|
Name |
Accession |
Description |
Interval |
E-value |
| SAM_liprin-alpha1,2,3,4_repeat1 |
cd09562 |
SAM domain of liprin-alpha1,2,3,4 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 ... |
864-934 |
2.14e-45 |
|
SAM domain of liprin-alpha1,2,3,4 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of liprin-alpha1,2,3,4 proteins is a protein-protein interaction domain. Liprin-alpha proteins contain three copies (repeats) of SAM domain. They may form heterodimers with liprin-beta proteins through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development and in axon guidance; in particular, liprin-alpha is involved in formation of the presynaptic active zone.
Pssm-ID: 188961 Cd Length: 71 Bit Score: 157.34 E-value: 2.14e-45
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17569509 864 FALWNGPTVVAWLELWVGMPAWYVAACRANVKSGAIMSALSDQEIQKEIGISNPLHRLKLRLAIQEMVSLT 934
Cdd:cd09562 1 FALWNGPTVVAWLELWVGMPAWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEMVSLT 71
|
|
| SAM_liprin-alpha1,2,3,4_repeat2 |
cd09565 |
SAM domain of liprin-alpha1,2,3,4 proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 ... |
951-1016 |
7.13e-40 |
|
SAM domain of liprin-alpha1,2,3,4 proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of liprin-alpha1,2,3,4 proteins is a protein-protein interaction domain. Liprin-alpha proteins contain three copies (repeats) of SAM domain. They may form heterodimers with liprin-beta proteins through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development, and in axon guidance; in particular, liprin-alpha is involved in formation of the presynaptic active zone.
Pssm-ID: 188964 Cd Length: 66 Bit Score: 141.46 E-value: 7.13e-40
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17569509 951 MNHEYIGNDWLPCLGLAQYRSAFMECLLDARMLEHLSKRDLRTHLRMVDTFHRTSLQYGIMCLKKV 1016
Cdd:cd09565 1 MNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRTHLKMVDSFHRTSLQYGILCLKRL 66
|
|
| SAM_liprin-alpha1,2,3,4_repeat3 |
cd09568 |
SAM domain of liprin-alpha1,2,3,4 proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 ... |
1036-1107 |
2.36e-36 |
|
SAM domain of liprin-alpha1,2,3,4 proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 of liprin-alpha1,2,3,4 proteins is a protein-protein interaction domain. Liprin-alpha proteins contain three copies (repeats) of SAM domain. They may form heterodimers with liprin-beta proteins through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development and in axon guidance; in particular, liprin-alpha is involved in formation of the presynaptic active zone.
Pssm-ID: 188967 Cd Length: 72 Bit Score: 131.67 E-value: 2.36e-36
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17569509 1036 DLLVWSNERVQRWVEEIGLGVFSRNLVDSGIHGALIALDETFDASAFAYALQIGSQDVPNRQLLEKKFIGLV 1107
Cdd:cd09568 1 DVLVWSNERVIRWVQSIGLREYANNLLESGVHGALIALDETFDANSFALALQIPTQNTQARQILEREFNNLL 72
|
|
| SAM_liprin-kazrin_repeat1 |
cd09494 |
SAM domain of liprin/kazrin proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of ... |
871-929 |
3.83e-28 |
|
SAM domain of liprin/kazrin proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of liprin/kazrin proteins is a protein-protein interaction domain. The long form of liprin/kazrin proteins contains three copies (repeats) of the SAM domain. Liprin-alpha may form heterodimers with liprin-beta through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development and in axon guidance. In particular, liprin-alpha is involved in formation of the presynaptic active zone; liprin-beta is involved in the maintenance of lymphatic vessel integrity. Kazrins are involved in interplay between desmosomes and adherens junctions; additionally they play a role in regulation of intercellular differentiation, junction assembly, and cytoskeletal organization.
Pssm-ID: 188893 Cd Length: 58 Bit Score: 107.70 E-value: 3.83e-28
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 17569509 871 TVVAWLELWVGMPaWYVAACRANVKSGAIMSALSDQEIQKEIGISNPLHRLKLRLAIQE 929
Cdd:cd09494 1 RVCAWLEDFGLMP-MYVIFCRQNVKSGHTLLTLSDQEMEKELGIKNPLHRKKLRLAIKE 58
|
|
| SAM_liprin-kazrin_repeat2 |
cd09495 |
SAM domain of liprin/kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of ... |
955-1014 |
3.60e-23 |
|
SAM domain of liprin/kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of liprin/kazrin proteins is a protein-protein interaction domain. The long form of liprin/kazrin proteins contains three copies (repeats) of SAM domain. Liprin-alpha may form heterodimers with liprin-beta through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development and in axon guidance. In particular, liprin-alpha is involved in formation of the presynaptic active zone; liprin-beta is involved in the maintenance of lymphatic vessel integrity. Kazrins are involved in interplay between desmosomes and in adheren junctions; additionally they play a role in regulation of intercellular differentiation, junction assembly, and cytoskeletal organization.
Pssm-ID: 188894 Cd Length: 60 Bit Score: 93.75 E-value: 3.60e-23
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 955 YIGNDWLPCLGLAQYRSAFMECLLDARMLEHLSKRDLRTHLRMVDTFHRTSLQYGIMCLK 1014
Cdd:cd09495 1 WWVTRWLDDIGLPQYKDQFHESLVDRRMLQYLTVNDLLVHLKVTSQLHHLSLKCGIHVLH 60
|
|
| SAM_kazrin_repeat1 |
cd09564 |
SAM domain of kazrin proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of kazrin ... |
867-929 |
4.61e-17 |
|
SAM domain of kazrin proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of kazrin proteins is a protein-protein interaction domain. The long isoform of kazrin contains three copies (repeats) of SAM domain. Kazrin can interact with periplakin. It is involved into interplay between desmosomes and in adheren junctions. Additionally kazrins play a role in regulation of intercellular differentiation, junction assembly, and cytoskeletal organization.
Pssm-ID: 188963 Cd Length: 70 Bit Score: 76.72 E-value: 4.61e-17
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17569509 867 WNGPTVVAWLELWVGMPAwYVAACRANVKSGAIMSALSDQEIQKEIGISNPLHRLKLRLAIQE 929
Cdd:cd09564 4 WKADMVLAWLEVVMHMPM-YSKACAENVKSGKVLLGLSDSELESGLGISNVLHRRKLRLAIEE 65
|
|
| SAM_kazrin_repeat3 |
cd09570 |
SAM domain of kazrin proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 of kazrin ... |
1036-1107 |
4.90e-16 |
|
SAM domain of kazrin proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 of kazrin proteins is a protein-protein interaction domain. The long isoform of kazrins contains three copies (repeats) of SAM domain. Kazrin can interact with periplakin. It is involved in interplay between desmosomes and in adheren junctions. Additionally kazrins play a role in regulation of intercellular differentiation, junction assembly, and cytoskeletal organization.
Pssm-ID: 188969 Cd Length: 72 Bit Score: 73.63 E-value: 4.90e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17569509 1036 DLLVWSNERVQRWVEEIGLGVFSRNLVDSGIHGALIALDETFDASAFAYALQIGSQDVPNRQLLEKKFIGLV 1107
Cdd:cd09570 1 DPVVWTNQRVIKWARSIDLKEYADNLRDSGVHGALMVLEPSFNSDTMATALGIPSSKNIIRRHLTTEMEALV 72
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
237-515 |
6.89e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 76.51 E-value: 6.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 237 ESANRLIEMQEALERMK---TELAN---SLKQSTEITTRNAELEDQLTE-----------DAREKHA-AQESIVRLKNQI 298
Cdd:COG1196 176 EAERKLEATEENLERLEdilGELERqlePLERQAEKAERYRELKEELKEleaellllklrELEAELEeLEAELEELEAEL 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 299 CELDAQRTDQETRITTFESRFLTAQRESTCIRDLNDKLEHQLANKDAAVRLNEEKVHSLQERLELAEKQLAQSLKKAESL 378
Cdd:COG1196 256 EELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEEL 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 379 PSVEAELQQRMEALTAAEQKSVSAEERIQRLDRNIQELSAELERAVQRERMNEEHSQRLSSTVDKLLSESNDRLQLHLKE 458
Cdd:COG1196 336 EEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLER 415
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 17569509 459 RMQALDDKNRLTQQLDGTKKIYDQAERIKDRLQRDNESLRQEIEALRQQLYNARTAQ 515
Cdd:COG1196 416 LERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEA 472
|
|
| SAM_kazrin_repeat2 |
cd09567 |
SAM domain of kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of kazrin ... |
950-1014 |
5.65e-13 |
|
SAM domain of kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of kazrin proteins is a protein-protein interaction domain. The long isoform of kazrins contains three copies (repeats) of SAM domain. Kazrin can interact with periplakin. It is involved in interplay between desmosomes and in adheren junctions. Additionally kazrins play a role in regulation of intercellular differentiation, junction assembly, and cytoskeletal organization.
Pssm-ID: 188966 Cd Length: 65 Bit Score: 64.74 E-value: 5.65e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17569509 950 DMNHEYIGNDWLPCLGLAQYRSAFMECLLDARMLEHLSKRDLRTHLRMVDTFHRTSLQYGIMCLK 1014
Cdd:cd09567 1 QLDHTWVAREWLRDLGLPQYSEAFREHLVDGRVLDTLSRKDLEKHLGVSKKFHQASLLRGIELLR 65
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
128-506 |
1.27e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 72.40 E-value: 1.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 128 LEHLECLVSRHERSLRMTVMKRQAQNHAGVSSEVEVLKALKSLFEHHKALDEKVRErlrvAMERVATLEEELSTKGDENS 207
Cdd:TIGR02168 202 LKSLERQAEKAERYKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEE----LTAELQELEEKLEELRLEVS 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 208 SLKARIATYAAEAEeamasnapingsissESANRLIEMQEALERMKTELANSLKQSTEITTRNAELEDQLTEDAREKHAA 287
Cdd:TIGR02168 278 ELEEEIEELQKELY---------------ALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAEL 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 288 QESIVRLKNQICELDAQRTDQETRITTFESRFLTAQRESTCIRDLNDKLEHQLANKDAAVRLNEEKVHSLQERLE----- 362
Cdd:TIGR02168 343 EEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRErlqqe 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 363 ----LAEKQLAQSLKKAESLPSVEAELQQRMEALTAAEQKSVSAEERIQRLDRNIQELSAELERAVQRERMNEEHSQRLS 438
Cdd:TIGR02168 423 ieelLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLE 502
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17569509 439 STVDKLLSESNDRLQLHlkermqalDDKNRLTQQLDGTKKiYDQA------ERIKDRLQRDNESLRQEIEALRQ 506
Cdd:TIGR02168 503 GFSEGVKALLKNQSGLS--------GILGVLSELISVDEG-YEAAieaalgGRLQAVVVENLNAAKKAIAFLKQ 567
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
30-505 |
1.34e-12 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 72.38 E-value: 1.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 30 PSDRdnieQLMMNmledrDKLQ-EQLENYKVQLENAGLRTKEVEkeRDMMKRQFEVHTQNLPQELQTMTRELCLLKEQLL 108
Cdd:PRK02224 148 PSDR----QDMID-----DLLQlGKLEEYRERASDARLGVERVL--SDQRGSLDQLKAQIEEKEEKDLHERLNGLESELA 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 109 EKDEEIVELKAERNNTRLLLEHLECLVSRHERSLrmtvmkrqaqnhagvsSEVEVLKALKSLFEHHKALDEKVRERLRva 188
Cdd:PRK02224 217 ELDEEIERYEEQREQARETRDEADEVLEEHEERR----------------EELETLEAEIEDLRETIAETEREREELA-- 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 189 mERVATLEEELSTKGDENSSLKARIATYAAEAEEAMASNAPINGSIsSESANRLIEMQEALERMKTELANSLKQSTEITT 268
Cdd:PRK02224 279 -EEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRD-EELRDRLEECRVAAQAHNEEAESLREDADDLEE 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 269 RNAELEDQLTEDAREKHAAQESIVRLKNQICELDAQRTDQETRITtfesrFLTAQREstcirDLNDKLEHQLANKDAAV- 347
Cdd:PRK02224 357 RAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFG-----DAPVDLG-----NAEDFLEELREERDELRe 426
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 348 RLNE--EKVHSLQERLELAEKQLA--------QSLKKAESLPSVEaELQQRMEALTAA-EQKSVSAEERIQRLDRniQEL 416
Cdd:PRK02224 427 REAEleATLRTARERVEEAEALLEagkcpecgQPVEGSPHVETIE-EDRERVEELEAElEDLEEEVEEVEERLER--AED 503
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 417 SAELERAVQRERMNEEHSQRLSSTVDKLLSESNDRLQlHLKERMQALDDKNRltQQLDGTKKIYDQAERIKDR---LQRD 493
Cdd:PRK02224 504 LVEAEDRIERLEERREDLEELIAERRETIEEKRERAE-ELRERAAELEAEAE--EKREAAAEAEEEAEEAREEvaeLNSK 580
|
490
....*....|..
gi 17569509 494 NESLRQEIEALR 505
Cdd:PRK02224 581 LAELKERIESLE 592
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
248-508 |
1.62e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 72.01 E-value: 1.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 248 ALERmKTELANSLKQSTEITTRNAELEDQLTEdarekhaAQESIVRLKNQICELDAQRTDQETRITTFESRFLTAQREST 327
Cdd:TIGR02168 672 ILER-RREIEELEEKIEELEEKIAELEKALAE-------LRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVE 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 328 CIRDLNDKLEHQLANKDAAVRLNEEKVHSLQERLELAEKQLAQslkkaeslpsVEAELQQRMEALTAAEQKSVSAEERIQ 407
Cdd:TIGR02168 744 QLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEE----------LEAQIEQLKEELKALREALDELRAELT 813
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 408 RLDRNIQELSAELERAVQRERMNEEHSQRLSSTVDKL-----------------LSESNDRLQLHLKERMQALDDKNRLT 470
Cdd:TIGR02168 814 LLNEEAANLRERLESLERRIAATERRLEDLEEQIEELsedieslaaeieeleelIEELESELEALLNERASLEEALALLR 893
|
250 260 270
....*....|....*....|....*....|....*...
gi 17569509 471 QQLDGTKKIYDQAERIKDRLQRDNESLRQEIEALRQQL 508
Cdd:TIGR02168 894 SELEELSEELRELESKRSELRRELEELREKLAQLELRL 931
|
|
| SAM_liprin-kazrin_repeat3 |
cd09496 |
SAM domain of liprin/kazrin proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 of ... |
1044-1103 |
2.66e-12 |
|
SAM domain of liprin/kazrin proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 of liprin/kazrin proteins is a protein-protein interaction domain. The long form of liprin/kazrin proteins contains three copies (repeats) of SAM domain. Liprin-alpha may form heterodimers with liprin-beta through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development and in axon guidance. In particular, liprin-alpha is involved in formation of the presynaptic active zone; liprin-beta is involved in the maintenance of lymphatic vessel integrity. Kazrins are involved in interplay between desmosomes and in adherens junctions; additionally they play a role in regulation of intercellular differentiation, junction assembly, and cytoskeletal organization.
Pssm-ID: 188895 Cd Length: 62 Bit Score: 62.94 E-value: 2.66e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 1044 RVQRWVEEIGLGVFSRNLVDSGIHGALIALDETFDASAFAYALQIGSQDVPNRQLLEKKF 1103
Cdd:cd09496 1 RVIHWIRSIDLREYANNLVESGVHGGLLVLEPNFDHNTMALVLQIPPQKTQARRHLETEF 60
|
|
| SAM_liprin-beta1,2_repeat1 |
cd09563 |
SAM domain of liprin-beta1,2 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of ... |
864-928 |
3.09e-12 |
|
SAM domain of liprin-beta1,2 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of liprin-beta1,2 proteins is a protein-protein interaction domain. Liprin-beta protein contain three copies (repeats) of SAM domain. They may form heterodimers with liprins-alpha through their SAM domains. It was suggested based on bioinformatic approaches that the second SAM domain of liprin-beta is potentially able to form polymers. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development, in axon guidance, and in the maintenance of lymphatic vessel integrity.
Pssm-ID: 188962 Cd Length: 64 Bit Score: 62.63 E-value: 3.09e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17569509 864 FALWNGPTVVAWL-ELWVGMpawYVAACRANVKSGAIMSALSDQEIQKEIGISNPLHRLKLRLAIQ 928
Cdd:cd09563 1 FAEWSTEQVCDWLaELGLGQ---YVDECRRWVKSGQTLLKASPQELEKELGIKHPLHRKKLQLALQ 63
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
103-507 |
3.07e-11 |
|
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: 68.17 E-value: 3.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 103 LKEQLLEKDEEIVELKAERNNTRLLLEHLECLVsrHERSLRMTVMKRQaqnHAGVSSEVEVLKAlkslfEHhkaldEKVR 182
Cdd:TIGR02169 672 EPAELQRLRERLEGLKRELSSLQSELRRIENRL--DELSQELSDASRK---IGEIEKEIEQLEQ-----EE-----EKLK 736
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 183 ERLRVAMERVATLEEELSTKGDENSSLKARIATYAAEAEEAMASNAPINGSISSEsanRLIEMQEALERMKTELAnslkq 262
Cdd:TIGR02169 737 ERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHS---RIPEIQAELSKLEEEVS----- 808
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 263 stEITTRNAELEDQLTEDAREKHAAQESIVRLKNQICELDAQRTDQETRITTFESRfltaqrestcIRDLNDKLehqlan 342
Cdd:TIGR02169 809 --RIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGK----------KEELEEEL------ 870
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 343 kdaavrlneekvhslqERLELAEKQLAQSLKKaeslpsVEAELQQRMEALTAAEQKSVSAEERIQRLDRNIQELSAELER 422
Cdd:TIGR02169 871 ----------------EELEAALRDLESRLGD------LKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEA 928
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 423 AVQRERMNEEHSQRLSSTVDKLLSESNDRLQLH-LKERMQALDDKNRLT-QQLDGTKKIYDQAERIKDRLQRDNESLRQE 500
Cdd:TIGR02169 929 LEEELSEIEDPKGEDEEIPEEELSLEDVQAELQrVEEEIRALEPVNMLAiQEYEEVLKRLDELKEKRAKLEEERKAILER 1008
|
....*..
gi 17569509 501 IEALRQQ 507
Cdd:TIGR02169 1009 IEEYEKK 1015
|
|
| SAM_liprin-beta1,2_repeat2 |
cd09566 |
SAM domain of liprin-beta1,2 proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of ... |
960-1014 |
2.00e-10 |
|
SAM domain of liprin-beta1,2 proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of liprin-beta1,2 proteins is a protein-protein interaction domain. Liprin-beta proteins contain three copies (repeats) of SAM domain. They may form heterodimers with liprin-alpha proteins through their SAM domains. It was suggested based on bioinformatic approaches that the second SAM domain of liprin-beta potentially is able to form polymers. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development, in axon guidance, and in the maintenance of lymphatic vessel integrity.
