|
Name |
Accession |
Description |
Interval |
E-value |
| 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 ... |
1098-1169 |
3.68e-44 |
|
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: 154.01 E-value: 3.68e-44
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 333805618 1098 DVLVWSNDRVIRWIQAIGLREYANNILESGVHGSLIALDENFDYSSLALLLQIPTQNTQARQILEREYNNLL 1169
Cdd:cd09568 1 DVLVWSNERVIRWVQSIGLREYANNLLESGVHGALIALDETFDANSFALALQIPTQNTQARQILEREFNNLL 72
|
|
| 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 ... |
895-965 |
6.55e-44 |
|
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: 153.10 E-value: 6.55e-44
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 333805618 895 FAQWDGPTVVAWLELWLGMPAWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEMVSLT 965
Cdd:cd09562 1 FALWNGPTVVAWLELWVGMPAWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEMVSLT 71
|
|
| SAM_liprin-alpha1,2,3,4_repeat2 |
cd09565 |
SAM domain of liprin-alpha1,2,3,4 proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 ... |
1013-1078 |
1.14e-43 |
|
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: 152.24 E-value: 1.14e-43
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 333805618 1013 MNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLKRL 1078
Cdd:cd09565 1 MNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRTHLKMVDSFHRTSLQYGILCLKRL 66
|
|
| SAM_liprin-kazrin_repeat2 |
cd09495 |
SAM domain of liprin/kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of ... |
1017-1076 |
2.31e-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: 116.86 E-value: 2.31e-31
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 1017 WIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLK 1076
Cdd:cd09495 1 WWVTRWLDDIGLPQYKDQFHESLVDRRMLQYLTVNDLLVHLKVTSQLHHLSLKCGIHVLH 60
|
|
| SAM_liprin-kazrin_repeat1 |
cd09494 |
SAM domain of liprin/kazrin proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of ... |
902-960 |
3.85e-27 |
|
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: 105.00 E-value: 3.85e-27
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 333805618 902 TVVAWLELWLGMPaWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQE 960
Cdd:cd09494 1 RVCAWLEDFGLMP-MYVIFCRQNVKSGHTLLTLSDQEMEKELGIKNPLHRKKLRLAIKE 58
|
|
| SAM_liprin-kazrin_repeat3 |
cd09496 |
SAM domain of liprin/kazrin proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 of ... |
1106-1167 |
7.51e-25 |
|
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: 98.38 E-value: 7.51e-25
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 333805618 1106 RVIRWIQAIGLREYANNILESGVHGSLIALDENFDYSSLALLLQIPTQNTQARQILEREYNN 1167
Cdd:cd09496 1 RVIHWIRSIDLREYANNLVESGVHGGLLVLEPNFDHNTMALVLQIPPQKTQARRHLETEFNN 62
|
|
| SAM_kazrin_repeat3 |
cd09570 |
SAM domain of kazrin proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 of kazrin ... |
1098-1169 |
1.46e-18 |
|
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: 80.95 E-value: 1.46e-18
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 333805618 1098 DVLVWSNDRVIRWIQAIGLREYANNILESGVHGSLIALDENFDYSSLALLLQIPTQNTQARQILEREYNNLL 1169
Cdd:cd09570 1 DPVVWTNQRVIKWARSIDLKEYADNLRDSGVHGALMVLEPSFNSDTMATALGIPSSKNIIRRHLTTEMEALV 72
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning]; |
201-533 |
5.41e-18 |
|
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 224117 [Multi-domain] Cd Length: 1163 Bit Score: 90.16 E-value: 5.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 201 RVSALEEELAAANQEIVALREQNVHIQRKMASSEgstesEHLEGMEPGQKVHEKRLSNGSIDSTDETSQIVELQELLEKQ 280
Cdd:COG1196 668 ELKELEEELAELEAQLEKLEEELKSLKNELRSLE-----DLLEELRRQLEELERQLEELKRELAALEEELEQLQSRLEEL 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 281 NYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRYLSAQRESTSIHDM 360
Cdd:COG1196 743 EEELEELEEELEELQERLEELEEELESLEEALAKLKEEIEELEEKRQALQEELEELEEELEEAERRLDALERELESLEQR 822
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 361 NDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQ 440
Cdd:COG1196 823 RERLEQEIEELEEEIEELEEKLDELEEELEELEKELEELKEELEELEAEKEELEDELKELEEEKEELEEELRELESELAE 902
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 441 LEEKNQEL-QRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAALEEK-------NVL-IQESETFRKNLEES 511
Cdd:COG1196 903 LKEEIEKLrERLEELEAKLERLEVELPELEEELEEEYEDTLETELEREIERLEEEiealgpvNLRaIEEYEEVEERYEEL 982
|
330 340
....*....|....*....|..
