPPPPEEGWARPGEErQPPQQDSLPQENTGDLSVQ-PPEEPELSDQPVTSVQPPEEPELSDQp 1084
Cdd:PRK14949 682 ATHQSVpeaalasgsapAPPPVPDPYDRPPWE-EAPEVASANDGPNNAAEGNlSESVEDASNSELQAVEQQATHQPQVQ- 759
|
410 420 430
....*....|....*....|....*....|....*..
gi 1907069526 1085 vTSVQPPEEPELSDQPVTSVQPPEE--PELSDQPVTG 1119
Cdd:PRK14949 760 -AEAQSPASTTALTQTSSEVQDTELnlVLLSSGSITG 795
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1245-1650 |
6.55e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.21 E-value: 6.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1245 EKLENIKKENAELMQKLSSYEQKIKESKKYVQETKKQNMILSDEAVKYKDKIKILEET-NVSLGDKAKSLRLQLESEREQ 1323
Cdd:PTZ00121 1070 EGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDArKAEEARKAEDARKAEEARKAE 1149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1324 NVKNQDLileNKKSIEKLKDVISMNASELSEVQVALN--EAKLSEENVKSECHRVQEENARLKKKKEqlqqqVEEWSKSH 1401
Cdd:PTZ00121 1150 DAKRVEI---ARKAEDARKAEEARKAEDAKKAEAARKaeEVRKAEELRKAEDARKAEAARKAEEERK-----AEEARKAE 1221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1402 -AELTEQIKSFEKSQEDLEIA-----LTHKDDNISALTNCITQLNRLECELESEDPDKggneSDDLANGEtggdrSEKIR 1475
Cdd:PTZ00121 1222 dAKKAEAVKKAEEAKKDAEEAkkaeeERNNEEIRKFEEARMAHFARRQAAIKAEEARK----ADELKKAE-----EKKKA 1292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1476 NRIKQMMDVSRTQTAVSIVEEDLKLLQLKLRASMSTKcNLEDQIKKLEDDRSSLQTAKAGLEDECKTL------------ 1543
Cdd:PTZ00121 1293 DEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKK-KADAAKKKAEEAKKAAEAAKAEAEAAADEAeaaeekaeaaek 1371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1544 -----RQKVEILNELYQQKEMALQKKLSQEEYERQDREQRLTAADEKVVLAAEEVKTYKRRIEEMEEELQKTERSFKNQI 1618
Cdd:PTZ00121 1372 kkeeaKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKK 1451
|
410 420 430
....*....|....*....|....*....|..
gi 1907069526 1619 AAHEKKAHDNWLKARAAERAMAEEKREAANLR 1650
Cdd:PTZ00121 1452 KAEEAKKAEEAKKKAEEAKKADEAKKKAEEAK 1483
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1515-1627 |
6.94e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.99 E-value: 6.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1515 LEDQIKKLEDDRSSLQTAKAGLEDECKTLRQKVEILNELYQQ----KEMALQKKLSQEEYERQDREQR-------LTAAD 1583
Cdd:COG4913 293 LEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGnggdRLEQLEREIERLERELEERERRrarlealLAALG 372
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1907069526 1584 EKVVLAAEEVKTYKRRIEEMEEELQKTERSFKNQIAAHEKKAHD 1627
Cdd:COG4913 373 LPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRD 416
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1343-1583 |
7.06e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.45 E-value: 7.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1343 DVISMNASELSEVQVALNEAKLSEENVKSECHRVQEENARLKKKKEQLQQQVEEWSKSHAELTEQIKSFEKSQEDLEIAL 1422
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1423 THKDDNISALTNCITQLNR---LECELESEDPDKGGNESDDLangetggdrSEKIRNRIKQMMDVSRTQTAVSIVEEDLK 1499
Cdd:COG4942 100 EAQKEELAELLRALYRLGRqppLALLLSPEDFLDAVRRLQYL---------KYLAPARREQAEELRADLAELAALRAELE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1500 LLQLKLRASMStkcNLEDQIKKLEDDRSSLQTAKAGLEDECKTLRQKVEILnelyQQKEMALQKKLSQEEYERQDREQRL 1579
Cdd:COG4942 171 AERAELEALLA---ELEEERAALEALKAERQKLLARLEKELAELAAELAEL----QQEAEELEALIARLEAEAAAAAERT 243
|
....