Pssm-ID: 188965 Cd Length: 63 Bit Score: 57.32 E-value: 2.00e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 17569509 960 WLPCLGLAQYRSAFMECLLDARMLEHLSKRDLrTHLRMVDTFHRTSLQYGIMCLK 1014
Cdd:cd09566 10 WLDDIGLPQYKDAFSEAKVDGRMLHYLTVDDL-LHLKVTSALHHASIRRGIQVLR 63
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
27-522 |
3.42e-10 |
|
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: 64.36 E-value: 3.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 27 IDEPSDRDNIEQLMMNMLEDRDKLQE-------QLENYKVQLENAGLRTKEVEKERDMMKRQFEVHtQNLPQELQTMTRE 99
Cdd:pfam05483 247 IQITEKENKMKDLTFLLEESRDKANQleektklQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQ-KALEEDLQIATKT 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 100 LCLLKEqllEKDEEIVELKAERNNTRLLLEHLECLVSRHERSLRmTVMKRQAQNHAGV----------SSEVEVLKALKS 169
Cdd:pfam05483 326 ICQLTE---EKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLR-TEQQRLEKNEDQLkiitmelqkkSSELEEMTKFKN 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 170 -----LFEHHKALDEKvrERLRVAMERVATLEEELSTKGDENSSLkariatYAAEAEEAMASNAPINGSISSESanrliE 244
Cdd:pfam05483 402 nkeveLEELKKILAED--EKLLDEKKQFEKIAEELKGKEQELIFL------LQAREKEIHDLEIQLTAIKTSEE-----H 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 245 MQEALERMKTELANSLKQSTEITTRNAELedqLTEDAREKHAAQESIVRLKNQICELDAQRTDQETRITTFEsrflTAQR 324
Cdd:pfam05483 469 YLKEVEDLKTELEKEKLKNIELTAHCDKL---LLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIE----NLEE 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 325 ESTCIRDLNDKLEHQLANKDAAVRL----NEEKVHSLQERLELAEKQLAQSLKKAESL-PSVE------AELQQRMEAL- 392
Cdd:pfam05483 542 KEMNLRDELESVREEFIQKGDEVKCkldkSEENARSIEYEVLKKEKQMKILENKCNNLkKQIEnknkniEELHQENKALk 621
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 393 --TAAEQKSVSAEE-RIQRLD-------RNIQELSAELERAVQRERMNEEH----SQRLSSTVD---KLLSESNDRLQLH 455
Cdd:pfam05483 622 kkGSAENKQLNAYEiKVNKLElelasakQKFEEIIDNYQKEIEDKKISEEKlleeVEKAKAIADeavKLQKEIDKRCQHK 701
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17569509 456 LKErMQALDDK-----NRLTQQLDGTKKIYDQAER----IKDRLQRDNESLRQEIEALRQQLYNARTAQFQSRMHA 522
Cdd:pfam05483 702 IAE-MVALMEKhkhqyDKIIEERDSELGLYKNKEQeqssAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEA 776
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
44-498 |
4.49e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 63.93 E-value: 4.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 44 LEDRDKLQEQLENYKVQLENAGLRTKEVEKErdmmKRQFEVHTQNLPQELQTMTRELCLLKEQ------LLEKDEEIVEL 117
Cdd:PRK03918 223 LEKLEKEVKELEELKEEIEELEKELESLEGS----KRKLEEKIRELEERIEELKKEIEELEEKvkelkeLKEKAEEYIKL 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 118 KAERNNTRLLLEHLECLVSRHERSLRmtVMKRQAQNHAGVSSEV-EVLKALKSLFEHHKALDEKVR--ERLRVAMERVAT 194
Cdd:PRK03918 299 SEFYEEYLDELREIEKRLSRLEEEIN--GIEERIKELEEKEERLeELKKKLKELEKRLEELEERHElyEEAKAKKEELER 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 195 LEEELstKGDENSSLKARIATYAAEAEEAMASNAPIN---GSISSESANR---LIEMQEA-------------------L 249
Cdd:PRK03918 377 LKKRL--TGLTPEKLEKELEELEKAKEEIEEEISKITariGELKKEIKELkkaIEELKKAkgkcpvcgrelteehrkelL 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 250 ERMKTELANSLKQSTEITTRNAELEDQLT--EDAREK-------HAAQESIVRLKNQICELDAQRTDQETR-ITTFESRF 319
Cdd:PRK03918 455 EEYTAELKRIEKELKEIEEKERKLRKELRelEKVLKKeseliklKELAEQLKELEEKLKKYNLEELEKKAEeYEKLKEKL 534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 320 LTAQREstcIRDLNDKLE--HQLANKDAAVrlnEEKVHSLQERLELAEKQLA--------------QSLKKAE----SLP 379
Cdd:PRK03918 535 IKLKGE---IKSLKKELEklEELKKKLAEL---EKKLDELEEELAELLKELEelgfesveeleerlKELEPFYneylELK 608
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 380 SVEAELQQRMEALTAAEQKSVSAEERIQRLDRNIQELSAELERAVQR------ERMNEEHsQRLSSTVDKLLSESnDRLQ 453
Cdd:PRK03918 609 DAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKyseeeyEELREEY-LELSRELAGLRAEL-EELE 686
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 17569509 454 LHLKERMQALDDKNRLTQQLDGTKKIYDQAERIKDRLQRDNESLR 498
Cdd:PRK03918 687 KRREEIKKTLEKLKEELEEREKAKKELEKLEKALERVEELREKVK 731
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
42-606 |
5.09e-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: 63.92 E-value: 5.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 42 NMLEDRDKLQEQLENYKVQLENAGLRTKEVEKERDMMKRQFEvhtqNLPQELQTMTRELCLLKEQLLEKDEEIVELKAER 121
Cdd:TIGR02168 313 NLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELE----SLEAELEELEAELEELESRLEELEEQLETLRSKV 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 122 NNTRL-----------LLEHLECLVSRHERSLRMTVMKRQAQNHAGVSSEVEVLKALKSLFEHHKALDEKVRERLRVAME 190
Cdd:TIGR02168 389 AQLELqiaslnneierLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELRE 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 191 RVATLEEELSTKGDENSSLKARIATYAAEAEEAMASNAPI-----NGSISSESANRLIEMQEALERMKTELA-------- 257
Cdd:TIGR02168 469 ELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVkallkNQSGLSGILGVLSELISVDEGYEAAIEaalggrlq 548
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 258 --------------NSLKQSTEITTRNAEL----EDQLTEDAREKHAAQESIVRLKNQICELD----------------A 303
Cdd:TIGR02168 549 avvvenlnaakkaiAFLKQNELGRVTFLPLdsikGTEIQGNDREILKNIEGFLGVAKDLVKFDpklrkalsyllggvlvV 628
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 304 QRTDQETRI---TTFESRFLTAQRESTCIRDL----NDKLEHQLANKDAAVRLNEEKVHSLQERLELAEKQLAQSLKKAE 376
Cdd:TIGR02168 629 DDLDNALELakkLRPGYRIVTLDGDLVRPGGVitggSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELE 708
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 377 SLPSVEAELQQRMEALT-----------AAEQKSVSAEERIQRLDRNIQELSAELERAVQRERMNEEHSQRLSSTVDKL- 444
Cdd:TIGR02168 709 ELEEELEQLRKELEELSrqisalrkdlaRLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELe 788
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 445 ----------------LSESNDRLQLHLKERMQALDDKNRLTQQLDGTKKIYDQAERIKDRLQRDNESLRQEIEALRQQL 508
Cdd:TIGR02168 789 aqieqlkeelkalreaLDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELI 868
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 509 YNARTAqfqsrmhaipFTHAQNIVQQQPQASIAQQSAYQmykqqpaqqyQTVGMRRPNKGRISALQDDPNKVQTLNEQEW 588
Cdd:TIGR02168 869 EELESE----------LEALLNERASLEEALALLRSELE----------ELSEELRELESKRSELRRELEELREKLAQLE 928
|
650
....*....|....*....
gi 17569509 589 DRLQQAHV-LANVQQAFSS 606
Cdd:TIGR02168 929 LRLEGLEVrIDNLQERLSE 947
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
179-508 |
5.18e-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: 63.92 E-value: 5.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 179 EKVRERLRVAMERVATLEEELSTKGDENSSLKARIATYAAeaeeamasnapingsissesanRLIEMQEALERMKTELAN 258
Cdd:TIGR02168 680 EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRK----------------------ELEELSRQISALRKDLAR 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 259 SLKQSTEITTRNAELEDQLTEDAREKHAAQESIVRLKNQICELDAQRTDQETRITTFESRFLTAQRESTCIRDLNDKLEH 338
Cdd:TIGR02168 738 LEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNE 817
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 339 QLANKDAAVRLNEEKVHSLQERLELAEKQLAQslkKAESLPSVEAELQQRMEALTAAEQKSVSAEERIQRLDRNIQELSA 418
Cdd:TIGR02168 818 EAANLRERLESLERRIAATERRLEDLEEQIEE---LSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRS 894
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 419 ELERAVQRERMNEEHSQRLsstvDKLLSESNDRLQlHLKERMQALDDK-NRLTQQLDGTKKI-YDQAERIKDRLQRDNES 496
Cdd:TIGR02168 895 ELEELSEELRELESKRSEL----RRELEELREKLA-QLELRLEGLEVRiDNLQERLSEEYSLtLEEAEALENKIEDDEEE 969
|
330
....*....|..
gi 17569509 497 LRQEIEALRQQL 508
Cdd:TIGR02168 970 ARRRLKRLENKI 981
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
98-416 |
1.89e-09 |
|
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: 62.00 E-value: 1.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 98 RELCLLKEQLLEKDEEIVELKAERNNTRLLLEHLECLVSRHERSLRMTVMKRQAQNHAGVSSEVEVLKALKSLFEHHKAL 177
Cdd:TIGR02168 677 REIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKEL 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 178 DEkVRERLRVAMERVATLEEELSTKGDENSSLKARIATYAAEAEEAMAsnapingsissesanRLIEMQEALERMKTELA 257
Cdd:TIGR02168 757 TE-LEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALRE---------------ALDELRAELTLLNEEAA 820
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 258 NSLKQSTEITTRNAELEDQLTEDAREKHAAQESIVRLKNQICELDAQRTDQETRITTFESRFLTAQRESTCIRDLNDKLE 337
Cdd:TIGR02168 821 NLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELS 900
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 338 HQLANKDAAVRLNE-------EKVHSLQERLELAEKQLAQSLKKAESLPSVEAELQQRMEALTAAEQKsvSAEERIQRLD 410
Cdd:TIGR02168 901 EELRELESKRSELRreleelrEKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEE--EARRRLKRLE 978
|
....*.
gi 17569509 411 RNIQEL 416
Cdd:TIGR02168 979 NKIKEL 984
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
102-428 |
4.86e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 60.72 E-value: 4.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 102 LLKEQLLEKDEEIVELKAERNNTRLLLEHLEclvSRHERslrmtvmKRQAQNHAgvssEVEVLKALKSLFEHHKALdEKV 181
Cdd:COG1196 236 ELEAELEELEAELEELEAELEELEAELAELE---AELEE-------LRLELEEL----ELELEEAQAEEYELLAEL-ARL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 182 RERLRVAMERVATLEEELSTKGDENSSLKARIATYA---AEAEEAMASNAPINgsisSESANRLIEMQEALERMKTELAN 258
Cdd:COG1196 301 EQDIARLEERRRELEERLEELEEELAELEEELEELEeelEELEEELEEAEEEL----EEAEAELAEAEEALLEAEAELAE 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 259 SLKQSTEITTRNAELEDQLTEDAREKHAAQESIVRLKNQICELDAQRTDQETRITTFESRFLTAQREstcirdlNDKLEH 338
Cdd:COG1196 377 AEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEA-------LEEAAE 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 339 QLANKDAAVRLNEEKVHSLQERLELAEKQLAQSLKKAESLpSVEAELQQRMEALTAAEQKSVSAEERIQRLDRNIQELSA 418
Cdd:COG1196 450 EEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEA-AARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAV 528
|
330
....*....|
gi 17569509 419 ELERAVQRER 428
Cdd:COG1196 529 LIGVEAAYEA 538
|
|
| SAM |
smart00454 |
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ... |
864-930 |
5.70e-09 |
|
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related tyrosine kinases, appears to mediate cell-cell initiated signal transduction via the binding of SH2-containing proteins to a conserved tyrosine that is phosphorylated. In many cases mediates homodimerisation.
Pssm-ID: 197735 Cd Length: 68 Bit Score: 53.45 E-value: 5.70e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17569509 864 FALWNGPTVVAWLELWvGMPAwYVAACRANVKSGAIMSALSDQEIQKEIGISNPLHRLKLRLAIQEM 930
Cdd:smart00454 1 VSQWSPESVADWLESI-GLEQ-YADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKL 65
|
|
| SAM_liprin-beta1,2_repeat3 |
cd09569 |
SAM domain of liprin-beta proteins repeat 3; SAM (sterile alpha motif) domain repea t3 of ... |
1036-1107 |
7.92e-09 |
|
SAM domain of liprin-beta proteins repeat 3; SAM (sterile alpha motif) domain repea t3 of liprin-beta1,2 proteins is a protein-protein interaction domain. Liprin-beta proteins contain three copies (repeats) of SAM domain. They may form heterodimers with liprin-alpha proteins through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development, in axon guidance, and in the maintenance of lymphatic vessel integrity.
Pssm-ID: 188968 Cd Length: 72 Bit Score: 53.23 E-value: 7.92e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17569509 1036 DLLVWSNERVQRWVEEIGLGVFSRNLVDSGIHGALIALDETFDASAFAYALQIGSQDVPNRQLLEKKFIGLV 1107
Cdd:cd09569 1 EVVLWTNHRVMEWLRSVDLAEYAPNLRGSGVHGALMVLEPRFTAETLAALLNIPPNKTLLRRHLATHFNQLL 72
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
33-392 |
8.48e-09 |
|
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: 60.07 E-value: 8.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 33 RDNIEQLmmnmlED-RDKLQEQLENYKVQLENA----GLRTKEVEKERDMMKRQFEVHTQNLPQ---ELQTMTRELCLLK 104
Cdd:TIGR02168 185 RENLDRL-----EDiLNELERQLKSLERQAEKAerykELKAELRELELALLVLRLEELREELEElqeELKEAEEELEELT 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 105 EQLLEKDEEIVELKAERNNTRLLLEHLEclvsrherslrmtvmkrqaqnhagvsSEVEVLKALKSLFEHHKALDEKVRER 184
Cdd:TIGR02168 260 AELQELEEKLEELRLEVSELEEEIEELQ--------------------------KELYALANEISRLEQQKQILRERLAN 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 185 LRVAMERVATLEEELSTKGDENSSLKARIatyaaeaeeamasnapingsissesANRLIEMQEALERMKTELANSLKQST 264
Cdd:TIGR02168 314 LERQLEELEAQLEELESKLDELAEELAEL-------------------------EEKLEELKEELESLEAELEELEAELE 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 265 EITTRNAELEDQLTEDAREKHAAQESIVRLKNQICELDAQRTDQETRITTFESRFLTAQREstciRDLNDKLEHQ--LAN 342
Cdd:TIGR02168 369 ELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKK----LEEAELKELQaeLEE 444
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 17569509 343 KDAAVRLNEEKVHSLQERLELAEKQLAQSLKKAESLPSVEAELQQRMEAL 392
Cdd:TIGR02168 445 LEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSL 494
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
27-505 |
9.11e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 59.67 E-value: 9.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 27 IDEPSDRDNIEQLmmNMLE-DRDKLQEQLENYKVQLENAgLRTKEVEKERDMMKRQFEVHTQNLPQELQTMT-------R 98
Cdd:PRK02224 196 IEEKEEKDLHERL--NGLEsELAELDEEIERYEEQREQA-RETRDEADEVLEEHEERREELETLEAEIEDLRetiaeteR 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 99 ELCLLKEQLLEKDEEIVELKAERNNTR-----------LLLEHLECLVSRHERSLRMTVMKRQAQNHAGVSSEvevlkal 167
Cdd:PRK02224 273 EREELAEEVRDLRERLEELEEERDDLLaeaglddadaeAVEARREELEDRDEELRDRLEECRVAAQAHNEEAE------- 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 168 kSLFEHHKALDEKVRErlrvAMERVATLEEELSTKGDENSSLKARIATYAAEAEEAMASNAPINGSISsESANRLIEMQE 247
Cdd:PRK02224 346 -SLREDADDLEERAEE----LREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLG-NAEDFLEELRE 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 248 ALERMK---TELANSLKQSTEITTRNAELED--------QLTEDAREKHAAQESivrlKNQICELDAQRTDQETRITTFE 316
Cdd:PRK02224 420 ERDELRereAELEATLRTARERVEEAEALLEagkcpecgQPVEGSPHVETIEED----RERVEELEAELEDLEEEVEEVE 495
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 317 SRFLTAQRestcIRDLNDKLEHQLANKDAAVRLNEEKvhslQERLELAEKQLAQSLKKAESLpsvEAELQQRMEALTAAE 396
Cdd:PRK02224 496 ERLERAED----LVEAEDRIERLEERREDLEELIAER----RETIEEKRERAEELRERAAEL---EAEAEEKREAAAEAE 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 397 QKSVSAEERIQRLDRNIQELSAE---LERAVQRERMNEEHSQRLSSTVDKL--LSESNDRLQLHLKERM----------- 460
Cdd:PRK02224 565 EEAEEAREEVAELNSKLAELKERiesLERIRTLLAAIADAEDEIERLREKReaLAELNDERRERLAEKRerkreleaefd 644
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 17569509 461 -----QALDDKNRLTQQLDGTKKIYDQAERIKDRLQRDNESLRQEIEALR 505
Cdd:PRK02224 645 earieEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELE 694
|
|
| SAM |
smart00454 |
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ... |
959-1015 |
1.11e-08 |
|
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related tyrosine kinases, appears to mediate cell-cell initiated signal transduction via the binding of SH2-containing proteins to a conserved tyrosine that is phosphorylated. In many cases mediates homodimerisation.
Pssm-ID: 197735 Cd Length: 68 Bit Score: 52.68 E-value: 1.11e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 17569509 959 DWLPCLGLAQYRSAFMECLLDARMLEHLSKRDLRTHLRMVDTFHRTSLQYGIMCLKK 1015
Cdd:smart00454 11 DWLESIGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKLKE 67
|
|
| SAM_1 |
pfam00536 |
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ... |
950-1014 |
1.21e-08 |
|
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily conserved protein binding domain that is involved in the regulation of numerous developmental processes in diverse eukaryotes. The SAM domain can potentially function as a protein interaction module through its ability to homo- and heterooligomerise with other SAM domains.
