|
Name |
Accession |
Description |
Interval |
E-value |
| 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 ... |
944-1009 |
6.48e-44 |
|
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: 153.01 E-value: 6.48e-44
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2017363561 944 MNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLKRL 1009
Cdd:cd09565 1 MNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRTHLKMVDSFHRTSLQYGILCLKRL 66
|
|
| 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 ... |
827-897 |
2.55e-42 |
|
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: 148.48 E-value: 2.55e-42
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2017363561 827 FAQWDGPTVVSWLELWVGMPAWYVAACRANVKSGAIMSALSDTEIQREIGISNALHRLKLRLAIQEMVSLT 897
Cdd:cd09562 1 FALWNGPTVVAWLELWVGMPAWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEMVSLT 71
|
|
| 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 ... |
1029-1100 |
3.36e-41 |
|
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: 145.54 E-value: 3.36e-41
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2017363561 1029 DVLVWTNDQVVHWVQSIGLRDYAGNLHESGVHGALLALDENFDHNTLALILQIPTQNTQARQVMEREFNNLL 1100
Cdd:cd09568 1 DVLVWSNERVIRWVQSIGLREYANNLLESGVHGALIALDETFDANSFALALQIPTQNTQARQILEREFNNLL 72
|
|
| SAM_liprin-kazrin_repeat2 |
cd09495 |
SAM domain of liprin/kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of ... |
948-1007 |
3.65e-31 |
|
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: 116.48 E-value: 3.65e-31
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 948 WIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLK 1007
Cdd:cd09495 1 WWVTRWLDDIGLPQYKDQFHESLVDRRMLQYLTVNDLLVHLKVTSQLHHLSLKCGIHVLH 60
|
|
| SAM_liprin-kazrin_repeat3 |
cd09496 |
SAM domain of liprin/kazrin proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 of ... |
1037-1098 |
7.19e-27 |
|
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: 104.16 E-value: 7.19e-27
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2017363561 1037 QVVHWVQSIGLRDYAGNLHESGVHGALLALDENFDHNTLALILQIPTQNTQARQVMEREFNN 1098
Cdd:cd09496 1 RVIHWIRSIDLREYANNLVESGVHGGLLVLEPNFDHNTMALVLQIPPQKTQARRHLETEFNN 62
|
|
| SAM_liprin-kazrin_repeat1 |
cd09494 |
SAM domain of liprin/kazrin proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of ... |
834-892 |
3.19e-25 |
|
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: 99.61 E-value: 3.19e-25
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 2017363561 834 TVVSWLELWVGMPaWYVAACRANVKSGAIMSALSDTEIQREIGISNALHRLKLRLAIQE 892
Cdd:cd09494 1 RVCAWLEDFGLMP-MYVIFCRQNVKSGHTLLTLSDQEMEKELGIKNPLHRKKLRLAIKE 58
|
|
| SAM_kazrin_repeat3 |
cd09570 |
SAM domain of kazrin proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 of kazrin ... |
1029-1100 |
2.09e-19 |
|
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: 83.26 E-value: 2.09e-19
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2017363561 1029 DVLVWTNDQVVHWVQSIGLRDYAGNLHESGVHGALLALDENFDHNTLALILQIPTQNTQARQVMEREFNNLL 1100
Cdd:cd09570 1 DPVVWTNQRVIKWARSIDLKEYADNLRDSGVHGALMVLEPSFNSDTMATALGIPSSKNIIRRHLTTEMEALV 72
|
|
| SAM_liprin-beta1,2_repeat3 |
cd09569 |
SAM domain of liprin-beta proteins repeat 3; SAM (sterile alpha motif) domain repea t3 of ... |
1029-1100 |
1.48e-16 |
|
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: 75.19 E-value: 1.48e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2017363561 1029 DVLVWTNDQVVHWVQSIGLRDYAGNLHESGVHGALLALDENFDHNTLALILQIPTQNTQARQVMEREFNNLL 1100
Cdd:cd09569 1 EVVLWTNHRVMEWLRSVDLAEYAPNLRGSGVHGALMVLEPRFTAETLAALLNIPPNKTLLRRHLATHFNQLL 72
|
|
| SAM_kazrin_repeat2 |
cd09567 |
SAM domain of kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of kazrin ... |
943-1007 |
2.48e-16 |
|
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: 74.37 E-value: 2.48e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2017363561 943 DMNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLK 1007
Cdd:cd09567 1 QLDHTWVAREWLRDLGLPQYSEAFREHLVDGRVLDTLSRKDLEKHLGVSKKFHQASLLRGIELLR 65
|
|
| SAM_liprin-beta1,2_repeat2 |
cd09566 |
SAM domain of liprin-beta1,2 proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of ... |
943-1007 |
2.54e-16 |
|
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: 74.27 E-value: 2.54e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2017363561 943 DMNHEWIgNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLrVHLKMVDSFHRTSLQYGIMCLK 1007
Cdd:cd09566 1 KLDTHWV-LRWLDDIGLPQYKDAFSEAKVDGRMLHYLTVDDL-LHLKVTSALHHASIRRGIQVLR 63
|
|
| SAM_kazrin_repeat1 |
cd09564 |
SAM domain of kazrin proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of kazrin ... |
828-892 |
1.09e-15 |
|
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: 72.87 E-value: 1.09e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2017363561 828 AQWDGPTVVSWLELWVGMPAwYVAACRANVKSGAIMSALSDTEIQREIGISNALHRLKLRLAIQE 892
Cdd:cd09564 2 SRWKADMVLAWLEVVMHMPM-YSKACAENVKSGKVLLGLSDSELESGLGISNVLHRRKLRLAIEE 65
|
|
| SAM_1 |
pfam00536 |
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ... |
943-1007 |
3.96e-14 |
|
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: 68.06 E-value: 3.96e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2017363561 943 DMNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRvHLKMVDSFHRTSLQYGIMCLK 1007
Cdd:pfam00536 1 DGWSVEDVGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDDLL-KLGVTLLGHRKKILYAIQRLK 64
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
221-469 |
5.04e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 73.82 E-value: 5.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 221 WKEDTGRVEELQELLEKQNFELSQARERlvtltttvteleedLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITT 300
Cdd:COG1196 241 LEELEAELEELEAELEELEAELAELEAE--------------LEELRLELEELELELEEAQAEEYELLAELARLEQDIAR 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 301 LEKRYLAAQ----REATSIHDLNDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELAQRIA 376
Cdd:COG1196 307 LEERRRELEerleELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAE 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 377 ALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLLSESNERLQLHLKERMAALEEKGRLS 456
Cdd:COG1196 387 ELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLA 466
|
250
....*....|...
gi 2017363561 457 EEIEKLRQEVDQL 469
Cdd:COG1196 467 ELLEEAALLEAAL 479
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
20-472 |
6.50e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 70.35 E-value: 6.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 20 ADADANFEQLMVNMLDEREKLLESLRESQETLAATQSRLQDAIHERDQLQRHLNSALpQEFATLTRELSMCREQLLEREE 99
Cdd:COG1196 329 EEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELA-EELLEALRAAAELAAQLEELEE 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 100 EISELKAERNNTRLLLEHLEclvSRHERSLRMTVVKRQAQSpsgvsSEVEVLKALKSLFEHHKALDEKVRERLRAALERV 179
Cdd:COG1196 408 AEEALLERLERLEEELEELE---EALAELEEEEEEEEEALE-----EAAEEEAELEEEEEALLELLAELLEEAALLEAAL 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 180 TTLEEQLAGAHQQVSALQQGAGVRDGAAEEEGTVELGPKR--------LWKEDTGRVEELQELLEKQNFELSQARERLVT 251
Cdd:COG1196 480 AELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLrglagavaVLIGVEAAYEAALEAALAAALQNIVVEDDEVA 559
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 252 LTTTVTELEEDLGTARR---DLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDkleneLAN 328
Cdd:COG1196 560 AAAIEYLKAAKAGRATFlplDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAAR-----LEA 634
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 329 KESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHgniEEHLRQLEGQLEEKNQELAR 408
Cdd:COG1196 635 ALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEE---ELELEEALLAEEEEERELAE 711
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2017363561 409 VRQREKMNEDHNKRLSDTVDRLLSESNERLQLHLKERMAALEEKGRLSEEIEKLRQEVDQLKGR 472
Cdd:COG1196 712 AEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLERE 775
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
159-474 |
7.19e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 69.97 E-value: 7.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 159 EHHKALDEKVRER-LRAALERVTTLEEQLAGAHQQVSALQqgagvrdgAAEEEGTVELgpkrlwKEDTGRVEELQELLEK 237
Cdd:COG1196 213 ERYRELKEELKELeAELLLLKLRELEAELEELEAELEELE--------AELEELEAEL------AELEAELEELRLELEE 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 238 QNFELSQARERLVTLTTTVTELEEDLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHD 317
Cdd:COG1196 279 LELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEA 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 318 LNDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEEHLRQLEG 397
Cdd:COG1196 359 ELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEE 438
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2017363561 398 QLEEKNQELARVRQREkmnedhnKRLSDTVDRLLSESNERLQLHLKERMAALEEKGRLSEEIEKLRQEVDQLKGRGG 474
Cdd:COG1196 439 EEEEALEEAAEEEAEL-------EEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLE 508
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
146-470 |
4.18e-11 |
|
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: 67.46 E-value: 4.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 146 SEVEVLKALKSLFEHHKALDEKVRERL--RAALERVTTLEEQLAGAHQQVSALQQGAGVRDGAAEEEGTVELGPKRLWKE 223
Cdd:pfam17380 266 TENEFLNQLLHIVQHQKAVSERQQQEKfeKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAME 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 224 DTGRVEELQelLEKQNFELSQARERLVTLTTTVTELEEDLGTARRDliKSEELsskhQRDLREALAQKEDMEERittlEK 303
Cdd:pfam17380 346 RERELERIR--QEERKRELERIRQEEIAMEISRMRELERLQMERQQ--KNERV----RQELEAARKVKILEEER----QR 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 304 RYLAAQREATSIhdlndKLENELANKESLHRQCEEKARHLQELLEvAEQKLQQTMrkaETLPEVEAELAQRIAALTKAEE 383
Cdd:pfam17380 414 KIQQQKVEMEQI-----RAEQEEARQREVRRLEEERAREMERVRL-EEQERQQQV---ERLRQQEEERKRKKLELEKEKR 484
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 384 RHGNIEEHLRQ-LEGQLEEKNQELARVRQREKM----NEDHNKRLSDTVDRLLSESNERLQLHLKER-------MAALEE 451
Cdd:pfam17380 485 DRKRAEEQRRKiLEKELEERKQAMIEEERKRKLlekeMEERQKAIYEEERRREAEEERRKQQEMEERrriqeqmRKATEE 564
|
330
....*....|....*....
gi 2017363561 452 KGRLsEEIEKLRQEVDQLK 470
Cdd:pfam17380 565 RSRL-EAMEREREMMRQIV 582
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
20-439 |
1.07e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 66.11 E-value: 1.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 20 ADADANFEQLMVNMLDEREKLLESLRESQETLAATQSRLQDAIHERDQLQRHLNSALPQEFATLTRELSmcreqlleREE 99
Cdd:COG1196 406 EEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAAL--------LEA 477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 100 EISELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSPSGVSSEVEVLKALKSLFEHH------KALDEKVRERLR 173
Cdd:COG1196 478 ALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAAleaalaAALQNIVVEDDE 557
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 174 AALERVTTLEEQLAGAHQQVSALQQGAGVRDGAAEEEGTVELGPKrlwkedtGRVEELQELLEKQNFELSQARERLVTLT 253
Cdd:COG1196 558 VAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVD-------LVASDLREADARYYVLGDTLLGRTLVAA 630
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 254 TTVTELEEDLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENELANKESLH 333
Cdd:COG1196 631 RLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELA 710
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 334 RQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEEHLRQLEGQLEEK---N----QEL 406
Cdd:COG1196 711 EAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEALgpvNllaiEEY 790
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 2017363561 407 ARVRQR-EKMNEDHN------KRLSDTVDRLLSESNERLQ 439
Cdd:COG1196 791 EELEERyDFLSEQREdleearETLEEAIEEIDRETRERFL 830
|
|
| SAM_liprin-beta1,2_repeat1 |
cd09563 |
SAM domain of liprin-beta1,2 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of ... |
827-891 |
1.12e-10 |
|
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: 58.39 E-value: 1.12e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2017363561 827 FAQWDGPTVVSWL-ELWVGMpawYVAACRANVKSGAIMSALSDTEIQREIGISNALHRLKLRLAIQ 891
Cdd:cd09563 1 FAEWSTEQVCDWLaELGLGQ---YVDECRRWVKSGQTLLKASPQELEKELGIKHPLHRKKLQLALQ 63
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
147-469 |
1.46e-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: 65.85 E-value: 1.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 147 EVEVLKALKSLFEHHKALDEkVRERLRAALERVTTLEEQLAGAHQQVSALQQGAGVRDGAAEEEGTVElgpkrlwKEDTG 226
Cdd:TIGR02168 711 EEELEQLRKELEELSRQISA-LRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEEL-------AEAEA 782
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 227 RVEELQELLEKQNFELSQARERLVTLTTTVTELEEDLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYL 306
Cdd:TIGR02168 783 EIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIE 862
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 307 AAQREATSIHDLNDKLENELANkeslhrqceekarhLQELLEVAEQKLQQTMrkaETLPEVEAELAQRIAALTKAEERHG 386
Cdd:TIGR02168 863 ELEELIEELESELEALLNERAS--------------LEEALALLRSELEELS---EELRELESKRSELRRELEELREKLA 925
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 387 NIEEHLRQLEGQLEEKNQelaRVRQREKMNEDHNKRLSDTVDRLLSESNERLQLHLKER-------MAALEEKGRLSEEI 459
Cdd:TIGR02168 926 QLELRLEGLEVRIDNLQE---RLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIkelgpvnLAAIEEYEELKERY 1002
|
330
....*....|
gi 2017363561 460 EKLRQEVDQL 469
Cdd:TIGR02168 1003 DFLTAQKEDL 1012
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
170-469 |
2.29e-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: 65.08 E-value: 2.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 170 ERLRAALERVT----TLEEQLAGAHQQVSALQQGAGVRdgaaEEEGTVELgpkRLWkedTGRVEELQELLEKQNFELSQA 245
Cdd:TIGR02168 182 ERTRENLDRLEdilnELERQLKSLERQAEKAERYKELK----AELRELEL---ALL---VLRLEELREELEELQEELKEA 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 246 RERLVtltttvteleedlgTARRDLIKSEELSSKHQRDLREalaqkedMEERITTLEKRYLAAQREatsIHDLNDKLENE 325
Cdd:TIGR02168 252 EEELE--------------ELTAELQELEEKLEELRLEVSE-------LEEEIEELQKELYALANE---ISRLEQQKQIL 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 326 LANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQE 405
Cdd:TIGR02168 308 RERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSK 387
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2017363561 406 LARVRQREKM-------NEDHNKRLSDTVDRLLSESNERLQ-LHLKERMAALEEKGRLSEEIEKLRQEVDQL 469
Cdd:TIGR02168 388 VAQLELQIASlnneierLEARLERLEDRRERLQQEIEELLKkLEEAELKELQAELEELEEELEELQEELERL 459
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
278-473 |
2.50e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 64.94 E-value: 2.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 278 SKHQRDLREALAQKEDMEERITTLE------KRYLAAQREATSIHDLNDKLENELAnkeslhrqcEEKARHLQELLEVAE 351