gi 333805618 512 LHDKERLAEEIEKLRSELDQLK 533
Cdd:COG1196 983 KSQREDLEEAKEKLLEVIEELD 1004
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning]; |
87-471 |
4.83e-17 |
|
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 224117 [Multi-domain] Cd Length: 1163 Bit Score: 87.08 E-value: 4.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 87 SLTGGLAGSKG--ADPPEFAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLRMtvvkrqaqsp 164
Cdd:COG1196 651 SITGGSRNKRSslAQKRELKELEEELAELEAQLEKLEEELKSLKNELRSLEDLLEELRRQLEELERQLEE---------- 720
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 165 sgvssevevlkaLKSLFEHHKALDEKVRERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMASSEgsTESEHLEG 244
Cdd:COG1196 721 ------------LKRELAALEEELEQLQSRLEELEEELEELEEELEELQERLEELEEELESLEEALAKLK--EEIEELEE 786
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 245 MEPGQKVHEKRLsNGSIDSTDEtsQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQR 324
Cdd:COG1196 787 KRQALQEELEEL-EEELEEAER--RLDALERELESLEQRRERLEQEIEELEEEIEELEEKLDELEEELEELEKELEELKE 863
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 325 DIREAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTmRKAE 404
Cdd:COG1196 864 ELEELEAEKEELEDELKELEEEKEELEEELRELESELAELKEEIEKLRERLEELEAKLERLEVELPELEEELEEE-YEDT 942
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 333805618 405 TLPEVEAELAQ---RIAAL----TKAEERHGNIEERMRHLEGQLEEKNQELQRARQR-EKMNEEHNKRLSDTVDR 471
Cdd:COG1196 943 LETELEREIERleeEIEALgpvnLRAIEEYEEVEERYEELKSQREDLEEAKEKLLEViEELDKEKRERFKETFDK 1017
|
|
| SAM_kazrin_repeat1 |
cd09564 |
SAM domain of kazrin proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of kazrin ... |
896-960 |
6.27e-17 |
|
SAM domain of kazrin proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of kazrin proteins is a protein-protein interaction domain. The long isoform of kazrin contains three copies (repeats) of SAM domain. Kazrin can interact with periplakin. It is involved into interplay between desmosomes and in adheren junctions. Additionally kazrins play a role in regulation of intercellular differentiation, junction assembly, and cytoskeletal organization.
Pssm-ID: 188963 Cd Length: 70 Bit Score: 76.34 E-value: 6.27e-17
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 333805618 896 AQWDGPTVVAWLELWLGMPAwYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQE 960
Cdd:cd09564 2 SRWKADMVLAWLEVVMHMPM-YSKACAENVKSGKVLLGLSDSELESGLGISNVLHRRKLRLAIEE 65
|
|
| SAM_kazrin_repeat2 |
cd09567 |
SAM domain of kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of kazrin ... |
1012-1076 |
1.83e-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: 74.75 E-value: 1.83e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 333805618 1012 DMNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLK 1076
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 ... |
1012-1076 |
1.89e-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: 74.65 E-value: 1.89e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 333805618 1012 DMNHEWIgNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLrVHLKMVDSFHRTSLQYGIMCLK 1076
Cdd:cd09566 1 KLDTHWV-LRWLDDIGLPQYKDAFSEAKVDGRMLHYLTVDDL-LHLKVTSALHHASIRRGIQVLR 63
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
83-481 |
6.33e-16 |
|
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: 83.57 E-value: 6.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 83 QDIESLTGGLAGSKGADPPEFAAL--TKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQ 160
Cdd:TIGR02168 650 LDGDLVRPGGVITGGSAKTNSSILerRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQIS 729
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 161 AQSPSGVSSEVEVLKALKSLFEHHKALDEkVRERLRVSLERVSALEEELAAANQEIVALREQnvhIQRkmASSEGSTESE 240
Cdd:TIGR02168 730 ALRKDLARLEAEVEQLEERIAQLSKELTE-LEAEIEELEERLEEAEEELAEAEAEIEELEAQ---IEQ--LKEELKALRE 803
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 241 HLEGMEPGQKVHEKRLSNGSIDSTDETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNT 320
Cdd:TIGR02168 804 ALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERA 883
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 321 KYQRDIREAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELAnkeailrQMEEKNRQLQERL-ELAEQKLQQT 399
Cdd:TIGR02168 884 SLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLE-------GLEVRIDNLQERLsEEYSLTLEEA 956
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 400 MRKAETLPEVEAELAQRIAALTKAEERHGNI-----------EERMRHLEGQLEeknqELQRARQR-----EKMNEEHNK 463
Cdd:TIGR02168 957 EALENKIEDDEEEARRRLKRLENKIKELGPVnlaaieeyeelKERYDFLTAQKE----DLTEAKETleeaiEEIDREARE 1032
|
410
....*....|....*...