Pssm-ID: 425739 Cd Length: 64 Bit Score: 52.27 E-value: 1.21e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17569509 950 DMNHEYIGNDWLPCLGLAQYRSAFMECLLDARMLEHLSKRDLRtHLRMVDTFHRTSLQYGIMCLK 1014
Cdd:pfam00536 1 DGWSVEDVGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDDLL-KLGVTLLGHRKKILYAIQRLK 64
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
36-579 |
1.62e-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: 58.98 E-value: 1.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 36 IEQLMMNMLEDRDKLQEQLENYKVQLENAGLRTKEVEKERDmmkrQFEVHTQNLPQELQTM-------TRELCLLKEQ-- 106
Cdd:pfam15921 326 VSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERD----QFSQESGNLDDQLQKLladlhkrEKELSLEKEQnk 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 107 -LLEKDE----EIVELKAERNNTRLLLEHLECLVsRHERSLRMTVMKRQAQNHAGVSSEVEVLKALKSLFEHHKALDEKV 181
Cdd:pfam15921 402 rLWDRDTgnsiTIDHLRRELDDRNMEVQRLEALL-KAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKV 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 182 RERL-----------RVAMERVATLEEE---LSTKGDENSSLKARIATYAAEAEEAMASNAPINGSISSESANRL----- 242
Cdd:pfam15921 481 VEELtakkmtlesseRTVSDLTASLQEKeraIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKLqmaek 560
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 243 ---IE-MQEALERMKTELANSLKQSTEITTRNAELEDQLTEDAREKHAAQESIVRLKNQICELDAQRTDQE---TRITTF 315
Cdd:pfam15921 561 dkvIEiLRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLElekVKLVNA 640
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 316 ESRFLTAQRESTCIRDlndklehQLANKdaaVRLNEEKVHSLQERLELAEKQLAQSLKKAES--------LPSVEAELQQ 387
Cdd:pfam15921 641 GSERLRAVKDIKQERD-------QLLNE---VKTSRNELNSLSEDYEVLKRNFRNKSEEMETttnklkmqLKSAQSELEQ 710
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 388 RMEALTAAE-------------QKSVSAEE-RIQRLDRNIQELSAELERAVQRERMNEEHSQRLSSTVDKLLSESNDRLQ 453
Cdd:pfam15921 711 TRNTLKSMEgsdghamkvamgmQKQITAKRgQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAG 790
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 454 LHLKERMQALDDKNRLTQQLDGTKKIYDQAERIKDRLQrdneslRQEIEALRQQLYNARTAQfqsRMHAIPFTHAQNIVQ 533
Cdd:pfam15921 791 ELEVLRSQERRLKEKVANMEVALDKASLQFAECQDIIQ------RQEQESVRLKLQHTLDVK---ELQGPGYTSNSSMKP 861
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 17569509 534 QQPQASIAQQSAYQMYKQQPAQQYQTVGMRRPNkgrisALQDDPNK 579
Cdd:pfam15921 862 RLLQPASFTRTHSNVPSSQSTASFLSHHSRKTN-----ALKEDPTR 902
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
329-507 |
1.93e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 58.77 E-value: 1.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 329 IRDLNDKLEHQLANKDAAVRL--------NEEKVHSLQERLELAEKQLAQslkkaeslpsVEAELQQRMEALTAAEQKSV 400
Cdd:COG4913 257 IRELAERYAAARERLAELEYLraalrlwfAQRRLELLEAELEELRAELAR----------LEAELERLEARLDALREELD 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 401 SAEERIQRLD-RNIQELSAELERAVQRERMNEEHSQRLSSTVDKL-LSESNDRLQLhLKERMQALDDKNRLTQQLDGTKK 478
Cdd:COG4913 327 ELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEALLAALgLPLPASAEEF-AALRAEAAALLEALEEELEALEE 405
|
170 180
....*....|....*....|....*....
gi 17569509 479 IYDQAERIKDRLQRDNESLRQEIEALRQQ 507
Cdd:COG4913 406 ALAEAEAALRDLRRELRELEAEIASLERR 434
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
33-508 |
2.04e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.79 E-value: 2.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 33 RDNIEQLmmnmLEDRDKLQEQLENYKVQLENAGLRTKEVEKERDMMKRQFEVHTQNLPQELQTMTRELCLLKEQLLEKDE 112
Cdd:COG1196 315 EERLEEL----EEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLE 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 113 EIVELKAERNNTRLLLEHLECLVSRHERSLRMTVMKRQAQNHAGV------SSEVEVLKALKSLFEHHKALDEKVRERLR 186
Cdd:COG1196 391 ALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEeeeeeeEALEEAAEEEAELEEEEEALLELLAELLE 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 187 VAMERVATLEEELSTKGDENSSLKARIATYAAEAEEAMASNAPINGSISSESANRLIEMQEALERMKTELANSL-KQSTE 265
Cdd:COG1196 471 EAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALaAALQN 550
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 266 ITTRNAELEDQLTEDAREKHAAQESIVRLkNQICELDAQRTDQETRITTFESRFLTAQRestciRDLNDKLEHQLANKDA 345
Cdd:COG1196 551 IVVEDDEVAAAAIEYLKAAKAGRATFLPL-DKIRARAALAAALARGAIGAAVDLVASDL-----READARYYVLGDTLLG 624
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 346 AVRLNEEKVHSLQERLELAEKQLAQSLKKAESLPSVEAELQQRMEALTAAEQKSVSAEERIQRLDRNIQELSAELERAVQ 425
Cdd:COG1196 625 RTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEE 704
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 426 RERMNEEHSQRLSStvdkllsesndRLQLHLKERMQALDDKNRLTQQLDGTKKIYDQAERIKDRLQRDNESLRQEIEALR 505
Cdd:COG1196 705 EERELAEAEEERLE-----------EELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLE 773
|
...
gi 17569509 506 QQL 508
Cdd:COG1196 774 REI 776
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
49-494 |
2.63e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 58.24 E-value: 2.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 49 KLQEQLENYKVQLENAGLRTKEVEKERDMMKRQfevhtqnlpQELQTMTRELCLLKEQLLEKDEEIVELKA---ERNNTR 125
Cdd:COG4717 92 ELQEELEELEEELEELEAELEELREELEKLEKL---------LQLLPLYQELEALEAELAELPERLEELEErleELRELE 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 126 LLLEHLECLVSRHERSLRMTVMKRQAQNHAGVSSEVEVLKALKSLFEHHKALDEKVRERLRVAMERVATLEEELSTKGDE 205
Cdd:COG4717 163 EELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 206 NSSLKARIATYAAEAEEAMASNAPINGSISSESANRLIEMQEALERMKTELANSLKQSTEittrnaELEDQLTEDAREKH 285
Cdd:COG4717 243 ERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGK------EAEELQALPALEEL 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 286 AAQEsivrLKNQICELDAQRTDQETRITTFESRFLTAQRESTCIRDLNDKLEHQLANKDAAVRLNEEKVHSLQERLELAE 365
Cdd:COG4717 317 EEEE----LEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALE 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 366 kQLAQSLKKAESLPSVEAELQQRMEALTA--AEQKSVSAEERIQRLDRNIQELSAELERAVQRERmneEHSQRLSSTvdk 443
Cdd:COG4717 393 -QAEEYQELKEELEELEEQLEELLGELEEllEALDEEELEEELEELEEELEELEEELEELREELA---ELEAELEQL--- 465
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 17569509 444 llsESNDRLQLHLKERMQALDDKNRLTQQLDGTKKIYDQAERIKDRLQRDN 494
Cdd:COG4717 466 ---EEDGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREER 513
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
350-519 |
3.65e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 58.00 E-value: 3.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 350 NEEKVHSLQERLELAEKQLAQSLKKAESLPSVEAELQQRMEALTAAEQKS------VSAEERIQRLDRNIQELSA----- 418
Cdd:COG4913 608 NRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSwdeidvASAEREIAELEAELERLDAssddl 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 419 -----ELERAVQRERMNEEHSQRLSSTVDKLLSESND--RLQLHLKERMQALDDKNRLTQQLDGTKK-----IYDQAERI 486
Cdd:COG4913 688 aaleeQLEELEAELEELEEELDELKGEIGRLEKELEQaeEELDELQDRLEAAEDLARLELRALLEERfaaalGDAVEREL 767
|
170 180 190
....*....|....*....|....*....|...
gi 17569509 487 KDRLQRDNESLRQEIEALRQQLYNARtAQFQSR 519
Cdd:COG4913 768 RENLEERIDALRARLNRAEEELERAM-RAFNRE 799
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
44-450 |
7.40e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 57.00 E-value: 7.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 44 LEDRDKLQEQLENYKVQLENAGLRTKEVEKER-------DMMKRQFEVHTQNLPQELQTMTRELCLLKEQLLEKDEEIVE 116
Cdd:TIGR02169 176 LEELEEVEENIERLDLIIDEKRQQLERLRRERekaeryqALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEK 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 117 LKAERNNTRLLLEHLECLVSRHERSLRMTVMKRQAQnhagVSSEVEVLKALKSLFEhhKALDEKVRErLRVAMERVATLE 196
Cdd:TIGR02169 256 LTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLR----VKEKIGELEAEIASLE--RSIAEKERE-LEDAEERLAKLE 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 197 EELSTKGDENSSLKARIAtyaaeaeeamasnapingsissESANRLIEMQEALERMKTELANSLKQSTEITTRNAELEDQ 276
Cdd:TIGR02169 329 AEIDKLLAEIEELEREIE----------------------EERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDE 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 277 LTEdarekhaAQESIVRLKNQICELdaqrtdqetrittfesrfltaQRESTCIRDLNDKLEHQLANKDAAVRLNEEKVHS 356
Cdd:TIGR02169 387 LKD-------YREKLEKLKREINEL---------------------KRELDRLQEELQRLSEELADLNAAIAGIEAKINE 438
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 357 LQERLELAEKQLAQSlkkaeslpsvEAELQQRMEALTAAEQKSVSAEERIQRLDRNIQELSAELERAVQRERMNEEhSQR 436
Cdd:TIGR02169 439 LEEEKEDKALEIKKQ----------EWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEE-RVR 507
|
410
....*....|....
gi 17569509 437 LSSTVDKLLSESND 450
Cdd:TIGR02169 508 GGRAVEEVLKASIQ 521
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
243-560 |
7.60e-08 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 56.90 E-value: 7.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 243 IEMQEALERMKTELANSLKQSTEITTRNAELEDQLTEDAREKHAAqesivRLKNQICELDAQRTD-QETRITtfeSRFLT 321
Cdd:TIGR00618 175 LDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHE-----RKQVLEKELKHLREAlQQTQQS---HAYLT 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 322 AQREStcirdLNDKLEHQLANKDAAVRlnEEKVHSLQERLELAEKQLAQSLKKAESLPSVEAELQQRMEALTAAEQKSVS 401
Cdd:TIGR00618 247 QKREA-----QEEQLKKQQLLKQLRAR--IEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSK 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 402 AEERIQRLDRNIQELSAELERAVQRERMNEEHSQ----RLSSTVDKLLSESNDRlQLHLKERMQAL-DDKNRLTQQLDGT 476
Cdd:TIGR00618 320 MRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQeihiRDAHEVATSIREISCQ-QHTLTQHIHTLqQQKTTLTQKLQSL 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 477 KKIYDQaeriKDRLQRDNESLRQEIEALRQQLYNARTA-QFQSRMHAIPFTHAQNIVQQQPQASIAQQSAYQMYKQQpAQ 555
Cdd:TIGR00618 399 CKELDI----LQREQATIDTRTSAFRDLQGQLAHAKKQqELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKER-EQ 473
|
....*
gi 17569509 556 QYQTV 560
Cdd:TIGR00618 474 QLQTK 478
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
244-519 |
8.33e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 56.61 E-value: 8.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 244 EMQEALERMKTELANSLKQStEITTRNAELEdqLTEDAREKHAAQESIVRLKNQICELDAQRTDQETRITTFESRFLTAQ 323
Cdd:TIGR02169 195 EKRQQLERLRREREKAERYQ-ALLKEKREYE--GYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIE 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 324 RE----STCIRDLND-----------KLEHQLANKDAAVRLNEEKVHSLQERLELAEKQLAQSLKKAESLPSVEAELQQR 388
Cdd:TIGR02169 272 QLleelNKKIKDLGEeeqlrvkekigELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKR 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 389 MEALTAAEQKSVSAEE----RIQRLDRNIQELSAELERAVQR-ERMNEEHSQrLSSTVDKLLSE----SNDRLQLH---- 455
Cdd:TIGR02169 352 RDKLTEEYAELKEELEdlraELEEVDKEFAETRDELKDYREKlEKLKREINE-LKRELDRLQEElqrlSEELADLNaaia 430
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17569509 456 --------LKERMQALDDK-NRLTQQLDGTKKIYDQAERIKDRLQRDNESLRQEIEALRQQLYNARTAQFQSR 519
Cdd:TIGR02169 431 gieakineLEEEKEDKALEiKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASE 503
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
272-508 |
1.03e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.46 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 272 ELEDQLtEDAREKHAAQESIVRLKNQICELDAQRTDQETRITTFesRFLTAQRESTCIRDLNDKLEHQLANKDAAVRLNE 351
Cdd:COG4913 239 RAHEAL-EDAREQIELLEPIRELAERYAAARERLAELEYLRAAL--RLWFAQRRLELLEAELEELRAELARLEAELERLE 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 352 EKVHSLQERLELAEKQLAQSlkKAESLPSVEAELQQRMEALTAAEQKSVSAEERIQRLDRNIQELSAELERAVQRermne 431
Cdd:COG4913 316 ARLDALREELDELEAQIRGN--GGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAE----- 388
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17569509 432 ehsqrlsstVDKLLSESNDRLQLHLKERMQALDDKNRLTQQLdgtkkiyDQAERIKDRLQRDNESLRQEIEALRQQL 508
Cdd:COG4913 389 ---------AAALLEALEEELEALEEALAEAEAALRDLRREL-------RELEAEIASLERRKSNIPARLLALRDAL 449
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
332-552 |
1.11e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 56.18 E-value: 1.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 332 LNDKLEHQLANKDAAVRLNEEKVHSLQERLELAEKQLAQsLKKAESLPSVEAELQQRMEALTAAEQKSVSAEERIQRLDR 411
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQLPELRKELEEAEAALEE-FRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEA 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 412 NIQELSAELERAVQrermnEEHSQRLSSTVDKLLSESNDrLQLHLKERMQALDDKN----RLTQQLDGTKK-IYDQAERI 486
Cdd:COG3206 241 RLAALRAQLGSGPD-----ALPELLQSPVIQQLRAQLAE-LEAELAELSARYTPNHpdviALRAQIAALRAqLQQEAQRI 314
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17569509 487 KDRLQRDNESLRQEIEALRQQLynartAQFQSRMHAIPfTHAQNIVQQQPQASIAQQsAYQMYKQQ 552
Cdd:COG3206 315 LASLEAELEALQAREASLQAQL-----AQLEARLAELP-ELEAELRRLEREVEVARE-LYESLLQR 373
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
275-520 |
2.27e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 54.38 E-value: 2.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 275 DQLTEDAREKHAAQESIVRLKNQICELDAQRTDQETRITTFESRFLTAQREstcirdlNDKLEHQLANKDAAVRLNEEKV 354
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARR-------IRALEQELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 355 HSLQERLELAEKQLAQSLKKAESL---PSVEAELQQrmEALTAAEQKSVSAEERIQRLDRNIQELSAELERAVQRERMNE 431
Cdd:COG4942 93 AELRAELEAQKEELAELLRALYRLgrqPPLALLLSP--EDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 432 EHSQRLSSTVDKLLSESNdRLQLHLKERMQALddkNRLTQQLDGTKKIYDQAERIKDRLQRDNESLRQEIEALRQQLYNA 511
Cdd:COG4942 171 AERAELEALLAELEEERA-ALEALKAERQKLL---ARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
|
....*....
gi 17569509 512 RTAQFQSRM 520
Cdd:COG4942 247 GFAALKGKL 255
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
244-523 |
3.05e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 55.07 E-value: 3.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 244 EMQEALERMKTELANSLKQSTEITTRNAELEDQLTEDAREKHAAQE-SIVRLKNQ---ICELDAQRTDQETRITTFESRF 319
Cdd:TIGR02169 167 EFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERyQALLKEKReyeGYELLKEKEALERQKEAIERQL 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 320 LTAQRESTCIRDLNDKLEHQLANKDAAVRLNEEKVHSLQERLELAEKQLAQSLK-KAESLPSVEAELQQRMEALTAAEQK 398
Cdd:TIGR02169 247 ASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEaEIASLERSIAEKERELEDAEERLAK 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 399 svsAEERIQRLDRNIQELSAELER-AVQRERMNEEhsqrlsstvdklLSESNDRLQLhLKERMQALDDKNRLT------- 470
Cdd:TIGR02169 327 ---LEAEIDKLLAEIEELEREIEEeRKRRDKLTEE------------YAELKEELED-LRAELEEVDKEFAETrdelkdy 390
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 17569509 471 -QQLDGTKKIYDQAERIKDRLQRDNESLRQEIEALRQQLYN--ARTAQFQSRMHAI 523
Cdd:TIGR02169 391 rEKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGieAKINELEEEKEDK 446
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
31-512 |
9.64e-07 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 53.10 E-value: 9.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 31 SDRDNIEQLMMNMLEDRDKLQEQLENYKVQLEnaglRTKEVEKERDMMKRQfevhTQNLPQELQTMTRELCLLKEQLLEK 110
Cdd:TIGR04523 180 KEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQ----KNKSLESQISELKKQ----NNQLKDNIEKKQQEINEKTTEISNT 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 111 DEEIVELKAERNNTRLLLEHLECLVSRHERSLrmTVMKRQAQNhagVSSEVEVLKA------LKSLFEHHKALDEKVRE- 183
Cdd:TIGR04523 252 QTQLNQLKDEQNKIKKQLSEKQKELEQNNKKI--KELEKQLNQ---LKSEISDLNNqkeqdwNKELKSELKNQEKKLEEi 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 184 ---------RLRVAMERVATLEEELSTKGDENSSLKARIATYAAEAEeamasnapingSISSESANRLIEMQEaLERMKT 254
Cdd:TIGR04523 327 qnqisqnnkIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIE-----------KLKKENQSYKQEIKN-LESQIN 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 255 ELANSLKQSTEIttrNAELEDQLTEDAREKHAAQESIVRLKNQICELDAQRTDQETRITTFEsrfltaqresTCIRDLND 334
Cdd:TIGR04523 395 DLESKIQNQEKL---NQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKE----------LIIKNLDN 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 335 KLEHQLANKDAAvrlnEEKVHSLQERLELAEKQLAQSLKKAESLPSVEAELQQRMEALTaaeQKSVSAEERIQRLDRNIQ 414
Cdd:TIGR04523 462 TRESLETQLKVL----SRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLT---KKISSLKEKIEKLESEKK 534
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 415 ELSAELERavQRERMNEEHSQRLSSTVDKLLSESNDRLQlHLKERMQALDDKNR-------------------------- 468
Cdd:TIGR04523 535 EKESKISD--LEDELNKDDFELKKENLEKEIDEKNKEIE-ELKQTQKSLKKKQEekqelidqkekekkdlikeieekekk 611
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 17569509 469 ---LTQQLDGTKKIYDQAERIKDRLQRDNESLRQEIEALRQQLYNAR 512
Cdd:TIGR04523 612 issLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIR 658
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
52-510 |
9.67e-07 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 53.43 E-value: 9.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 52 EQLENYKVQLENAGLRTKEVEKERDMMKRQFEVHTQNLPQE-------LQTMTRELCLLKE-------------QLLEKD 111
Cdd:TIGR00618 173 FPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMpdtyherKQVLEKELKHLREalqqtqqshayltQKREAQ 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 112 EEIVELKAERNNTRLLLEHLECLVSRHERSLRMTVMKRQAQNHAGVSSEVEVLKalKSLFEHHKALDEKVRERLRVAMER 191
Cdd:TIGR00618 253 EEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQIE--QQAQRIHTELQSKMRSRAKLLMKR 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 192 VATLEEELSTKGDENSSLKARIATYAAEAEEAMASNAPINGSISSESANRLIEMQEALERMKtELANSLKQSTEITTR-- 269
Cdd:TIGR00618 331 AAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLT-QKLQSLCKELDILQReq 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 270 -NAELEDQLTEDAREKHAAQESIVRLKNQICELDAQRTDQETRITTFESRFLTAQRESTcirdlnDKLEHQLANKDaAVR 348
Cdd:TIGR00618 410 aTIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSL------KEREQQLQTKE-QIH 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 349 LNEEKVHSLQERLELAEKQLAQSLKKAESLPSVEAEL-------QQRMEALTAAEQKSVSAEERI----QRLDRNIQELS 417
Cdd:TIGR00618 483 LQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDidnpgplTRRMQRGEQTYAQLETSEEDVyhqlTSERKQRASLK 562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 418 AELERAVQRERMNEEHSQRLSSTVDKLLSESnDRLQLHLKERMQALDDKNRLTQQLDGTKKIYDQAERIKDRLQRDNESL 497
Cdd:TIGR00618 563 EQMQEIQQSFSILTQCDNRSKEDIPNLQNIT-VRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQEL 641
|
490
....*....|...