Cdd:COG4913 231 VEHFDDLERAHEALEDAREQIELLEpirelaERYAAARERLAELEYLRAALRLWFA---------QRRLELLEAELEELR 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 352 QKLQQTMRKAETLPEVEAELAQRIAALTKAEERHG-----NIEEHLRQLEGQLEEKNQELARVRQREKM-------NEDH 419
Cdd:COG4913 302 AELARLEAELERLEARLDALREELDELEAQIRGNGgdrleQLEREIERLERELEERERRRARLEALLAAlglplpaSAEE 381
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2017363561 420 NKRLSDTVDRLLSESNERLQLHLKERMAALEEKGRLSEEIEKLRQEVDQLKGRG 473
Cdd:COG4913 382 FAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRK 435
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
159-468 |
2.53e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 65.16 E-value: 2.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 159 EHHKALDEKVRERLRAALERVTTLEEQLAGAHQQVSALQQGAGVRDgaAEEEGTVElgPKRLWKEDTG----RVEELQEL 234
Cdd:PTZ00121 1514 EAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKK--AEEKKKAE--EAKKAEEDKNmalrKAEEAKKA 1589
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 235 LEKQNFELSQARERLVTLTTTVTELEEDLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQREATs 314
Cdd:PTZ00121 1590 EEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAK- 1668
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 315 ihdlndKLENELANKESLHRQCEEKARHLQELLEVAEQKlqqtmRKAETLPEVEAELAQRIAALTKAEERHGNIEEHLRQ 394
Cdd:PTZ00121 1669 ------KAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEA-----KKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKK 1737
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2017363561 395 lEGQLEEKNQELARVRQREKmnedhnkrlsDTVDRLLSESNERLQLHLKERMAALEEKgrLSEEIEKLRQEVDQ 468
Cdd:PTZ00121 1738 -EAEEDKKKAEEAKKDEEEK----------KKIAHLKKEEEKKAEEIRKEKEAVIEEE--LDEEDEKRRMEVDK 1798
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
218-472 |
6.04e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 63.93 E-value: 6.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 218 KRLWKEDTGRVEELQELLEKQNFELSQARERLVTLTTTVTELEEDLGTARRDLIKSEE----LSSKHQRDLREALAQKED 293
Cdd:TIGR02169 155 RRKIIDEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERyqalLKEKREYEGYELLKEKEA 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 294 MEERITTLEKRYLAAQREATSIHDLNDKLENELANKESLHRQCEEKARHL--QELLEVAEQ--KLQQTMRKAE-TLPEVE 368
Cdd:TIGR02169 235 LERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgeEEQLRVKEKigELEAEIASLErSIAEKE 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 369 AELAQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQ-----REKMN------EDHNKRLSDTVDRL------L 431
Cdd:TIGR02169 315 RELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEeyaelKEELEdlraelEEVDKEFAETRDELkdyrekL 394
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 2017363561 432 SESNERLQLHLKERMAALEEKGRLSEEIEKLRQEVDQLKGR 472
Cdd:TIGR02169 395 EKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAK 435
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
267-472 |
1.12e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 63.03 E-value: 1.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 267 RRDLIksEELS--SKHQRDLREALAQKEDMEERIT-------TLEKRY--LAAQRE-ATSIHDLNDKLEnELANKESLHR 334
Cdd:COG1196 157 RRAII--EEAAgiSKYKERKEEAERKLEATEENLErledilgELERQLepLERQAEkAERYRELKEELK-ELEAELLLLK 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 335 qceekARHLQELLEVAEQKLQQTMRKAETLpevEAELAQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQREK 414
Cdd:COG1196 234 -----LRELEAELEELEAELEELEAELEEL---EAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIA 305
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2017363561 415 MNEDHNKRLSDTVDRL---LSESNERLQLHLKERMAALEEKGRLSEEIEKLRQEVDQLKGR 472
Cdd:COG1196 306 RLEERRRELEERLEELeeeLAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEA 366
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
37-409 |
1.79e-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: 62.38 E-value: 1.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 37 REKLLESLRESQETLAatqsRLQDAIHERD-QLQR-HLNSALPQEFATLTRELSmcREQLLEREEEISELKAERNNTRLL 114
Cdd:TIGR02168 174 RKETERKLERTRENLD----RLEDILNELErQLKSlERQAEKAERYKELKAELR--ELELALLVLRLEELREELEELQEE 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 115 LEHLECLVSRHERSLRMTvvkrqaqspsgvSSEVEVLKALKSlfEHHKALDEkVRERLRAALERVTTLEEQLAGAHQQVS 194
Cdd:TIGR02168 248 LKEAEEELEELTAELQEL------------EEKLEELRLEVS--ELEEEIEE-LQKELYALANEISRLEQQKQILRERLA 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 195 ALQQGAGVRDGAAEEEGTVELGPKRLWKEDTGRVEELQELLEKQNFELSQARERLVTLTTTVTELEEDLGTARRDLIKSE 274
Cdd:TIGR02168 313 NLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLE 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 275 ELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQREATS-----IHDLNDKLENELANKESLHRQCEEKARHLQELLEV 349
Cdd:TIGR02168 393 LQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEaelkeLQAELEELEEELEELQEELERLEEALEELREELEE 472
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 350 AEQKLQQTMRKaetlpevEAELAQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARV 409
Cdd:TIGR02168 473 AEQALDAAERE-------LAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVL 525
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
34-470 |
3.71e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 61.23 E-value: 3.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 34 LDEREKLLESLRESQETLAATQSRLQDAIHERDQLQRHLNS---------ALPQEFATLTRELSMCREQLLEREEEISEL 104
Cdd:PRK03918 240 IEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEkvkelkelkEKAEEYIKLSEFYEEYLDELREIEKRLSRL 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 105 KAERNNTRLLLEHLECLVSR-HERSLRMTVVKRQAQSPSGVSSEVEVLKALKSLFEHHKALD-----EKVRERLRAALER 178
Cdd:PRK03918 320 EEEINGIEERIKELEEKEERlEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLtgltpEKLEKELEELEKA 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 179 VTTLEEQLAGAHQQVSALQQGAGVRDGAAEE----EGTVELGPKRLWKEDTGRV-EELQELLEKQNFELSQARERLVTLT 253
Cdd:PRK03918 400 KEEIEEEISKITARIGELKKEIKELKKAIEElkkaKGKCPVCGRELTEEHRKELlEEYTAELKRIEKELKEIEEKERKLR 479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 254 TTVTELEEDLGTARR--------DLIKS--EELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDK-- 321
Cdd:PRK03918 480 KELRELEKVLKKESEliklkelaEQLKEleEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKla 559
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 322 -LENELANKES----LHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEEHLRQLE 396
Cdd:PRK03918 560 eLEKKLDELEEelaeLLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETE 639
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 397 GQLEEKNQELARVRQreKMNEDHNKRLSDTVDRL------LSESNERLQLHLKERMAALEEKGRLSEEIEKLRQEVDQLK 470
Cdd:PRK03918 640 KRLEELRKELEELEK--KYSEEEYEELREEYLELsrelagLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLE 717
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
38-469 |
4.79e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 60.82 E-value: 4.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 38 EKLLESLRESQETLAATQSRLQDA-IHERdqlqrhLNsALPQEFATLTRElsmcreqllereeeISELKAERNNTRLLLE 116
Cdd:PRK02224 179 ERVLSDQRGSLDQLKAQIEEKEEKdLHER------LN-GLESELAELDEE--------------IERYEEQREQARETRD 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 117 HLECLVSRHERSLrmtvvkrqaqspsgvsSEVEVLKALKSLFEHHKALDEKVRERLRaalERVTTLEEQLAGAHQQVSAL 196
Cdd:PRK02224 238 EADEVLEEHEERR----------------EELETLEAEIEDLRETIAETEREREELA---EEVRDLRERLEELEEERDDL 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 197 QQGAGVRDGAAEeegTVELGPKRLWKEDtgrvEELQELLEKQNFELSQARERLVTLTTTVTELEEDLGTARRDLIKSEEL 276
Cdd:PRK02224 299 LAEAGLDDADAE---AVEARREELEDRD----EELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESE 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 277 SSKHQRDLREALAQKEDMEERITTLEKRYLAAqreATSIHDLNDKLENELANKESLHRQCEEkarhlqelLEVAEQKLQQ 356
Cdd:PRK02224 372 LEEAREAVEDRREEIEELEEEIEELRERFGDA---PVDLGNAEDFLEELREERDELREREAE--------LEATLRTARE 440
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 357 TMRKAETL------PEVEAEL--AQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQRekmnedhnKRLSDTVD 428
Cdd:PRK02224 441 RVEEAEALleagkcPECGQPVegSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDL--------VEAEDRIE 512
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 2017363561 429 RLLsESNERLQLHLKERMAALEEKgrlSEEIEKLRQEVDQL 469
Cdd:PRK02224 513 RLE-ERREDLEELIAERRETIEEK---RERAEELRERAAEL 549
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
280-472 |
1.61e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 59.16 E-value: 1.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 280 HQRDLREALAQK----EDMEERITTLEKRYLAAQREAtsihdlnDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQ 355
Cdd:COG4913 590 HEKDDRRRIRSRyvlgFDNRAKLAALEAELAELEEEL-------AEAEERLEALEAELDALQERREALQRLAEYSWDEID 662
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 356 qTMRKAETLPEVEAELAQRIAA---LTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLLS 432
Cdd:COG4913 663 -VASAEREIAELEAELERLDASsddLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAED 741
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2017363561 433 ESNERLQLHLKERMAALEEKGRLSEEIEKLRQEVDQLKGR 472
Cdd:COG4913 742 LARLELRALLEERFAAALGDAVERELRENLEERIDALRAR 781
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
227-474 |
1.79e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.92 E-value: 1.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 227 RVEELQELLEKQNFELSQARERLVTLTTTVTELEEDLGTARRDLIKSEELSSK---HQRDLREALAQKEDMEERITTLEK 303
Cdd:PRK03918 187 RTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEieeLEKELESLEGSKRKLEEKIRELEE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 304 RylaaqreatsIHDLNDKLEnELANKESLHRQCEEKA---RHLQELLEVAEQKLQQTMRKAETLPEVEAELAQRIAALTK 380
Cdd:PRK03918 267 R----------IEELKKEIE-ELEEKVKELKELKEKAeeyIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEE 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 381 AEERHGNIEEHLRQLE---GQLEEKNQELARVRQREKMNEDHNKRLSDtvdrllsESNERLQLHLKErmaALEEKGRLSE 457
Cdd:PRK03918 336 KEERLEELKKKLKELEkrlEELEERHELYEEAKAKKEELERLKKRLTG-------LTPEKLEKELEE---LEKAKEEIEE 405
|
250
....*....|....*..
gi 2017363561 458 EIEKLRQEVDQLKGRGG 474
Cdd:PRK03918 406 EISKITARIGELKKEIK 422
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
9-469 |
1.87e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 58.63 E-value: 1.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 9 NEGDRLGPPHGADADANFEQL--MVNMLDEREKLLESLRESQETLAATQSRLQDAIHERDQLQRHLNS--------ALPQ 78
Cdd:COG4717 53 KEADELFKPQGRKPELNLKELkeLEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKlekllqllPLYQ 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 79 EFATLTRELSMCREQLLEREEEISELKAERNNTRLLLEHLEclvsRHERSLRMTVVKRQAQSPSGVSSEVEVLKALKSLF 158
Cdd:COG4717 133 ELEALEAELAELPERLEELEERLEELRELEEELEELEAELA----ELQEELEELLEQLSLATEEELQDLAEELEELQQRL 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 159 EHHKALDEKVRERLRAALERVTTLEEQLAGAH--QQVSALQQGAGVRDGAAEEEGTVELGPKRLWKED------TGRVEE 230
Cdd:COG4717 209 AELEEELEEAQEELEELEEELEQLENELEAAAleERLKEARLLLLIAAALLALLGLGGSLLSLILTIAgvlflvLGLLAL 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 231 LQELLEKQNFELSQARERLVTLTTTVTELEEDLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQR 310
Cdd:COG4717 289 LFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEEL 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 311 EATSIHDLND---KLENELANKESLHRQCEEkarhLQELLEVAEQKLqqtmrkAETLPEVEAELAQriAALTKAEERHGN 387
Cdd:COG4717 369 EQEIAALLAEagvEDEEELRAALEQAEEYQE----LKEELEELEEQL------EELLGELEELLEA--LDEEELEEELEE 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 388 IEEHLRQLEGQLEEKNQELARvrqrekmnedhnkrlsdtvdrllsesnerlqlhLKERMAALEEKGRLSE---EIEKLRQ 464
Cdd:COG4717 437 LEEELEELEEELEELREELAE---------------------------------LEAELEQLEEDGELAEllqELEELKA 483
|
....*
gi 2017363561 465 EVDQL 469
Cdd:COG4717 484 ELREL 488
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
262-475 |
2.29e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.54 E-value: 2.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 262 DLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENELANKESLHRQCEEKAR 341
Cdd:PRK03918 159 DYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKE 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 342 HLQEL----------LEVAEQKLQQTMRKAETLPEVEAEL---AQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELAR 408
Cdd:PRK03918 239 EIEELekeleslegsKRKLEEKIRELEERIEELKKEIEELeekVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSR 318
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2017363561 409 VRQREKMNEDHNKRLSDTVDRLlsESNERLQLHLKERMAALEEKGRLSEEIEKLRQEVDQLKGRGGP 475
Cdd:PRK03918 319 LEEEINGIEERIKELEEKEERL--EELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTG 383
|
|
| SAM |
smart00454 |
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ... |
827-893 |
3.43e-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: 51.53 E-value: 3.43e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2017363561 827 FAQWDGPTVVSWLELWvGMPAwYVAACRANVKSGAIMSALSDTEIQREIGISNALHRLKLRLAIQEM 893
Cdd:smart00454 1 VSQWSPESVADWLESI-GLEQ-YADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKL 65
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
229-470 |
4.07e-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: 57.77 E-value: 4.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 229 EELQELLEKQNFELSQARERLVTLTTTVTELEEDLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRyLAA 308
Cdd:TIGR02169 691 SSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEAR-IEE 769
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 309 QREAtsIHDLNDKLEN--------ELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELAQRIAALtk 380
Cdd:TIGR02169 770 LEED--LHKLEEALNDlearlshsRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDL-- 845
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 381 aEERHGNIEEHLRQLEGQLEEKNQELARVRQREKmneDHNKRLSDtvdrlLSESNERLQLHLKErmaALEEKGRLSEEIE 460
Cdd:TIGR02169 846 -KEQIKSIEKEIENLNGKKEELEEELEELEAALR---DLESRLGD-----LKKERDELEAQLRE---LERKIEELEAQIE 913
|
250
....*....|
gi 2017363561 461 KLRQEVDQLK 470
Cdd:TIGR02169 914 KKRKRLSELK 923
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
272-470 |
4.36e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.47 E-value: 4.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 272 KSEELSSKHQRDLREALAQKEDMEERIttlekrylaaqREATSIHDLNDKLENELANKESLHRQCEEKARHLQELLEVAE 351
Cdd:COG4717 54 EADELFKPQGRKPELNLKELKELEEEL-----------KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 352 QKLQQTMRKAEtLPEVEAELAQRIAALTKAEERHgnieEHLRQLEGQLEEKNQELARVRQREkmnEDHNKRLSDTVDRLL 431
Cdd:COG4717 123 KLLQLLPLYQE-LEALEAELAELPERLEELEERL----EELRELEEELEELEAELAELQEEL---EELLEQLSLATEEEL 194
|
170 180 190
....*....|....*....|....*....|....*....