gi 333805618 464 RLSDTVDRLltesNERLQ 481
Cdd:TIGR02168 1033 RFKDTFDQV----NENFQ 1046
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning]; |
269-539 |
6.65e-16 |
|
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 224117 [Multi-domain] Cd Length: 1163 Bit Score: 83.23 E-value: 6.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 269 QIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRYl 348
Cdd:COG1196 233 KLKELRKELEELEEELSRLEEELEELQEELEEAEKEIEELKSELEELREELEELQEELLELKEEIEELEGEISLLRERL- 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 349 saqrestsihdmnDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERH- 427
Cdd:COG1196 312 -------------EELENELEELEERLEELKEKIEALKEELEERETLLEELEQLLAELEEAKEELEEKLSALLEELEELf 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 428 GNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTE------SNERLQLHLKERMAALEEKNVLIQES 501
Cdd:COG1196 379 EALREELAELEAELAEIRNELEELKREIESLEERLERLSERLEDLKEElkeleaELEELQTELEELNEELEELEEQLEEL 458
|
250 260 270
....*....|....*....|....*....|....*...
gi 333805618 502 ETFRKNLEESLhdkERLAEEIEKLRSELDQLKMRTGSL 539
Cdd:COG1196 459 RDRLKELEREL---AELQEELQRLEKELSSLEARLDRL 493
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
40-529 |
1.87e-15 |
|
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: 82.03 E-value: 1.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 40 DERDRLLDTLRETQESLSLAQQRLQDVIYDRDSLQRQLNSALPQdIESLTGGLAGSKGadppEFAALTKELNACREQLLE 119
Cdd:TIGR02168 309 ERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEE-LESLEAELEELEA----ELEELESRLEELEEQLET 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 120 KEEEISELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSPSGVSSEvevLKALKSLFEHHKALDEKVRERLRVSL 199
Cdd:TIGR02168 384 LRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAE---LKELQAELEELEEELEELQEELERLE 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 200 ERVSALEEELAAANQEIVALREQNVHIQRKMASSEgsTESEHLEGMEPGQK--VHEKRLSNG---------SIDSTDET- 267
Cdd:TIGR02168 461 EALEELREELEEAEQALDAAERELAQLQARLDSLE--RLQENLEGFSEGVKalLKNQSGLSGilgvlseliSVDEGYEAa 538
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 268 -----------------SQIVELQELLEKQNYEMAQMKE----RLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQR-- 324
Cdd:TIGR02168 539 ieaalggrlqavvvenlNAAKKAIAFLKQNELGRVTFLPldsiKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKal 618
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 325 -----------DIREAMAQ--KEDMEERITTLE-----KRYLSAQRESTSIHDMNDKlENELANKEAILRQMEEKNRQLQ 386
Cdd:TIGR02168 619 syllggvlvvdDLDNALELakKLRPGYRIVTLDgdlvrPGGVITGGSAKTNSSILER-RREIEELEEKIEELEEKIAELE 697
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 387 ERLELAEQKLQQTMRKAETLPEVEAELAQRIAA----LTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHN 462
Cdd:TIGR02168 698 KALAELRKELEELEEELEQLRKELEELSRQISAlrkdLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEEL 777
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 333805618 463 KRLSD---TVDRLLTESNERLQLhLKERMAALEEK----NVLIQESETFRKNLEESLHDKERLAEEIEKLRSEL 529
Cdd:TIGR02168 778 AEAEAeieELEAQIEQLKEELKA-LREALDELRAEltllNEEAANLRERLESLERRIAATERRLEDLEEQIEEL 850
|
|
| SAM_liprin-beta1,2_repeat3 |
cd09569 |
SAM domain of liprin-beta proteins repeat 3; SAM (sterile alpha motif) domain repea t3 of ... |
1098-1169 |
2.53e-15 |
|
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: 71.72 E-value: 2.53e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 333805618 1098 DVLVWSNDRVIRWIQAIGLREYANNILESGVHGSLIALDENFDYSSLALLLQIPTQNTQARQILEREYNNLL 1169
Cdd:cd09569 1 EVVLWTNHRVMEWLRSVDLAEYAPNLRGSGVHGALMVLEPRFTAETLAALLNIPPNKTLLRRHLATHFNQLL 72
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
267-534 |
3.22e-15 |
|