gi 17569509 498 RQEIEALRQQLYN 510
Cdd:TIGR00618 642 ALKLTALHALQLT 654
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
237-606 |
1.69e-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: 52.37 E-value: 1.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 237 ESANRLIEMQEALERMKTELAnslkqsteittrnaELEDQLTEDAREKHAAQESIvRLKNQICELDAQrtdqetrittfe 316
Cdd:TIGR02168 176 ETERKLERTRENLDRLEDILN--------------ELERQLKSLERQAEKAERYK-ELKAELRELELA------------ 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 317 srfLTAQRestcIRDLNDKLEHQLANKDAAvrlnEEKVHSLQERLELAEKQLAQSLKKAESLPSVEAELQQRMEALTAae 396
Cdd:TIGR02168 229 ---LLVLR----LEELREELEELQEELKEA----EEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALAN-- 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 397 qksvsaeeRIQRLDRNIQELSAELERAVQRERMNEEHSQRLSSTVDKL---LSESNDRLQLhLKERMQALDDK-NRLTQQ 472
Cdd:TIGR02168 296 --------EISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELaeeLAELEEKLEE-LKEELESLEAElEELEAE 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 473 LDGTKKIYDQAERIKDRLQRDNESLRQEIEALRQQLYNART-----AQFQSRMHAIPFTHAQNIVQQQPQASIAQQSAYQ 547
Cdd:TIGR02168 367 LEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEArlerlEDRRERLQQEIEELLKKLEEAELKELQAELEELE 446
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 548 MYKQQPAQQYQTVGMRRPN-KGRISALQddpNKVQTLNEQEWDRLQQAHVLANVQQAFSS 606
Cdd:TIGR02168 447 EELEELQEELERLEEALEElREELEEAE---QALDAAERELAQLQARLDSLERLQENLEG 503
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
350-558 |
2.39e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 51.30 E-value: 2.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 350 NEEKVHSLQERLELAEKQLAQSLKKAESLPSVEAELQQRMEALTAAEQKsvsAEERIQRLDRNIQELSAELERAVQRErm 429
Cdd:COG4942 25 AEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRA---LEQELAALEAELAELEKEIAELRAEL-- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 430 nEEHSQRLSSTVDKL-LSESNDRLQLHLK-ERMQALDDKNRLTQQLdgTKKIYDQAERIKDRLQRDNEsLRQEIEALRQQ 507
Cdd:COG4942 100 -EAQKEELAELLRALyRLGRQPPLALLLSpEDFLDAVRRLQYLKYL--APARREQAEELRADLAELAA-LRAELEAERAE 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 17569509 508 LYNARTAQFQSRMHAIPFTHAQNIVQQQPQASIAQQSAYQMYKQQPAQQYQ 558
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELE 226
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
238-514 |
2.73e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.60 E-value: 2.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 238 SANRLIEMQEALERMKTELANSLKQSTEITTRNAELEDQLTEDAREkhaaqesIVRLKNQICELDAQRTDQETRITTFES 317
Cdd:PRK03918 163 AYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLRE-------INEISSELPELREELEKLEKEVKELEE 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 318 rfltaqrestcIRDLNDKLEHQLANKDAAVRLNEEKVHSLQERLELAEKQLAQSLKKAESLPSVE--AELQQRMEAL-TA 394
Cdd:PRK03918 236 -----------LKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKekAEEYIKLSEFyEE 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 395 AEQKSVSAEERIQRLDRNIQELSAELERAVQRERMNEEHSQRLSSTVDKLlSESNDRLQLhLKERMQALDDKNRLTQQLD 474
Cdd:PRK03918 305 YLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRL-EELEERHEL-YEEAKAKKEELERLKKRLT 382
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 17569509 475 G-----TKKIYDQAERIKDRLQRDNESLRQEIEALRQQLYNARTA 514
Cdd:PRK03918 383 GltpekLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKA 427
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
32-508 |
3.58e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 51.26 E-value: 3.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 32 DRDNIEQLMMNMLEDRDKLQEQLENYKVQLENAGLRTKEVEKERDMMKRQFEvhtQNLPQELQTMTRELCLLKEQLLEKD 111
Cdd:pfam05483 177 EREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHFKLKEDHEKIQHLE---EEYKKEINDKEKQVSLLLIQITEKE 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 112 EEIVELKAERNNTRLLLEHLECLVSRHERSLRMTVMKrqaQNHagVSSEVEVLK-ALKSLFEHHKALDEKvrerLRVAME 190
Cdd:pfam05483 254 NKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEK---KDH--LTKELEDIKmSLQRSMSTQKALEED----LQIATK 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 191 RVATLEEELSTKGDENSSLKAriaTYAAEAEEAMASNAPINGSISSESaNRLIEMQEALERMKTELANSLKQSTEIT--T 268
Cdd:pfam05483 325 TICQLTEEKEAQMEELNKAKA---AHSFVVTEFEATTCSLEELLRTEQ-QRLEKNEDQLKIITMELQKKSSELEEMTkfK 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 269 RNAELEdqlTEDAREKHAAQESIVRLKNQICELDAQRTDQETRITtfesrFLTAQRESTcIRDLNDKL-------EHQLA 341
Cdd:pfam05483 401 NNKEVE---LEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELI-----FLLQAREKE-IHDLEIQLtaiktseEHYLK 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 342 N-KDAAVRLNEEKVHSLQ-----ERLELAEKQLAQSLKkaeslpSVEAELQQRMEALTAAEQKsvsaEERIQRLDRNIQE 415
Cdd:pfam05483 472 EvEDLKTELEKEKLKNIEltahcDKLLLENKELTQEAS------DMTLELKKHQEDIINCKKQ----EERMLKQIENLEE 541
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 416 LSAELERAVqrERMNEEHSQRlSSTVDKLLSESNDRLQLHLKERMQALDDKNRLTQQLDGTKKIYDQAERIKDRLQRDNE 495
Cdd:pfam05483 542 KEMNLRDEL--ESVREEFIQK-GDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENK 618
|
490
....*....|...
gi 17569509 496 SLRQEIEALRQQL 508
Cdd:pfam05483 619 ALKKKGSAENKQL 631
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
249-440 |
5.08e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.54 E-value: 5.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 249 LERMKTELANSLKQSTEITTRNAELEDQLTEDAREKHAAQESIVRLKNQICELDAQRTDQETRITTFESRFLTAQRESTC 328
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 329 IRDLND--KLEHQLANKDAAVRLNEEKV---HSLQERLELAEKQLAQSLKKAESL-----PSVEAELQQRMEALTAAEQK 398
Cdd:COG4717 128 LPLYQEleALEAELAELPERLEELEERLeelRELEEELEELEAELAELQEELEELleqlsLATEEELQDLAEELEELQQR 207
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 17569509 399 SVSAEERIQRLDRNIQELSAELERaVQRERMNEEHSQRLSST 440
Cdd:COG4717 208 LAELEEELEEAQEELEELEEELEQ-LENELEAAALEERLKEA 248
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
232-485 |
5.25e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.15 E-value: 5.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 232 GSISSESANRLIEMQEALERMKTELANSLKQSTEITTRNAELEDQLTEdarekhaAQESIVRLKNQICELDAQRTDQETR 311
Cdd:COG4942 12 ALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAA-------LERRIAALARRIRALEQELAALEAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 312 ITTFESRFLTAQREstcIRDLNDKLEHQLAnkdAAVRLNEEKvhslQERLELAEKQLAQSLKKAESLPSVEAELQQRMEA 391
Cdd:COG4942 85 LAELEKEIAELRAE---LEAQKEELAELLR---ALYRLGRQP----PLALLLSPEDFLDAVRRLQYLKYLAPARREQAEE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 392 LTAAEQKSVSAEERIQRLDRNIQELSAELERavQRERMNEEHSQRlsstvDKLLSESNDRLQLHLKERMQALDDKNRLTQ 471
Cdd:COG4942 155 LRADLAELAALRAELEAERAELEALLAELEE--ERAALEALKAER-----QKLLARLEKELAELAAELAELQQEAEELEA 227
|
250
....*....|....
gi 17569509 472 QLDGTKKIYDQAER 485
Cdd:COG4942 228 LIARLEAEAAAAAE 241
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
246-558 |
5.73e-06 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 50.72 E-value: 5.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 246 QEALERMKT---ELANSLKQSTEITtrnAELEDQLTEDAREKHAAQESIVRLKNQICELDAQRTDQETRITTFEsRFLTA 322
Cdd:COG3096 346 QEKIERYQEdleELTERLEEQEEVV---EEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDVQQTRAIQYQ-QAVQA 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 323 QRESTCIRDLNDKLEHQLANKDAAVRLNEEKVHS----LQERLELAEKQLAQSLKKAESLPSVEAEL------QQRMEAL 392
Cdd:COG3096 422 LEKARALCGLPDLTPENAEDYLAAFRAKEQQATEevleLEQKLSVADAARRQFEKAYELVCKIAGEVersqawQTARELL 501
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 393 -TAAEQKSVSaeERIQRLDRNIQELSAELERAVQRERMNEEHSQRLSSTVDkllseSNDRLQLHLKERMQALDDknrLTQ 471
Cdd:COG3096 502 rRYRSQQALA--QRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLD-----AAEELEELLAELEAQLEE---LEE 571
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 472 QLdgtkkiydqAERIKDR--LQRDNESLRQEIEALRQQLYNARTAqfQSRMHAI------PFTHAQNiVQQQPQASIAQQ 543
Cdd:COG3096 572 QA---------AEAVEQRseLRQQLEQLRARIKELAARAPAWLAA--QDALERLreqsgeALADSQE-VTAAMQQLLERE 639
|
330
....*....|....*
gi 17569509 544 SAYQMYKQQPAQQYQ 558
Cdd:COG3096 640 REATVERDELAARKQ 654
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
344-616 |
5.82e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.83 E-value: 5.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 344 DAAVRLNEEKVHSLQERLELAEKQLAQSLKKAESLPSVEAELQQRMEaltAAEQKSVSAEERIQRLDRNIQELSAELE-- 421
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELE---ALQAEIDKLQAEIAEAEAEIEERREELGer 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 422 -RAVQRermneehSQRLSSTVDKLLSESN-----DRLQLhlkeRMQALDDKNRLTQQLDGTKKIYDQAERIKDRLQRDNE 495
Cdd:COG3883 92 aRALYR-------SGGSVSYLDVLLGSESfsdflDRLSA----LSKIADADADLLEELKADKAELEAKKAELEAKLAELE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 496 SLRQEIEALRQQLyNARTAQFQSRMHAIPFTHAQNIVQQQPQASIAQQSAYQMYKQQPAQQYQTVGMRRPNKGRISALQD 575
Cdd:COG3883 161 ALKAELEAAKAEL-EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 239
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 17569509 576 DPNKVQTLNEQEWDRLQQAHVLANVQQAFSSSPSLADVGQS 616
Cdd:COG3883 240 AAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAAAS 280
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
231-424 |
6.08e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 50.40 E-value: 6.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 231 NGSISSESANRLIEMQeaLERMKTELANSLKQSTEITTRNAELEDQLTEDAREKHAAQES--IVRLKNQICELDAQRTDQ 308
Cdd:COG3206 205 NGLVDLSEEAKLLLQQ--LSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSpvIQQLRAQLAELEAELAEL 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 309 ETRITTFESRFLTAQREstcIRDLNDKLEHQLANKDAAVRLNEEkvhSLQERLELAEKQLAQSLKKAESLPSVEAELQQR 388
Cdd:COG3206 283 SARYTPNHPDVIALRAQ---IAALRAQLQQEAQRILASLEAELE---ALQAREASLQAQLAQLEARLAELPELEAELRRL 356
|
170 180 190
....*....|....*....|....*....|....*....
gi 17569509 389 MEALTAAEQKSVSAEERIQ--RLDRNIQELSAE-LERAV 424
Cdd:COG3206 357 EREVEVARELYESLLQRLEeaRLAEALTVGNVRvIDPAV 395
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
132-508 |
6.69e-06 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 49.89 E-value: 6.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 132 ECLVSRHErslrmtVMKRQAQNHAGVSSEVEVLKALKSLFEH-HKALDEKV---RERLRVAMERVATLEEELSTKGDENS 207
Cdd:pfam07888 38 ECLQERAE------LLQAQEAANRQREKEKERYKRDREQWERqRRELESRVaelKEELRQSREKHEELEEKYKELSASSE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 208 SLKARIATYAAEAEEAMASNAPINGSISSESaNRLIEMQEALERMKTELANSLKQSTEITTRNAELEDQLTEDAREKHAA 287
Cdd:pfam07888 112 ELSEEKDALLAQRAAHEARIRELEEDIKTLT-QRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSL 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 288 QESIVRLKNQICELDAQRTDQETRITTFESRFLTAQRestcirdlndklehqlanKDAAVRLNEEKVHSLQERLELAEKQ 367
Cdd:pfam07888 191 SKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHR------------------KEAENEALLEELRSLQERLNASERK 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 368 LAQSLKKAESLPS----VEAELQQ-RMEA-----------LTAAEQKSVSAEERiQRLDRN-------IQELSAELERAv 424
Cdd:pfam07888 253 VEGLGEELSSMAAqrdrTQAELHQaRLQAaqltlqladasLALREGRARWAQER-ETLQQSaeadkdrIEKLSAELQRL- 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 425 qRERMNEEHSQRLSSTVDKLLSESNDRLQLHLKER-MQALDDKNRLTQqldgtkkiydqaeRIKDRLQRDNESLRQEIEA 503
Cdd:pfam07888 331 -EERLQEERMEREKLEVELGREKDCNRVQLSESRReLQELKASLRVAQ-------------KEKEQLQAEKQELLEYIRQ 396
|
....*
gi 17569509 504 LRQQL 508
Cdd:pfam07888 397 LEQRL 401
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
33-507 |
7.38e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 50.40 E-value: 7.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 33 RDNIEQlmmNMLEDRDKLQEQLENYKVQLENagLRTKEVEKERDmmKRQFEVHTQNLPQELQTMTRELCLLKEQLLEKDE 112
Cdd:TIGR04523 31 QDTEEK---QLEKKLKTIKNELKNKEKELKN--LDKNLNKDEEK--INNSNNKIKILEQQIKDLNDKLKKNKDKINKLNS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 113 EIVELKAERNNTRLLLEHLECLVSRHERSLR---------MTVMKRQAQNHAGVSS-------EVEVLKALKSLFEHHKA 176
Cdd:TIGR04523 104 DLSKINSEIKNDKEQKNKLEVELNKLEKQKKenkknidkfLTEIKKKEKELEKLNNkyndlkkQKEELENELNLLEKEKL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 177 LDEKVRERLRVAMERVATLEEELSTKGDENSSLKARIATYAAEAEEAMASNAPINGSIS------SESANRLIEMQEALE 250
Cdd:TIGR04523 184 NIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINektteiSNTQTQLNQLKDEQN 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 251 RMKTELANSLKQSTEITTRNAELEDQLTE-----DAREKHAAQESIVRLKNQICELDAQRTDQETRITTFESRfltaqre 325
Cdd:TIGR04523 264 KIKKQLSEKQKELEQNNKKIKELEKQLNQlkseiSDLNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKI------- 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 326 stcIRDLND---KLEHQLANKDAAvrlNEEKVHSLQER---LELAEKQLAQSLKKAESLPSVEAELQQRMEaltAAEQKS 399
Cdd:TIGR04523 337 ---ISQLNEqisQLKKELTNSESE---NSEKQRELEEKqneIEKLKKENQSYKQEIKNLESQINDLESKIQ---NQEKLN 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 400 VSAEERIQRLDRNIQELSAELERAVQRERMNEEHSQRLSS--TVDKLLSESNDRLQLHLKERMQALDDK-NRLTQQLDGT 476
Cdd:TIGR04523 408 QQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNqdSVKELIIKNLDNTRESLETQLKVLSRSiNKIKQNLEQK 487
|
490 500 510
....*....|....*....|....*....|.
gi 17569509 477 KKIYDQAERIKDRLQRDNESLRQEIEALRQQ 507
Cdd:TIGR04523 488 QKELKSKEKELKKLNEEKKELEEKVKDLTKK 518
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
12-515 |
8.12e-06 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 50.22 E-value: 8.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 12 IMPTISEDGVdngGPIDEPSDRDNIEqlmmNMLEDRDKLQ---------EQLENYKVQLENAGLRTKEVEKERdmmkRQF 82
Cdd:pfam12128 202 IVAILEDDGV---VPPKSRLNRQQVE----HWIRDIQAIAgimkirpefTKLQQEFNTLESAELRLSHLHFGY----KSD 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 83 EVHTQNLPQELQTMTRELcllKEQLLEKDEEIVELKAERNNTRLLL--------EHLECLVSRHERSLRMTVMKRQA--Q 152
Cdd:pfam12128 271 ETLIASRQEERQETSAEL---NQLLRTLDDQWKEKRDELNGELSAAdaavakdrSELEALEDQHGAFLDADIETAAAdqE 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 153 NHAGVSSEVEVL-KALKSLFEHHKALDEKVRERLRVAMER----VATLEEELSTKGDENSSLKARIATYAAEAEEAMASN 227
Cdd:pfam12128 348 QLPSWQSELENLeERLKALTGKHQDVTAKYNRRRSKIKEQnnrdIAGIKDKLAKIREARDRQLAVAEDDLQALESELREQ 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 228 APINGSISSESANRLIEmqeALERMKTELANSlkQSTEITTRNAELEDQLTEDAREKH-AAQESIVRLKNQICELDAQRT 306
Cdd:pfam12128 428 LEAGKLEFNEEEYRLKS---RLGELKLRLNQA--TATPELLLQLENFDERIERAREEQeAANAEVERLQSELRQARKRRD 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 307 DQETRITTFESRFLtaQRESTCirdlnDKLEHQLA----------NKDAAV-RLNEEKVHS--LQERLELAEKQLAQSLK 373
Cdd:pfam12128 503 QASEALRQASRRLE--ERQSAL-----DELELQLFpqagtllhflRKEAPDwEQSIGKVISpeLLHRTDLDPEVWDGSVG 575
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 374 KAESLPSV-------------------EAELQQRMEALTAAEQKSVSAEERIQRLDRNIQELSAELERAVQRERMNEEHS 434
Cdd:pfam12128 576 GELNLYGVkldlkridvpewaaseeelRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDL 655
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 435 QRLSSTVDKLlsesNDRLQLHLKERMQAlddKNRLTQQLDGTKKIYD-QAERIKDRLQRDNESLRQEIEALRQQLYNART 513
Cdd:pfam12128 656 RRLFDEKQSE----KDKKNKALAERKDS---ANERLNSLEAQLKQLDkKHQAWLEEQKEQKREARTEKQAYWQVVEGALD 728
|
..
gi 17569509 514 AQ 515
Cdd:pfam12128 729 AQ 730
|
|
| SAM_STIM-1,2-like |
cd09504 |
SAM domain of STIM-1,2-like proteins; SAM (sterile alpha motif) domain of STIM-1,2-like ... |
867-925 |
9.22e-06 |
|
SAM domain of STIM-1,2-like proteins; SAM (sterile alpha motif) domain of STIM-1,2-like (Stromal interaction molecule) proteins is a putative protein-protein interaction domain. STIM1 and STIM2 human proteins are type I transmembrane proteins. The N-terminal part of them includes "hidden" EF-hand and SAM domains. This region is responsible for sensing changes in store-operated and basal cytoplasmic Ca2+ levels and initiates oligomerization. "Hidden" EF hand and SAM domains have a stable intramolecular association, and the SAM domain is a component that regulates stability within STIM proteins. Destabilization of the EF-SAM association during Ca2+ depletion leads to partial unfolding and aggregation (homooligomerization), thus activating the store-operated Ca2+ entry. Immunoprecipitation analysis indicates that STIM1 and STIM2 can form co-precipitable oligomeric associations in vivo. It was suggested that STIM1 and STIM2 are involved in opposite regulation of store operated channels in plasma membrane.