gi 2017363561 432 SESNERLQLHLKERMAALEEKGRLSEEIEKLRQEVDQLK 470
Cdd:COG4717 195 QDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLE 233
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
31-461 |
5.36e-08 |
|
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: 57.42 E-value: 5.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 31 VNMLDEREKLL-ESLRESQETLAATQSRLQDAiheRDQLQRHLNS--ALPQEFATLTRELSMCREQLLEREEE------- 100
Cdd:pfam05483 270 ANQLEEKTKLQdENLKELIEKKDHLTKELEDI---KMSLQRSMSTqkALEEDLQIATKTICQLTEEKEAQMEElnkakaa 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 101 ----ISELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSpsgvsSEVEVLKALKS-----LFEHHKALDEKvrER 171
Cdd:pfam05483 347 hsfvVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKS-----SELEEMTKFKNnkeveLEELKKILAED--EK 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 172 LRAALERVTTLEEQLAGAHQQVSALQQGAGVRDGAAEEEGTVELGPKRLWKEDtgrVEELQELLEKQ---NFELSQARER 248
Cdd:pfam05483 420 LLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKE---VEDLKTELEKEklkNIELTAHCDK 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 249 LVTLTTTVTELEEDLgtarrdlikSEELSsKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHD----LNDKLEN 324
Cdd:pfam05483 497 LLLENKELTQEASDM---------TLELK-KHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREefiqKGDEVKC 566
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 325 ELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELAQRIAALTK---AEERHGNIEE-HLRQLEGQLE 400
Cdd:pfam05483 567 KLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKkgsAENKQLNAYEiKVNKLELELA 646
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2017363561 401 EKNQELarvrqrEKMNEDHNKRLSdtvDRLLSEsnERLQLHLKERMAALEEKGRLSEEIEK 461
Cdd:pfam05483 647 SAKQKF------EEIIDNYQKEIE---DKKISE--EKLLEEVEKAKAIADEAVKLQKEIDK 696
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
21-639 |
5.75e-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: 57.44 E-value: 5.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 21 DADANFEQLMVNMLDErEKLLESLREsqeTLAATQSRLQDAIHERDQLQ----RHLNSALPQEFATLTRELSMCREQLLE 96
Cdd:pfam15921 167 DSNTQIEQLRKMMLSH-EGVLQEIRS---ILVDFEEASGKKIYEHDSMStmhfRSLGSAISKILRELDTEISYLKGRIFP 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 97 REEEISELKAE-RNNTRLLLEH----LECLVSRHERSL-----RMTVVKRQAQSpsgVSSEVEV------------LKAL 154
Cdd:pfam15921 243 VEDQLEALKSEsQNKIELLLQQhqdrIEQLISEHEVEItglteKASSARSQANS---IQSQLEIiqeqarnqnsmyMRQL 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 155 KSLFEHHKALDEKVRERLRAALERVTTLEEQLAGAHqqvSALQQGAGVRDGAAEEEGTV----------------ELG-- 216
Cdd:pfam15921 320 SDLESTVSQLRSELREAKRMYEDKIEELEKQLVLAN---SELTEARTERDQFSQESGNLddqlqklladlhkrekELSle 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 217 ---PKRLWKEDTG-----------------RVEELQELLEKQNFELSQARERLVTLTTTVTELEEDLG--TARRDLIKS- 273
Cdd:pfam15921 397 keqNKRLWDRDTGnsitidhlrrelddrnmEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSslTAQLESTKEm 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 274 -----EELSSKHQ---------RDLREALAQKEDMEE----RITTLEKRYLAAQREATSIHDLNDKLENELANKESLHRQ 335
Cdd:pfam15921 477 lrkvvEELTAKKMtlessertvSDLTASLQEKERAIEatnaEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQ 556
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 336 CEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELAQriaaltkaeerhgnIEEHLRQLEGQLEE----KNQELARVRQ 411
Cdd:pfam15921 557 MAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQ--------------LEKEINDRRLELQEfkilKDKKDAKIRE 622
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 412 REkmnedhnKRLSDtvdrllsesnerLQLHLKERMAALEEKGRLSEEIeklRQEVDQLkgrggpfvdgvhsrshMGSAAD 491
Cdd:pfam15921 623 LE-------ARVSD------------LELEKVKLVNAGSERLRAVKDI---KQERDQL----------------LNEVKT 664
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 492 VRFSLGTTTHAPPGVHRRYSALREEsaKDWETSPLPGMLAPAAGPAFDSDPEISDVdEDEPGGLVGSA-----DVVSPSG 566
Cdd:pfam15921 665 SRNELNSLSEDYEVLKRNFRNKSEE--METTTNKLKMQLKSAQSELEQTRNTLKSM-EGSDGHAMKVAmgmqkQITAKRG 741
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2017363561 567 HSDA-QTLAMMLQEQLDAINEEIRMIQEEKE--STELRAEEIETRVTSGSMEALNLKQLRKRGSIPTSLTALSLAS 639
Cdd:pfam15921 742 QIDAlQSKIQFLEEAMTNANKEKHFLKEEKNklSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKAS 817
|
|
| SAM |
smart00454 |
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ... |
952-1007 |
6.75e-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: 50.37 E-value: 6.75e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2017363561 952 EWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLK 1007
Cdd:smart00454 11 DWLESIGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKLK 66
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
142-472 |
1.13e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 56.23 E-value: 1.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 142 SGVSSEVEVLKALKSLFEHHKALDEKVRERLRAALERVTTLEEQLAGAHQQVSALqqgagvrdgaaeeegtvelgpkrlw 221
Cdd:PRK03918 224 EKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEEL------------------------- 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 222 KEDTGRVEELQElLEKQNFELSQARERLVTLTTTVTELEEDLGTARRDLIKS-EELSSKHQRdLREALAQKEDMEERITT 300
Cdd:PRK03918 279 EEKVKELKELKE-KAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERiKELEEKEER-LEELKKKLKELEKRLEE 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 301 LEKRYLAAQrEATSIHDLNDKLENELANKESlhrqceEKarhLQELLEVAEQKLQQTMRKAETLPEVEAELAQRIAALTK 380
Cdd:PRK03918 357 LEERHELYE-EAKAKKEELERLKKRLTGLTP------EK---LEKELEELEKAKEEIEEEISKITARIGELKKEIKELKK 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 381 AEER-----------HGNIEEHLRqlEGQLEEKNQELARVRQREKMNEDHNKRLSD---TVDRLLSESNERLQLH-LKER 445
Cdd:PRK03918 427 AIEElkkakgkcpvcGRELTEEHR--KELLEEYTAELKRIEKELKEIEEKERKLRKelrELEKVLKKESELIKLKeLAEQ 504
|
330 340 350
....*....|....*....|....*....|....*.
gi 2017363561 446 MAALEEK---------GRLSEEIEKLRQEVDQLKGR 472
Cdd:PRK03918 505 LKELEEKlkkynleelEKKAEEYEKLKEKLIKLKGE 540
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
135-470 |
2.53e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 55.53 E-value: 2.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 135 KRQAQSPSGVSSEVEVLKALKSLFEHHKALDE--KVRERLRAALERVTTLEEQLAGAHQQVSALQQGAGVRDGAAEEEGT 212
Cdd:PTZ00121 1417 KKKADEAKKKAEEKKKADEAKKKAEEAKKADEakKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAK 1496
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 213 VELGPKRLWKEDTGRVEELQELLEKQNF-ELSQARERLVTLTTTVTELEEDLGTARrdliKSEELssKHQRDLREALAQK 291
Cdd:PTZ00121 1497 KKADEAKKAAEAKKKADEAKKAEEAKKAdEAKKAEEAKKADEAKKAEEKKKADELK----KAEEL--KKAEEKKKAEEAK 1570
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 292 EDMEERITTLEKRYLAAQREATSIHDLNDKLENELANKESLHRQCEEKARHLQELLEVAEQKlqqtmRKAETLPEVEAEL 371
Cdd:PTZ00121 1571 KAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEK-----KKVEQLKKKEAEE 1645
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 372 AQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDtvdrllsESNERLQLHLKErmaalEE 451
Cdd:PTZ00121 1646 KKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAE-------EAKKAEELKKKE-----AE 1713
|
330 340
....*....|....*....|...
gi 2017363561 452 KGRLSEEIEKLRQE----VDQLK 470
Cdd:PTZ00121 1714 EKKKAEELKKAEEEnkikAEEAK 1736
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
146-470 |
3.36e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 55.06 E-value: 3.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 146 SEVEVLKALKSLFEHHKALDEkVRERLRAALERVTTLEEQLAGAHQQVSALQQGAGVRDGAAEEEgtvelgpkrlwkedT 225
Cdd:TIGR02168 223 RELELALLVLRLEELREELEE-LQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEEL--------------Q 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 226 GRVEELQELLEKQNFELSQARERLVTLTTTVTELEEDLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRY 305
Cdd:TIGR02168 288 KELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAEL 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 306 LAAqreatsiHDLNDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEerh 385
Cdd:TIGR02168 368 EEL-------ESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKE--- 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 386 gnieehlrqLEGQLEEKNQELARVRQREkmnEDHNKRLSDTVDRLLSESNERLQL-----HLKERMAALEekgRLSEEIE 460
Cdd:TIGR02168 438 ---------LQAELEELEEELEELQEEL---ERLEEALEELREELEEAEQALDAAerelaQLQARLDSLE---RLQENLE 502
|
330
....*....|
gi 2017363561 461 KLRQEVDQLK 470
Cdd:TIGR02168 503 GFSEGVKALL 512
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
35-470 |
3.87e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 54.68 E-value: 3.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 35 DEREKLLESLRESQETLAATQSRLQDAIHERDQLqrhlNSALPQefatLTRELSMcreqLLEREEEISELKAERNNTRLL 114
Cdd:PRK03918 179 ERLEKFIKRTENIEELIKEKEKELEEVLREINEI----SSELPE----LREELEK----LEKEVKELEELKEEIEELEKE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 115 LEHLECLVSRHERSLRMTV-----VKRQAQSPSGVSSEVEVLKALKSLFEHHKALDEKVRERLRAALERVTTLEEQLAGA 189
Cdd:PRK03918 247 LESLEGSKRKLEEKIRELEerieeLKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGI 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 190 HQQVSALQQG-----------AGVRDGAAEEEGTVELG-------------PKRLWKEDTGRVEELQELLEKQNFELSQA 245
Cdd:PRK03918 327 EERIKELEEKeerleelkkklKELEKRLEELEERHELYeeakakkeelerlKKRLTGLTPEKLEKELEELEKAKEEIEEE 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 246 RERLVTLTTTVTELEEDLGTARRDLIKS----------------EELSSKHQRDLREALAQKEDMEERITTLEKR----- 304
Cdd:PRK03918 407 ISKITARIGELKKEIKELKKAIEELKKAkgkcpvcgrelteehrKELLEEYTAELKRIEKELKEIEEKERKLRKElrele 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 305 -YLAAQREATSIHDLNDKLEN-----ELANKESLHRQCEEkARHLQELLEVAEQKLQQTMRKAETLPEVEAELAQRIAAL 378
Cdd:PRK03918 487 kVLKKESELIKLKELAEQLKEleeklKKYNLEELEKKAEE-YEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKL 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 379 TKAEERHGNIEEHLRQL----EGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLlsesnERLQLHLKErmaALEEKGR 454
Cdd:PRK03918 566 DELEEELAELLKELEELgfesVEELEERLKELEPFYNEYLELKDAEKELEREEKEL-----KKLEEELDK---AFEELAE 637
|
490
....*....|....*.
gi 2017363561 455 LSEEIEKLRQEVDQLK 470
Cdd:PRK03918 638 TEKRLEELRKELEELE 653
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
281-470 |
4.95e-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: 53.61 E-value: 4.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 281 QRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRK 360
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 361 AETLpevEAELAQRIAALTK------------------AEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKR 422
Cdd:COG4942 99 LEAQ---KEELAELLRALYRlgrqpplalllspedfldAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2017363561 423 LSDTVDRlLSESNERLQLHLKERMAALEekgRLSEEIEKLRQEVDQLK 470
Cdd:COG4942 176 LEALLAE-LEEERAALEALKAERQKLLA---RLEKELAELAAELAELQ 219
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
284-464 |
5.41e-07 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 52.23 E-value: 5.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 284 LREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENELANKESLHRQCEEKARHLQELL-EVAEQKLQQTMRKae 362
Cdd:COG1579 19 LDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLgNVRNNKEYEALQK-- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 363 tlpEVEAelaqriaaltkAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLLSESNERLQLHL 442
Cdd:COG1579 97 ---EIES-----------LKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELE 162
|
170 180
....*....|....*....|...
gi 2017363561 443 KERMAALEE-KGRLSEEIEKLRQ 464
Cdd:COG1579 163 AEREELAAKiPPELLALYERIRK 185
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
34-474 |
6.84e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 53.89 E-value: 6.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 34 LDEREKLLESLRESQE---TLAATQSRLQDAIHERDQlqrhlnsalpqEFATLTRELSMCREQLLEREEEISELKAERNN 110
Cdd:PRK02224 236 RDEADEVLEEHEERREeleTLEAEIEDLRETIAETER-----------EREELAEEVRDLRERLEELEEERDDLLAEAGL 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 111 TRL----LLEHLECLVSRHERSLRMTVVKRQAQSPSGVSSEVEVLKAL------KSLFEHHKALD---EKVRERLRAALE 177
Cdd:PRK02224 305 DDAdaeaVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADdleeraEELREEAAELEselEEAREAVEDRRE 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 178 RVTTLEEQLAGAHQQVS----ALQQGAGVRDGAAEEEGTVELGPKRL---WKEDTGRVEELQELLEK-------QNFELS 243
Cdd:PRK02224 385 EIEELEEEIEELRERFGdapvDLGNAEDFLEELREERDELREREAELeatLRTARERVEEAEALLEAgkcpecgQPVEGS 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 244 QARERLVTLTTTVTELEEDLGTARRDLiksEELSSKHQR--DLREALAQKEDMEERITTLEKRylAAQREATsIHDLNDK 321
Cdd:PRK02224 465 PHVETIEEDRERVEELEAELEDLEEEV---EEVEERLERaeDLVEAEDRIERLEERREDLEEL--IAERRET-IEEKRER 538
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 322 LENELANKESLHRQCEEKARHLQELLEVAEQKLQqtmrKAETLPEVEAELAQRIAALTKAEERHGNIEEHLRQLEgQLEE 401
Cdd:PRK02224 539 AEELRERAAELEAEAEEKREAAAEAEEEAEEARE----EVAELNSKLAELKERIESLERIRTLLAAIADAEDEIE-RLRE 613
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2017363561 402 KNQELArvrqreKMNEDHNKRLSDTVDR---LLSESNE-RLQLHLKERMAALEEKGRLSEEIEKLRQEVDQLKGRGG 474
Cdd:PRK02224 614 KREALA------ELNDERRERLAEKRERkreLEAEFDEaRIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIG 684
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
34-470 |
7.05e-07 |
|
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: 53.69 E-value: 7.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 34 LDEREKLLESLRESQETLAATQSRLQDAIHERDQLQRHLNSALPQEFATLTRELSmcrEQLLEREEEISELKAERNNTRl 113
Cdd:pfam12128 246 LQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWK---EKRDELNGELSAADAAVAKDR- 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 114 llEHLECLVSRHERSLRMTVVKR---QAQSPSgVSSEVEVL-KALKSLFEHHKALDEKVrERLRAAleRVTTLEEQLAGA 189
Cdd:pfam12128 322 --SELEALEDQHGAFLDADIETAaadQEQLPS-WQSELENLeERLKALTGKHQDVTAKY-NRRRSK--IKEQNNRDIAGI 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 190 HQQVSALQQGAgVRdGAAEEEGTVElgpkrlwkedtGRVEELQELLEKQNFELSQARERLVTLTTTVTELEEDLgTARRD 269
Cdd:pfam12128 396 KDKLAKIREAR-DR-QLAVAEDDLQ-----------ALESELREQLEAGKLEFNEEEYRLKSRLGELKLRLNQA-TATPE 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 270 LIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENELANK-ESLHRQCEEKARHLQELLE 348
Cdd:pfam12128 462 LLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSAlDELELQLFPQAGTLLHFLR 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 349 VAEQKLQQTMRK---AETL------PEV-----------------------------EAELAQRIAALTKA----EERHG 386
Cdd:pfam12128 542 KEAPDWEQSIGKvisPELLhrtdldPEVwdgsvggelnlygvkldlkridvpewaasEEELRERLDKAEEAlqsaREKQA 621
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 387 NIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDtvdrllsesnERLQLHLKERMAALEEKGRLSEEIEKLRQEV 466
Cdd:pfam12128 622 AAEEQLVQANGELEKASREETFARTALKNARLDLRRLFD----------EKQSEKDKKNKALAERKDSANERLNSLEAQL 691
|
....