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: 81.26 E-value: 3.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 267 TSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKR 346
Cdd:TIGR02168 711 EEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQ 790
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 347 YLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEER 426
Cdd:TIGR02168 791 IEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEE 870
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 427 hgnIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRL---LTESNERL-QLHLKERMAALEEKNVLIQESE 502
Cdd:TIGR02168 871 ---LESELEALLNERASLEEALALLRSELEELSEELRELESKRSELrreLEELREKLaQLELRLEGLEVRIDNLQERLSE 947
|
250 260 270
....*....|....*....|....*....|..
gi 333805618 503 TFRKNLEESLHDKERLAEEIEKLRSELDQLKM 534
Cdd:TIGR02168 948 EYSLTLEEAEALENKIEDDEEEARRRLKRLEN 979
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
288-541 |
4.72e-15 |
|
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: 80.49 E-value: 4.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 288 KERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENE 367
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 368 LANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLpevEAELAQRIAALTKAEERH-------GNIEERMRHLEGQ 440
Cdd:TIGR02168 756 LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQL---KEELKALREALDELRAELtllneeaANLRERLESLERR 832
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 441 LEEKNQELQRARQREKMNEEHNKRLSDTVDRL---LTESNERLQLHLKER-------MAALEEKNVLIQESETFRKNLEE 510
Cdd:TIGR02168 833 IAATERRLEDLEEQIEELSEDIESLAAEIEELeelIEELESELEALLNERasleealALLRSELEELSEELRELESKRSE 912
|
250 260 270
....*....|....*....|....*....|.
gi 333805618 511 SLHDKERLAEEIEKLRSELDQLKMRTGSLIE 541
Cdd:TIGR02168 913 LRRELEELREKLAQLELRLEGLEVRIDNLQE 943
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning]; |
283-535 |
6.62e-15 |
|
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 224117 [Multi-domain] Cd Length: 1163 Bit Score: 80.14 E-value: 6.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 283 EMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRYLSAQRESTSIHDMND 362
Cdd:COG1196 668 ELKELEEELAELEAQLEKLEEELKSLKNELRSLEDLLEELRRQLEELERQLEELKRELAALEEELEQLQSRLEELEEELE 747
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 363 KLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTmrkAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLE 442
Cdd:COG1196 748 ELEEELEELQERLEELEEELESLEEALAKLKEEIEEL---EEKRQALQEELEELEEELEEAERRLDALERELESLEQRRE 824
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 443 EKNQELQRARQREKMNEEHNKRLSDTVDRLlTESNERLQLHLKERMAALEEKNVLIQESETFRKNLEESL----HDKERL 518
Cdd:COG1196 825 RLEQEIEELEEEIEELEEKLDELEEELEEL-EKELEELKEELEELEAEKEELEDELKELEEEKEELEEELreleSELAEL 903
|
250
....*....|....*..
gi 333805618 519 AEEIEKLRSELDQLKMR 535
Cdd:COG1196 904 KEEIEKLRERLEELEAK 920
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
263-535 |
6.68e-15 |
|
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: 80.10 E-value: 6.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 263 STDETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITT 342
Cdd:TIGR02168 665 SAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQ 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 343 LEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTmrkAETLPEVEAELAQRIAALTK 422
Cdd:TIGR02168 745 LEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKAL---REALDELRAELTLLNEEAAN 821
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 423 AEERHGNIEERMRHLEGQLEEKNQELQRAR-QREKMNEEHNKrlsdtVDRLLTESNERLQLHLKERMAALEEKNVLIQES 501
Cdd:TIGR02168 822 LRERLESLERRIAATERRLEDLEEQIEELSeDIESLAAEIEE-----LEELIEELESELEALLNERASLEEALALLRSEL 896
|
250 260 270
....*....|....*....|....*....|....