gi 1907069526 1580 TAAD 1583
Cdd:COG4942 244 PAAG 247
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1322-1573 |
7.83e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 47.70 E-value: 7.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1322 EQNVKNQDLILENKKSIeklkDVISMNASELSEvQVALNEAKLSEENVKSEchrvqEENARLKKKKEQLQQQVEEWSKSH 1401
Cdd:PHA02562 167 EMDKLNKDKIRELNQQI----QTLDMKIDHIQQ-QIKTYNKNIEEQRKKNG-----ENIARKQNKYDELVEEAKTIKAEI 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1402 AELTEQIKSFEKSQEDLEIALTHKDDNISALTNCITQLNRLECELE------------SEDPDKGGNESDDLANGETGGD 1469
Cdd:PHA02562 237 EELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKMYEkggvcptctqqiSEGPDRITKIKDKLKELQHSLE 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1470 RSEKIRNRIKQMMDVSRTQTAVsiveedLKLLQLKLRASMSTKCNLEDQIKKLEDDRSSLQTAKAGLEDECKTLRQ-KVE 1548
Cdd:PHA02562 317 KLDTAIDELEEIMDEFNEQSKK------LLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDeLDK 390
|
250 260
....*....|....*....|....*
gi 1907069526 1549 ILNELyqqkemalqKKLSQEEYERQ 1573
Cdd:PHA02562 391 IVKTK---------SELVKEKYHRG 406
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1238-1624 |
1.09e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 47.41 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1238 VTEKQISEKLENIKKEN-AELMQKLSSYEQKIKESKKYVQETKK--QNMILSDEAVKYKDKIKILEETNVSLGDKAKSLR 1314
Cdd:pfam05483 147 IKENNATRHLCNLLKETcARSAEKTKKYEYEREETRQVYMDLNNniEKMILAFEELRVQAENARLEMHFKLKEDHEKIQH 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1315 LQLESEREQNVKNQD---LILENKKSIEKLKDVISMNASELSEVQVALNEAKLSEENVKSECHRvqeenarlkkkkeqLQ 1391
Cdd:pfam05483 227 LEEEYKKEINDKEKQvslLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEK--------------KD 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1392 QQVEEWSKSHAELTEQIKSFEKSQEDLEIAlthkddnisalTNCITQLNRlECELESEDPDKGGNESDDLANgetggdrs 1471
Cdd:pfam05483 293 HLTKELEDIKMSLQRSMSTQKALEEDLQIA-----------TKTICQLTE-EKEAQMEELNKAKAAHSFVVT-------- 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1472 eKIRNRIKQMMDVSRT-QTAVSIVEEDLKLLQLKLRASMStkcNLEDQIKKLEDDRSSLQTAKAGLEDECKTL--RQKVE 1548
Cdd:pfam05483 353 -EFEATTCSLEELLRTeQQRLEKNEDQLKIITMELQKKSS---ELEEMTKFKNNKEVELEELKKILAEDEKLLdeKKQFE 428
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907069526 1549 ILNELYQQKEMALQKKLSQEEYERQDREQRLTAadekvVLAAEEvkTYKRRIEEMEEELQKtERSFKNQIAAHEKK 1624
Cdd:pfam05483 429 KIAEELKGKEQELIFLLQAREKEIHDLEIQLTA-----IKTSEE--HYLKEVEDLKTELEK-EKLKNIELTAHCDK 496
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1248-1622 |
1.22e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.96 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1248 ENIKKENAELMQKLSSYEQKIKESKKYVQETKKQnmilsdeAVKYKDKIKILEETNVSLGDKAKSLRLQLESEREQnvkn 1327
Cdd:PRK02224 310 EAVEARREELEDRDEELRDRLEECRVAAQAHNEE-------AESLREDADDLEERAEELREEAAELESELEEAREA---- 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1328 qdlILENKKSIEKLKDVISMNASELSEVQVALNEAKLSEENVKSECHRVQEENARLKKKKEQLQQQVEEwsksHAELTEQ 1407
Cdd:PRK02224 379 ---VEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEE----AEALLEA 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1408 IKSFEKSQ--EDLEIA--LTHKDDNISALTncitqLNRLECELESEDPDKGGNESDDLANGETGGDRSEKIRNRIKQMMD 1483
Cdd:PRK02224 452 GKCPECGQpvEGSPHVetIEEDRERVEELE-----AELEDLEEEVEEVEERLERAEDLVEAEDRIERLEERREDLEELIA 526
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1484 VSRTqtavSIVEEDLKLLQL-----KLRASMSTK--------------------CN-----LEDQIKKLEDDRSSLQTAk 1533
Cdd:PRK02224 527 ERRE----TIEEKRERAEELreraaELEAEAEEKreaaaeaeeeaeeareevaeLNsklaeLKERIESLERIRTLLAAI- 601
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1534 AGLEDECKTLRQKVEILNELY-QQKEMALQKKLSQEEYERQDREQRLTAADEKVVLAA---EEVKTYKRRIEEMEEELQK 1609
Cdd:PRK02224 602 ADAEDEIERLREKREALAELNdERRERLAEKRERKRELEAEFDEARIEEAREDKERAEeylEQVEEKLDELREERDDLQA 681
|
410
....*....|...
gi 1907069526 1610 TERSFKNQIAAHE 1622
Cdd:PRK02224 682 EIGAVENELEELE 694
|
|
| PHA03369 |
PHA03369 |
capsid maturational protease; Provisional |
1010-1137 |
1.23e-04 |
|
capsid maturational protease; Provisional
Pssm-ID: 223061 [Multi-domain] Cd Length: 663 Bit Score: 46.92 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1010 RYQYSGVETAPLVTPPPPEEGWARP--GEERQP---PQQDSLPQENTGDLSVQPPEEPELSDQPVTSV--QP-PEEPELS 1081
Cdd:PHA03369 342 KAHNEILKTASLTAPSRVLAAAAKVavIAAPQThtgPADRQRPQRPDGIPYSVPARSPMTAYPPVPQFcgDPgLVSPYNP 421
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907069526 1082 DQPVTSVQPPEEPELSDQPVTSVQPPEepELSDQPVTGYTSTSEVSQKPDTKKDID 1137
Cdd:PHA03369 422 QSPGTSYGPEPVGPVPPQPTNPYVMPI--SMANMVYPGHPQEHGHERKRKRGGELK 475
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1351-1612 |
1.71e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 46.60 E-value: 1.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1351 ELSEVQVALNEAKLSEENVKSECHRVQEE--NARLKKKKEQLQQQVEEWSKSHA--ELTEQIKSFEKSQEDLEIALTHKD 1426
Cdd:TIGR02169 178 ELEEVEENIERLDLIIDEKRQQLERLRREreKAERYQALLKEKREYEGYELLKEkeALERQKEAIERQLASLEEELEKLT 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1427 DNISALTNCITQLNRLECELESEDPDKGGNESddlangetggdrsekirnrikqmmdvSRTQTAVSIVEEDLKLLQLKLR 1506
Cdd:TIGR02169 258 EEISELEKRLEEIEQLLEELNKKIKDLGEEEQ--------------------------LRVKEKIGELEAEIASLERSIA 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1507 ASMSTKCNLEDQIKKLEDDRSSLQTAKAGLEDECKTLRQKVEILNELYQQKEmalqkklsqEEYErqDREQRLTAADEKV 1586
Cdd:TIGR02169 312 EKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELK---------EELE--DLRAELEEVDKEF 380
|
250 260
....*....|....*....|....*.