gi 2017363561 467 DQLK 470
Cdd:pfam12128 692 KQLD 695
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
25-467 |
8.73e-07 |
|
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: 53.58 E-value: 8.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 25 NFEQLMVNMLDEREKLLESLRESQETLAATQSRLQDAIHErdqlqrhlnsalpQEFATLTRELSMcreqllereeeisel 104
Cdd:pfam15921 114 DLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHE-------------LEAAKCLKEDML--------------- 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 105 kaerNNTRLLLEHLECLVSRHE---RSLRMTVVKRQAQSPSGVsSEVEVLKALkslfeHHKALDEKVRERLRAALERVTT 181
Cdd:pfam15921 166 ----EDSNTQIEQLRKMMLSHEgvlQEIRSILVDFEEASGKKI-YEHDSMSTM-----HFRSLGSAISKILRELDTEISY 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 182 LEEQLAGAHQQVSALQqgagvrdgaAEEEGTVELgpkrLWKEDTGRVE--------ELQELLEKQNFELSQARERLVTLT 253
Cdd:pfam15921 236 LKGRIFPVEDQLEALK---------SESQNKIEL----LLQQHQDRIEqlisehevEITGLTEKASSARSQANSIQSQLE 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 254 TTVTELEEDLGTARRDLIKSEELSSKHQRDLREAlaqKEDMEERITTLEKRYLAAQREATSIHDLNDKLENELAN-KESL 332
Cdd:pfam15921 303 IIQEQARNQNSMYMRQLSDLESTVSQLRSELREA---KRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNlDDQL 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 333 HRQCEEKARHLQELLEVAEQKLQ---QTMRKAETLPEVEAEL------AQRIAALTKA--EERHGNIEEHLRQLEGqlee 401
Cdd:pfam15921 380 QKLLADLHKREKELSLEKEQNKRlwdRDTGNSITIDHLRRELddrnmeVQRLEALLKAmkSECQGQMERQMAAIQG---- 455
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2017363561 402 KNQELARVRQREKMNEDHNKRLSDTVDRLLS-----ESNERLqlhLKERMAALEEKGRLSE----EIEKLRQEVD 467
Cdd:pfam15921 456 KNESLEKVSSLTAQLESTKEMLRKVVEELTAkkmtlESSERT---VSDLTASLQEKERAIEatnaEITKLRSRVD 527
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
342-472 |
9.40e-07 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 51.46 E-value: 9.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 342 HLQELLEVAE--QKLQQTMRKAETLP----EVEAELAQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQR--- 412
Cdd:COG1579 5 DLRALLDLQEldSELDRLEHRLKELPaelaELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQlgn 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 413 -----------------EKMNEDHNKRLSDTVDRL--LSESNERLQLHLKERMAALEE-KGRLSEEIEKLRQEVDQLKGR 472
Cdd:COG1579 85 vrnnkeyealqkeieslKRRISDLEDEILELMERIeeLEEELAELEAELAELEAELEEkKAELDEELAELEAELEELEAE 164
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
13-484 |
1.03e-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: 53.30 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 13 RLGPPHGADADANFEQLMVNMLDEREKLLESLRESQETLAATQSRLQDAIHERDQLQRHLNSALPQEFATLTRELSMCRE 92
Cdd:pfam12128 445 RLGELKLRLNQATATPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDE 524
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 93 QLLEREEEISELKA-ERNNTRLLLEHLECLVSR---HERSLRMTVVKRQAQSPS---GVSSEVEVLKALKSLFeHHKALD 165
Cdd:pfam12128 525 LELQLFPQAGTLLHfLRKEAPDWEQSIGKVISPellHRTDLDPEVWDGSVGGELnlyGVKLDLKRIDVPEWAA-SEEELR 603
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 166 E---KVRERLRAALERVTTLEEQLAGAHQQVSALQqgAGVRDGAAEEEGTvELGPKRLWKEDTGRVEELQELLEKQNFEL 242
Cdd:pfam12128 604 ErldKAEEALQSAREKQAAAEEQLVQANGELEKAS--REETFARTALKNA-RLDLRRLFDEKQSEKDKKNKALAERKDSA 680
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 243 SQARERLVTLTTTVTELEEDLGTARRDliKSEELSSKHQRDLREALAQKEDMEERI-TTLEKRYLAAQREATSIHDLNDk 321
Cdd:pfam12128 681 NERLNSLEAQLKQLDKKHQAWLEEQKE--QKREARTEKQAYWQVVEGALDAQLALLkAAIAARRSGAKAELKALETWYK- 757
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 322 leNELANK--------------ESLHRQCEEKARHLQELLE----VAEQKLQQTMRKAETLPEVEA---ELAQRIAALTK 380
Cdd:pfam12128 758 --RDLASLgvdpdviaklkreiRTLERKIERIAVRRQEVLRyfdwYQETWLQRRPRLATQLSNIERaisELQQQLARLIA 835
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 381 -AEERHGNIEEHLRQLEGQLEEKNQELARVRQR-EKMNEDHnkrlsdtvdrlLSESNERLQLHLKERMAALEE-KGRLSE 457
Cdd:pfam12128 836 dTKLRRAKLEMERKASEKQQVRLSENLRGLRCEmSKLATLK-----------EDANSEQAQGSIGERLAQLEDlKLKRDY 904
|
490 500
....*....|....*....|....*..
gi 2017363561 458 EIEKLRQEVDQLKGrggpfVDGVHSRS 484
Cdd:pfam12128 905 LSESVKKYVEHFKN-----VIADHSGS 926
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
34-465 |
1.21e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.02 E-value: 1.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 34 LDEREKLLESLRESQETLAATQSRL-QDAIHERDQLQRHLNSA--LPQEFATLTRELSMCREQLLEREEEISELKAERNN 110
Cdd:COG1196 276 LEELELELEEAQAEEYELLAELARLeQDIARLEERRRELEERLeeLEEELAELEEELEELEEELEELEEELEEAEEELEE 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 111 TRLLLEHLECLVSRHERSLRMTVVKRQAQSPSGVSSEVEVLKALKSLFEHHKALDEKVRERLRAALERvTTLEEQLAGAH 190
Cdd:COG1196 356 AEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEEL-EELEEALAELE 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 191 QQVSALQQGAGVRDGAAEEEGTVELGPKRLWKEDTGRVEELQELLEKQNFELSQARERLVTLTTTVTELEEDLGTARRDL 270
Cdd:COG1196 435 EEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAAL 514
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 271 IKS------------------------EELSSKHQRDLREALAQ--------KEDMEERITTLEKRyLAAQREATSIHDL 318
Cdd:COG1196 515 LLAglrglagavavligveaayeaaleAALAAALQNIVVEDDEVaaaaieylKAAKAGRATFLPLD-KIRARAALAAALA 593
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 319 NDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEEHLRQLEGQ 398
Cdd:COG1196 594 RGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAA 673
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2017363561 399 LEEKNQELARVRQREKMNEDHNKRLSDTVDRLLSESNERLQLHLKERMAALEEKGRLSEEIEKLRQE 465
Cdd:COG1196 674 LLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEE 740
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
232-465 |
1.34e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.07 E-value: 1.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 232 QELLEKQNFELSQARERLVTLTTTVTELEEDLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQRE 311
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 312 atsIHDLNDKLENELANKESLHRQCEEKarhlqelLEVAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERhgnieeh 391
Cdd:COG4942 99 ---LEAQKEELAELLRALYRLGRQPPLA-------LLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAE------- 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2017363561 392 LRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLLSESNERLQLHLKERMAALEEKGRLSEEIEKLRQE 465
Cdd:COG4942 162 LAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
123-472 |
1.56e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 52.65 E-value: 1.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 123 SRHERSLRMTVVKRqaqspsgVSSEVEVLKALKSLFEHHKALDEKVRErLRAALERVTTLEE--QLAGAHQQ--VSAL-Q 197
Cdd:PRK04863 275 MRHANERRVHLEEA-------LELRRELYTSRRQLAAEQYRLVEMARE-LAELNEAESDLEQdyQAASDHLNlvQTALrQ 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 198 QGAGVRdgaAEEEgtvelgpkrlwkedtgrVEELQELLEKQNFELSQARERlvtltttvteleedlgtarrdLIKSEELS 277
Cdd:PRK04863 347 QEKIER---YQAD-----------------LEELEERLEEQNEVVEEADEQ---------------------QEENEARA 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 278 SKHQRDLREALAQKEDMEERITTLEKR---YLAAQREATSIHDLNDKLENELANKESLHRQCEEKARHLQELLEVAEQKL 354
Cdd:PRK04863 386 EAAEEEVDELKSQLADYQQALDVQQTRaiqYQQAVQALERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKL 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 355 Q-------------QTMRKAetLPEVEAELAQRIA--ALTKAEErHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDH 419
Cdd:PRK04863 466 SvaqaahsqfeqayQLVRKI--AGEVSRSEAWDVAreLLRRLRE-QRHLAEQLQQLRMRLSELEQRLRQQQRAERLLAEF 542
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 420 NKRLS------DTVDRLLSESNERLQlHLKERMAAL-EEKGRLSEEIEKLRQEVDQLKGR 472
Cdd:PRK04863 543 CKRLGknlddeDELEQLQEELEARLE-SLSESVSEArERRMALRQQLEQLQARIQRLAAR 601
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
281-468 |
1.82e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 51.75 E-value: 1.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 281 QRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENELankESLHRQCEEKARHLQELLEVAEQKLQQTMRK 360
Cdd:COG3883 22 QKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEI---DKLQAEIAEAEAEIEERREELGERARALYRS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 361 AETLPEVEA--------ELAQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLLS 432
Cdd:COG3883 99 GGSVSYLDVllgsesfsDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQA 178
|
170 180 190
....*....|....*....|....*....|....*.
gi 2017363561 433 ESNERLQLHLKERMAALEEKGRLSEEIEKLRQEVDQ 468
Cdd:COG3883 179 EQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAA 214
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
229-407 |
2.38e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 50.31 E-value: 2.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 229 EELQELLEKQNF--ELSQARERLVTLTTTVTELEEDLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRyl 306
Cdd:COG1579 4 EDLRALLDLQELdsELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQ-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 307 aaQREATSIHDLNDkLENELANKESLHRQCEEKARHLQELLEVAEQKLQqtmrkaetlpEVEAELAQRIAALTKAEERHG 386
Cdd:COG1579 82 --LGNVRNNKEYEA-LQKEIESLKRRISDLEDEILELMERIEELEEELA----------ELEAELAELEAELEEKKAELD 148
|
170 180
....*....|....*....|.
gi 2017363561 387 NIEEHLRQLEGQLEEKNQELA 407
Cdd:COG1579 149 EELAELEAELEELEAEREELA 169
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
229-430 |
2.45e-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: 2.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 229 EELQELLEKQNFELSQARERLVTLTTTVTELEEDLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYlAA 308
Cdd:COG4942 30 EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEEL-AE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 309 QREATSIHDLNDKLENELANKESLhrQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERhgnI 388
Cdd:COG4942 109 LLRALYRLGRQPPLALLLSPEDFL--DAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAE---L 183
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2017363561 389 EEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRL 430
Cdd:COG4942 184 EEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEEL 225
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
32-468 |
2.92e-06 |
|
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: 51.89 E-value: 2.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 32 NMLDEREKLLESLRESQETLAATQsRLQDAIHERDQLQRHLNSALPQEfATLTRELSmcreqllereeEISELKAERNNT 111
Cdd:TIGR00618 223 VLEKELKHLREALQQTQQSHAYLT-QKREAQEEQLKKQQLLKQLRARI-EELRAQEA-----------VLEETQERINRA 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 112 RllleHLECLVsrhERSLRMTVVKRQAQspsgvssevevlkalkslfEHHKALDEKVRERLRAALERVTTLEEQLAGAHQ 191
Cdd:TIGR00618 290 R----KAAPLA---AHIKAVTQIEQQAQ-------------------RIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQ 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 192 QVSA---LQQGAGVRDGAAEEEGTVELGPKRlwKEDTGRVEELQELLEKQNfELSQARERLVTLTTTVTELEEDLGTARR 268
Cdd:TIGR00618 344 RRLLqtlHSQEIHIRDAHEVATSIREISCQQ--HTLTQHIHTLQQQKTTLT-QKLQSLCKELDILQREQATIDTRTSAFR 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 269 DLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHdlnDKLENELANKESLHRQCEEK-ARHLQELL 347
Cdd:TIGR00618 421 DLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSL---KEREQQLQTKEQIHLQETRKkAVVLARLL 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 348 EVAEQklQQTMRKAETLPEVEAELAQRIAALT----KAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRL 423
Cdd:TIGR00618 498 ELQEE--PCPLCGSCIHPNPARQDIDNPGPLTrrmqRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSIL 575
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 2017363561 424 SDTVDRLLSESNERLQL-----HLKERMAALEEKGRLSEEIEKLRQEVDQ 468
Cdd:TIGR00618 576 TQCDNRSKEDIPNLQNItvrlqDLTEKLSEAEDMLACEQHALLRKLQPEQ 625
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
35-472 |
2.96e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 51.60 E-value: 2.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 35 DEREKLLESLRESQETLAATQSRLQDAIHERDQLQRHLNS------ALPQEFATLTRELSMCREQLLEREEEISELKAER 108
Cdd:TIGR02168 309 ERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEElkeeleSLEAELEELEAELEELESRLEELEEQLETLRSKV 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 109 NNTRL-----------LLEHLECLVSRHER------SLRMTVVKRQAQSPSGVSSEVE-VLKALKSLFEHHKALDEKVRE 170
Cdd:TIGR02168 389 AQLELqiaslnneierLEARLERLEDRRERlqqeieELLKKLEEAELKELQAELEELEeELEELQEELERLEEALEELRE 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 171 RLRAALERVTTLEEQLAGAHQQVSALQQGAGVRDGAAEEEGTVELGPKRLwKEDTGRVEEL------------------- 231
Cdd:TIGR02168 469 ELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGL-SGILGVLSELisvdegyeaaieaalggrl 547
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 232 --------------QELLEKQN------FELSQARERLVTLTTTVTELEED--LGTARrDLIKSEELSSK-------HQR 282
Cdd:TIGR02168 548 qavvvenlnaakkaIAFLKQNElgrvtfLPLDSIKGTEIQGNDREILKNIEgfLGVAK-DLVKFDPKLRKalsyllgGVL 626
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 283 ---DLREALAQ--KEDMEERITTLE-----KRYLAAQREATSIHDLNDKlENELANKESLHRQCEEKARHLQELLEVAEQ 352
Cdd:TIGR02168 627 vvdDLDNALELakKLRPGYRIVTLDgdlvrPGGVITGGSAKTNSSILER-RREIEELEEKIEELEEKIAELEKALAELRK 705
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 353 KLQQTMRKAETLPEVEAELAQRIAA----LTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSD--- 425
Cdd:TIGR02168 706 ELEELEEELEQLRKELEELSRQISAlrkdLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAeie 785
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 2017363561 426 TVDRLLSESNERLQLhLKERMAALE-EKGRLSEEIEKLRQEVDQLKGR 472
Cdd:TIGR02168 786 ELEAQIEQLKEELKA-LREALDELRaELTLLNEEAANLRERLESLERR 832
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
272-470 |
4.14e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 51.17 E-value: 4.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 272 KSEELSSKHQRDLREALAQKEDMEERITTLEKrylaaqreatSIHDLND---KLENELANKES----LHRQCEEKARHLQ 344
Cdd:TIGR04523 304 KEQDWNKELKSELKNQEKKLEEIQNQISQNNK----------IISQLNEqisQLKKELTNSESenseKQRELEEKQNEIE 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 345 ELLEVAEQKLQQTmrkaETLPEVEAELAQRIaalTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLS 424
Cdd:TIGR04523 374 KLKKENQSYKQEI----KNLESQINDLESKI---QNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLT 446
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2017363561 425 --DTVDRLLSESNERLQLHLKERMAALEekgrlsEEIEKLRQEVDQLK 470
Cdd:TIGR04523 447 nqDSVKELIIKNLDNTRESLETQLKVLS------RSINKIKQNLEQKQ 488
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
163-414 |
5.22e-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: 51.11 E-value: 5.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 163 ALDEKVRERLRAALERVTTLEEQLAgahQQVSALQQGAGVRDGAAEEEGTVE--LGPKRLWKEDT--GRVEELQELLEkq 238
Cdd:COG3096 829 AFAPDPEAELAALRQRRSELERELA---QHRAQEQQLRQQLDQLKEQLQLLNklLPQANLLADETlaDRLEELREELD-- 903
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 239 nfELSQARERLVTLTTTVTELEEDLGTARRDLIKSEELsskhQRDLREALAQKEDMEERITTLEkrYLAAQREATSIHD- 317
Cdd:COG3096 904 --AAQEAQAFIQQHGKALAQLEPLVAVLQSDPEQFEQL----QADYLQAKEQQRRLKQQIFALS--EVVQRRPHFSYEDa 975
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 318 ---------LNDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELAQRIAAL-----TKAEE 383
Cdd:COG3096 976 vgllgensdLNEKLRARLEQAEEARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEELgvqadAEAEE 1055
|
250 260 270
....*....|....*....|....*....|.