gi 333805618 502 ETFRKNLEESLHDKERLAEEIEKLRSELDQLKMR 535
Cdd:TIGR02168 897 EELSEELRELESKRSELRRELEELREKLAQLELR 930
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning]; |
265-535 |
7.91e-15 |
|
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 224117 [Multi-domain] Cd Length: 1163 Bit Score: 79.76 E-value: 7.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 265 DETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQ-------EAETARKDLIKTEEM----NTKYQRDIREAMAQK 333
Cdd:COG1196 162 EEAAGVSKYKERKEEAERKLERTEENLERLEDLLEELEKqleklerQAEKAERYQELKAELreleLALLLAKLKELRKEL 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 334 EDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAEL 413
Cdd:COG1196 242 EELEEELSRLEEELEELQEELEEAEKEIEELKSELEELREELEELQEELLELKEEIEELEGEISLLRERLEELENELEEL 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 414 AQRIAALtkaEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAALEE 493
Cdd:COG1196 322 EERLEEL---KEKIEALKEELEERETLLEELEQLLAELEEAKEELEEKLSALLEELEELFEALREELAELEAELAEIRNE 398
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 333805618 494 KNVLIQESETFRKNLEESLHDKERLAEEIEKLRSELDQLKMR 535
Cdd:COG1196 399 LEELKREIESLEERLERLSERLEDLKEELKELEAELEELQTE 440
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning]; |
231-534 |
1.14e-14 |
|
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 224117 [Multi-domain] Cd Length: 1163 Bit Score: 79.37 E-value: 1.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 231 ASSEGSTESEHLEGMEPGQKVHEKRLSNGSIDSTDETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARK 310
Cdd:COG1196 665 QKRELKELEEELAELEAQLEKLEEELKSLKNELRSLEDLLEELRRQLEELERQLEELKRELAALEEELEQLQSRLEELEE 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 311 DLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLE 390
Cdd:COG1196 745 ELEELEEELEELQERLEELEEELESLEEALAKLKEEIEELEEKRQALQEELEELEEELEEAERRLDALERELESLEQRRE 824
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 391 LAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEErhgNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVD 470
Cdd:COG1196 825 RLEQEIEELEEEIEELEEKLDELEEELEELEKELE---ELKEELEELEAEKEELEDELKELEEEKEELEEELRELESELA 901
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 333805618 471 RLLTEsNERLQLHLKERMAALEEKNVLIQESETFRKNLEESLHDKErLAEEIEKLRSELDQLKM 534
Cdd:COG1196 902 ELKEE-IEKLRERLEELEAKLERLEVELPELEEELEEEYEDTLETE-LEREIERLEEEIEALGP 963
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
174-527 |
1.23e-14 |
|
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: 79.33 E-value: 1.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 174 LKALKSLFEHHKALDEKVRERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMASSEGSTESEHLEGMEPGQKVHE 253
Cdd:TIGR02168 700 LAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAE 779
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 254 KRlsngsidstdetSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQK 333
Cdd:TIGR02168 780 AE------------AEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQI 847
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 334 EDMEERITTLEKRYLSAQREStsihdmnDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQqtmrkaetlpEVEAEL 413
Cdd:TIGR02168 848 EELSEDIESLAAEIEELEELI-------EELESELEALLNERASLEEALALLRSELEELSEELR----------ELESKR 910
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 414 AQRIAALTKAEERHGNIEERMRHLEGQLEEKnqeLQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLhLKERMAALEE 493
Cdd:TIGR02168 911 SELRRELEELREKLAQLELRLEGLEVRIDNL---QERLSEEYSLTLEEAEALENKIEDDEEEARRRLKR-LENKIKELGP 986
|
330 340 350
....*....|....*....|....*....|....*
gi 333805618 494 KNVL-IQESETFRKNLEESLHDKERLAEEIEKLRS 527