Pssm-ID: 188903 Cd Length: 74 Bit Score: 44.63 E-value: 9.22e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17569509 867 WNGPTVVAWLELWVGMPAwYVAACRANVKSGAIMSALSDQE---IQKEIGISNPLHRLKLRL 925
Cdd:cd09504 5 WTVEDTVEWLVNSVELPQ-YVEAFKENGVDGSALPRLAVNNpsfLTSVLGIKDPIHRQKLSL 65
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
13-420 |
9.24e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 50.07 E-value: 9.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 13 MPTISEDGVDNGGPIDEPSDRDNIEQLmmNMLEDRDKLQ---EQLENYKVQLENAGLRTKEVEKERDMMKRQFEVHTQNL 89
Cdd:TIGR02169 641 MVTLEGELFEKSGAMTGGSRAPRGGIL--FSRSEPAELQrlrERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKI 718
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 90 PQ---ELQTMTRELCLLKEQLLEKDEEIVELKAERNNTRLLLEHLECLVSRHERSLrmtvmkrqaqnhAGVSSEVEVLKA 166
Cdd:TIGR02169 719 GEiekEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDL------------HKLEEALNDLEA 786
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 167 --LKSLFEHHKALDEKVRERLRVAMERVATLEEELSTKGDENSSLKARIATYAAEAEEAMASNAPINGSISSESAnRLIE 244
Cdd:TIGR02169 787 rlSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNG-KKEE 865
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 245 MQEALERMKTELANSLKQSTEITTRNAELEDQLTEDAREKHAAQESIVRLKNQICELDAQRTDQETRITTFESRFLTAQR 324
Cdd:TIGR02169 866 LEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEE 945
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 325 ESTCIRDLnDKLEHQLANKDAAVRLNEEKVHSLQERLELAEKQLAQSLKKAESLPSVEAELQQRMEALTaaEQKSVSAEE 404
Cdd:TIGR02169 946 IPEEELSL-EDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYE--KKKREVFME 1022
|
410
....*....|....*.
gi 17569509 405 RIQRLDRNIQELSAEL 420
Cdd:TIGR02169 1023 AFEAINENFNEIFAEL 1038
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
49-504 |
1.50e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 49.40 E-value: 1.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 49 KLQEQLENYKVQLENAGLRTKEVEKERDMMKRQFEVHTQNLPQELQTMTRELCLLKEQLLEKDEEIV-------ELKAER 121
Cdd:pfam01576 180 KLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQaalarleEETAQK 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 122 NNTRLLLEHLECLVSRHERSLRMtvmKRQAQNHA-----GVSSEVEVLKA-LKSLFEHHKALDEKVRERLRVAMERVATL 195
Cdd:pfam01576 260 NNALKKIRELEAQISELQEDLES---ERAARNKAekqrrDLGEELEALKTeLEDTLDTTAAQQELRSKREQEVTELKKAL 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 196 EEElsTKGDENSSLKARIATYAAEAEEAMASNAPINGSISSESANRLIEMQEALERMKTELANSLKQSTEITTRNA---- 271
Cdd:pfam01576 337 EEE--TRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLegql 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 272 -ELEDQLTEDAREKHAAQESIVRLKNQICELDAQRTDQETR-------ITTFESRFLTAQRE-----------STCIRDL 332
Cdd:pfam01576 415 qELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKniklskdVSSLESQLQDTQELlqeetrqklnlSTRLRQL 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 333 NDK---LEHQLANKDAAVRLNEEKVHSLQERLELAEKQLAQSLKKAESLPSVEAELQQRMEALTAAEQKSVSAEERIQRL 409
Cdd:pfam01576 495 EDErnsLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKT 574
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 410 DRNIQELSAELERAVQRERMNEEHSQRLSSTVDKLLSESNDRLQLHLKERMQA-LDDKNRLTQQLDGTKKIyDQAERIKD 488
Cdd:pfam01576 575 KNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAeAEAREKETRALSLARAL-EEALEAKE 653
|
490
....*....|....*.
gi 17569509 489 RLQRDNESLRQEIEAL 504
Cdd:pfam01576 654 ELERTNKQLRAEMEDL 669
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
237-503 |
1.59e-05 |
|
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: 48.97 E-value: 1.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 237 ESANRLIEMQEALERMKTEL----------ANSLKQSTEITT-RNAELEDQLT-----EDAREKhAAQESIVRLKNQICE 300
Cdd:pfam05557 6 ESKARLSQLQNEKKQMELEHkrarielekkASALKRQLDRESdRNQELQKRIRllekrEAEAEE-ALREQAELNRLKKKY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 301 LDAQRTDQETRittfESRFLTAQRESTCIRDLNDKLEHQLANKDAAVRLNEEKVHSLQERLELAEKQLaqslkkaeslps 380
Cdd:pfam05557 85 LEALNKKLNEK----ESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKA------------ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 381 veAELQQRMEALTAAEQKSVSAEERIQRLdrnIQELSAELERAVQRERMNEEHSQrlsstVDKLLSESnDRLQLHLKERM 460
Cdd:pfam05557 149 --SEAEQLRQNLEKQQSSLAEAEQRIKEL---EFEIQSQEQDSEIVKNSKSELAR-----IPELEKEL-ERLREHNKHLN 217
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 17569509 461 QALDDKNRLTQQLDGTKKIYDQAERIKDR---LQRDNESLRQEIEA 503
Cdd:pfam05557 218 ENIENKLLLKEEVEDLKRKLEREEKYREEaatLELEKEKLEQELQS 263
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
246-512 |
1.71e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 49.27 E-value: 1.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 246 QEALERMKTELANslKQSTEITTRNAELEDQLTEdarekhaAQESIVRLKNQICELDAQRTDQETRITTFESRFLTAQRE 325
Cdd:PRK02224 186 RGSLDQLKAQIEE--KEEKDLHERLNGLESELAE-------LDEEIERYEEQREQARETRDEADEVLEEHEERREELETL 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 326 STCIRDLNDKLEHQLANKDAAvrlnEEKVHSLQERLELAEKQLAQSLKKAEsLPSVEAE-LQQRMEALTAAEqksVSAEE 404
Cdd:PRK02224 257 EAEIEDLRETIAETEREREEL----AEEVRDLRERLEELEEERDDLLAEAG-LDDADAEaVEARREELEDRD---EELRD 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 405 RIQRLDRNIQELSAELERAVQRERMNEEHSQRLSSTVDKLLSE-SNDRLQLH-LKERMQALDDKNR-LTQQLDGTKKIYD 481
Cdd:PRK02224 329 RLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESElEEAREAVEdRREEIEELEEEIEeLRERFGDAPVDLG 408
|
250 260 270
....*....|....*....|....*....|.
gi 17569509 482 QAERIKDRLQRDNESLRQEIEALRQQLYNAR 512
Cdd:PRK02224 409 NAEDFLEELREERDELREREAELEATLRTAR 439
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
237-426 |
1.75e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 47.61 E-value: 1.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 237 ESANRLIEMQEALermkTELANSLKQSTEITTRNAELEDQLTEDAREKHAAQESIVRLKNQICELDAQRTDQETRITTFE 316
Cdd:COG1579 4 EDLRALLDLQELD----SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 317 SRFLTAQREstciRDLNDkLEHQLANKDAAVRLNEEKVHSLQERLELAEKQLAQslkkaeslpsVEAELQQRMEALTAAE 396
Cdd:COG1579 80 EQLGNVRNN----KEYEA-LQKEIESLKRRISDLEDEILELMERIEELEEELAE----------LEAELAELEAELEEKK 144
|
170 180 190
....*....|....*....|....*....|
gi 17569509 397 QKsvsAEERIQRLDRNIQELSAELERAVQR 426
Cdd:COG1579 145 AE---LDEELAELEAELEELEAEREELAAK 171
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
28-362 |
1.78e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.88 E-value: 1.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 28 DEPSDRDNIEQLMMNMLEDRDKLQEQLENYKVQLENAGLRTKEVEKERDMMKrqfeVHTQNLPQELQTMTRELCLLKEQL 107
Cdd:PRK02224 402 DAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGK----CPECGQPVEGSPHVETIEEDRERV 477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 108 LEKDEEIVELKAERNNTRLLLEHLECLV---SRHERSL--RMTVMKRQAQNHAGVSSEVEVLKALKSLFEHHKALDEKVR 182
Cdd:PRK02224 478 EELEAELEDLEEEVEEVEERLERAEDLVeaeDRIERLEerREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKR 557
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 183 ERLRVAMERVATLEEELSTKGDENSSLKARIATYAAEAEEAMASNApingsiSSESANRLIEMQEALERMKTELANSLKQ 262
Cdd:PRK02224 558 EAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAAIAD------AEDEIERLREKREALAELNDERRERLAE 631
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 263 STEittRNAELEDQLTED----AREKHA-AQESIVRLKNQICELDAQRTDQETRITTFESrfltaqrESTCIRDLNDKLE 337
Cdd:PRK02224 632 KRE---RKRELEAEFDEArieeAREDKErAEEYLEQVEEKLDELREERDDLQAEIGAVEN-------ELEELEELRERRE 701
|
330 340
....*....|....*....|....*
gi 17569509 338 HqLANKDAAVrlneEKVHSLQERLE 362
Cdd:PRK02224 702 A-LENRVEAL----EALYDEAEELE 721
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
45-511 |
1.89e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.91 E-value: 1.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 45 EDRDKLQEQ---LENYKVQLENAGLRTKEVEKERDMMKRqFEVHTQNLpqelqtmtrelcllKEQLLEKDEEIVELKAER 121
Cdd:PRK03918 145 ESREKVVRQilgLDDYENAYKNLGEVIKEIKRRIERLEK-FIKRTENI--------------EELIKEKEKELEEVLREI 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 122 NNTRLLLEHLECLVSrherslrmtvmkrqaqnhaGVSSEVEVLKALKSLFEHHKALDEKVRERLRVAMERVATLEEELST 201
Cdd:PRK03918 210 NEISSELPELREELE-------------------KLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEE 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 202 KGDENSSLKARIATYAAEAeeamasnapingsissESANRLIEMQEALERMKTELANSLKQSTEITTRNAELEDQLTE-- 279
Cdd:PRK03918 271 LKKEIEELEEKVKELKELK----------------EKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKEle 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 280 -DAREKHAAQESIVRLKNQICELDAQ-RTDQETRITTFESRFLTAQRESTCIRDLNDKLEhQLANKDAAVRLNEEKVHSL 357
Cdd:PRK03918 335 eKEERLEELKKKLKELEKRLEELEERhELYEEAKAKKEELERLKKRLTGLTPEKLEKELE-ELEKAKEEIEEEISKITAR 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 358 QERLELAEKQLAQS---LKKAESL-PSVEAEL--QQRMEALTAAEQKSVSAEERIQRLDRNIQELSAELERaVQRERMNE 431
Cdd:PRK03918 414 IGELKKEIKELKKAieeLKKAKGKcPVCGRELteEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRE-LEKVLKKE 492
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 432 EHSQRLSSTVDKLLSESNDRLQLHLKERMQALDDKNRLTQQLDGTKKiydQAERIKDRLQRDNEsLRQEIEALRQQLYNA 511
Cdd:PRK03918 493 SELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKG---EIKSLKKELEKLEE-LKKKLAELEKKLDEL 568
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
329-593 |
2.44e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.97 E-value: 2.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 329 IRDLNDKLEHQLANKDAAVRLNEEKVHSLQERLELAEKQLAQslkkaeslpsVEAELQQRMEALTAAEQKSVSAEERIQR 408
Cdd:COG4372 15 LFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQ----------AREELEQLEEELEQARSELEQLEEELEE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 409 LDRNIQELSAELERAVQRERMNEEHSQRLSSTVDKLLsesndrlqlhlKERMQALDDKNRLTQQLDGTKKIYDQAERIKD 488
Cdd:COG4372 85 LNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQ-----------KERQDLEQQRKQLEAQIAELQSEIAEREEELK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 489 RLQRDNESLRQEIEALRQQLYNARTAQFQSRMHAIPFTHAQNIVQQQPQASIAQQSAYQMYKQQPAQQYQTVGMRRPNKG 568
Cdd:COG4372 154 ELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGL 233
|
250 260
....*....|....*....|....*
gi 17569509 569 RISALQDDPNKVQTLNEQEWDRLQQ 593
Cdd:COG4372 234 ALSALLDALELEEDKEELLEEVILK 258
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
239-426 |
2.59e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.47 E-value: 2.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 239 ANRLIE--MQEALERMKTELANSL----KQSTEITTRNAELEDQLtEDAREKH----------AAQESIVRLKNQICELD 302
Cdd:COG3206 154 ANALAEayLEQNLELRREEARKALefleEQLPELRKELEEAEAAL-EEFRQKNglvdlseeakLLLQQLSELESQLAEAR 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 303 AQRTDQETRITTFESRF------LTAQRESTCIRDLNDK---LEHQLANKDAAVRLNEEKVHSLQERLELAEKQLAQSLK 373
Cdd:COG3206 233 AELAEAEARLAALRAQLgsgpdaLPELLQSPVIQQLRAQlaeLEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQ 312
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17569509 374 K--------AESLPSVEAELQQRMEALTAAEQKSVSAEERIQRLDRNIQELSAELERAVQR 426
Cdd:COG3206 313 RilasleaeLEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQR 373
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
332-515 |
2.61e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.23 E-value: 2.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 332 LNDKLEHQLANKDAAVRLNEEKVHSLQERLELAEKQLAQsLKKAESLPSVEAELQQRMEALTAAEQKSVSAEERIQRLDR 411
Cdd:COG4717 68 LNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEE-LEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 412 NIQELSAELERAVQRERMNEEHSQRLSSTVDKLLSESNDRLQLHLKERMQALDDKNRLTQQLDgtkkiydQAERIKDRLQ 491
Cdd:COG4717 147 RLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLA-------ELEEELEEAQ 219
|
170 180
....*....|....*....|....
gi 17569509 492 RDNESLRQEIEALRQQLYNARTAQ 515
Cdd:COG4717 220 EELEELEEELEQLENELEAAALEE 243
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
354-514 |
4.01e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 46.46 E-value: 4.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 354 VHSLQERL-ELAE--KQLAQSLKKAESLPSVEAELQQRMEA----LTAAEQKSVSAEERIQRLDRNIQELSAELERAvqR 426
Cdd:COG1579 2 MPEDLRALlDLQEldSELDRLEHRLKELPAELAELEDELAAlearLEAAKTELEDLEKEIKRLELEIEEVEARIKKY--E 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 427 ERMNEEHSQRLSSTVDKLLSESNDRLQLHLKERMQALDDKNRLTQQLDGTKKIYDQAERIKDRLQRDNESLRQEIEALRQ 506
Cdd:COG1579 80 EQLGNVRNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELE 159
|
....*...
gi 17569509 507 QLYNARTA 514
Cdd:COG1579 160 ELEAEREE 167
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
47-511 |
5.17e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.45 E-value: 5.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 47 RDKLQEQLENYKVQLENAGLRTKEVEKERDMMKRQFEVHTQNLPQELQTMTRELCLLKEQLLEKDEEIVELKAERNNTRL 126
Cdd:COG4717 44 RAMLLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 127 LLEHLeclvsrherslrmtvmkrqaqnhagvssevEVLKALKSLFEHHKALDEKVrERLRVAMERVATLEEELSTKGDEN 206
Cdd:COG4717 124 LLQLL------------------------------PLYQELEALEAELAELPERL-EELEERLEELRELEEELEELEAEL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 207 SSLKARIATYAAEAEEAMASNApingsisSESANRLIEMQEALERMKTELANSLKQSTEITTRNAELEDQL-TEDAREKH 285
Cdd:COG4717 173 AELQEELEELLEQLSLATEEEL-------QDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELeAAALEERL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 286 AAQESIVRLKNQICELDAQRTDQETRITTFESRFLTAQRESTCIRDLNDKLEHQLANKDAAV-------RLNEEKVHSLQ 358
Cdd:COG4717 246 KEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELqalpaleELEEEELEELL 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 359 ERLELAEkqlAQSLKKAESLPSVEAELQQRMEALTAAEQK---SVSAEERIQRLDRNIQELSAELERAVQRERMNEEHSQ 435
Cdd:COG4717 326 AALGLPP---DLSPEELLELLDRIEELQELLREAEELEEElqlEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKE 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 436 RLSSTVDKLLSESNDRLQLH-------LKERMQALDDK-NRLTQQLDGTKKIYDQAERIKDRLQRDNE--SLRQEIEALR 505
Cdd:COG4717 403 ELEELEEQLEELLGELEELLealdeeeLEEELEELEEElEELEEELEELREELAELEAELEQLEEDGElaELLQELEELK 482
|
....*.
gi 17569509 506 QQLYNA 511
Cdd:COG4717 483 AELREL 488
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
323-508 |
5.47e-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: 47.37 E-value: 5.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 323 QRESTCIRDLNDKLEHQLANKDAAVRLNEEKVHSLQERLELAEKQLAQSLKKAESLpsvEAELQQRMEALTAAEQKSVSA 402
Cdd:TIGR02169 687 KRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEEL---EEDLSSLEQEIENVKSELKEL 763
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 403 EERIQRLDRNIQELSAELERAVQRERMNE-EHSQRLSSTVDKLLSesndRLQLHLKERMQALDDKNRLTQQLDgtKKIYD 481
Cdd:TIGR02169 764 EARIEELEEDLHKLEEALNDLEARLSHSRiPEIQAELSKLEEEVS----RIEARLREIEQKLNRLTLEKEYLE--KEIQE 837
|
170 180
....*....|....*....|....*..