gi 2017363561 384 RhgnIEEHLRQLEGQLeekNQELARVRQREK 414
Cdd:COG3096 1056 R---ARIRRDELHEEL---SQNRSRRSQLEK 1080
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
42-469 |
5.52e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 50.81 E-value: 5.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 42 ESLRESQETLAATQSRLQDAIHE-RDQLQRHLNSA----------------LPQEFATLTRELSMCREQLLEREEEISEL 104
Cdd:PRK02224 310 EAVEARREELEDRDEELRDRLEEcRVAAQAHNEEAeslredaddleeraeeLREEAAELESELEEAREAVEDRREEIEEL 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 105 KAERNNTRL-----------LLEHLECLVSRHERslrmtVVKRQAQSPSGVSSEVEVLKALKSLFEHHKA-------LDE 166
Cdd:PRK02224 390 EEEIEELRErfgdapvdlgnAEDFLEELREERDE-----LREREAELEATLRTARERVEEAEALLEAGKCpecgqpvEGS 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 167 KVRERLRAALERVTTLEEQLAGAHQQVSALQQgagvRDGAAEEEGTVELGPKRLWKedtgRVEELQELLEKQNFELSQAR 246
Cdd:PRK02224 465 PHVETIEEDRERVEELEAELEDLEEEVEEVEE----RLERAEDLVEAEDRIERLEE----RREDLEELIAERRETIEEKR 536
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 247 ERLVTLTTTVTELEEDLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKrylaaqreatsIHDLNDKLENEL 326
Cdd:PRK02224 537 ERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLER-----------IRTLLAAIADAE 605
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 327 ANKESLhrqcEEKARHLQELLEVAEQKLQQtmrKAETLPEVEAELAQriAALTKAEERHGNIEEHLRQLEGQLEEKNQEL 406
Cdd:PRK02224 606 DEIERL----REKREALAELNDERRERLAE---KRERKRELEAEFDE--ARIEEAREDKERAEEYLEQVEEKLDELREER 676
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2017363561 407 ARVRQREKMNEDHNKRLSDtvdrllsesnerlqlhLKERMAALEEKgrlSEEIEKLRQEVDQL 469
Cdd:PRK02224 677 DDLQAEIGAVENELEELEE----------------LRERREALENR---VEALEALYDEAEEL 720
|
|
| SAM |
smart00454 |
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ... |
1030-1101 |
6.00e-06 |
|
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: 44.98 E-value: 6.00e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2017363561 1030 VLVWTNDQVVHWVQSIGLRDYAGNLHESGVHGALLALDENFDHntlalILQIPTQNTQARQVMEREFNNLLA 1101
Cdd:smart00454 1 VSQWSPESVADWLESIGLEQYADNFRKNGIDGALLLLLTSEED-----LKELGITKLGHRKKILKAIQKLKE 67
|
|
| SAM_superfamily |
cd09487 |
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ... |
952-1003 |
6.83e-06 |
|
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: 44.54 E-value: 6.83e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 2017363561 952 EWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRvHLKMVDSFHRTSLQYGI 1003
Cdd:cd09487 4 EWLESLGLEQYADLFRKNEIDGDALLLLTDEDLK-ELGITSPGHRKKILRAI 54
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
169-465 |
7.81e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 50.45 E-value: 7.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 169 RERLRAALERVTTLEEQLAGAHQQVSALQQGAG-VRDGAAEEEGTVELGPKRLwkedtgrvEELQELLEKQNFELSQARE 247
Cdd:TIGR02169 673 PAELQRLRERLEGLKRELSSLQSELRRIENRLDeLSQELSDASRKIGEIEKEI--------EQLEQEEEKLKERLEELEE 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 248 RLVTLTTTVTELEEDLGTARRDLIKSEELSSKhqrdLREALAQKEDM--EERITTLEKRYlaaqreatsihdlnDKLENE 325
Cdd:TIGR02169 745 DLSSLEQEIENVKSELKELEARIEELEEDLHK----LEEALNDLEARlsHSRIPEIQAEL--------------SKLEEE 806
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 326 LANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELAQRIAAL-TKAEERHGNIEEH---LRQLEGQLEE 401
Cdd:TIGR02169 807 VSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLnGKKEELEEELEELeaaLRDLESRLGD 886
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2017363561 402 KNQElaRVRQREKMNEDHNKRlsdtvdRLLSESNERLQLHLKERMAALEEKGRLSEEIEKLRQE 465
Cdd:TIGR02169 887 LKKE--RDELEAQLRELERKI------EELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGE 942
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
45-463 |
7.95e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 50.32 E-value: 7.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 45 RESQETLAATQ---SRLQDAIHE----RDQLQRHLNSAlpQEFATLTRELSmcREQLLEREEEISELKAERNNTRLLLEH 117
Cdd:COG1196 175 EEAERKLEATEenlERLEDILGElerqLEPLERQAEKA--ERYRELKEELK--ELEAELLLLKLRELEAELEELEAELEE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 118 LECLVSRHERSLRMTVVKRQAQSPSGVSSEVEVLKALKSLFEHHKALD--EKVRERLRAALERVTTLEEQLAGAHQQVSA 195
Cdd:COG1196 251 LEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELArlEQDIARLEERRRELEERLEELEEELAELEE 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 196 LQQGAGVRDGAAEEEGTVELGPKRLWKEDTGRVEELQELLEKQNFELSQARERLVTLTTTVTELEEDLGTARRDLIKSEE 275
Cdd:COG1196 331 ELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEE 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 276 LSSKHQRDLREALAQKEDMEERITTLEKRYLAAQREATS-IHDLNDKLENELANKESLHRQCEEKARHLQELLEVAEQKL 354
Cdd:COG1196 411 ALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEeEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAA 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 355 QQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLLSES 434
Cdd:COG1196 491 ARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAK 570
|
410 420
....*....|....*....|....*....
gi 2017363561 435 NERLQLHLKERMAALEEKGRLSEEIEKLR 463
Cdd:COG1196 571 AGRATFLPLDKIRARAALAAALARGAIGA 599
|
|
| SAM_2 |
pfam07647 |
SAM domain (Sterile alpha motif); |
1030-1100 |
9.02e-06 |
|
SAM domain (Sterile alpha motif);
Pssm-ID: 429573 Cd Length: 66 Bit Score: 44.57 E-value: 9.02e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2017363561 1030 VLVWTNDQVVHWVQSIGLRDYAGNLHESGVHGALLALdeNFDHNTLAlilQIPTQNTQARQVMEREFNNLL 1100
Cdd:pfam07647 1 VESWSLESVADWLRSIGLEQYTDNFRDQGITGAELLL--RLTLEDLK---RLGITSVGHRRKILKKIQELK 66
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
262-472 |
9.81e-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: 9.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 262 DLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENELANKESLHR------- 334
Cdd:TIGR02169 689 ELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKelearie 768
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 335 QCEEKARHLQELLE-----VAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQEL-AR 408
Cdd:TIGR02169 769 ELEEDLHKLEEALNdlearLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLkEQ 848
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2017363561 409 VRQREKMNEDHNKRLSDTVDRLlsesnERLQLHLKErmaALEEKGRLSEEIEKLRQEVDQLKGR 472
Cdd:TIGR02169 849 IKSIEKEIENLNGKKEELEEEL-----EELEAALRD---LESRLGDLKKERDELEAQLRELERK 904
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
34-396 |
1.48e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.38 E-value: 1.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 34 LDEREKLLESLRESQETLAATQSRLQDAIherDQLQRHLNSALPQEFATLTRELSMCREQLLEREEEISELKAERNNTRL 113
Cdd:COG4717 151 LEERLEELRELEEELEELEAELAELQEEL---EELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEE 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 114 LLEHLECLVSRHER--------------SLRMTVVKRQAQSPSGVSSEVEVLKALKSLFEHHKALDEKVRERLRAALERV 179
Cdd:COG4717 228 ELEQLENELEAAALeerlkearlllliaAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEEL 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 180 TTLEEQLAGAHQQVSALQQGAGVRDGAAEEEGTVELGPKRLWKEDTGRVEELQEllekqnfELSQARERLVTLTTTVTEL 259
Cdd:COG4717 308 QALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEE-------ELQLEELEQEIAALLAEAG 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 260 EEDLGTARRDLIKSEElsskhQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDkLENELANKESLHRQCEEK 339
Cdd:COG4717 381 VEDEEELRAALEQAEE-----YQELKEELEELEEQLEELLGELEELLEALDEEELEEELEE-LEEELEELEEELEELREE 454
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 2017363561 340 ARHLQELLEVAE--QKLQQTMRKAETLPEVEAELAQRIAALTKAEErhgNIEEHLRQLE 396
Cdd:COG4717 455 LAELEAELEQLEedGELAELLQELEELKAELRELAEEWAALKLALE---LLEEAREEYR 510
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
35-469 |
2.53e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 48.81 E-value: 2.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 35 DEREKLLeSLRESQETLAATQSRLQDAIHERDQLQRHLNSALpQEFATLTRELSMCREQLLEREEEISELKAERNNTRLL 114
Cdd:TIGR00618 421 DLQGQLA-HAKKQQELQQRYAELCAAAITCTAQCEKLEKIHL-QESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLE 498
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 115 LEHLECLVsrhERSLRMTVVKRQAQSPSGVSSEvEVLKALKSLFEHHKALdEKVRERLRAALERVTTLEEQLAGAHQQVS 194
Cdd:TIGR00618 499 LQEEPCPL---CGSCIHPNPARQDIDNPGPLTR-RMQRGEQTYAQLETSE-EDVYHQLTSERKQRASLKEQMQEIQQSFS 573
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 195 ALQQ-----GAGVRDGAAEEEGTVELGPKRLWKEDTGRvEELQELLEKQNFELSQARERLVTLTTTVTELEEDLGTARrd 269
Cdd:TIGR00618 574 ILTQcdnrsKEDIPNLQNITVRLQDLTEKLSEAEDMLA-CEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHA-- 650
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 270 liksEELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENELANKESLHRQCEEKARHLQEL--- 346
Cdd:TIGR00618 651 ----LQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIena 726
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 347 -----------LEVAEQKLQQTMRKAET-LPEVEAELAQRIAALTKAEERHGNIEEHLRQLEGQ---LEEKNQELARVRQ 411
Cdd:TIGR00618 727 ssslgsdlaarEDALNQSLKELMHQARTvLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFnrlREEDTHLLKTLEA 806
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 2017363561 412 REKMNEDHNKRLSDTVDRLLSESNERLQLHLKERMAALEEKGRLSEEIEKLRQEVDQL 469
Cdd:TIGR00618 807 EIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQL 864
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
320-470 |
2.73e-05 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 46.60 E-value: 2.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 320 DKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAEtlPEVEAELAQRIAALTKAEERHG-----------NI 388
Cdd:pfam04012 39 VKARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQAALTKGN--EELAREALAEKKSLEKQAEALEtqlaqqrsaveQL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 389 EEHLRQLEGQLEEKNQELARVRQREKMNEdHNKRLSDTVDRLLSESNERLQLHLKERMAALEEKGRLSEEIEK---LRQE 465
Cdd:pfam04012 117 RKQLAALETKIQQLKAKKNLLKARLKAAK-AQEAVQTSLGSLSTSSATDSFERIEEKIEEREARADAAAELASavdLDAK 195
|
....*
gi 2017363561 466 VDQLK 470
Cdd:pfam04012 196 LEQAG 200
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
281-472 |
5.10e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 47.73 E-value: 5.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 281 QRDLREALAQKEDMEERIttlekrylaaqrEATSIHDLNDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRK 360
Cdd:PRK02224 182 LSDQRGSLDQLKAQIEEK------------EEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEER 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 361 AETLPEVEAELAQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLLSESNERLQL 440
Cdd:PRK02224 250 REELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDR 329
|
170 180 190
....*....|....*....|....*....|..
gi 2017363561 441 HLKERMAAleekGRLSEEIEKLRQEVDQLKGR 472
Cdd:PRK02224 330 LEECRVAA----QAHNEEAESLREDADDLEER 357
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
33-380 |
8.42e-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: 46.98 E-value: 8.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 33 MLDEREKLLESLRESQETLAATQSRLQDAIHERDQLQRHLNsALPQEFATLTRELSMCREQLLEREEEISELKAErnntr 112
Cdd:TIGR02169 686 LKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIE-QLEQEEEKLKERLEELEEDLSSLEQEIENVKSE----- 759
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 113 llLEHLECLVSRHERSLrmtvVKRQAQ--------SPSGVSsevEVLKALKSLFEHHKALDEKVRErLRAALERVTTLEE 184
Cdd:TIGR02169 760 --LKELEARIEELEEDL----HKLEEAlndlearlSHSRIP---EIQAELSKLEEEVSRIEARLRE-IEQKLNRLTLEKE 829
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 185 QLAGAHQQvsALQQGAGVRDGAAEEEGTVElgpkrlwkEDTGRVEELQELLEKQNFELSQARERlvtltttvteleedLG 264
Cdd:TIGR02169 830 YLEKEIQE--LQEQRIDLKEQIKSIEKEIE--------NLNGKKEELEEELEELEAALRDLESR--------------LG 885
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 265 TARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENELANK---ESLHRQCEEKAR 341
Cdd:TIGR02169 886 DLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEElslEDVQAELQRVEE 965
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 2017363561 342 HLQELLEV---AEQKLQQTMR-------KAETLPEVEAELAQRIAALTK 380
Cdd:TIGR02169 966 EIRALEPVnmlAIQEYEEVLKrldelkeKRAKLEEERKAILERIEEYEK 1014
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
283-468 |
1.01e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 46.82 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 283 DLREALAQKEDMEERITTLEKRYLAAQREATSIHDLND----KLENELANKESLHRQCEEKARHLQELLEvaeqklqqtm 358
Cdd:PRK01156 581 DIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDksirEIENEANNLNNKYNEIQENKILIEKLRG---------- 650
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 359 rKAETLPEVEAELAQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVdrllSESNERL 438
Cdd:PRK01156 651 -KIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRI----NDINETL 725
|
170 180 190
....*....|....*....|....*....|....*.
gi 2017363561 439 QlHLKERMAALEEKGRLSEEIEK------LRQEVDQ 468
Cdd:PRK01156 726 E-SMKKIKKAIGDLKRLREAFDKsgvpamIRKSASQ 760
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
313-423 |
1.13e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 46.36 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 313 TSIHDLNDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAEL---AQRIA--ALTKAEERHGN 387
Cdd:PRK00409 509 KLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLleeAEKEAqqAIKEAKKEADE 588
|
90 100 110
....*....|....*....|....*....|....*....