Cdd:TIGR02168 987 VNLAaIEEYEELKERYDFLTAQKEDLTEAKETLEE 1021
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
102-589 |
1.27e-14 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 78.93 E-value: 1.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 102 EFAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLrmtvvkrqaqspsgvsSEVEVLKALKSLF 181
Cdd:PRK02224 200 EEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERR----------------EELETLEAEIEDL 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 182 EHHKALDEKVRERLRVSLERVSALEEELAAANQEIVALREqnvhiqrkMASSEGSTESEHLEGMEPGQKVHEKRLSNGSI 261
Cdd:PRK02224 264 RETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAG--------LDDADAEAVEARREELEDRDEELRDRLEECRV 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 262 DSTDETSQIVELqellekqnyemaqmKERLAALSSRVGEVEQEAETARKDLIKTEEmntkyqrDIREAMAQKEDMEERIT 341
Cdd:PRK02224 336 AAQAHNEEAESL--------------REDADDLEERAEELREEAAELESELEEARE-------AVEDRREEIEELEEEIE 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 342 TLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQklqqtMRKAETLPEVEAEL--AQRIAA 419
Cdd:PRK02224 395 ELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEA-----LLEAGKCPECGQPVegSPHVET 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 420 LTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLS--DTVDRLLTESNERLQlHLKERMAAL-EEKNV 496
Cdd:PRK02224 470 IEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEErrEDLEELIAERRETIE-EKRERAEELrERAAE 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 497 LIQESETFRKNLEESLHDKERLAEEIEKLRSELDQLKMRTGSLiePTIpRTHLDTSAELRYSVGSLVDSQSDYRTTKVIR 576
Cdd:PRK02224 549 LEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESL--ERI-RTLLAAIADAEDEIERLREKREALAELNDER 625
|
490
....*....|...
gi 333805618 577 RPRRGRMGVRRDE 589
Cdd:PRK02224 626 RERLAEKRERKRE 638
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
114-533 |
2.50e-14 |
|
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: 78.19 E-value: 2.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 114 REQLLEKEEEISELKAERNNTRLLLEHLECLVsrHERSLRMTVVKRQAqspSGVSSEVEVLKAlkslfEHhkaldEKVRE 193
Cdd:TIGR02169 673 PAELQRLRERLEGLKRELSSLQSELRRIENRL--DELSQELSDASRKI---GEIEKEIEQLEQ-----EE-----EKLKE 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 194 RLRVSLERVSALEEELAAANQEIVALREQnvhIQRKMAssegstesehlegmepgqKVHEKRLSNGSIDSTDETSQIVEL 273
Cdd:TIGR02169 738 RLEELEEDLSSLEQEIENVKSELKELEAR---IEELEE------------------DLHKLEEALNDLEARLSHSRIPEI 796
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 274 QELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARkdliktEEMNTKyQRDIREAMAQKEDMEERITTLEKRYlsaqre 353
Cdd:TIGR02169 797 QAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLE------KEIQEL-QEQRIDLKEQIKSIEKEIENLNGKK------ 863
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 354 stsihdmnDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLpEVEAELAQRIAALTKAeeRHGNIEER 433
Cdd:TIGR02169 864 --------EELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEEL-EAQIEKKRKRLSELKA--KLEALEEE 932
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 434 MRHLE---GQLEEKNQELQRARQREKMNEEhnkrlsdtvdrlltesnerlqlhLKERMAALEEKNVL-IQESETFRKNLE 509
Cdd:TIGR02169 933 LSEIEdpkGEDEEIPEEELSLEDVQAELQR-----------------------VEEEIRALEPVNMLaIQEYEEVLKRLD 989
|
410 420
....*....|....*....|....*..
gi 333805618 510 ESLHDKERLAEE---IEKLRSELDQLK 533
Cdd:TIGR02169 990 ELKEKRAKLEEErkaILERIEEYEKKK 1016
|
|
| SAM_1 |
pfam00536 |
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ... |
1012-1076 |
6.90e-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 heterooligomerize with other SAM domains.