gi 17569509 482 QAERIKDrLQRDNESLRQEIEALRQQL 508
Cdd:TIGR02169 838 LQEQRID-LKEQIKSIEKEIENLNGKK 863
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
403-508 |
6.21e-05 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 46.50 E-value: 6.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 403 EERIQRLDRNIQELSAELEravqrerMNEEHSQRLSSTVDKLLSESNDrlQLHLKERMQALDDK-----NRLTQQLDGTK 477
Cdd:PRK09039 52 DSALDRLNSQIAELADLLS-------LERQGNQDLQDSVANLRASLSA--AEAERSRLQALLAElagagAAAEGRAGELA 122
|
90 100 110
....*....|....*....|....*....|.
gi 17569509 478 KIYDQAERIKDRLQRDNESLRQEIEALRQQL 508
Cdd:PRK09039 123 QELDSEKQVSARALAQVELLNQQIAALRRQL 153
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
262-506 |
6.46e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 47.26 E-value: 6.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 262 QSTEITTRNAELEDQL--TEDAREKHA-AQESIVRLKNQICELDAQRTDQETRITTFESRFLTAQREStcirdlndkLEH 338
Cdd:PRK04863 450 KEQEATEELLSLEQKLsvAQAAHSQFEqAYQLVRKIAGEVSRSEAWDVARELLRRLREQRHLAEQLQQ---------LRM 520
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 339 QLanKDAAVRLNEEKvhSLQERLELAEKQLAQSLKKAESLPSVEAELQQRMEALTaaEQKSVSAEERIQrLDRNIQELSA 418
Cdd:PRK04863 521 RL--SELEQRLRQQQ--RAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLS--ESVSEARERRMA-LRQQLEQLQA 593
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 419 ELERAVQRERMNEEHSQRLSstvdkllsesndRLQLHLKErmqALDDKNRLTQQLDGTKKIYDQAERIKDRLQRDNESLR 498
Cdd:PRK04863 594 RIQRLAARAPAWLAAQDALA------------RLREQSGE---EFEDSQDVTEYMQQLLERERELTVERDELAARKQALD 658
|
....*...
gi 17569509 499 QEIEALRQ 506
Cdd:PRK04863 659 EEIERLSQ 666
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
182-504 |
6.93e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.22 E-value: 6.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 182 RERLRVAMERVATLEEELSTKGDENSSLKARIATYAAEAEEAMASNAPINGSISSESANRLIEmqeALERMKTELANSLK 261
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIA---ELEAELERLDASSD 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 262 QSTEITTRNAELEDQLTEDAREKHAAQESIVRLKNQICELDAQRTDQETRITTFESRFLTAQREstcirDLNDKLEHQLA 341
Cdd:COG4913 686 DLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRA-----LLEERFAAALG 760
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 342 -NKDAAVRLN-EEKVHSLQERLELAEKQLAQSLKK---------------AESLPSVEAELQQ-RMEALTAAEQKsvsAE 403
Cdd:COG4913 761 dAVERELRENlEERIDALRARLNRAEEELERAMRAfnrewpaetadldadLESLPEYLALLDRlEEDGLPEYEER---FK 837
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 404 ERIQRL-DRNIQELSAELERAVQ--RERMNEehsqrlsstVDKLLSESN----DRLQLHLKER--------MQALDDKNR 468
Cdd:COG4913 838 ELLNENsIEFVADLLSKLRRAIReiKERIDP---------LNDSLKRIPfgpgRYLRLEARPRpdpevrefRQELRAVTS 908
|
330 340 350
....*....|....*....|....*....|....*....
gi 17569509 469 LTQQLDG--TKKIYDQAERIKDRLQ-RDNESLRQEIEAL 504
Cdd:COG4913 909 GASLFDEelSEARFAALKRLIERLRsEEEESDRRWRARV 947
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
236-556 |
8.76e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 46.87 E-value: 8.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 236 SESANRLIEMQEALERMKTELAnslkqstEITTRNAELEDQLtEDAREKHA-------AQESIVRLKNQICELDAQRTDQ 308
Cdd:PRK04863 296 YTSRRQLAAEQYRLVEMARELA-------ELNEAESDLEQDY-QAASDHLNlvqtalrQQEKIERYQADLEELEERLEEQ 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 309 ETRITTFESRFLTAQRESTCIRDLNDKLEHQLAnkDAAVRLNEEKVHSLQ-----ERLELAEKQLAQ---SLKKAES-LP 379
Cdd:PRK04863 368 NEVVEEADEQQEENEARAEAAEEEVDELKSQLA--DYQQALDVQQTRAIQyqqavQALERAKQLCGLpdlTADNAEDwLE 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 380 SVEAELQQRMEALTAAEQKSVSAEERIQRLDRN---IQELSAELERA----VQRERMNEEHSQRLsstvdklLSESNDRL 452
Cdd:PRK04863 446 EFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAyqlVRKIAGEVSRSeawdVARELLRRLREQRH-------LAEQLQQL 518
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 453 QLHLKERMQALDDKNRLTQQLDGTKKIYDQAERIKDRLQRDNESLRQEIEALRQQLYNARtaQFQSRMHAIPFTHAQNI- 531
Cdd:PRK04863 519 RMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEAR--ERRMALRQQLEQLQARIq 596
|
330 340
....*....|....*....|....*..
gi 17569509 532 --VQQQPQASIAQQSAYQMYKQQPAQQ 556
Cdd:PRK04863 597 rlAARAPAWLAAQDALARLREQSGEEF 623
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
269-418 |
9.08e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 46.87 E-value: 9.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 269 RNAELEDQLTEdAREKHAAQESIVRLKNQICELDAQRTDQETRITTFESRfLTAQRE------STCIRDLNDkLEHQLAN 342
Cdd:COG3096 513 RLQQLRAQLAE-LEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAE-LEAQLEeleeqaAEAVEQRSE-LRQQLEQ 589
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17569509 343 KDAAVRLNEEKV---HSLQERLELAEKQLAQSLkkaESLPSVEAELQQRMEALTAAEQKSVSAEERIQRLDRNIQELSA 418
Cdd:COG3096 590 LRARIKELAARApawLAAQDALERLREQSGEAL---ADSQEVTAAMQQLLEREREATVERDELAARKQALESQIERLSQ 665
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
237-506 |
9.55e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 46.87 E-value: 9.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 237 ESANRLIEMQE-ALERMKTELANSLKQSTEITTRNAELEDQL--TEDAREKH-AAQESIVRLKNQICELDAQRTDQETrI 312
Cdd:COG3096 423 EKARALCGLPDlTPENAEDYLAAFRAKEQQATEEVLELEQKLsvADAARRQFeKAYELVCKIAGEVERSQAWQTAREL-L 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 313 TTFESRFLTAQRESTCIRDLNDkLEHQLANKDAAVRLNEEkvhslqerlelAEKQLAQSLKKAESLPSVEAELQQRMEAL 392
Cdd:COG3096 502 RRYRSQQALAQRLQQLRAQLAE-LEQRLRQQQNAERLLEE-----------FCQRIGQQLDAAEELEELLAELEAQLEEL 569
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 393 TaaEQKSVSAEERIQrLDRNIQELSAELERAVQRE---RMNEEHSQRLSSTVDKLLSESNDrlqlhLKERMQALDDKNRl 469
Cdd:COG3096 570 E--EQAAEAVEQRSE-LRQQLEQLRARIKELAARApawLAAQDALERLREQSGEALADSQE-----VTAAMQQLLERER- 640
|
250 260 270
....*....|....*....|....*....|....*..
gi 17569509 470 tqqldgtkkiydQAERIKDRLQRDNESLRQEIEALRQ 506
Cdd:COG3096 641 ------------EATVERDELAARKQALESQIERLSQ 665
|
|
| SAM_1 |
pfam00536 |
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ... |
867-930 |
1.06e-04 |
|
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily conserved protein binding domain that is involved in the regulation of numerous developmental processes in diverse eukaryotes. The SAM domain can potentially function as a protein interaction module through its ability to homo- and heterooligomerise with other SAM domains.
Pssm-ID: 425739 Cd Length: 64 Bit Score: 41.10 E-value: 1.06e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17569509 867 WNGPTVVAWLElWVGMPAwYVAACRANVKSGAIMSALSDQEIQKeIGISNPLHRLKLRLAIQEM 930
Cdd:pfam00536 3 WSVEDVGEWLE-SIGLGQ-YIDSFRAGYIDGDALLQLTEDDLLK-LGVTLLGHRKKILYAIQRL 63
|
|
| SAM |
smart00454 |
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ... |
1039-1109 |
1.07e-04 |
|
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related tyrosine kinases, appears to mediate cell-cell initiated signal transduction via the binding of SH2-containing proteins to a conserved tyrosine that is phosphorylated. In many cases mediates homodimerisation.
Pssm-ID: 197735 Cd Length: 68 Bit Score: 41.51 E-value: 1.07e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17569509 1039 VWSNERVQRWVEEIGLGVFSRNLVDSGIHGALIALDETFDasafaYALQIGSQDVPNRQLLEKKFIGLVND 1109
Cdd:smart00454 3 QWSPESVADWLESIGLEQYADNFRKNGIDGALLLLLTSEE-----DLKELGITKLGHRKKILKAIQKLKEQ 68
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
305-514 |
1.38e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.19 E-value: 1.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 305 RTDQETRITTFESRFltAQRESTCIRDLNDKLEHQLANKDAAVRLNEEKVHSLQERLELAEKQLAQSLKKAESLPSVEAE 384
Cdd:PRK02224 182 LSDQRGSLDQLKAQI--EEKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 385 LQQRMEALTAAEQKSVSAEERIQRLDRNIQELSAELERAVQRERMNEEHSQRLSSTVDKL----------LSESNDRLQL 454
Cdd:PRK02224 260 IEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELedrdeelrdrLEECRVAAQA 339
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17569509 455 HLKERMQALDDKNRLTQQldgTKKIYDQAERIKDRLQRDNESL---RQEIEALRQQLYNARTA 514
Cdd:PRK02224 340 HNEEAESLREDADDLEER---AEELREEAAELESELEEAREAVedrREEIEELEEEIEELRER 399
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
50-515 |
1.48e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 45.94 E-value: 1.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 50 LQEQLEN-----YKVQLENAGLRTKEVEKERDMMkrQFEVHTQNLPQELQTMTRELCLLKEQLLEKDEEIVELKAERNNT 124
Cdd:pfam01576 108 LEEQLDEeeaarQKLQLEKVTTEAKIKKLEEDIL--LLEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKH 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 125 RLLLEHLECLVSRHERS-LRMTVMKRQAQnhaGVSSEV-EVLKALKSLFEHHKALDEKVRERLRVAMERvatLEEELSTK 202
Cdd:pfam01576 186 EAMISDLEERLKKEEKGrQELEKAKRKLE---GESTDLqEQIAELQAQIAELRAQLAKKEEELQAALAR---LEEETAQK 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 203 gdeNSSLKARIATYAAEAEEAMASNAPINGSISSESANRliEMQEALERMKTELANSL-----------KQSTEITTRNA 271
Cdd:pfam01576 260 ---NNALKKIRELEAQISELQEDLESERAARNKAEKQRR--DLGEELEALKTELEDTLdttaaqqelrsKREQEVTELKK 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 272 ELEDQLT------EDAREKHAAQesIVRLKNQICELDAQRTDQETRITTFESRFLTAQRESTCIRDLNDKLEHQLANKDA 345
Cdd:pfam01576 335 ALEEETRsheaqlQEMRQKHTQA--LEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEG 412
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 346 AV-----RLNE---------EKVHSLQERLE----LAEKQLAQSLKKAESLPSVEAELQQRMEALTAAEQKSVSAEERIQ 407
Cdd:pfam01576 413 QLqelqaRLSEserqraelaEKLSKLQSELEsvssLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLR 492
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 408 RLDRNIQELSAELERAVQRERMNEEHSQRLS---STVDKLLSESNDRLQLHLKERMQALDDKNRLTQQLDGTKKIYDQAE 484
Cdd:pfam01576 493 QLEDERNSLQEQLEEEEEAKRNVERQLSTLQaqlSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLE 572
|
490 500 510
....*....|....*....|....*....|.
gi 17569509 485 RIKDRLQRDNESLRQEIEALRQQLYNARTAQ 515
Cdd:pfam01576 573 KTKNRLQQELDDLLVDLDHQRQLVSNLEKKQ 603
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
247-518 |
1.62e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 46.12 E-value: 1.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 247 EALERMKTELANSLKQSTEITtrnaELEDQLT-----EDAREKHAAQESIVRLKNQICELDAQRTDQETRITTF------ 315
Cdd:pfam02463 173 EALKKLIEETENLAELIIDLE----ELKLQELklkeqAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLqellrd 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 316 -ESRFLTAQRESTCIRDLNDKLEHQLANKDAAVRLNEEKVHSLQERLELAEKQLAQSLKKAESLPSVEAELQQRMEALTA 394
Cdd:pfam02463 249 eQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEK 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 395 AEQKSVSAEERIQRLDRNIQELSAELERAVQRERMNEEHSQRLSSTVDKLLSESNDRLQLHLKERMQALDDKNRLTQQLD 474
Cdd:pfam02463 329 ELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQ 408
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 17569509 475 GTKKIYDQAERIKDRLQrdNESLRQEIEALRQQLYNARTAQFQS 518
Cdd:pfam02463 409 LLLELARQLEDLLKEEK--KEELEILEEEEESIELKQGKLTEEK 450
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
159-526 |
2.07e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 45.50 E-value: 2.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 159 SEVEVLKALKSLFEHHKALDEKVRERL--RVAMERVATLEEELSTKGDENSSLKariatyaaEAEEAMASNAPINGSISS 236
Cdd:pfam17380 266 TENEFLNQLLHIVQHQKAVSERQQQEKfeKMEQERLRQEKEEKAREVERRRKLE--------EAEKARQAEMDRQAAIYA 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 237 ESANRLIEMQEALERMKTE---LANSLKQSTEIT---TRNAELED-QLTEDAREKHAAQESIVRLKNQICELDAQRTDQE 309
Cdd:pfam17380 338 EQERMAMERERELERIRQEerkRELERIRQEEIAmeiSRMRELERlQMERQQKNERVRQELEAARKVKILEEERQRKIQQ 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 310 TRITTFESRfltAQRESTCIRDLNdKLEHQLANKDAAVRLNEEKVHSLQERLELAEKQlaQSLKKaeslpsVEAELQQRM 389
Cdd:pfam17380 418 QKVEMEQIR---AEQEEARQREVR-RLEEERAREMERVRLEEQERQQQVERLRQQEEE--RKRKK------LELEKEKRD 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 390 EALTAAEQKSVSAEERIQRLDRNIQElsaELERAVQRERMnEEHSQRLSSTVDKLLSESNDRLQLHLKERMQALDDKNRL 469
Cdd:pfam17380 486 RKRAEEQRRKILEKELEERKQAMIEE---ERKRKLLEKEM-EERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKA 561
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17569509 470 TQQ---LDGTKKiydqaERIKDRLQRDNESLRQEIEALRQ-----QLYNARTAQFQS---RMHAIPFT 526
Cdd:pfam17380 562 TEErsrLEAMER-----EREMMRQIVESEKARAEYEATTPittikPIYRPRISEYQPpdvESHMIRFT 624
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
229-535 |
2.56e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.89 E-value: 2.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 229 PINGSISSESANRLIEMQEALERMKTELANSLKQSTEITTRNAELEDQLTEDAREKHAAQESIVRLKNQICELDAQRTDQ 308
Cdd:COG4372 20 PKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 309 ETRITTFESRFLTAQR-------ESTCIRDLNDKLEHQLANKDAAVRLNEEKVHSLQERLELAEKQLAQSLKKAESLPSV 381
Cdd:COG4372 100 QEELESLQEEAEELQEeleelqkERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 382 EAELQQRMEALTAAEQKSVSAEERIQRLDRNIQELSAELERAVQRERMNEEHSQRLSSTVDKLLSESNDRLQLHLKERMQ 461
Cdd:COG4372 180 EAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKE 259
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17569509 462 ALDDKNRLTQQLDGTKKIYDQAERIKDRLQRDNESLRQEIEALRQQLYNARTAQFQSRMHAIPFTHAQNIVQQQ 535
Cdd:COG4372 260 IEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALA 333
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
69-498 |
2.72e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 45.21 E-value: 2.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 69 KEVEKERDMMKRQFEV---HTQNLPQELQT-MTRELCLLKEQLLEKDEEIVELKAERNN---TRLLLEHLECLVSRHERS 141
Cdd:pfam12128 397 DKLAKIREARDRQLAVaedDLQALESELREqLEAGKLEFNEEEYRLKSRLGELKLRLNQataTPELLLQLENFDERIERA 476
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 142 lrmtvMKRQAQNHAGVSSEVEVLKALKSLFEhhKALDEKVRERLRVamERVATLEEELSTKGD------------ENSSL 209
Cdd:pfam12128 477 -----REEQEAANAEVERLQSELRQARKRRD--QASEALRQASRRL--EERQSALDELELQLFpqagtllhflrkEAPDW 547
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 210 KARIATYAAEAEEAMASNAPINGSISSESANRLIEMQEALERMktELANSLKQSTEITTRNAELEDQLtEDAREKHAAQE 289
Cdd:pfam12128 548 EQSIGKVISPELLHRTDLDPEVWDGSVGGELNLYGVKLDLKRI--DVPEWAASEEELRERLDKAEEAL-QSAREKQAAAE 624
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 290 SIVRLKNQicELDAQRTDQETRITTFESRFLTAQRESTCIRDLNDKLEHQLAnkdAAVRLNEEKVHSLQERLELAEKQLA 369
Cdd:pfam12128 625 EQLVQANG--ELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALA---ERKDSANERLNSLEAQLKQLDKKHQ 699
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 370 Q------------SLKKAESLPSVEAELQQRMEALTAAEQKSVSA----------------------EERIQRLDRNIQE 415
Cdd:pfam12128 700 AwleeqkeqkreaRTEKQAYWQVVEGALDAQLALLKAAIAARRSGakaelkaletwykrdlaslgvdPDVIAKLKREIRT 779
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 416 LSAELERAVQRERMNEEHSQRLSSTvdklLSESNDRLQLHLKERMQALDD-KNRLTQQLDGTK----KIYDQAERIKDRL 490
Cdd:pfam12128 780 LERKIERIAVRRQEVLRYFDWYQET----WLQRRPRLATQLSNIERAISElQQQLARLIADTKlrraKLEMERKASEKQQ 855
|
....*...