gi 2017363561 388 IEEHLRQLE--GQLEEKNQELARVRQR-EKMNEDHNKRL 423
Cdd:PRK00409 589 IIKELRQLQkgGYASVKAHELIEARKRlNKANEKKEKKK 627
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
301-472 |
1.32e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.30 E-value: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 301 LEKRYLAAQREATSIHDLNDKLE-NELANKESLHRQCEEKARHLQELlevaEQKLQQTMRKAETLPEVEAELAQRIAALT 379
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNlKELKELEEELKEAEEKEEEYAEL----QEELEELEEELEELEAELEELREELEKLE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 380 KAEERHGNIEEhLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLLSESNERLQLHLKERMAALEEKGRLSEEI 459
Cdd:COG4717 123 KLLQLLPLYQE-LEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEEL 201
|
170
....*....|...
gi 2017363561 460 EKLRQEVDQLKGR 472
Cdd:COG4717 202 EELQQRLAELEEE 214
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
18-471 |
1.59e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 46.26 E-value: 1.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 18 HGADADANFEQLMVNMLDEREKLLESLRESQETLAATQSRLQDAIHERDQLQR---HLNSALPQEFATL---TRELSMCR 91
Cdd:pfam15921 318 QLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQesgNLDDQLQKLLADLhkrEKELSLEK 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 92 EQLLE-------REEEISELKAERNNTRLLLEHLECLVsrheRSLRMTVVKRQAQSPSGVSSEVEVLKALKSLfehhKAL 164
Cdd:pfam15921 398 EQNKRlwdrdtgNSITIDHLRRELDDRNMEVQRLEALL----KAMKSECQGQMERQMAAIQGKNESLEKVSSL----TAQ 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 165 DEKVRERLRAALERVTTLEEQLAGAHQQVSALQQGAgvrdgaAEEEGTVELGPKRLWKEDTGRVEELQEL--LEKQNFEL 242
Cdd:pfam15921 470 LESTKEMLRKVVEELTAKKMTLESSERTVSDLTASL------QEKERAIEATNAEITKLRSRVDLKLQELqhLKNEGDHL 543
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 243 SQARERLVTLTTTVTELEEDLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERIT----TLEKRYLAAQREATSIHDL 318
Cdd:pfam15921 544 RNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINdrrlELQEFKILKDKKDAKIREL 623
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 319 NDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEV--EAELAQRiAALTKAEErhgnIEEHLRQLE 396
Cdd:pfam15921 624 EARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLseDYEVLKR-NFRNKSEE----METTTNKLK 698
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 397 GQLEEKNQELARVRQREKMNEDHN-----------KRLS---DTVDRLLSESN---ERLQLHLKERMAALEEKGRLSEEI 459
Cdd:pfam15921 699 MQLKSAQSELEQTRNTLKSMEGSDghamkvamgmqKQITakrGQIDALQSKIQfleEAMTNANKEKHFLKEEKNKLSQEL 778
|
490
....*....|..
gi 2017363561 460 EKLRQEVDQLKG 471
Cdd:pfam15921 779 STVATEKNKMAG 790
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
227-417 |
1.67e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 45.28 E-value: 1.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 227 RVEELQELLEKQNFELSQARERLVTLTTTVTELEEDLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYL 306
Cdd:COG4372 46 ELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQ 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 307 AAQREATSIHDLNDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMrkaetlpevEAELAQRIAALTKAEERHG 386
Cdd:COG4372 126 DLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALS---------EAEAEQALDELLKEANRNA 196
|
170 180 190
....*....|....*....|....*....|.
gi 2017363561 387 NIEEHLRQLEGQLEEKNQELARVRQREKMNE 417
Cdd:COG4372 197 EKEEELAEAEKLIESLPRELAEELLEAKDSL 227
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
222-469 |
2.36e-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: 45.33 E-value: 2.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 222 KEDTGRVEELQELLEKQNFELS-QARERLVTLTTTVTELEEDLGTARRDLIKSEELSSKHQRdlREALAQKEDMEERITT 300
Cdd:COG5185 274 AESSKRLNENANNLIKQFENTKeKIAEYTKSIDIKKATESLEEQLAAAEAEQELEESKRETE--TGIQNLTAEIEQGQES 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 301 LEKRYLAAQREATSIHDLND------KLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAEtlpeveaelaqr 374
Cdd:COG5185 352 LTENLEAIKEEIENIVGEVElsksseELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTLKAAD------------ 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 375 iaalTKAEERHGNIEEHLRQLEgQLEEKNQELAR--VRQREKMNEDHNKRLSDTVDRLLSE-------SNERLQlHLKER 445
Cdd:COG5185 420 ----RQIEELQRQIEQATSSNE-EVSKLLNELISelNKVMREADEESQSRLEEAYDEINRSvrskkedLNEELT-QIESR 493
|
250 260
....*....|....*....|....*....
gi 2017363561 446 MAAL-----EEKGRLSEEIEKLRQEVDQL 469
Cdd:COG5185 494 VSTLkatleKLRAKLERQLEGVRSKLDQV 522
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
281-470 |
2.63e-04 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 45.07 E-value: 2.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 281 QRDLREALAQKEDMEERITTLekRYLAAQREATSIHDLND-KLENE---LANKESLHRQCEEKARHLQELLEVAEQKLQQ 356
Cdd:COG0497 171 KKELEELRADEAERARELDLL--RFQLEELEAAALQPGEEeELEEErrrLSNAEKLREALQEALEALSGGEGGALDLLGQ 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 357 TMRKAETLPEVEAELAQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQRekMNEDHN--KRLSDTVDRLLSes 434
Cdd:COG0497 249 ALRALERLAEYDPSLAELAERLESALIELEEAASELRRYLDSLEFDPERLEEVEER--LALLRRlaRKYGVTVEELLA-- 324
|
170 180 190
....*....|....*....|....*....|....*.
gi 2017363561 435 nerLQLHLKERMAALEEkgrLSEEIEKLRQEVDQLK 470
Cdd:COG0497 325 ---YAEELRAELAELEN---SDERLEELEAELAEAE 354
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
222-470 |
2.93e-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: 45.35 E-value: 2.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 222 KEDTGRVEELQELLEKQNFELSQARErlvtltttvteleedLGTARRDLIKSEELSSKHQRDLREaLAQKEDMEERITTL 301
Cdd:pfam02463 166 RLKRKKKEALKKLIEETENLAELIID---------------LEELKLQELKLKEQAKKALEYYQL-KEKLELEEEYLLYL 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 302 EKRYLAAQREATSIHDLNDK------------LENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEA 369
Cdd:pfam02463 230 DYLKLNEERIDLLQELLRDEqeeiesskqeieKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRK 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 370 ELAQRIaaLTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLLSESNERLQLHLKERMAAL 449
Cdd:pfam02463 310 VDDEEK--LKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLS 387
|
250 260
....*....|....*....|.
gi 2017363561 450 EEKGRLSEEIEKLRQEVDQLK 470
Cdd:pfam02463 388 SAAKLKEEELELKSEEEKEAQ 408
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
135-472 |
3.49e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.76 E-value: 3.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 135 KRQAQSPSGVSSEVEVL-KALKSLFEHHKALDEKV--RERLRAALERVTTLEEQLAGAHQQVSALQQGAGVRDGAAEEEG 211
Cdd:COG4717 60 KPQGRKPELNLKELKELeEELKEAEEKEEEYAELQeeLEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 212 TVELGPKRL--WKEDTGRVEELQELLEKQNFELSQARER-LVTLTTTVTELEEDLGTARRDLIKSEELSSKHQRDLREAL 288
Cdd:COG4717 140 ELAELPERLeeLEERLEELRELEEELEELEAELAELQEElEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQ 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 289 AQKEDMEERITTLEKRYLAAQRE-------------------ATSIHDLNDKLEN-----------------ELANKESL 332
Cdd:COG4717 220 EELEELEEELEQLENELEAAALEerlkearlllliaaallalLGLGGSLLSLILTiagvlflvlgllallflLLAREKAS 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 333 HRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELAQR-IAALTKAEERHGNIEEHLRQLE-GQLEEKNQEL---- 406
Cdd:COG4717 300 LGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLElLDRIEELQELLREAEELEEELQlEELEQEIAALlaea 379
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2017363561 407 ---------ARVRQREKMNEDhNKRLSDTVDRLLSESNERLQLHLKERMAALEEK-GRLSEEIEKLRQEVDQLKGR 472
Cdd:COG4717 380 gvedeeelrAALEQAEEYQEL-KEELEELEEQLEELLGELEELLEALDEEELEEElEELEEELEELEEELEELREE 454
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
169-465 |
3.80e-04 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 44.47 E-value: 3.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 169 RERLRAALERVTTLEEQLAGAHQQVSALQQGAGVRDGAAEEEGTVELGPKRLWKEDTGRVEE-----LQELLEKQNFELS 243
Cdd:pfam02029 12 RRRAREERRRQKEEEEPSGQVTESVEPNEHNSYEEDSELKPSGQGGLDEEEAFLDRTAKREErrqkrLQEALERQKEFDP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 244 QA---------RERLVTLTTTVTELEEDLGTARRDLIKSEELSSK----HQRDLREALAQ---KEDMEERITTLEKRYLA 307
Cdd:pfam02029 92 TIadekesvaeRKENNEEEENSSWEKEEKRDSRLGRYKEEETEIRekeyQENKWSTEVRQaeeEGEEEEDKSEEAEEVPT 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 308 AQREATSIHDLNDKLENELA--NKESLHRQ---CEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELAQRIAALTKAE 382
Cdd:pfam02029 172 ENFAKEEVKDEKIKKEKKVKyeSKVFLDQKrghPEVKSQNGEEEVTKLKVTTKRRQGGLSQSQEREEEAEVFLEAEQKLE 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 383 ErhgnieehLRQLEGQLEEKNQELARVRQREKMNE-DHNKRLSDTVDRLLSESNERLQLHLKERMAALEE-KGRLSEEIE 460
Cdd:pfam02029 252 E--------LRRRRQEKESEEFEKLRQKQQEAELElEELKKKREERRKLLEEEEQRRKQEEAERKLREEEeKRRMKEEIE 323
|
....*
gi 2017363561 461 KLRQE 465
Cdd:pfam02029 324 RRRAE 328
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
283-470 |
3.90e-04 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 44.68 E-value: 3.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 283 DLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMR--- 359
Cdd:pfam05622 1 DLSEAQEEKDELAQRCHELDQQVSLLQEEKNSLQQENKKLQERLDQLESGDDSGTPGGKKYLLLQKQLEQLQEENFRlet 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 360 -------KAETLPEVEAELAQRIAALTKAEE------------RHGNieEHLRQLEGQLE---EKNQELARVRQREKMNE 417
Cdd:pfam05622 81 arddyriKCEELEKEVLELQHRNEELTSLAEeaqalkdemdilRESS--DKVKKLEATVEtykKKLEDLGDLRRQVKLLE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 418 DHN----------------------------KRLSDTVDRLLSESN--ERLQL---HLKERMAALE-EKGRLSEEIEKLR 463
Cdd:pfam05622 159 ERNaeymqrtlqleeelkkanalrgqletykRQVQELHGKLSEESKkaDKLEFeykKLEEKLEALQkEKERLIIERDTLR 238
|
....*..
gi 2017363561 464 QEVDQLK 470
Cdd:pfam05622 239 ETNEELR 245
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
228-468 |
4.21e-04 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 43.48 E-value: 4.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 228 VEELQELLEKQNFELSQARERLVTLTTTVTELEEDLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRyla 307
Cdd:pfam00261 10 LDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERGRKVLENR--- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 308 AQREATSIHDLNDKLENELANKESLHRQCEEKARHLQelleVAEQKLQQTMRKAETLPEVEAELaqriaaltkaEERHGN 387
Cdd:pfam00261 87 ALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLV----VVEGDLERAEERAELAESKIVEL----------EEELKV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 388 IEEHLRQLEGQLEEKNqelarvrQREKMNEDH----NKRLSDTVDRllSESNERLQLHLKERMAALEEKGRLS-EEIEKL 462
Cdd:pfam00261 153 VGNNLKSLEASEEKAS-------EREDKYEEQirflTEKLKEAETR--AEFAERSVQKLEKEVDRLEDELEAEkEKYKAI 223
|
....*.
gi 2017363561 463 RQEVDQ 468
Cdd:pfam00261 224 SEELDQ 229
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
286-411 |
4.65e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 44.52 E-value: 4.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 286 EALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLEnELANKEslhrQCEEKARHLQELLEVAEQKLQQTMRKAETLP 365
Cdd:PRK11281 33 GDLPTEADVQAQLDALNKQKLLEAEDKLVQQDLEQTLA-LLDKID----RQKEETEQLKQQLAQAPAKLRQAQAELEALK 107
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 2017363561 366 EVEA-ELAQRIAALTkaeerhgnieehLRQLEGQLEEKNQELARVRQ 411
Cdd:PRK11281 108 DDNDeETRETLSTLS------------LRQLESRLAQTLDQLQNAQN 142
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
316-465 |
4.67e-04 |
|
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: 43.65 E-value: 4.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 316 HDLNDKLENELANKESLHRQCEEKARHLQEL-LEVA--EQKLQQTMR-KAETLPEVEaELAQRIAALTKAEERHGNIEEH 391
Cdd:pfam15905 166 NKLEAKMKEVMAKQEGMEGKLQVTQKNLEHSkGKVAqlEEKLVSTEKeKIEEKSETE-KLLEYITELSCVSEQVEKYKLD 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 392 LRQLEGQLEEKNQELARVRQREKMNEDHN-----------KRLSDTVDRLLSESNERLQLHLKErMAALEEKGRL-SEEI 459
Cdd:pfam15905 245 IAQLEELLKEKNDEIESLKQSLEEKEQELskqikdlnekcKLLESEKEELLREYEEKEQTLNAE-LEELKEKLTLeEQEH 323
|
....*.
gi 2017363561 460 EKLRQE 465
Cdd:pfam15905 324 QKLQQK 329
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
135-470 |
5.18e-04 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 44.36 E-value: 5.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 135 KRQAQSPSGVSSEV-EVLKALKSLFEHHKALDEKVRERLRAALERVTTLEEQLAGAHQQVSALQQGAGVRdgAAEEEgtV 213
Cdd:pfam09731 88 QVKIPRQSGVSSEVaEEEKEATKDAAEAKAQLPKSEQEKEKALEEVLKEAISKAESATAVAKEAKDDAIQ--AVKAH--T 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 214 ELGPKRLWKEDTGRVEELQELLEKQNFELSQARERLVTLTTTVTELEEDLGTARRDLIKSeelsSKHQRDLREALAQKED 293
Cdd:pfam09731 164 DSLKEASDTAEISREKATDSALQKAEALAEKLKEVINLAKQSEEEAAPPLLDAAPETPPK----LPEHLDNVEEKVEKAQ 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 294 MEERITTLEKRYLAA-----QREATSIH-DLNDKL-ENELANKESLHRQCEekarHLQELLEVAEQKLQqTMRKAETLpE 366
Cdd:pfam09731 240 SLAKLVDQYKELVASerivfQQELVSIFpDIIPVLkEDNLLSNDDLNSLIA----HAHREIDQLSKKLA-ELKKREEK-H 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 367 VEAELAQRIAALTKAEER-HGNIEEHLRQLEGQLEEKNQElARVRQREKM-----------NEDHNKRLSDTVDRLLSES 434
Cdd:pfam09731 314 IERALEKQKEELDKLAEElSARLEEVRAADEAQLRLEFER-EREEIRESYeeklrtelerqAEAHEEHLKDVLVEQEIEL 392
|
330 340 350
....*....|....*....|....*....|....*.