Pssm-ID: 425739 Cd Length: 64 Bit Score: 67.29 E-value: 6.90e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 333805618 1012 DMNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRvHLKMVDSFHRTSLQYGIMCLK 1076
Cdd:pfam00536 1 DGWSVEDVGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDDLL-KLGVTLLGHRKKILYAIQRLK 64
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning]; |
41-697 |
1.79e-13 |
|
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 224117 [Multi-domain] Cd Length: 1163 Bit Score: 75.52 E-value: 1.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 41 ERDRLLDTLRETQESLSLAQQRLQDVIYDRDSLQRQLNSALpQDIESLTGglagskgadppEFAALTKELNACREQLLEK 120
Cdd:COG1196 226 ELALLLAKLKELRKELEELEEELSRLEEELEELQEELEEAE-KEIEELKS-----------ELEELREELEELQEELLEL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 121 EEEISELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSpSGVSSEVEVLKALKSLFEHHKALDEKVRERLRVSLE 200
Cdd:COG1196 294 KEEIEELEGEISLLRERLEELENELEELEERLEELKEKIEALK-EELEERETLLEELEQLLAELEEAKEELEEKLSALLE 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 201 ----RVSALEEELAAANQEIVALREQNVHIQRKMASSEGSTESEHLEGMEPGQKVHEKRLSNGSIDSTDET--SQIVELQ 274
Cdd:COG1196 373 eleeLFEALREELAELEAELAEIRNELEELKREIESLEERLERLSERLEDLKEELKELEAELEELQTELEElnEELEELE 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 275 ELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTL------EKRYL 348
Cdd:COG1196 453 EQLEELRDRLKELERELAELQEELQRLEKELSSLEARLDRLEAEQRASQGVRAVLEALESGLPGVYGPVaelikvKEKYE 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 349 SA--------------------------------------------QRESTSIHDMNDKL-----------ENELANKeA 373
Cdd:COG1196 533 TAleaalgnrlqavvveneevakkaieflkenkagratflpldrikPLRSLKSDAAPGFLglasdlidfdpKYEPAVR-F 611
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 374 ILRQ-----MEEKNRQLQERLEL---------------------AEQKLQQTMRKAEtLPEVEAELAQRIAALTKAEERH 427
Cdd:COG1196 612 VLGDtlvvdDLEQARRLARKLRIkyrivtldgdlvepsgsitggSRNKRSSLAQKRE-LKELEEELAELEAQLEKLEEEL 690
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 428 GNIEERMRHLEGQLEEKNQELQRARqrekMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAALEEKNVLIQESETFRKN 507
Cdd:COG1196 691 KSLKNELRSLEDLLEELRRQLEELE----RQLEELKRELAALEEELEQLQSRLEELEEELEELEEELEELQERLEELEEE 766
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 508 LEESLHDKERLAEEIEKLRSELDQLKMRTGSLIEptiprthldTSAELRYSVGSLVDSQSDYRTTKVIRRPRRGRMGVRR 587
Cdd:COG1196 767 LESLEEALAKLKEEIEELEEKRQALQEELEELEE---------ELEEAERRLDALERELESLEQRRERLEQEIEELEEEI 837
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 588 DE--PKVKSLGDHEWNRTQQIGVLSSHPFESDTEMSDIDDDdretifssmdllspsgHSDAQTLAMMLQEQLDAINKEIR 665
Cdd:COG1196 838 EEleEKLDELEEELEELEKELEELKEELEELEAEKEELEDE----------------LKELEEEKEELEEELRELESELA 901
|
730 740 750
....*....|....*....|....*....|..
gi 333805618 666 LIQEEKESTELRAEEIENRVASVSLEGLNLAR 697
Cdd:COG1196 902 ELKEEIEKLRERLEELEAKLERLEVELPELEE 933
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
290-533 |
2.31e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 75.09 E-value: 2.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 290 RLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELA 369
Cdd:TIGR02168 226 ELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQ 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 370 NKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRI----AALTKAEERHGNIEERMRHLEGQLEEKN 445
Cdd:TIGR02168 306 ILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELesleAELEELEAELEELESRLEELEEQLETLR 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 446 QELQRARQREKMNEEHNKRLSDTVDRlLTESNERLQLHLKERMAALEEKNV--LIQESETFRKNLEESLHDKERLAEEIE 523
Cdd:TIGR02168 386 SKVAQLELQIASLNNEIERLEARLER-LEDRRERLQQEIEELLKKLEEAELkeLQAELEELEEELEELQEELERLEEALE 464
|
250
....*....|
gi 333805618 524 KLRSELDQLK 533
Cdd:TIGR02168 465 ELREELEEAE 474
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
269-539 |
3.41e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 74.71 E-value: 3.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 269 QIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRYL 348
Cdd:TIGR02168 233 RLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLA 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 349 SAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQqtmrkaetlpEVEAELAQRIAALTKAEERHG 428
Cdd:TIGR02168 313 NLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELE----------ELEAELEELESRLEELEEQLE 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 429 NIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAALE-EKNVLIQESETFRKN 507
Cdd:TIGR02168 383 TLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEeELEELQEELERLEEA 462
|
250 260 270
....*....|....*....|....*....|..