gi 17569509 491 QRDNESLR 498
Cdd:pfam12128 856 VRLSENLR 863
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
48-504 |
2.80e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.52 E-value: 2.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 48 DKLQEQLENYKVQLENAGLRTKEVEKERDMMKRQfevhtqnlpQELQTMTRELCLLKEQLLEKDEEIVELKAERNNTRLL 127
Cdd:PTZ00121 1353 EAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKK---------AEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEA 1423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 128 LEHLEcLVSRHERSLRMTVMKRQAQNHAGVSSEVEVLKALKSLFEHHKALDE--KVRERLRVAmERVATLEEELSTKGDE 205
Cdd:PTZ00121 1424 KKKAE-EKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEakKKAEEAKKA-DEAKKKAEEAKKKADE 1501
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 206 nsSLKARIATYAAEAEEAMASNAPINGSISSESANRLIEMQEALERMKtelANSLKQSTEIttRNAElEDQLTEDAREKH 285
Cdd:PTZ00121 1502 --AKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKK---ADELKKAEEL--KKAE-EKKKAEEAKKAE 1573
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 286 AAQESIVRLKNQICELDAQRTDQETRITTFESRFLTAQRestcirdlndKLEHQLANKDAAVRLNEE--KVHSLQERLEL 363
Cdd:PTZ00121 1574 EDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEA----------KKAEEAKIKAEELKKAEEekKKVEQLKKKEA 1643
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 364 AEKQLAQSLKKAESLPSVEAELQQRMEALTAAEQKSVSAEERIQRLDRNIQELSAELERAVQRERMNEEHSQRLSSTVDK 443
Cdd:PTZ00121 1644 EEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKK 1723
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17569509 444 LLSESNDRLQlHLKERMQALDDKNRLTQQLDGTKKiydQAERIKDRLQRDNESLRQEIEAL 504
Cdd:PTZ00121 1724 AEEENKIKAE-EAKKEAEEDKKKAEEAKKDEEEKK---KIAHLKKEEEKKAEEIRKEKEAV 1780
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
46-523 |
2.97e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 45.06 E-value: 2.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 46 DRDKLQEQLENYKVQLENAGLRTKEVEKERDMMKRQFEVHTQNLPQELQTMTREL-----------CLLKEQLLEKDEEI 114
Cdd:TIGR02169 245 QLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELeaeiaslersiAEKERELEDAEERL 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 115 VELKAERNNTRLLLEHLEclvsrheRSLRmtvmkRQAQNHAGVSSEVEVLKA-LKSLFEHHKALDEKVRErlrvAMERVA 193
Cdd:TIGR02169 325 AKLEAEIDKLLAEIEELE-------REIE-----EERKRRDKLTEEYAELKEeLEDLRAELEEVDKEFAE----TRDELK 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 194 TLEEELSTKGDENSSLKARIATYAAEAEEAMAsnapingsissesanRLIEMQEALERMKTELANSLKQSTEITTRNAEL 273
Cdd:TIGR02169 389 DYREKLEKLKREINELKRELDRLQEELQRLSE---------------ELADLNAAIAGIEAKINELEEEKEDKALEIKKQ 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 274 EDQLTEDAREKHAAQESIVRLKNQICELDAQRTDQETRITTFESRFLTAQRESTCIRDLNDKL----------------- 336
Cdd:TIGR02169 454 EWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLkasiqgvhgtvaqlgsv 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 337 --EHQLANKDAA-VRLN----------EEKVHSLQER-------LELAEKQLAQSLKKAESLPSV--------------- 381
Cdd:TIGR02169 534 geRYATAIEVAAgNRLNnvvveddavaKEAIELLKRRkagratfLPLNKMRDERRDLSILSEDGVigfavdlvefdpkye 613
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 382 -------------------------------EAELQQRMEALT-------AAEQKSVSAEERIQRLDRNIQELSAELERA 423
Cdd:TIGR02169 614 pafkyvfgdtlvvedieaarrlmgkyrmvtlEGELFEKSGAMTggsraprGGILFSRSEPAELQRLRERLEGLKRELSSL 693
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 424 VQRERMNEEHSQRLSStvdkLLSESNDRLQLHLKERMQALDDKNRltqqldgtkkiydQAERIKDrLQRDNESLRQEIEA 503
Cdd:TIGR02169 694 QSELRRIENRLDELSQ----ELSDASRKIGEIEKEIEQLEQEEEK-------------LKERLEE-LEEDLSSLEQEIEN 755
|
570 580
....*....|....*....|..
gi 17569509 504 LRQQL--YNARTAQFQSRMHAI 523
Cdd:TIGR02169 756 VKSELkeLEARIEELEEDLHKL 777
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
247-544 |
4.52e-04 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 44.18 E-value: 4.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 247 EALERMKTELANSLKQSTEI--------TTRNAELEDQLTEDAREKHAAQESIV-RLKNQICELDAQRTDQETRITTFES 317
Cdd:COG5185 246 EDLAQTSDKLEKLVEQNTDLrleklgenAESSKRLNENANNLIKQFENTKEKIAeYTKSIDIKKATESLEEQLAAAEAEQ 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 318 RFLTAQRESTcirDLNDKLEHQLANKDAAVRLNEEKVHSLQERLElAEKQLAQSLKKAES----LPSVEAELQQRMEALT 393
Cdd:COG5185 326 ELEESKRETE---TGIQNLTAEIEQGQESLTENLEAIKEEIENIV-GEVELSKSSEELDSfkdtIESTKESLDEIPQNQR 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 394 AAEQKSVSAEER-IQRLDRNIQELSAELERAVQRERMNEEHSQRLSSTVDKLLSESNDRLQLHLKERMQALddKNRLTQQ 472
Cdd:COG5185 402 GYAQEILATLEDtLKAADRQIEELQRQIEQATSSNEEVSKLLNELISELNKVMREADEESQSRLEEAYDEI--NRSVRSK 479
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17569509 473 LDGTKKIYDQAER----IKDRLQRDNESLRQEIEALRQQLyNARTAQFQSRMHAIPFTHAQNIVQQQPQASIAQQS 544
Cdd:COG5185 480 KEDLNEELTQIESrvstLKATLEKLRAKLERQLEGVRSKL-DQVAESLKDFMRARGYAHILALENLIPASELIQAS 554
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
162-432 |
6.43e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.14 E-value: 6.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 162 EVLKALKSLFEHHKALDEkVRERLRVAMERVATLEEeLSTKGDENSSLKARIATYAAEaeeamasnapingsissESANR 241
Cdd:COG4913 222 DTFEAADALVEHFDDLER-AHEALEDAREQIELLEP-IRELAERYAAARERLAELEYL-----------------RAALR 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 242 LIEMQEALERMKTELAnslkqstEITTRNAELEDQLTEDAREKHAAQESIVRLKNQICELDAQRTDQ-ETRITTFESRFL 320
Cdd:COG4913 283 LWFAQRRLELLEAELE-------ELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQlEREIERLERELE 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 321 TAQREStcirdlnDKLEHQLANKDAAVRLNEEKVHSLQERLelaeKQLAQSLKKAESlpSVEAELQQRMEALTAAEQKSV 400
Cdd:COG4913 356 ERERRR-------ARLEALLAALGLPLPASAEEFAALRAEA----AALLEALEEELE--ALEEALAEAEAALRDLRRELR 422
|
250 260 270
....*....|....*....|....*....|..
gi 17569509 401 SAEERIQRLDRNIQELSAELERAvqRERMNEE 432
Cdd:COG4913 423 ELEAEIASLERRKSNIPARLLAL--RDALAEA 452
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
236-463 |
6.98e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 43.75 E-value: 6.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 236 SESANRLIEMQEALERMKTELANSLKQSTEITTR---NAELEDQLTEDAREKHAAQESIVRLKNqicelDAQRtdQETRI 312
Cdd:PRK11281 145 AEYNSQLVSLQTQPERAQAALYANSQRLQQIRNLlkgGKVGGKALRPSQRVLLQAEQALLNAQN-----DLQR--KSLEG 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 313 TTFESRFLTAQRESTCIRdlNDKLEHQLANkdaavrlneekvhsLQErlELAEKQLAQSLKKAEslpsveaELQQRMEAL 392
Cdd:PRK11281 218 NTQLQDLLQKQRDYLTAR--IQRLEHQLQL--------------LQE--AINSKRLTLSEKTVQ-------EAQSQDEAA 272
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17569509 393 TAAEQKSVSAEeriqrLDRNIQeLSAELERAVqrERMNE--EHSQRLSSTVDKLL-SESNdrlqlhLKERMQAL 463
Cdd:PRK11281 273 RIQANPLVAQE-----LEINLQ-LSQRLLKAT--EKLNTltQQNLRVKNWLDRLTqSERN------IKEQISVL 332
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
162-508 |
7.69e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.79 E-value: 7.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 162 EVLKALKSLFEHHKALdEKVRERLRVAMERVATLEEELSTKGDENSSLKARIATYAaeaeeamasnapiNGSISSESANR 241
Cdd:PRK04863 287 EALELRRELYTSRRQL-AAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNLVQ-------------TALRQQEKIER 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 242 lieMQEALErmktELANSLKQSTEITtrnAELEDQLTEDAREKHAAQESIVRLKNQICE----LDAQRT----------- 306
Cdd:PRK04863 353 ---YQADLE----ELEERLEEQNEVV---EEADEQQEENEARAEAAEEEVDELKSQLADyqqaLDVQQTraiqyqqavqa 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 307 ---------DQETRITTFESRFLTAQRESTCIRDLNDKLEHQLANKDAAVRLNEEKVHSLQ------ERLElAEKQLAQS 371
Cdd:PRK04863 423 lerakqlcgLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRkiagevSRSE-AWDVAREL 501
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 372 LKKAESLPSVEAELQQRMEALTAAEQKSVSAEERIQRLDRNIQELSAELERAVQRERMNEEHSQRLSSTVDKLLSESNDR 451
Cdd:PRK04863 502 LRRLREQRHLAEQLQQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERR 581
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 17569509 452 LQLHlKERMQALDDKNRLTQQLDGTKKIYDQAERIKDRLQRDNESlRQEIEALRQQL 508
Cdd:PRK04863 582 MALR-QQLEQLQARIQRLAARAPAWLAAQDALARLREQSGEEFED-SQDVTEYMQQL 636
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
241-472 |
1.01e-03 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 42.49 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 241 RLIEMQEALERMKTELANSLKQSTEITTRNAELEDQLTEDAREKHAaqesivrLKNQICELDAQRTdqeTRITTFESRFL 320
Cdd:pfam15905 95 RLQALEEELEKVEAKLNAAVREKTSLSASVASLEKQLLELTRVNEL-------LKAKFSEDGTQKK---MSSLSMELMKL 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 321 TAQRESTC--IRDLNDKLEHQLANKDAAVRLNEEKVHSLQERLELAEKQLAQSLKKAESLPSVEAELQQRMEALTAAEQK 398
Cdd:pfam15905 165 RNKLEAKMkeVMAKQEGMEGKLQVTQKNLEHSKGKVAQLEEKLVSTEKEKIEEKSETEKLLEYITELSCVSEQVEKYKLD 244
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17569509 399 SVSAEERIQRLDRNIQELSAELERAVQR--ERMNE--EHSQRLSSTVDKLLSESNDRLQLHLKErMQALDDKNRLTQQ 472
Cdd:pfam15905 245 IAQLEELLKEKNDEIESLKQSLEEKEQElsKQIKDlnEKCKLLESEKEELLREYEEKEQTLNAE-LEELKEKLTLEEQ 321
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
334-587 |
1.21e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 43.25 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 334 DKLEHQLAnkdAAVRLNEEKVHSLQERLEL---AEKQLA-------QSLKKAESLPSVEAELQQRMEALTAAEQKSVSAE 403
Cdd:PRK10246 201 EKLQAQAS---GVALLTPEQVQSLTASLQVltdEEKQLLtaqqqqqQSLNWLTRLDELQQEASRRQQALQQALAAEEKAQ 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 404 ERIQRLD------------RNIQELSAELERAvqRERMNE-----EHSQRLSSTVDKLLSESNDRLQLHLKERMQALDDK 466
Cdd:PRK10246 278 PQLAALSlaqparqlrphwERIQEQSAALAHT--RQQIEEvntrlQSTMALRARIRHHAAKQSAELQAQQQSLNTWLAEH 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 467 NRL---TQQLDGTKKIYDQAERIKDRLQRDNE---SLRQEIEAL--------RQQLYNARTAQFQSR--MHAIPFTHAQN 530
Cdd:PRK10246 356 DRFrqwNNELAGWRAQFSQQTSDREQLRQWQQqltHAEQKLNALpaitltltADEVAAALAQHAEQRplRQRLVALHGQI 435
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 17569509 531 IVQQQPQASIaqQSAYQMYKQQPAQQYQTVGMRRPnkgRISALQDDPNKVQTLNEQE 587
Cdd:PRK10246 436 VPQQKRLAQL--QVAIQNVTQEQTQRNAALNEMRQ---RYKEKTQQLADVKTICEQE 487
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
88-213 |
1.33e-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: 41.83 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 88 NLPQELQTMTRELCLLKEQLLEKDEEIVELKAERNNTRLLLEHLECLVSRHERSLrMTVMK-RQAQNhagVSSEVEVLKA 166
Cdd:COG1579 28 ELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQL-GNVRNnKEYEA---LQKEIESLKR 103
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 17569509 167 LKSLFEhhkaldekvrERLRVAMERVATLEEELSTKGDENSSLKARI 213
Cdd:COG1579 104 RISDLE----------DEILELMERIEELEEELAELEAELAELEAEL 140
|
|
| DUF724 |
pfam05266 |
Protein of unknown function (DUF724); This family contains several uncharacterized proteins ... |
40-132 |
1.67e-03 |
|
Protein of unknown function (DUF724); This family contains several uncharacterized proteins found in Arabidopsis thaliana and other plants. This region is often found associated with Agenet domains and may contain coiled-coil.
Pssm-ID: 428400 [Multi-domain] Cd Length: 188 Bit Score: 40.72 E-value: 1.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 40 MMNMLEDRDKLQEQLENYKVQLENAGLRTKEVEKERDMMKRQFevhtqnlpQELQtmtRELCLLKEQLLEKDEEIVELKA 119
Cdd:pfam05266 97 LLSLKDRQTKLLEELKKLEKKIAEEESEKRKLEEEIDELEKKI--------LELE---RQLALAKEKKEAADKEIARLKS 165
|
90
....*....|...
gi 17569509 120 ERNNTRLLLEHLE 132
Cdd:pfam05266 166 EAEKLEQEIQDVE 178
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
45-447 |
1.93e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 42.33 E-value: 1.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 45 EDRDKLQEQLENYKVQLENAGLRTKEVEKERDMMKRQFEvhtqNLPQELQTMTRELCLLKEQLLEKDEEIVELKAERNNT 124
Cdd:PRK02224 363 EEAAELESELEEAREAVEDRREEIEELEEEIEELRERFG----DAPVDLGNAEDFLEELREERDELREREAELEATLRTA 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 125 R-------LLLE---------------HLECLVSRHERSLRMTVMKRQAQ-NHAGVSSEVEVLKALKSLfehhKALDEKV 181
Cdd:PRK02224 439 RerveeaeALLEagkcpecgqpvegspHVETIEEDRERVEELEAELEDLEeEVEEVEERLERAEDLVEA----EDRIERL 514
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 182 RERLRVAMERVATLEEELSTKGDENSSLKARIATYAAEAEEAMASnapinGSISSESANRLIEMQEALERMKTELANSLK 261
Cdd:PRK02224 515 EERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREA-----AAEAEEEAEEAREEVAELNSKLAELKERIE 589
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 262 QSTEITTRNAELED--QLTEDAREKHAaqesivrlknQICELDAQRTDQetrittfesrfLTAQREStcIRDLNDKLEhq 339
Cdd:PRK02224 590 SLERIRTLLAAIADaeDEIERLREKRE----------ALAELNDERRER-----------LAEKRER--KRELEAEFD-- 644
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 340 lankdaavrlnEEKVHSLQERLELAEKQLAQSLKKAESLPSVEAELQQRMEALTAAEQKSVSAEERIQRLDRNIQELSAE 419
Cdd:PRK02224 645 -----------EARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEELRERREALENRVEALEAL 713
|
410 420 430
....*....|....*....|....*....|..
gi 17569509 420 LERAVQRERM----NEEHSQRLSSTVDKLLSE 447
Cdd:PRK02224 714 YDEAEELESMygdlRAELRQRNVETLERMLNE 745
|
|
| SAM_superfamily |
cd09487 |
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ... |
959-1010 |
2.04e-03 |
|
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of approximately 70 amino acids. This domain is found in the Fungi/Metazoa group and in a restricted number of bacteria. Proteins with SAM domains are represented by a wide variety of domain architectures and have different intracellular localization, including nucleus, cytoplasm and membranes. SAM domains have diverse functions. They can interact with proteins, RNAs and membrane lipids, contain site of phosphorylation and/or kinase docking site, and play a role in protein homo and hetero dimerization/oligomerization in processes ranging from signal transduction to regulation of transcription. Mutations in SAM domains have been linked to several diseases.
Pssm-ID: 188886 [Multi-domain] Cd Length: 56 Bit Score: 37.60 E-value: 2.04e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 17569509 959 DWLPCLGLAQYRSAFMECLLDARMLEHLSKRDLRThLRMVDTFHRTSLQYGI 1010
Cdd:cd09487 4 EWLESLGLEQYADLFRKNEIDGDALLLLTDEDLKE-LGITSPGHRKKILRAI 54
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
291-462 |
2.08e-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: 41.06 E-value: 2.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 291 IVRLKNQICELDAQRTDQETRITTFESRFLTAQREstcirdlndklehqLANKDAAVRLNEEKVHSLQERLELAEKQLAQ 370
Cdd:COG1579 19 LDRLEHRLKELPAELAELEDELAALEARLEAAKTE--------------LEDLEKEIKRLELEIEEVEARIKKYEEQLGN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 371 sLKKAEslpsveaELQQRMEALTAAEQKSVSAEERIQRLDRNIQELSAELERAVQRERMNEEHSQRLSSTVDKLLSESND 450
Cdd:COG1579 85 -VRNNK-------EYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEA 156
|
170
....*....|..
gi 17569509 451 RLQLHLKERMQA 462
Cdd:COG1579 157 ELEELEAEREEL 168
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
351-523 |
2.17e-03 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 42.15 E-value: 2.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 351 EEKVHSLQERLELAEKQLAQ-SLKKAESLpsvEAELQQRMEALTAAEQKSVSA-----------EERIQRLDRNIQELSA 418
Cdd:pfam06160 236 DKEIQQLEEQLEENLALLENlELDEAEEA---LEEIEERIDQLYDLLEKEVDAkkyveknlpeiEDYLEHAEEQNKELKE 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 419 ELERAVQRERMNEEHSQRLSSTVDKL--LSESNDRLQLHLKERMQA----LDDKNRLTQQLDgtkKIYDQAERIKDRLQr 492
Cdd:pfam06160 313 ELERVQQSYTLNENELERVRGLEKQLeeLEKRYDEIVERLEEKEVAyselQEELEEILEQLE---EIEEEQEEFKESLQ- 388
|
170 180 190
....*....|....*....|....*....|.
gi 17569509 493 dneSLRQEIEALRQQLynartAQFQSRMHAI 523
Cdd:pfam06160 389 ---SLRKDELEAREKL-----DEFKLELREI 411
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
93-426 |
2.37e-03 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 41.59 E-value: 2.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 93 LQTMTRELCLLKEQLLEKDEEIVELKAERNNTRLLLEHLECLVSRHERSLRMTVmKRQAQNHAGVSSEVEVLKALKSLFE 172
Cdd:pfam19220 36 IEAILRELPQAKSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEELV-ARLAKLEAALREAEAAKEELRIELR 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 173 HHKALDEKVRERLRVAMERVATLEEELSTKGDENSSLKARIatyaaeaeeamasnapingsisSESANRLIEMQEALERM 252
Cdd:pfam19220 115 DKTAQAEALERQLAAETEQNRALEEENKALREEAQAAEKAL----------------------QRAEGELATARERLALL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 253 KTEL----ANSLKQSTEI---TTRNAELEDQLTE-----DAREKHAAQESIVRLKNQiCELDAQRTDQETRITTFESRFL 320
Cdd:pfam19220 173 EQENrrlqALSEEQAAELaelTRRLAELETQLDAtrarlRALEGQLAAEQAERERAE-AQLEEAVEAHRAERASLRMKLE 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 321 TAQRESTCIRDLNDKLEHQLANKDAAVRLNEEKVHSLQERLELAEKQLAQslkkaeslpsVEAELQQRMEALTAAEQKSV 400
Cdd:pfam19220 252 ALTARAAATEQLLAEARNQLRDRDEAIRAAERRLKEASIERDTLERRLAG----------LEADLERRTQQFQEMQRARA 321
|
330 340
....*....|....*....|....*.
gi 17569509 401 SAEERIQRLDRNIQELSAELERAVQR 426
Cdd:pfam19220 322 ELEERAEMLTKALAAKDAALERAEER 347
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
236-432 |
2.66e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.35 E-value: 2.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 236 SESANRLIEMQEALERMKTELANSLKQSTEITTRNAELEDQLTEDAREKHAAQESIVRLKNQICELDAQ-----RTDQET 310
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREElgeraRALYRS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 311 -RITTFESRFLTAQrestcirDLNDKLEhQLANKDAAVRLNEEKVHSLQERLELAEKQLAQSLKKAESLPSVEAELQQRM 389
Cdd:COG3883 99 gGSVSYLDVLLGSE-------SFSDFLD-RLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAK 170
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 17569509 390 EALtaaEQKSVSAEERIQRLDRNIQELSAELERAVQRERMNEE 432
Cdd:COG3883 171 AEL---EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEA 210
|
|
| SAM_superfamily |
cd09487 |
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ... |
872-929 |
2.79e-03 |
|
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of approximately 70 amino acids. This domain is found in the Fungi/Metazoa group and in a restricted number of bacteria. Proteins with SAM domains are represented by a wide variety of domain architectures and have different intracellular localization, including nucleus, cytoplasm and membranes. SAM domains have diverse functions. They can interact with proteins, RNAs and membrane lipids, contain site of phosphorylation and/or kinase docking site, and play a role in protein homo and hetero dimerization/oligomerization in processes ranging from signal transduction to regulation of transcription. Mutations in SAM domains have been linked to several diseases.