gi 1907069526 1587 VLAAEEVKTYKRRIEEMEEELQKTER 1612
Cdd:TIGR02169 381 AETRDELKDYREKLEKLKREINELKR 406
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
1022-1132 |
1.91e-04 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 46.62 E-value: 1.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1022 VTPPPPEEGWARPGEERQPPQQDSLPQEntgdlSVQPPEEPELSDQPVTSVQPPEEPELSDQPVTSVQPPEEPELSDQPV 1101
Cdd:PRK10263 756 QQPVAPQQQYQQPQQPVAPQPQYQQPQQ-----PVAPQPQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQQPVAPQPQY 830
|
90 100 110
....*....|....*....|....*....|....
gi 1907069526 1102 TSVQPPEEPELSD---QPVTGYTSTSEVSQKPDT 1132
Cdd:PRK10263 831 QQPQQPVAPQPQDtllHPLLMRNGDSRPLHKPTT 864
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1238-1656 |
2.03e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.60 E-value: 2.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1238 VTEKQISEKLENIKKENAELMQKLSSYEqkIKESKKYVQETKKQNMILSDEA----VKYKDKIKILEETNVSLGDKAKSL 1313
Cdd:PRK03918 97 LKYLDGSEVLEEGDSSVREWVERLIPYH--VFLNAIYIRQGEIDAILESDESrekvVRQILGLDDYENAYKNLGEVIKEI 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1314 RLQLES-----EREQNVKNqdLILENKKSIEKLKDVISMNASELSEVQVALNEA---KLSEENVKSECHRVQEENARLKK 1385
Cdd:PRK03918 175 KRRIERlekfiKRTENIEE--LIKEKEKELEEVLREINEISSELPELREELEKLekeVKELEELKEEIEELEKELESLEG 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1386 KKEQLQQQVEEWSKSHAELTEQIKSFEKSQEDLEiALTHKDDNISAL----TNCITQLNRLECELESEDPDKGGNEsDDL 1461
Cdd:PRK03918 253 SKRKLEEKIRELEERIEELKKEIEELEEKVKELK-ELKEKAEEYIKLsefyEEYLDELREIEKRLSRLEEEINGIE-ERI 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1462 ANGETGGDRSEKIRNRIKQmmdvsrTQTAVSIVEEDLKLLQlKLRASMSTKCNLEDQIK-----KLEDDRSSLQTAKAGL 1536
Cdd:PRK03918 331 KELEEKEERLEELKKKLKE------LEKRLEELEERHELYE-EAKAKKEELERLKKRLTgltpeKLEKELEELEKAKEEI 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1537 EDECKTLRQKVEILNELYQQKEMALQK-------------KLSQEEYERQDREQRLTAAD--EKVVLAAEEVKTYKRRIE 1601
Cdd:PRK03918 404 EEEISKITARIGELKKEIKELKKAIEElkkakgkcpvcgrELTEEHRKELLEEYTAELKRieKELKEIEEKERKLRKELR 483
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1907069526 1602 EMEEELQKTERSFKNQIAAHEKKAHDNWLKaRAAERAMAEEKREAANLRHKLLEM 1656
Cdd:PRK03918 484 ELEKVLKKESELIKLKELAEQLKELEEKLK-KYNLEELEKKAEEYEKLKEKLIKL 537
|
|
| RND_1 |
NF037998 |
protein translocase SecDF, variant type; Members of this family are identified by TCDB as ... |
1204-1357 |
3.97e-04 |
|
protein translocase SecDF, variant type; Members of this family are identified by TCDB as belonging to 2.A.6.4.4, a variant 12-TM type SecDF, as found in Spiroplasma, Mesoplasma, and Acholeplasma.
Pssm-ID: 468306 Cd Length: 1237 Bit Score: 45.54 E-value: 3.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1204 LPWQPVIITAVLGIVSFAIFSwRTILVVKSRvyqvteKQISEKlenIKKENAELMQKLSSYEQKIKESKkyvqetKKQNM 1283
Cdd:NF037998 1006 VPITFEILIAFVSIIGFAIAS-AIIILGKAK------SLISSK---NKKELENYFKKEIEHRAQIKRLR------RELNN 1069
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907069526 1284 ILSDEAVKYKDKIKILEETNVSLgdKAKSLRLQLESEREQNVKN-QDLILENKKSIEKLKDVISMNASE---LSEVQV 1357
Cdd:NF037998 1070 ELFALKVEYKEEIKKLKIKNPKP--EKKELKKEFKEFKKQKKLDfKDLKKKIKKEKKANKKEINRVSKEnnfLKEVFN 1145
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1437-1671 |
5.77e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.51 E-value: 5.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1437 TQLNRLECELESEDPDKGGNESDDLANGETGGDRSEKIRNRIKQMM-DVSRTQTAVSIVEEDLKLLQLKLRAsmstkcnL 1515
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLReELEQAREELEQLEEELEQARSELEQ-------L 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1516 EDQIKKLEDDRSSLQTAKAGLEDECKTLRQKVEILNELYQQkemaLQKKLSQEEYERQDREQRLTAADEKVVLAAEEVKT 1595
Cdd:COG4372 79 EEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEE----LQKERQDLEQQRKQLEAQIAELQSEIAEREEELKE 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907069526 1596 YKRRIEEMEEELQKTERSFKNQIAAHEKKAHDNWLKARAAERAMAEEKREAANLRHKLLEMTQKMAMRQDEPVIVK 1671
Cdd:COG4372 155 LEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAK 230
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1239-1660 |
5.84e-04 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 44.73 E-value: 5.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1239 TEKQISEKLENIKKENAELMQKLSSYEQKIKESKKYVQETKKQNMILSDEAVKYKDKIKILEETNVSLgdKAKSLRLQlE 1318
Cdd:pfam05557 98 QLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSL--AEAEQRIK-E 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1319 SEREQNVKNQD-LILENKKS-------IEKLKDVI-SMNA--------SELSEVQVALNEAKLS-EENVKSECHRVQEEN 1380
Cdd:pfam05557 175 LEFEIQSQEQDsEIVKNSKSelaripeLEKELERLrEHNKhlnenienKLLLKEEVEDLKRKLErEEKYREEAATLELEK 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1381 ARLKKkkeqlqqQVEEWSK----------SHAELTEQIKSFEksQEDleiaLTHKDDNiSALTNCITQLNRLECELESE- 1449
Cdd:pfam05557 255 EKLEQ-------ELQSWVKlaqdtglnlrSPEDLSRRIEQLQ--QRE----IVLKEEN-SSLTSSARQLEKARRELEQEl 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1450 --------DPDKG-----------------------------GNESDDLANGETGGDRSEKIRNrIKQMMDvsRTQTAVS 1492
Cdd:pfam05557 321 aqylkkieDLNKKlkrhkalvrrlqrrvllltkerdgyrailESYDKELTMSNYSPQLLERIEE-AEDMTQ--KMQAHNE 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1493 IVEEDLKLLQ-----LKLRASMstkcnLEDQIKKLeddRSSLQTAKAGL-EDECKTLRQKVEILneLYQQKEMALQKKLS 1566
Cdd:pfam05557 398 EMEAQLSVAEeelggYKQQAQT-----LERELQAL---RQQESLADPSYsKEEVDSLRRKLETL--ELERQRLREQKNEL 467
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1567 QEEYERQDREQRLTAADEKVV-------LAAEEVKtyKRRIEEMEEELQKTERSFKNQIAAHEKKAHDNwlkaraaERAM 1639
Cdd:pfam05557 468 EMELERRCLQGDYDPKKTKVLhlsmnpaAEAYQQR--KNQLEKLQAEIERLKRLLKKLEDDLEQVLRLP-------ETTS 538
|
490 500
....*....|....*....|.