gi 2017363561 435 NERLQLHLKERMAalEEKGRLSEEIEKLRQEVDQLK 470
Cdd:pfam09731 393 QREFLQDIKEKVE--EERAGRLLKLNELLANLKGLE 426
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
46-476 |
5.57e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.56 E-value: 5.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 46 ESQETLAATQSRlqdaihERDQLQRHLNSALpqefaTLTRELSMCREQLLEREEEISELKAE---RNNTRLLLE------ 116
Cdd:PRK04863 265 ESTNYVAADYMR------HANERRVHLEEAL-----ELRRELYTSRRQLAAEQYRLVEMARElaeLNEAESDLEqdyqaa 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 117 --HLECLvsrherslrMTVVKRQAQspsGVSSEVEVLKALKSLFEHHKALDE------KVRERLRAALERVTTLEEQLAG 188
Cdd:PRK04863 334 sdHLNLV---------QTALRQQEK---IERYQADLEELEERLEEQNEVVEEadeqqeENEARAEAAEEEVDELKSQLAD 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 189 AHQQVSALQQGAGVRDGAAEeegtvelgpkrlwkedtgRVEELQELLEKQNFELSQARERLVTLTTTVTELEEDLGTARR 268
Cdd:PRK04863 402 YQQALDVQQTRAIQYQQAVQ------------------ALERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQ 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 269 DLIKSEELSSKHQRDLR---------EALAQKEDMEERITTLEK-RYLAAQREAtsihdlndkLENELANKESLHRQcee 338
Cdd:PRK04863 464 KLSVAQAAHSQFEQAYQlvrkiagevSRSEAWDVARELLRRLREqRHLAEQLQQ---------LRMRLSELEQRLRQ--- 531
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 339 kARHLQELLEVAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNED 418
Cdd:PRK04863 532 -QQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAARAPAWLAAQD 610
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2017363561 419 HNKRLSDTVDRLLSESN---ERLQLHLKERMAALEEKGRLSEEIEKLRQEVDQLKGRGGPF 476
Cdd:PRK04863 611 ALARLREQSGEEFEDSQdvtEYMQQLLERERELTVERDELAARKQALDEEIERLSQPGGSE 671
|
|
| SAM_STIM-1,2-like |
cd09504 |
SAM domain of STIM-1,2-like proteins; SAM (sterile alpha motif) domain of STIM-1,2-like ... |
830-888 |
5.59e-04 |
|
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: 39.62 E-value: 5.59e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2017363561 830 WDGPTVVSWLELWVGMPAwYVAACRANVKSGAIMSALSDTE---IQREIGISNALHRLKLRL 888
Cdd:cd09504 5 WTVEDTVEWLVNSVELPQ-YVEAFKENGVDGSALPRLAVNNpsfLTSVLGIKDPIHRQKLSL 65
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
24-472 |
7.53e-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: 43.90 E-value: 7.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 24 ANFEQLMVNMLDEREKLLESLRESQETLAATQSRLQDAIHERDQLQRHLnSALPQEFATLTRELSMCREQLLEREEEISE 103
Cdd:TIGR02169 360 AELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKREL-DRLQEELQRLSEELADLNAAIAGIEAKINE 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 104 LKAERNNTRLLLEHLE-------CLVSRHERSLRMTVVKRQAQSP--SGVSSEVEVLKALKSLFEHHKALDEKVRERLRA 174
Cdd:TIGR02169 439 LEEEKEDKALEIKKQEwkleqlaADLSKYEQELYDLKEEYDRVEKelSKLQRELAEAEAQARASEERVRGGRAVEEVLKA 518
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 175 ALERVTTLEEQLAGAHQQ-VSALQQGAGVRDGA--AEEEGTVELGPKRLWKEDTGRV-----------EELQELLEKQNF 240
Cdd:TIGR02169 519 SIQGVHGTVAQLGSVGERyATAIEVAAGNRLNNvvVEDDAVAKEAIELLKRRKAGRAtflplnkmrdeRRDLSILSEDGV 598
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 241 --------ELSQARERLVTLTTTVTELEEDLGTARRDLIKSE------EL-------------SSKHQRDLREALAQKED 293
Cdd:TIGR02169 599 igfavdlvEFDPKYEPAFKYVFGDTLVVEDIEAARRLMGKYRmvtlegELfeksgamtggsraPRGGILFSRSEPAELQR 678
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 294 MEERITTLEKRYLAAQREATSIHDLNDKLENELANKESLHR-------QCEEKARHLQELLEVAEQKLQQTMRKAET--- 363
Cdd:TIGR02169 679 LRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGeiekeieQLEQEEEKLKERLEELEEDLSSLEQEIENvks 758
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 364 -LPEVEAELAQRIAALTKAEERHGNIEEHL-----RQLEGQLEEKNQELARVRQR-----EKMNEDHNKR--LSDTVDRL 430
Cdd:TIGR02169 759 eLKELEARIEELEEDLHKLEEALNDLEARLshsriPEIQAELSKLEEEVSRIEARlreieQKLNRLTLEKeyLEKEIQEL 838
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 2017363561 431 LSESNErLQLHLKERMAALEE----KGRLSEEIEKLRQEVDQLKGR 472
Cdd:TIGR02169 839 QEQRID-LKEQIKSIEKEIENlngkKEELEEELEELEAALRDLESR 883
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
274-459 |
7.71e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.90 E-value: 7.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 274 EELSSKHQRDLREALAQKEDMEERITTLEKRY------LAAQREATSIHDLNDKLENELANKESLHRQCEEKARHLQELL 347
Cdd:PRK03918 570 EELAELLKELEELGFESVEELEERLKELEPFYneylelKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKEL 649
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 348 EVAEQKLQQT--MRKAETLPEVEAELAQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKrlsd 425
Cdd:PRK03918 650 EELEKKYSEEeyEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERVEE---- 725
|
170 180 190
....*....|....*....|....*....|....
gi 2017363561 426 tvdrlLSESNERLQLHLKERmaALEEKGRLSEEI 459
Cdd:PRK03918 726 -----LREKVKKYKALLKER--ALSKVGEIASEI 752
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
274-412 |
9.97e-04 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 43.14 E-value: 9.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 274 EELSSKHQR-----DLREALAQ-KEDMEERITTLEKRYLAAQREATSIHDLNDKLENELANKESLHRQCEEKARHLQ--- 344
Cdd:COG0497 209 EELEEERRRlsnaeKLREALQEaLEALSGGEGGALDLLGQALRALERLAEYDPSLAELAERLESALIELEEAASELRryl 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 345 -------ELLEVAEQKLQ---QTMRK----AETLPEVEAELAQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVR 410
Cdd:COG0497 289 dslefdpERLEEVEERLAllrRLARKygvtVEELLAYAEELRAELAELENSDERLEELEAELAEAEAELLEAAEKLSAAR 368
|
..
gi 2017363561 411 QR 412
Cdd:COG0497 369 KK 370
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
367-470 |
1.06e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 43.31 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 367 VEAELAQRIAALTKAEERHGNIEEHlrQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLlSESNERLQLHLKERM 446
Cdd:COG2433 378 IEEALEELIEKELPEEEPEAEREKE--HEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEK-DERIERLERELSEAR 454
|
90 100
....*....|....*....|....
gi 2017363561 447 AALEEKGRLSEEIEKLRQEVDQLK 470
Cdd:COG2433 455 SEERREIRKDREISRLDREIERLE 478
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
122-464 |
1.13e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.59 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 122 VSRHERSLRMTVVKR---------QAQSPSGVSSEVEVLKALKSLFEHH-------KALDEKVRERLRAALERVTTLEEQ 185
Cdd:PTZ00121 1217 ARKAEDAKKAEAVKKaeeakkdaeEAKKAEEERNNEEIRKFEEARMAHFarrqaaiKAEEARKADELKKAEEKKKADEAK 1296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 186 LAGAHQQVSALQQGAGVRDGA------AEEEGTVELGPKRLWKEDTGRVEELQELLEKQNFELSQARERLVTLTTTVTEL 259
Cdd:PTZ00121 1297 KAEEKKKADEAKKKAEEAKKAdeakkkAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEA 1376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 260 EEDLGTARR---DLIKSEELSSKHQRD------LREALAQKEDMEERITTLEKRYLAAQ-----REATSIHDLNDKLEnE 325
Cdd:PTZ00121 1377 KKKADAAKKkaeEKKKADEAKKKAEEDkkkadeLKKAAAAKKKADEAKKKAEEKKKADEakkkaEEAKKADEAKKKAE-E 1455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 326 LANKESLHRQCEEKaRHLQELLEVAEQKlqqtmRKAETLPEVEAELAQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQE 405
Cdd:PTZ00121 1456 AKKAEEAKKKAEEA-KKADEAKKKAEEA-----KKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKK 1529
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2017363561 406 LARVRQREKMNEDHNKRLSDTVDRL--LSESNERLQLHLKERmaALEEKGRLSEEIEKLRQ 464
Cdd:PTZ00121 1530 AEEAKKADEAKKAEEKKKADELKKAeeLKKAEEKKKAEEAKK--AEEDKNMALRKAEEAKK 1588
|
|
| SAM_1 |
pfam00536 |
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ... |
829-893 |
1.28e-03 |
|
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: 38.40 E-value: 1.28e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2017363561 829 QWDGPTVVSWLElWVGMPAwYVAACRANVKSGAIMSALSDTEIqREIGISNALHRLKLRLAIQEM 893
Cdd:pfam00536 2 GWSVEDVGEWLE-SIGLGQ-YIDSFRAGYIDGDALLQLTEDDL-LKLGVTLLGHRKKILYAIQRL 63
|
|
| SAM_2 |
pfam07647 |
SAM domain (Sterile alpha motif); |
952-1007 |
1.63e-03 |
|
SAM domain (Sterile alpha motif);
Pssm-ID: 429573 Cd Length: 66 Bit Score: 38.02 E-value: 1.63e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 2017363561 952 EWLPSLGLPQYRSYFMECLVD-ARMLDHLTKKDLRvHLKMVDSFHRTSLQYGIMCLK 1007
Cdd:pfam07647 11 DWLRSIGLEQYTDNFRDQGITgAELLLRLTLEDLK-RLGITSVGHRRKILKKIQELK 66
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
272-383 |
1.73e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.46 E-value: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 272 KSEELSSKHQRDLREALAQKEDMEERittLEKRYLAAQREATSIHDLNDKLENELANKESLHRQCEEKARHLQELLEVAE 351
Cdd:PRK12704 65 EIHKLRNEFEKELRERRNELQKLEKR---LLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQL 141
|
90 100 110
....*....|....*....|....*....|....*...
gi 2017363561 352 QKLQQTMR------KAETLPEVEAELAQRIAALTKAEE 383
Cdd:PRK12704 142 QELERISGltaeeaKEILLEKVEEEARHEAAVLIKEIE 179
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
165-470 |
1.80e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 42.73 E-value: 1.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 165 DEKVRERLRAALERVTTLEEQLAGAHQQVSALQQGAGVRDGAAEEEgtvelgpkRLWKEDTGRVEELQELLEKQNFELSQ 244
Cdd:TIGR00606 790 DVTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQ--------HELDTVVSKIELNRKLIQDQQEQIQH 861
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 245 ARERLVTLTTTVTELEEDLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLEN 324
Cdd:TIGR00606 862 LKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQD 941
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 325 ELankESLHRQCEEKARHLQELlevaEQKLQQTmrKAETLPEVEAELAQRIAALTKAEERHGNIEEHLRQLEgqleeknQ 404
Cdd:TIGR00606 942 KV---NDIKEKVKNIHGYMKDI----ENKIQDG--KDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMR-------Q 1005
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2017363561 405 ELARVRQREKMNEDHNKRLsdTVDRLLSESNERLQLHLKE--RMAALEEKgrlsEEIEKLRQEVDQLK 470
Cdd:TIGR00606 1006 DIDTQKIQERWLQDNLTLR--KRENELKEVEEELKQHLKEmgQMQVLQMK----QEHQKLEENIDLIK 1067
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
270-470 |
2.17e-03 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 41.41 E-value: 2.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 270 LIKSEELSSKHQRDLREALAQkeDMEERITTLE-------KRYLAAQREATSIHDLNDK--------LENELANKESlhr 334
Cdd:cd16269 107 CKQNEEASSKRCQALLQELSA--PLEEKISQGSysvpggyQLYLEDREKLVEKYRQVPRkgvkaeevLQEFLQSKEA--- 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 335 qcEEKArHLQ--ELLEVAEQKLQQTMRKAETLpEVEAELAQRIAALT--KAEERHGNIEEHLRQLEGQLEEKNQelarvr 410
Cdd:cd16269 182 --EAEA-ILQadQALTEKEKEIEAERAKAEAA-EQERKLLEEQQRELeqKLEDQERSYEEHLRQLKEKMEEERE------ 251
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 411 qrekmnedhnkrlsdtvdRLLSESNERLQLHLKErMAALEEKGrLSEEIEKLRQEVDQLK 470
Cdd:cd16269 252 ------------------NLLKEQERALESKLKE-QEALLEEG-FKEQAELLQEEIRSLK 291
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
230-452 |
2.21e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 42.40 E-value: 2.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 230 ELQELLEKQNFELSQARERLVTLTTTVTELEEDLGTARRDLIKSEELSSKHQRDLREALAQK----EDMEERITTLEKRY 305
Cdd:pfam05483 545 NLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKnkniEELHQENKALKKKG 624
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 306 LAAQREATSIHDLNDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELAQRI--AALTKAEE 383
Cdd:pfam05483 625 SAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIdkRCQHKIAE 704
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 384 RHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNK----RLSDTVDRLLS---------ESNERLQLHLKERMAALE 450
Cdd:pfam05483 705 MVALMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAaleiELSNIKAELLSlkkqleiekEEKEKLKMEAKENTAILK 784
|
..
gi 2017363561 451 EK 452
Cdd:pfam05483 785 DK 786
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
272-474 |
2.37e-03 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 42.15 E-value: 2.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 272 KSEELSSKHQRDLREALAQKEdMEERITTLEKRylAAQREATSIHDLNDKLenelanKESLHRQCEEKARHLQELLEVAE 351
Cdd:PLN03229 555 KAEKLKAEINKKFKEVMDRPE-IKEKMEALKAE--VASSGASSGDELDDDL------KEKVEKMKKEIELELAGVLKSMG 625
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 352 QKLQQTMRKAETLPEVEA--ELAQRIAALTkaEERHGNIEEHLR--QLEGQLEEKNQELARVrqrekmnedhnkrlSDTV 427
Cdd:PLN03229 626 LEVIGVTKKNKDTAEQTPppNLQEKIESLN--EEINKKIERVIRssDLKSKIELLKLEVAKA--------------SKTP 689
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2017363561 428 DRLLSESNERLQLHLKERMAALEEKGRLSEEIEKLRQEVDQLKGRGG 474
Cdd:PLN03229 690 DVTEKEKIEALEQQIKQKIAEALNSSELKEKFEELEAELAAARETAA 736
|
|
| SAM_Neurabin-like |
cd09512 |
SAM domain of SAM_Neurabin-like subfamily; SAM (sterile alpha motif) domain of Neurabin-like ... |
1030-1069 |
2.54e-03 |
|
SAM domain of SAM_Neurabin-like subfamily; SAM (sterile alpha motif) domain of Neurabin-like (Neural actin-binding) subfamily is a putative protein-protein interaction domain. This group currently includes the SAM domains of neurobin-I, SAMD14 and neurobin-I/SAMD14-like proteins. Most are multidomain proteins and in addition to SAM domain they contain other protein-binding domains such as PDZ and actin-binding domains. Members of this subfamily participate in signal transduction. Neurabin-I is involved in the regulation of Ca signaling intensity in alpha-adrenergic receptors; it forms a functional pair of opposing regulators with neurabin-II. Neurabins are expressed almost exclusively in neuronal cells. They are known to interact with protein phosphatase 1 and inhibit its activity; they also can bind actin filaments; however, the exact role of the SAM domain is unclear, since SAM doesn't participate in these interactions.