Pssm-ID: 188886 [Multi-domain] Cd Length: 56 Bit Score: 37.22 E-value: 2.79e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 17569509 872 VVAWLElWVGMPaWYVAACRANVKSGAIMSALSDQEIqKEIGISNPLHRLKLRLAIQE 929
Cdd:cd09487 2 VAEWLE-SLGLE-QYADLFRKNEIDGDALLLLTDEDL-KELGITSPGHRKKILRAIQR 56
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
329-460 |
4.13e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 41.22 E-value: 4.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 329 IRDLNDKLEHQLANKDAAVRLNEEKVhslQERLELAEKQLAQSLKKAESLPSVEAELQQRMEALTAAEQKSVSAEERIQR 408
Cdd:COG0542 413 LDELERRLEQLEIEKEALKKEQDEAS---FERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRYGKIPE 489
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 17569509 409 LDRNIQELSAELERAVQ--RERMNEEH-SQRLSS-T---VDKLLSESNDRLqLHLKERM 460
Cdd:COG0542 490 LEKELAELEEELAELAPllREEVTEEDiAEVVSRwTgipVGKLLEGEREKL-LNLEEEL 547
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
368-508 |
4.53e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.90 E-value: 4.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 368 LAQSLKKAESLPSVEAELQQRMEALTAAEQKSVSAEERIQRLDRNIQELSAELERAVQRERMNEEHSQRLSSTVDKlLSE 447
Cdd:COG4942 12 ALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAE-LEK 90
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17569509 448 SNDRLQLHLKERMQALDDKNRLTQQLDGTKKI--------YDQAERIKDRLQRDNESLRQEIEALRQQL 508
Cdd:COG4942 91 EIAELRAELEAQKEELAELLRALYRLGRQPPLalllspedFLDAVRRLQYLKYLAPARREQAEELRADL 159
|
|
| I-BAR_IMD |
cd07605 |
Inverse (I)-BAR, also known as the IRSp53/MIM homology Domain (IMD), a dimerization module ... |
323-474 |
4.71e-03 |
|
Inverse (I)-BAR, also known as the IRSp53/MIM homology Domain (IMD), a dimerization module that binds and bends membranes; Inverse (I)-BAR (or IMD) is a member of the Bin/Amphiphysin/Rvs (BAR) domain family. It is a dimerization and lipid-binding module that bends membranes and induces membrane protrusions in the opposite direction compared to classical BAR and F-BAR domains, which produce membrane invaginations. IMD domains are found in Insulin Receptor tyrosine kinase Substrate p53 (IRSp53), Missing in Metastasis (MIM), and Brain-specific Angiogenesis Inhibitor 1-Associated Protein 2-like (BAIAP2L) proteins. These are multi-domain proteins that act as scaffolding proteins and transducers of a variety of signaling pathways that link membrane dynamics and the underlying actin cytoskeleton. Most members contain an N-terminal IMD, an SH3 domain, and a WASP homology 2 (WH2) actin-binding motif at the C-terminus, exccept for MIM which does not carry an SH3 domain. Some members contain additional domains and motifs. The IMD domain binds and bundles actin filaments, binds membranes and produces membrane protrusions, and interacts with the small GTPase Rac.
Pssm-ID: 153289 [Multi-domain] Cd Length: 223 Bit Score: 40.04 E-value: 4.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 323 QRESTCIRDLNDKLEHQLAnkdaavRLNEEKVHSLQERLELAEKQLAQSLKKAESlpsveaELQQRMEALTAAEQ----- 397
Cdd:cd07605 71 KQIVDTHKSIEASLEQVAK------AFHGELILPLEKKLELDQKVINKFEKDYKK------EYKQKREDLDKARSelkkl 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 398 ----KSVSAEERIQRLDRNIQELS---AELERAVQ---RERMNEEHsQRLSSTVDKLLSESNDRLQLHLKErMQALDDKN 467
Cdd:cd07605 139 qkksQKSGTGKYQEKLDQALEELNdkqKELEAFVSqglRDALLEER-RRYCFLVDKHCSVAKHEIAYHAKA-MTLLSTRL 216
|
....*..
gi 17569509 468 RLTQQLD 474
Cdd:cd07605 217 PLWQELC 223
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
286-602 |
5.13e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 40.98 E-value: 5.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 286 AAQESIVRLKNQICELDAQRTDQETRITTFESRFLTAQREstcIRDLNDKLEHQLANKDAAVRLN----EEKVHSLQERL 361
Cdd:pfam12128 248 QEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAE---LNQLLRTLDDQWKEKRDELNGElsaaDAAVAKDRSEL 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 362 ELAEKQLAQSLK--------KAESLPSVEAELQQRMEALTAAEQKSVSAEERIQRLDRNI-QELSAELERavqrermNEE 432
Cdd:pfam12128 325 EALEDQHGAFLDadietaaaDQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIkEQNNRDIAG-------IKD 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 433 HSQRLSSTVDKLLSESNDRLqlhlkermQALDdkNRLTQQLDGTK-KIYDQAERIKDRLQRDNESLRQEI---EALRQQl 508
Cdd:pfam12128 398 KLAKIREARDRQLAVAEDDL--------QALE--SELREQLEAGKlEFNEEEYRLKSRLGELKLRLNQATatpELLLQL- 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 509 ynartAQFQSRMHAipfthaqnivqqqpqASIAQQSAyqmykqqpaqqyqtvgmrrpNKGRiSALQDDPNKVQTLNEQEW 588
Cdd:pfam12128 467 -----ENFDERIER---------------AREEQEAA--------------------NAEV-ERLQSELRQARKRRDQAS 505
|
330
....*....|....
gi 17569509 589 DRLQQAHVLANVQQ 602
Cdd:pfam12128 506 EALRQASRRLEERQ 519
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
265-514 |
5.61e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 41.09 E-value: 5.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 265 EITTRNAELEDQLTEDAREKHAAQESIVRLKNQICELDAQR--------TDQETRITTFESRFLTAQRESTCIRDLNDKL 336
Cdd:COG3096 840 ALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLLNKLLpqanlladETLADRLEELREELDAAQEAQAFIQQHGKAL 919
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 337 EhQLANKDAAVRLNEEKVHSLQERLELAEKQLAQSLKKAESLpsveAELQQRMEALT---AAEQKSVSAE--ERI-QRLD 410
Cdd:COG3096 920 A-QLEPLVAVLQSDPEQFEQLQADYLQAKEQQRRLKQQIFAL----SEVVQRRPHFSyedAVGLLGENSDlnEKLrARLE 994
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 411 RniqelsAELERAVQRERMN------EEHSQRLSStvdkLLSESNDRLQLH--LKERMQAL-------------DDKNRL 469
Cdd:COG3096 995 Q------AEEARREAREQLRqaqaqySQYNQVLAS----LKSSRDAKQQTLqeLEQELEELgvqadaeaeerarIRRDEL 1064
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 17569509 470 TQQLDGTKKIYDQAERIKDRLQRDNESLRQEIEALRQQLYNARTA 514
Cdd:COG3096 1065 HEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQEREQ 1109
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
353-520 |
5.95e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 39.42 E-value: 5.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 353 KVHSLQERLELAEKQLAQSLKKAEslpsveAELQQRMEAL--TAAEQKSvsAEERIQRLDRNIQELSAELERAVQRERmn 430
Cdd:COG1842 13 NINALLDKAEDPEKMLDQAIRDME------EDLVEARQALaqVIANQKR--LERQLEELEAEAEKWEEKARLALEKGR-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 431 eEHSQRlsstvdkllsesndrlqlhlkermQALDDKNRLTQQLDGTKKIYDQAERIKDRLQRDNESLRQEIEALRQQLY- 509
Cdd:COG1842 83 -EDLAR------------------------EALERKAELEAQAEALEAQLAQLEEQVEKLKEALRQLESKLEELKAKKDt 137
|
170
....*....|....
gi 17569509 510 ---NARTAQFQSRM 520
Cdd:COG1842 138 lkaRAKAAKAQEKV 151
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
91-508 |
6.19e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 40.93 E-value: 6.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 91 QELQTMTRELCLLKEQLLEKDEEIVEL--------------------------KAERNNTRL------LLEHLECLVSR- 137
Cdd:pfam01576 5 EEMQAKEEELQKVKERQQKAESELKELekkhqqlceeknalqeqlqaetelcaEAEEMRARLaarkqeLEEILHELESRl 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 138 ---HERSLRMTVMKRQAQNHagvssevevlkaLKSLFEHhkaLDEKVRERLRVAMERVAT------LEEELSTKGDENSS 208
Cdd:pfam01576 85 eeeEERSQQLQNEKKKMQQH------------IQDLEEQ---LDEEEAARQKLQLEKVTTeakikkLEEDILLLEDQNSK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 209 LkariaTYAAEAEEAMASNAPINGSISSESANRLIEMQEALERMKTELANSLKQstEITTRNaELEDQLTEDAREKHAAQ 288
Cdd:pfam01576 150 L-----SKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKK--EEKGRQ-ELEKAKRKLEGESTDLQ 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 289 ESIVRLKNQICELDAQRTDQETRITTFESRF--LTAQRESTC--IRDL---NDKLEHQLANKDAAVRLNEEKVHSLQERL 361
Cdd:pfam01576 222 EQIAELQAQIAELRAQLAKKEEELQAALARLeeETAQKNNALkkIRELeaqISELQEDLESERAARNKAEKQRRDLGEEL 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 362 ELAEKQLAQS--------------------LKKA--ESLPSVEAELQQR-----------MEALTAAEQKSVSAEERIQR 408
Cdd:pfam01576 302 EALKTELEDTldttaaqqelrskreqevteLKKAleEETRSHEAQLQEMrqkhtqaleelTEQLEQAKRNKANLEKAKQA 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 409 LDRNIQELSAELeRAVQRERMNEEHSQRlssTVDKLLSESNDRLQLHLKERMQALDDKNRLTQQLDGTKKIYDQAERIKD 488
Cdd:pfam01576 382 LESENAELQAEL-RTLQQAKQDSEHKRK---KLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNI 457
|
490 500
....*....|....*....|
gi 17569509 489 RLQRDNESLRQEIEALRQQL 508
Cdd:pfam01576 458 KLSKDVSSLESQLQDTQELL 477
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
357-508 |
6.46e-03 |
|
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.
Pssm-ID: 460211 [Multi-domain] Cd Length: 175 Bit Score: 38.78 E-value: 6.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 357 LQERLELAEKQLAQSLKKaeSLPSVEAELQQRMEALTAAEQKSVsaEERIQRLDRNIQELSAELERAVQ--RERMN---E 431
Cdd:pfam01442 27 LVDRLEKETEALRERLQK--DLEEVRAKLEPYLEELQAKLGQNV--EELRQRLEPYTEELRKRLNADAEelQEKLApygE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 432 EHSQRLSSTVDKL---LSESNDRLQLHLKERMQALddKNRLTQQLDGTKkiydqaERIKDRLQRDNESLRQEIEALRQQL 508
Cdd:pfam01442 103 ELRERLEQNVDALrarLAPYAEELRQKLAERLEEL--KESLAPYAEEVQ------AQLSQRLQELREKLEPQAEDLREKL 174
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
105-507 |
7.21e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.89 E-value: 7.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 105 EQLLEKDEEIVELKAERNNTRLLLEHLECLV-------------SRHERSLRMTVMKRQAQnHAGVSSEVEVLKALKSLF 171
Cdd:PTZ00121 1233 EEAKKDAEEAKKAEEERNNEEIRKFEEARMAhfarrqaaikaeeARKADELKKAEEKKKAD-EAKKAEEKKKADEAKKKA 1311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 172 EHHKALDE---KVRERLRVAMERVATLEEelSTKGDENSSLKARIATYAAEAEEAMASNAPINGSIS---SESANRLIEM 245
Cdd:PTZ00121 1312 EEAKKADEakkKAEEAKKKADAAKKKAEE--AKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAkkkADAAKKKAEE 1389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 246 QEALERMKTELANSLKQSTEITTRNAELE--DQLTEDAREKHAAQESIVRLKNQICELDAQRTDQETRITTFESRFLTAQ 323
Cdd:PTZ00121 1390 KKKADEAKKKAEEDKKKADELKKAAAAKKkaDEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEA 1469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 324 REStciRDLNDKLEHQLANKDAAVRLNEEKVHSLQERLELAEKQLAQSLKKAESLPSVEaELQQRMEALTAAEQKSVSAE 403
Cdd:PTZ00121 1470 KKA---DEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKAD-EAKKAEEAKKADEAKKAEEK 1545
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 404 ERIQRLDRNIQELSAELERAVQRERMNEEHSQRLSSTVDKLLSESNDRLQLHLKERMQALDDKNRLTQQldgtkkiyDQA 483
Cdd:PTZ00121 1546 KKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKK--------AEE 1617
|
410 420
....*....|....*....|....
gi 17569509 484 ERIKDRLQRDNESLRQEIEALRQQ 507
Cdd:PTZ00121 1618 AKIKAEELKKAEEEKKKVEQLKKK 1641
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
182-512 |
7.41e-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: 40.58 E-value: 7.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 182 RERLRVAMERVATLEEELSTKGDENSSLKARIATYAAEAeeamasnapiNGSISSESANRLIEMQEA----LERMKTELA 257
Cdd:pfam10174 184 TRRIAEAEMQLGHLEVLLDQKEKENIHLREELHRRNQLQ----------PDPAKTKALQTVIEMKDTkissLERNIRDLE 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 258 ---NSLKQSTEITTrnaeleDQLTEDAREKHAAQESIVRLKNQICELDAQRTDQETRITTFESRFLTAQRESTCIRDLND 334
Cdd:pfam10174 254 devQMLKTNGLLHT------EDREEEIKQMEVYKSHSKFMKNKIDQLKQELSKKESELLALQTKLETLTNQNSDCKQHIE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 335 KLEHQLANKDAAVRLNEEKVHSLQERLELAEKQLAQSLKKAESLPSVEAELQQRMEALtaaEQKSVSAEERIQRLDRNIQ 414
Cdd:pfam10174 328 VLKESLTAKEQRAAILQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDL---KDMLDVKERKINVLQKKIE 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 415 ELSAELeravqRERmneehsqrlsstvDKLLSEsndrlqlhLKERMQALD-DKNRLTQQLDGTKKIYDQAERIKDRLQ-- 491
Cdd:pfam10174 405 NLQEQL-----RDK-------------DKQLAG--------LKERVKSLQtDSSNTDTALTTLEEALSEKERIIERLKeq 458
|
330 340
....*....|....*....|...
gi 17569509 492 --RDNESLRQEIEALRQQLYNAR 512
Cdd:pfam10174 459 reREDRERLEELESLKKENKDLK 481
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
42-398 |
7.46e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.52 E-value: 7.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 42 NMLEDRDKLQEQLENYKVQLENAGLRTKEVEKERDmmkRQFEVHTQNLPQELQTMTRELCLLKEQLLEKDEEIVELKAER 121
Cdd:COG4717 160 ELEEELEELEAELAELQEELEELLEQLSLATEEEL---QDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENEL 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 122 NNTRLLLEHLECLVSRHERSLRMTVMKRQAQNHAGVSSEVEVLKALKSLFEHHKALDEKVRERLRVAMERVATLEEELST 201
Cdd:COG4717 237 EAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEEL 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 202 KGDENSSLKARIatyaaeaeeamasnaPINGSISSESANRLIEMQEALERMKTELANSLKQSteittRNAELEDQLTEDA 281
Cdd:COG4717 317 EEEELEELLAAL---------------GLPPDLSPEELLELLDRIEELQELLREAEELEEEL-----QLEELEQEIAALL 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569509 282 REKHAAQESIVRlknQICELDAQRTDQETRITTFESRFLTAQRESTCIRDLNDK--LEHQLANKDAAVRLNEEKVHSLQE 359
Cdd:COG4717 377 AEAGVEDEEELR---AALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEeeLEEELEELEEELEELEEELEELRE 453
|
330 340 350
....*....|....*....|....*....|....*....
gi 17569509 360 RLELAEKQLAQsLKKAESLPSVEAELQQRMEALTAAEQK 398
Cdd:COG4717 454 ELAELEAELEQ-LEEDGELAELLQELEELKAELRELAEE 491
|
|
| SAM_2 |
pfam07647 |
SAM domain (Sterile alpha motif); |
1039-1073 |
9.16e-03 |
|
SAM domain (Sterile alpha motif);
Pssm-ID: 429573 Cd Length: 66 Bit Score: 35.71 E-value: 9.16e-03
10 20 30
....*....|....*....|....*....|....*
gi 17569509 1039 VWSNERVQRWVEEIGLGVFSRNLVDSGIHGALIAL 1073
Cdd:pfam07647 3 SWSLESVADWLRSIGLEQYTDNFRDQGITGAELLL 37
|
|
| |