gi 1907069526 1640 AEEKREAANLRHKLLEMTQKM 1660
Cdd:pfam05557 539 TMNFKEVLDLRKELESAELKN 559
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1239-1586 |
6.56e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 44.67 E-value: 6.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1239 TEKQISEK---LENIKKENAELMQKLSSYEQKIKEskkyvqETKKQNMILSDEAVKYKDKIKILEETNVSLGDKAKSLRL 1315
Cdd:TIGR02169 242 IERQLASLeeeLEKLTEEISELEKRLEEIEQLLEE------LNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKER 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1316 QLESEREQNVKNQDLILENKKSIEKLKDVISMNASELSEVQVALNEAKLSEENVKSEchrvqeenarlkkkkeqlqqqVE 1395
Cdd:TIGR02169 316 ELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAE---------------------LE 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1396 EWSKSHAELTEQIKSFEKSqedleialthkddnISALTNCITQLNRLECELesedpdkggnesddlangetgGDRSEKIR 1475
Cdd:TIGR02169 375 EVDKEFAETRDELKDYREK--------------LEKLKREINELKRELDRL---------------------QEELQRLS 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1476 NRIKQMmdvsrtqtavsivEEDLKLLQLKLRASMSTKcnlEDQIKKLEDDRSSLQTAKAGLEDECKTLRQKVEILNELyQ 1555
Cdd:TIGR02169 420 EELADL-------------NAAIAGIEAKINELEEEK---EDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRV-E 482
|
330 340 350
....*....|....*....|....*....|...
gi 1907069526 1556 QKEMALQKKLSQEEYERQ--DREQRLTAADEKV 1586
Cdd:TIGR02169 483 KELSKLQRELAEAEAQARasEERVRGGRAVEEV 515
|
|
| PRK11633 |
PRK11633 |
cell division protein DedD; Provisional |
1033-1117 |
6.63e-04 |
|
cell division protein DedD; Provisional
Pssm-ID: 236940 [Multi-domain] Cd Length: 226 Bit Score: 43.07 E-value: 6.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1033 RPGEERQPpqqDSLPQENTGdLSVQPPE----EPELSDQPVTSVQP--------PEEPELSDQPVTSVQPPEEPELSDQP 1100
Cdd:PRK11633 46 KPGDRDEP---DMMPAATQA-LPTQPPEgaaeAVRAGDAAAPSLDPatvappntPVEPEPAPVEPPKPKPVEKPKPKPKP 121
|
90
....*....|....*..
gi 1907069526 1101 VTSVQPPEEPELSDQPV 1117
Cdd:PRK11633 122 QQKVEAPPAPKPEPKPV 138
|
|
| PTZ00449 |
PTZ00449 |
104 kDa microneme/rhoptry antigen; Provisional |
1034-1130 |
8.51e-04 |
|
104 kDa microneme/rhoptry antigen; Provisional
Pssm-ID: 185628 [Multi-domain] Cd Length: 943 Bit Score: 44.30 E-value: 8.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1034 PGEERQP---PQQDSLPQENTGDLSVQPPEEPELSDQPVTSVQP-----PEEPELSDQPvTSVQPPEEPELSDQPVtSVQ 1105
Cdd:PTZ00449 563 PAKEHKPskiPTLSKKPEFPKDPKHPKDPEEPKKPKRPRSAQRPtrpksPKLPELLDIP-KSPKRPESPKSPKRPP-PPQ 640
|
90 100
....*....|....*....|....*
gi 1907069526 1106 PPEEPELSDQPVTGYTSTSEVSQKP 1130
Cdd:PTZ00449 641 RPSSPERPEGPKIIKSPKPPKSPKP 665
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1514-1622 |
9.14e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 44.05 E-value: 9.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1514 NLEDQIKKLEDDRSSLQTAKAgledECKTLRQKVEILNELYQQKEMALQKKLsQEEYERQDREqrltaadekvvlAAEEV 1593
Cdd:PRK00409 517 KLNELIASLEELERELEQKAE----EAEALLKEAEKLKEELEEKKEKLQEEE-DKLLEEAEKE------------AQQAI 579
|
90 100
....*....|....*....|....*....