Pssm-ID: 188911 [Multi-domain] Cd Length: 70 Bit Score: 37.63 E-value: 2.54e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 2017363561 1030 VLVWTNDQVVHWVQSIGLRDYAGNLHESGVHG-ALLALDEN 1069
Cdd:cd09512 4 VSEWSVQQVCQWLMGLGLEQYIPEFTANNIDGqQLLQLDSS 44
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
227-377 |
2.78e-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: 40.68 E-value: 2.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 227 RVEELQELLEKQNFELSQARERLVTLTTTVTELEEDLGTARRDLIKSEEL--SSKHQRDLREALAQKEDMEERITTLEKR 304
Cdd:COG1579 32 ELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQlgNVRNNKEYEALQKEIESLKRRISDLEDE 111
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2017363561 305 YLaaqreatsihDLNDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELAQRIAA 377
Cdd:COG1579 112 IL----------ELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIPP 174
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
159-472 |
2.85e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.05 E-value: 2.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 159 EHHKALDEKVRERLRAALERVTTLEEQLAGAHQQVSALQQgagvrdgaAEEEGTVELGPKrlwKEDTGRVEELQELLE-- 236
Cdd:PTZ00121 1168 EARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARK--------AEEERKAEEARK---AEDAKKAEAVKKAEEak 1236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 237 KQNFELSQA-RERLVTLTTTVTELEEDLGTARRDLIKSEElsSKHQRDLREALAQKEDMEERITTLEKRYLAAQR---EA 312
Cdd:PTZ00121 1237 KDAEEAKKAeEERNNEEIRKFEEARMAHFARRQAAIKAEE--ARKADELKKAEEKKKADEAKKAEEKKKADEAKKkaeEA 1314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 313 TSIHDLNDKLENELANKESLHRQCEE-----------------KARHLQELLEVAEQKLQQTMRKAETLPEVEAELAQRI 375
Cdd:PTZ00121 1315 KKADEAKKKAEEAKKKADAAKKKAEEakkaaeaakaeaeaaadEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKAD 1394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 376 AALTKAEERHGNIEEHLRQLEgqlEEKNQELARVRQREKMNEDHNKRLSDTVDRLLSESNERLQLHLKERMAALEEKGRL 455
Cdd:PTZ00121 1395 EAKKKAEEDKKKADELKKAAA---AKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKK 1471
|
330 340
....*....|....*....|
gi 2017363561 456 SEEIEKLRQE---VDQLKGR 472
Cdd:PTZ00121 1472 ADEAKKKAEEakkADEAKKK 1491
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
81-324 |
3.35e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.82 E-value: 3.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 81 ATLTRELSMCREQLLEREEEISELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSpsgVSSEVE-------VLKA 153
Cdd:COG4913 613 AALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAE---LEAELErldassdDLAA 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 154 LKSLFEHHKALDEKVRERLRAALERVTTLEEQLAGAHQQVSALQQGAGVRDGAAEEEGTVELGPKRLWKEDTGRVEELQE 233
Cdd:COG4913 690 LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRE 769
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 234 LLEKQNFELSQARERLVTLTTTV--------TELEEDLGT---------ARRDLIKSEELsSKHQRDLREALaqKEDMEE 296
Cdd:COG4913 770 NLEERIDALRARLNRAEEELERAmrafnrewPAETADLDAdleslpeylALLDRLEEDGL-PEYEERFKELL--NENSIE 846
|
250 260
....*....|....*....|....*....
gi 2017363561 297 RITTLEKRYLAAQREATS-IHDLNDKLEN 324
Cdd:COG4913 847 FVADLLSKLRRAIREIKErIDPLNDSLKR 875
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
28-385 |
3.43e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 41.59 E-value: 3.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 28 QLMVNMLDEREKLLESLRESQETLAATQSRLQDAihERDQLQRHLNSALPQEfATLTRELSMCREQLLEREEEISELKAE 107
Cdd:TIGR02169 190 DLIIDEKRQQLERLRREREKAERYQALLKEKREY--EGYELLKEKEALERQK-EAIERQLASLEEELEKLTEEISELEKR 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 108 RNNTRLLLEHLECLVSRhERSLRMTVVKRQAQSpsgVSSEVEVLK-ALKSLFEHHKALDEKVR---ERLRAALERVTTLE 183
Cdd:TIGR02169 267 LEEIEQLLEELNKKIKD-LGEEEQLRVKEKIGE---LEAEIASLErSIAEKERELEDAEERLAkleAEIDKLLAEIEELE 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 184 EQLAGAHQQVSALQqgAGVRDGAAEEEGTVElgpkrlwkedtgRVEELQELLEKQNFELSQARERLVTLTTTVTELeedL 263
Cdd:TIGR02169 343 REIEEERKRRDKLT--EEYAELKEELEDLRA------------ELEEVDKEFAETRDELKDYREKLEKLKREINEL---K 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 264 GTARRDLIKSEELSSKhQRDLREALAQKED----MEERITTLEKRYLAAQREATSIHDLNDKLENELANKESLHRQCEEK 339
Cdd:TIGR02169 406 RELDRLQEELQRLSEE-LADLNAAIAGIEAkineLEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKE 484
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 2017363561 340 ARHLQELLEVAEQKLQQTMRKAETLPEVEAELAQRI-------AALTKAEERH 385
Cdd:TIGR02169 485 LSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIqgvhgtvAQLGSVGERY 537
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
267-472 |
3.49e-03 |
|
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: 41.88 E-value: 3.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 267 RRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIhDLNDKLENELANKESLHRQCEEKARHLQEL 346
Cdd:pfam02463 154 RRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKL-KEQAKKALEYYQLKEKLELEEEYLLYLDYL 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 347 LEVAEQK---------LQQTMRKAETLPEVEAELAQRIAALTKAEER-HGNIEEHLRQLEGQLEEKNQELARVRQREKMN 416
Cdd:pfam02463 233 KLNEERIdllqellrdEQEEIESSKQEIEKEEEKLAQVLKENKEEEKeKKLQEEELKLLAKEEEELKSELLKLERRKVDD 312
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2017363561 417 EDhNKRLSDTVDRLLSESNERLQLHLKERMAALEEKGRLSEEIEKLRQEVDQLKGR 472
Cdd:pfam02463 313 EE-KLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEK 367
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
273-410 |
4.75e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 40.72 E-value: 4.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 273 SEELSSKHQR---------DLREALA----QKEDMEERITTLEKRYLAAQREatsihdlNDKLENELANKESLHRQCEEK 339
Cdd:PRK09039 45 SREISGKDSAldrlnsqiaELADLLSlerqGNQDLQDSVANLRASLSAAEAE-------RSRLQALLAELAGAGAAAEGR 117
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2017363561 340 ARHLQELLEVAEQKLQQTMRKAETLPEVEAELAQRIAAL--------TKAEERHGNIEEHLRQLEGQLEEKNQELARVR 410
Cdd:PRK09039 118 AGELAQELDSEKQVSARALAQVELLNQQIAALRRQLAALeaaldaseKRDRESQAKIADLGRRLNVALAQRVQELNRYR 196
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
274-465 |
5.11e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 41.16 E-value: 5.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 274 EELSSKHQRDLREALAQKE---DMEERITTLEKRY--LAAQREA--TSIHDLNDKLENELANKESLHRQCEEKArhlQEL 346
Cdd:TIGR04523 422 ELLEKEIERLKETIIKNNSeikDLTNQDSVKELIIknLDNTRESleTQLKVLSRSINKIKQNLEQKQKELKSKE---KEL 498
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 347 LEVAEQKlQQTMRKAETLPEVEAELAQRIAAL----TKAEERHGNIEEHL---------RQLEGQLEEKNQELARVRQRE 413
Cdd:TIGR04523 499 KKLNEEK-KELEEKVKDLTKKISSLKEKIEKLesekKEKESKISDLEDELnkddfelkkENLEKEIDEKNKEIEELKQTQ 577
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2017363561 414 KMNEDHNKRLSDTVDRLLSESNErlqlhLKERMAALEEK-GRLSEEIEKLRQE 465
Cdd:TIGR04523 578 KSLKKKQEEKQELIDQKEKEKKD-----LIKEIEEKEKKiSSLEKELEKAKKE 625
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
169-412 |
5.35e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.77 E-value: 5.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 169 RERLRAAL----ERVTTLEEQLAGAHQQVSALQQGAGVRDGAAEEEGTVElgpkrlwkedtgRVEELQELLEKQNFELSQ 244
Cdd:COG3206 170 REEARKALefleEQLPELRKELEEAEAALEEFRQKNGLVDLSEEAKLLLQ------------QLSELESQLAEARAELAE 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 245 ARERLVTLTTTVteleedlgtARRDLIKSEELSSKHQRDLREALAQkedMEERITTLEKRYLAAQREATSihdlndkLEN 324
Cdd:COG3206 238 AEARLAALRAQL---------GSGPDALPELLQSPVIQQLRAQLAE---LEAELAELSARYTPNHPDVIA-------LRA 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 325 ELANKEslhrqceekarhlQELLEVAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQ 404
Cdd:COG3206 299 QIAALR-------------AQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARE 365
|
....*...
gi 2017363561 405 ELARVRQR 412
Cdd:COG3206 366 LYESLLQR 373
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
30-415 |
5.47e-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: 40.44 E-value: 5.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 30 MVNMLDEREKLLESLRESQETLAATQSRLQDAIHERDQLQRHLNS------ALPQEFATLTRELSmcreqllereeeisE 103
Cdd:pfam19220 15 MADRLEDLRSLKADFSQLIEPIEAILRELPQAKSRLLELEALLAQeraaygKLRRELAGLTRRLS--------------A 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 104 LKAERNNTRLLLEHLECLVSRHER---SLRMTVVKRQAQSPS---GVSSEVEVLKALKslfEHHKALdekvRERLRAALE 177
Cdd:pfam19220 81 AEGELEELVARLAKLEAALREAEAakeELRIELRDKTAQAEAlerQLAAETEQNRALE---EENKAL----REEAQAAEK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 178 RVTTLEEQLAGAHQQVSALQQGAGVRDGAAEEEG--TVELGpkRLWKEDTGRVEELQELLEKQNFELSQARERLVTLTTT 255
Cdd:pfam19220 154 ALQRAEGELATARERLALLEQENRRLQALSEEQAaeLAELT--RRLAELETQLDATRARLRALEGQLAAEQAERERAEAQ 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 256 VTELEEDLGTARRDL-IKSEELSSKH---QRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENELANKES 331
Cdd:pfam19220 232 LEEAVEAHRAERASLrMKLEALTARAaatEQLLAEARNQLRDRDEAIRAAERRLKEASIERDTLERRLAGLEADLERRTQ 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 332 LHrQCEEKARhlQELLEVAEqklqqTMRKAetlpeveaeLAQRIAALTKAEERHGNIEEHLRQLEGQ-------LEEKNQ 404
Cdd:pfam19220 312 QF-QEMQRAR--AELEERAE-----MLTKA---------LAAKDAALERAEERIASLSDRIAELTKRfeveraaLEQANR 374
|
410
....*....|.
gi 2017363561 405 ELARVRQREKM 415
Cdd:pfam19220 375 RLKEELQRERA 385
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
291-470 |
5.56e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 40.77 E-value: 5.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 291 KEDMEERITTLEKRYLAAQREATSIHDLNDK---LENELANKESLHRQCEEKARHLQ---ELLEVAEQKLQQTMRKAETl 364
Cdd:TIGR04523 362 QRELEEKQNEIEKLKKENQSYKQEIKNLESQindLESKIQNQEKLNQQKDEQIKKLQqekELLEKEIERLKETIIKNNS- 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 365 pEVEaELAQRIAALTKAEERHGNIEEHLRQ----LEGQ-------LEEKNQELARVRQREKMNEDHNKRLSDTVDRLLSE 433
Cdd:TIGR04523 441 -EIK-DLTNQDSVKELIIKNLDNTRESLETqlkvLSRSinkikqnLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKK 518
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2017363561 434 SNErlqlhLKERMAALE------------------------EKGRLSEEIEKLRQEVDQLK 470
Cdd:TIGR04523 519 ISS-----LKEKIEKLEsekkekeskisdledelnkddfelKKENLEKEIDEKNKEIEELK 574
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
269-484 |
5.97e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 40.77 E-value: 5.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 269 DLIKSE-ELSSKHQRDLREALAQkedmeeRITTLEKRYLAAQREATSIHDLNDKLENELANkesLHRQCEEKARHLQEL- 346
Cdd:PHA02562 191 DHIQQQiKTYNKNIEEQRKKNGE------NIARKQNKYDELVEEAKTIKAEIEELTDELLN---LVMDIEDPSAALNKLn 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 347 -------LEVAE-QKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNED 418
Cdd:PHA02562 262 taaakikSKIEQfQKVIKMYEKGGVCPTCTQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSKKLLE 341
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2017363561 419 HNKRLSdTVDRLLS---ESNERLQLHLKErmaALEEKGRLSEEIEKLRQEVDQLKGRGGPFVDGVHSRS 484
Cdd:PHA02562 342 LKNKIS-TNKQSLItlvDKAKKVKAAIEE---LQAEFVDNAEELAKLQDELDKIVKTKSELVKEKYHRG 406
|
|
| SAM_SARM1-like_repeat1 |
cd09501 |
SAM domain ot SARM1-like proteins, repeat 1; SAM (sterile alpha motif) domain repeat 1 of ... |
952-996 |
6.94e-03 |
|
SAM domain ot SARM1-like proteins, repeat 1; SAM (sterile alpha motif) domain repeat 1 of SARM1-like adaptor proteins is a protein-protein interaction domain. SARM1-like proteins contain two tandem SAM domains. SARM1-like proteins are involved in TLR (Toll-like receptor) signaling. They are responsible for targeted localization of the whole protein to post-synaptic regions of axons. In humans SARM1 expression is detected in kidney and liver.
Pssm-ID: 188900 [Multi-domain] Cd Length: 69 Bit Score: 36.51 E-value: 6.94e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 2017363561 952 EWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHR 996
Cdd:cd09501 11 TWLKQIGFEDYAEKFSESQVDGDLLLQLTEDELKQDLGMSSGLLR 55
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
343-470 |
7.08e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 40.61 E-value: 7.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 343 LQELLEVAEQKLQQTMRKAETLPEVE-AELAQRIAALtkaEERHGNIEEHLRQLEGQLEEKNQELARVRQR---EKMNED 418
Cdd:COG2433 382 LEELIEKELPEEEPEAEREKEHEERElTEEEEEIRRL---EEQVERLEAEVEELEAELEEKDERIERLERElseARSEER 458
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 2017363561 419 HNKRLSDTVDRLLSEsNERLQLHLKErmaaleekgrLSEEIEKLRQEVDQLK 470
Cdd:COG2433 459 REIRKDREISRLDRE-IERLERELEE----------ERERIEELKRKLERLK 499
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
223-469 |
9.36e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 40.16 E-value: 9.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 223 EDTGRVEE--LQELLEKQNF---ELSQARERLVTLTTTVTELEEDLGTARRDLikSEELSSKHQRDLrEALAQKEDMEER 297
Cdd:pfam01576 337 EEETRSHEaqLQEMRQKHTQaleELTEQLEQAKRNKANLEKAKQALESENAEL--QAELRTLQQAKQ-DSEHKRKKLEGQ 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 298 ITTLEKRYLAAQREATSIHDLNDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMrkaETLPEveaELAQRIAA 377
Cdd:pfam01576 414 LQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQ---ELLQE---ETRQKLNL 487
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363561 378 LTKAEErhgnIEEHLRQLEGQLEEknqELARVRQREKMNEDHNKRLSDTVDRL---------LSESNERLQLHLKERMAA 448
Cdd:pfam01576 488 STRLRQ----LEDERNSLQEQLEE---EEEAKRNVERQLSTLQAQLSDMKKKLeedagtleaLEEGKKRLQRELEALTQQ 560
|
250 260
....*....|....*....|....*
gi 2017363561 449 LEEKGRLSEEIEK----LRQEVDQL 469
Cdd:pfam01576 561 LEEKAAAYDKLEKtknrLQQELDDL 585
|
|
| |