gi 1907069526 1594 KTYKRRIEEMEEELQKTERSFKNQIAAHE 1622
Cdd:PRK00409 580 KEAKKEADEIIKELRQLQKGGYASVKAHE 608
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1468-1659 |
9.39e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.28 E-value: 9.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1468 GDRSEKIRNRIKQMM----DVSRTQTAVSIVEEDLKLLQLKLRASMSTKCNLEDQIKKLEDDRSSLQTAKAGLEDECKTL 1543
Cdd:PRK03918 199 EKELEEVLREINEISselpELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEEL 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1544 RQKVEILNEL----------------YQQKEMALQKKLSQEEYERQDREQRLTAADEKVvlaaEEVKTYKRRIEEMEEEL 1607
Cdd:PRK03918 279 EEKVKELKELkekaeeyiklsefyeeYLDELREIEKRLSRLEEEINGIEERIKELEEKE----ERLEELKKKLKELEKRL 354
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1907069526 1608 QKTERSFKNQIAAHEKKAHDNWLKARAAERAMAEEKREAANLRHKLLEMTQK 1659
Cdd:PRK03918 355 EELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEE 406
|
|
| PTZ00449 |
PTZ00449 |
104 kDa microneme/rhoptry antigen; Provisional |
1020-1168 |
9.83e-04 |
|
104 kDa microneme/rhoptry antigen; Provisional
Pssm-ID: 185628 [Multi-domain] Cd Length: 943 Bit Score: 44.30 E-value: 9.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1020 PLVTPPPpeEGWARPGEERQP--PQQDSLPQENTGDLSVQPPEEPELSDQPvTSVQPPEEPELSDQPVTSVQP--PEEPE 1095
Cdd:PTZ00449 573 PTLSKKP--EFPKDPKHPKDPeePKKPKRPRSAQRPTRPKSPKLPELLDIP-KSPKRPESPKSPKRPPPPQRPssPERPE 649
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907069526 1096 -----LSDQPVTSVQPPEEPELSDQPVTGYTSTSevSQKPDTKKDIDLGPVMEggPVGAGDVQKQLETIAEEPAAVPP 1168
Cdd:PTZ00449 650 gpkiiKSPKPPKSPKPPFDPKFKEKFYDDYLDAA--AKSKETKTTVVLDESFE--SILKETLPETPGTPFTTPRPLPP 723
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1240-1623 |
1.02e-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: 44.27 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1240 EKQISEKLENIKKENAELMQ------------KLSSYEQKIKESKKYVQETKKQNMILSDEAVKYKDKIKILEEtNVSLg 1307
Cdd:TIGR01612 1324 KKELQKNLLDAQKHNSDINLylneianiynilKLNKIKKIIDEVKEYTKEIEENNKNIKDELDKSEKLIKKIKD-DINL- 1401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1308 dkaKSLRLQLESERE--------QNVK-NQDLILENKKSIeklkDVISMNASELSEvQVALNEAKLSEENVKSE-CHRVQ 1377
Cdd:TIGR01612 1402 ---EECKSKIESTLDdkdideciKKIKeLKNHILSEESNI----DTYFKNADENNE-NVLLLFKNIEMADNKSQhILKIK 1473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1378 EENARLKKKKEQLQQQvEEWSKSHAELTEQIKSFEKSQEDLEIALTHKDDnisaltncITQLNRLECELESEDP-DKGGN 1456
Cdd:TIGR01612 1474 KDNATNDHDFNINELK-EHIDKSKGCKDEADKNAKAIEKNKELFEQYKKD--------VTELLNKYSALAIKNKfAKTKK 1544
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1457 EsddlangetggdrSEKIRNRIKQMMDVSRTQTAVSiveedlkllQLKLRASMSTKCNLEDQIKKleDDRSS-----LQT 1531
Cdd:TIGR01612 1545 D-------------SEIIIKEIKDAHKKFILEAEKS---------EQKIKEIKKEKFRIEDDAAK--NDKSNkaaidIQL 1600
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1532 AKAGLEDECKTLRQKVEILNELYQQKEmALQKKLSQEEYERQDREQRLTAADEKVVLA-AEEVKTYKRRIEEMEEELQKT 1610
Cdd:TIGR01612 1601 SLENFENKFLKISDIKKKINDCLKETE-SIEKKISSFSIDSQDTELKENGDNLNSLQEfLESLKDQKKNIEDKKKELDEL 1679
|
410
....*....|....*.
gi 1907069526 1611 E---RSFKNQIAAHEK 1623
Cdd:TIGR01612 1680 DseiEKIEIDVDQHKK 1695
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
1011-1174 |
1.07e-03 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 44.31 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1011 YQYSGVETAPLVTPPPPEEGWARPGEERQPPQQDSL----PQENTGDLSVQP-PEEPELSDQPVTSVQPPEEPELSDQPV 1085
Cdd:PRK10263 420 YYAPAPEQPAQQPYYAPAPEQPVAGNAWQAEEQQSTfapqSTYQTEQTYQQPaAQEPLYQQPQPVEQQPVVEPEPVVEET 499
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1086 TSVQPP----EEPELS-----DQPVTSVQPPEEPELSDQPVTGYTSTSEVSQKPdtkkdiDLGPVMEGGPVGAGDVQKQL 1156
Cdd:PRK10263 500 KPARPPlyyfEEVEEKrarerEQLAAWYQPIPEPVKEPEPIKSSLKAPSVAAVP------PVEAAAAVSPLASGVKKATL 573
|
170
....*....|....*...
gi 1907069526 1157 ETIAEEPAAVPPLESAFG 1174
Cdd:PRK10263 574 ATGAAATVAAPVFSLANS 591
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1469-1627 |
1.23e-03 |
|
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: 43.90 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1469 DRSEKIRNRIKQMMD-VSRTQTAVSIVEEDLKLLQLKLRASMSTKCNLEDQIK----KLEDDRSSLQTAKAGLEDECKTL 1543
Cdd:TIGR02169 695 SELRRIENRLDELSQeLSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSsleqEIENVKSELKELEARIEELEEDL 774
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1544 RQKVEILNELYQQKEMA----LQKKLSQEEYERQDREQRLTAADekvvlAAEEVKTYKRRIEEME-EELQKTERSFKNQI 1618
Cdd:TIGR02169 775 HKLEEALNDLEARLSHSripeIQAELSKLEEEVSRIEARLREIE-----QKLNRLTLEKEYLEKEiQELQEQRIDLKEQI 849
|
....*....
gi 1907069526 1619 AAHEKKAHD 1627
Cdd:TIGR02169 850 KSIEKEIEN 858
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
1012-1172 |
1.39e-03 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 43.92 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1012 QYSGVETAPLVTPPPPEEGWARPGEERQPPQQDSLPQENTGDLSVQPPEEPELSDQPVTSVQPPEEPELSDQPVTSVQPP 1091
Cdd:PRK10263 388 QPAVQYNEPLQQPVQPQQPYYAPAAEQPAQQPYYAPAPEQPAQQPYYAPAPEQPVAGNAWQAEEQQSTFAPQSTYQTEQT 467
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1092 EEPELSDQPVTSVQPPEEPELSDQPVTGYTST----------SEVSQKPDTKKDiDLG----PVMEggPVGAGDVQKQlE 1157
Cdd:PRK10263 468 YQQPAAQEPLYQQPQPVEQQPVVEPEPVVEETkparpplyyfEEVEEKRARERE-QLAawyqPIPE--PVKEPEPIKS-S 543
|
170
....*....|....*
gi 1907069526 1158 TIAEEPAAVPPLESA 1172
Cdd:PRK10263 544 LKAPSVAAVPPVEAA 558
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1247-1613 |
1.51e-03 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 43.67 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1247 LENIKKENAELmqKLSSYEQKIKESKKYVQETKKQ--NMILSDEAVKYKDKIKILEETNVSLGDKAKSLRLQLESEREQN 1324
Cdd:PTZ00440 839 LQKFPTEDENL--NLKELEKEFNENNQIVDNIIKDieNMNKNINIIKTLNIAINRSNSNKQLVEHLLNNKIDLKNKLEQH 916
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1325 VK----------NQDLILEN-----KKSIEKLKDVISMNASELsEVQVALNEAKLSEENVKSECHRVQEENARLKKKKEQ 1389
Cdd:PTZ00440 917 MKiintdniiqkNEKLNLLNnlnkeKEKIEKQLSDTKINNLKM-QIEKTLEYYDKSKENINGNDGTHLEKLDKEKDEWEH 995
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1390 LQQQVEEWSKSHAELTEQIKSFEKSQEDLEIAL-----THKDDNISALT-NCITQLNRLECELESEDpdkggnESDDLAN 1463
Cdd:PTZ00440 996 FKSEIDKLNVNYNILNKKIDDLIKKQHDDIIELidkliKEKGKEIEEKVdQYISLLEKMKTKLSSFH------FNIDIKK 1069
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1464 getggDRSEKIRNRIK----QMMDVSRtqtavSIVEEDLKLLQLKLRAS---MSTKCNLEDQIKKLEDDRSSLQTAKAGL 1536
Cdd:PTZ00440 1070 -----YKNPKIKEEIKlleeKVEALLK-----KIDENKNKLIEIKNKSHehvVNADKEKNKQTEHYNKKKKSLEKIYKQM 1139
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1537 EDECKTLRQKVEILNELYQQKEMALQkklsqeeYER---QDREQRLTAADEKVVLAAEEVKTYKRRIEEMEEELQKTERS 1613
Cdd:PTZ00440 1140 EKTLKELENMNLEDITLNEVNEIEIE-------YERiliDHIVEQINNEAKKSKTIMEEIESYKKDIDQVKKNMSKERND 1212
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1242-1363 |
1.54e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.22 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1242 QISEKLENIKKENAELMQKLSSYEQKIKESKKYVQETKKQNMILSDEAVKYKDKIKILEE--TNVSLGDKAKSLRLQLES 1319
Cdd:COG1579 21 RLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEqlGNVRNNKEYEALQKEIES 100
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1907069526 1320 EREQNVKNQDLILENKKSIEKLKDVISMNASELSEVQVALNEAK 1363
Cdd:COG1579 101 LKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKK 144
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1239-1658 |
1.54e-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: 43.42 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1239 TEKQISEKLENIKKENAELMQKLSSYEQKIKESKKYVQETKKQNmilsdeavKYKDKIKILEETNVSLGDKAKSLRLQLE 1318
Cdd:TIGR00618 227 ELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIE--------ELRAQEAVLEETQERINRARKAAPLAAH 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1319 SER-EQNVKNQDLILENKKSIEKLKDVISMNASELSEVQVALNEAKLSEENVKSECHRVQEENARLKKKKEQLQQQVEE- 1396
Cdd:TIGR00618 299 IKAvTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLt 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1397 -----WS--KSHAELTEQIKSFEKSQEDLEIALTH---------KDDNISALTNCITQLNRLE-CELESEDPDKGGNESD 1459
Cdd:TIGR00618 379 qhihtLQqqKTTLTQKLQSLCKELDILQREQATIDtrtsafrdlQGQLAHAKKQQELQQRYAElCAAAITCTAQCEKLEK 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1460 DLANgetggDRSEKIRNRIKQMMDV-------SRTQTAVSIVEEDLKLLQLKLRASMSTKCNLEDQIKKLEDDRSSLQta 1532
Cdd:TIGR00618 459 IHLQ-----ESAQSLKEREQQLQTKeqihlqeTRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQ-- 531
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1533 kaGLEDECKTLRQKVEILnELYQQKEMALQKKLSQEEYERQDREQRLTAADEKVVLAAEEVKTYKRRIEEMEEELQKTER 1612
Cdd:TIGR00618 532 --RGEQTYAQLETSEEDV-YHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAED 608
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1907069526 1613 SFKNQIAAHEKKAHDNWLKARAAERAMAEEKREAANLRHK---LLEMTQ 1658
Cdd:TIGR00618 609 MLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALhalQLTLTQ 657
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
1019-1117 |
2.16e-03 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 43.05 E-value: 2.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1019 APLVTPPPPEEGWARPGEERQPPQQDSLPQENTGDLSVQPPEEPELSDQPvtsVQPPEEPelsdQPVTSVQPPEEPELSD 1098
Cdd:PRK07764 702 APAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPPDP---AGAPAQP----PPPPAPAPAAAPAAAP 774
|
90
....*....|....*....
gi 1907069526 1099 QPVTSVQPPEEPELSDQPV 1117
Cdd:PRK07764 775 PPSPPSEEEEMAEDDAPSM 793
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1024-1127 |
2.72e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 43.00 E-value: 2.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1024 PPPPEEGWARPGEERQPPQQDSLPQENTGDLSVQPPEEPELSDQPVTSVQPPEEPELSDQPVTSVQP-----------PE 1092
Cdd:PHA03247 2891 VSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGavpqpwlgalvPG 2970
|
90 100 110
....*....|....*....|....*....|....*.
gi 1907069526 1093 EPELSDQPVTSVQPPEE-PELSDQPVTGYtSTSEVS 1127
Cdd:PHA03247 2971 RVAVPRFRVPQPAPSREaPASSTPPLTGH-SLSRVS 3005
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1226-1615 |
3.55e-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: 42.12 E-value: 3.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1226 RTILVVKSRVYQVTEKqiseKLENikkenaeLMQKLSSYEQKIKESKKYVQ--ETKKQNmilSDEAvkykdkIKILEEtn 1303
Cdd:pfam10174 386 KDMLDVKERKINVLQK----KIEN-------LQEQLRDKDKQLAGLKERVKslQTDSSN---TDTA------LTTLEE-- 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1304 vSLGDKAKSL-RLQLESEREQNVKnQDLILENKKSIEKLKDVISMNASELSEVQVALNEAK-----LSEENVKSECH--- 1374
Cdd:pfam10174 444 -ALSEKERIIeRLKEQREREDRER-LEELESLKKENKDLKEKVSALQPELTEKESSLIDLKehassLASSGLKKDSKlks 521
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1375 -----RVQEENARLKKKKEQLQQQVEEWSKSHAELTEQIKSFEKsqedlEIALtHKDDNisalTNCITQLNRL-----EC 1444
Cdd:pfam10174 522 leiavEQKKEECSKLENQLKKAHNAEEAVRTNPEINDRIRLLEQ-----EVAR-YKEES----GKAQAEVERLlgilrEV 591
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1445 ELESEDPDKGGNESDDLANGEtGGDRSEKIRNrIKQMMDVSRTQTAvsiveedlKLLQLKLRASMSTKCN-----LEDQI 1519
Cdd:pfam10174 592 ENEKNDKDKKIAELESLTLRQ-MKEQNKKVAN-IKHGQQEMKKKGA--------QLLEEARRREDNLADNsqqlqLEELM 661
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1520 KKLEDDRSSLQTAKAGLEDECKTLRQKVEILNELYQQKEMALQKKLSQeeyerqdREQRLTAA----DEKVVL------- 1588
Cdd:pfam10174 662 GALEKTRQELDATKARLSSTQQSLAEKDGHLTNLRAERRKQLEEILEM-------KQEALLAAisekDANIALlelsssk 734
|
410 420 430
....*....|....*....|....*....|.
gi 1907069526 1589 ---AAEEVKTYKRRIEEMEEEL-QKTERSFK 1615
Cdd:pfam10174 735 kkkTQEEVMALKREKDRLVHQLkQQTQNRMK 765
|
|
| Trypan_PARP |
pfam05887 |
Procyclic acidic repetitive protein (PARP); This family consists of several Trypanosoma brucei ... |
1026-1110 |
3.71e-03 |
|
Procyclic acidic repetitive protein (PARP); This family consists of several Trypanosoma brucei procyclic acidic repetitive protein (PARP) like sequences. The procyclic acidic repetitive protein (parp) genes of Trypanosoma brucei encode a small family of abundant surface proteins whose expression is restricted to the procyclic form of the parasite. They are found at two unlinked loci, parpA and parpB; transcription of both loci is developmentally regulated.
Pssm-ID: 368653 Cd Length: 134 Bit Score: 39.39 E-value: 3.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1026 PPEEGWARPGEERQPPQQDSLPQENTGDLSVQPPEEPELSDQPVTSVQPPEEPELSDQPvtsvQPPEEPELSDQPVTSVQ 1105
Cdd:pfam05887 31 PEDKGLTKGGKGKGKGTKVSDDDTNGTDPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEP----EPEPEPEPEPEPEPEPE 106
|
....*
gi 1907069526 1106 PPEEP 1110
Cdd:pfam05887 107 PEPEP 111
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1436-1611 |
4.48e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.06 E-value: 4.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1436 ITQLNRLECELESEDPDKGGNES--DDLANGETGGDRSEKIRNRIKQMMDVSRTQTAVSIVEEDLKLLQLKLRASMSTKC 1513
Cdd:COG4717 70 LKELKELEEELKEAEEKEEEYAElqEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1514 NLEDQIKKLEDdrssLQTAKAGLEDECKTLRQKveiLNELYQQKEMALQKKLSQEEYERQDREQRLTAADEKVVLAAEEV 1593
Cdd:COG4717 150 ELEERLEELRE----LEEELEELEAELAELQEE---LEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEEL 222
|
170
....*....|....*...
gi 1907069526 1594 KTYKRRIEEMEEELQKTE 1611
Cdd:COG4717 223 EELEEELEQLENELEAAA 240
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1250-1611 |
5.00e-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: 5.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1250 IKKENAELMQKLSSYEQKIKESKkyvQETKKQNMILSDEAVKYKDKikilEETNVSLGDKAKSLRLQLESereqnvKNQD 1329
Cdd:pfam01576 382 LESENAELQAELRTLQQAKQDSE---HKRKKLEGQLQELQARLSES----ERQRAELAEKLSKLQSELES------VSSL 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1330 LILENKKSIEKLKDVISMNaSELSEVQVALNEAKLSEENVKSECHRVQEENArlkkkkeQLQQQVEEWSKSHAELTEQIK 1409
Cdd:pfam01576 449 LNEAEGKNIKLSKDVSSLE-SQLQDTQELLQEETRQKLNLSTRLRQLEDERN-------SLQEQLEEEEEAKRNVERQLS 520
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1410 SFEKSQEDLEIALTHKDDNISALTNCITQLNRlecELESEdpdkggneSDDLANGETGGDRSEKIRNRIKQMMDvsrtqt 1489
Cdd:pfam01576 521 TLQAQLSDMKKKLEEDAGTLEALEEGKKRLQR---ELEAL--------TQQLEEKAAAYDKLEKTKNRLQQELD------ 583
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1490 avsiveeDLKLLQLKLRASMStkcNLEDQIKKLEDDRSSLQTAKAGLEDEcktlRQKVEILNELYQQKEMALQKKLSQ-- 1567
Cdd:pfam01576 584 -------DLLVDLDHQRQLVS---NLEKKQKKFDQMLAEEKAISARYAEE----RDRAEAEAREKETRALSLARALEEal 649
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907069526 1568 ---EEYERQDREQRLTAAD---------------EKVVLAAE-EVKTYKRRIEEMEEELQKTE 1611
Cdd:pfam01576 650 eakEELERTNKQLRAEMEDlvsskddvgknvhelERSKRALEqQVEEMKTQLEELEDELQATE 712
|
|
| ADIP |
pfam11559 |
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ... |
1500-1627 |
5.18e-03 |
|
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at cell-cell adherens junctions, and in Sch. pombe and other fungi where it anchors spindle-pole bodies to spindle microtubules. It is a coiled-coil structure, and in pombe, it is required for anchoring the minus end of spindle microtubules to the centrosome equivalent, the spindle-pole body. The name ADIP derives from the family being composed of Afadin- and alpha -Actinin-Binding Proteins localized at Cell-Cell Adherens Junctions.
Pssm-ID: 463295 [Multi-domain] Cd Length: 151 Bit Score: 39.61 E-value: 5.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1500 LLQLKLRaSMSTKCNLEDQIKKLEDDRSSLQTAKAGLEDECKTLRQKVEilneLYQQKEMALQKKLSQEEyeRQDREQRl 1579
Cdd:pfam11559 43 LLQQRDR-DLEFRESLNETIRTLEAEIERLQSKIERLKTQLEDLERELA----LLQAKERQLEKKLKTLE--QKLKNEK- 114
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1907069526 1580 taadekvvlaaeevktykrrieemeEELQKTER---SFKNQiAAHEKKAHD 1627
Cdd:pfam11559 115 -------------------------EELQRLKNalqQIKTQ-FAHEVKKRD 139
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1240-1420 |
5.78e-03 |
|
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: 41.54 E-value: 5.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1240 EKQISEKLENIKKENAELmqklssyEQKIKESKKYVQETKKQNmilsdeavkykDKIKILEETNVSLGDKAKSLRL---Q 1316
Cdd:TIGR04523 467 ETQLKVLSRSINKIKQNL-------EQKQKELKSKEKELKKLN-----------EEKKELEEKVKDLTKKISSLKEkieK 528
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1317 LESEREQnvKNQDlILENKKSIEKLKDVISMNA--SELSEVQVALNEAKLSEENVKSECHRVQEENARLKKKKEQLQQQV 1394
Cdd:TIGR04523 529 LESEKKE--KESK-ISDLEDELNKDDFELKKENleKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEI 605
|
170 180
....*....|....*....|....*.
gi 1907069526 1395 EEWSKSHAELTEQIKSFEKSQEDLEI 1420
Cdd:TIGR04523 606 EEKEKKISSLEKELEKAKKENEKLSS 631
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1237-1609 |
6.25e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.46 E-value: 6.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1237 QVTEKQISEKLENIKKENAELMQKLSSYEQKIKESKKYVQETKKQNMILSDEAVKYKDKIKILEETNVSLGDKAKSLRLQ 1316
Cdd:COG1196 392 LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEE 471
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1317 LESEREQNVKNQDLILENKKSIEKLKDVISMNASELSEVQVALNEAK-------LSEENVKSECHRVQEENA------RL 1383
Cdd:COG1196 472 AALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGlrglagaVAVLIGVEAAYEAALEAAlaaalqNI 551
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1384 KKKKEQLQQQVEEWSKSHAELTEQIKSFEKSQEDLEIALTHKDDNISALTNCITQLNRLECELESEDPDKGGNESDDLAN 1463
Cdd:COG1196 552 VVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAAR 631
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1464 GETGGDRSEKIRNRIKQM---MDVSRTQTAVSIVEEDLKLLQLKLRASMSTKcnLEDQIKKLEDDRSSLQTAKAGLEDEC 1540
Cdd:COG1196 632 LEAALRRAVTLAGRLREVtleGEGGSAGGSLTGGSRRELLAALLEAEAELEE--LAERLAEEELELEEALLAEEEEEREL 709
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907069526 1541 KTLRQKVEILNELYQQKEMALQKKLSQEEYERQDREQRLTAADEKVVLAAEEVKTYKRRIEEMEEELQK 1609
Cdd:COG1196 710 AEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEA 778
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
1212-1328 |
7.40e-03 |
|
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase
Pssm-ID: 440475 [Multi-domain] Cd Length: 152 Bit Score: 39.00 E-value: 7.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069526 1212 TAVLGIVSFAIFSWRTILVVKSRVYQVTE---KQISEKLENIKKENAELMQKLSSYEQKIKESKKyvqetKKQNMIlsDE 1288
Cdd:COG0711 2 TLFWQLINFLILVLLLKKFAWPPILKALDerqEKIADGLAEAERAKEEAEAALAEYEEKLAEARA-----EAAEII--AE 74
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1907069526 1289 AVKYKDKIK--ILEETNVSLGDKAKSLRLQLESEREQ---NVKNQ 1328
Cdd:COG0711 75 ARKEAEAIAeeAKAEAEAEAERIIAQAEAEIEQERAKalaELRAE 119
|
|
| |