gi 333805618 508 LEESLHDKERLAEEIEKLRSELDQLKMRTGSL 539
Cdd:TIGR02168 463 LEELREELEEAEQALDAAERELAQLQARLDSL 494
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning]; |
115-443 |
4.51e-13 |
|
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 224117 [Multi-domain] Cd Length: 1163 Bit Score: 73.98 E-value: 4.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 115 EQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSPSGVSSEVEVLKALKSLFEHHKALDEKVR-- 192
Cdd:COG1196 179 RKLERTEENLERLEDLLEELEKQLEKLERQAEKAERYQELKAELRELELALLLAKLKELRKELEELEEELSRLEEELEel 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 193 -ERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMASSEGSTE------SEHLEGMEPGQKVHEKRLSNGSIDSTD 265
Cdd:COG1196 259 qEELEEAEKEIEELKSELEELREELEELQEELLELKEEIEELEGEISllrerlEELENELEELEERLEELKEKIEALKEE 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 266 ETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEK 345
Cdd:COG1196 339 LEERETLLEELEQLLAELEEAKEELEEKLSALLEELEELFEALREELAELEAELAEIRNELEELKREIESLEERLERLSE 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 346 RYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEE 425
Cdd:COG1196 419 RLEDLKEELKELEAELEELQTELEELNEELEELEEQLEELRDRLKELERELAELQEELQRLEKELSSLEARLDRLEAEQR 498
|
330
....*....|....*...
gi 333805618 426 RHGNIEERMRHLEGQLEE 443
Cdd:COG1196 499 ASQGVRAVLEALESGLPG 516
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning]; |
114-478 |
5.62e-13 |
|
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 224117 [Multi-domain] Cd Length: 1163 Bit Score: 73.98 E-value: 5.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 114 REQLLEKEEEISELKAERNNTRLLLEHLEclvsrhERSLRMTVVKRQaqspsgVSSEVEVLKALKSLFEHHKALDEKVRE 193
Cdd:COG1196 157 RRKLIEEAAGVSKYKERKEEAERKLERTE------ENLERLEDLLEE------LEKQLEKLERQAEKAERYQELKAELRE 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 194 -RLRVSLERVSALEEELAAANQEIVALREQnvHIQRKMASSEGSTESEHLEgmepgQKVHEKRLsngsiDSTDETSQIVE 272
Cdd:COG1196 225 lELALLLAKLKELRKELEELEEELSRLEEE--LEELQEELEEAEKEIEELK-----SELEELRE-----ELEELQEELLE 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 273 LQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLE-KRYLSAQ 351
Cdd:COG1196 293 LKEEIEELEGEISLLRERLEELENELEELEERLEELKEKIEALKEELEERETLLEELEQLLAELEEAKEELEeKLSALLE 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 352 RESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIE 431
Cdd:COG1196 373 ELEELFEALREELAELEAELAEIRNELEELKREIESLEERLERLSERLEDLKEELKELEAELEELQTELEELNEELEELE 452
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 333805618 432 ERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNE 478
Cdd:COG1196 453 EQLEELRDRLKELERELAELQEELQRLEKELSSLEARLDRLEAEQRA 499
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
31-533 |
8.71e-13 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 223496 [Multi-domain] Cd Length: 908 Bit Score: 72.87 E-value: 8.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 31 FEQLMVNMLDERDRLLDTLRETQEsLSLAQQRLQDVIYD----RDSLQRQLNSALPQDIESLTGGLAGSKGADPPEFAAL 106
Cdd:COG0419 145 FDAFLKSKPKERKEILDELFGLEK-YEKLSELLKEVIKEakakIEELEGQLSELLEDIEDLLEALEEELKELKKLEEIQE 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 107 TKELNACREQLLEKEEEISELKAERNNTRLLLEHLEclvsrHERSLRMTVVKRQAQSpsgvssEVEVLKALKSLFEHHKA 186
Cdd:COG0419 224 EQEEEELEQEIEALEERLAELEEEKERLEELKARLL-----EIESLELEALKIREEE------LRELERLLEELEEKIER 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 187 LDEKVRE--RLRVSLERVSALEEELAAANQEIVALREQNVHIQRKM--ASSEGSTESEHLEGMEPGQKVHEKRLSNGSID 262
Cdd:COG0419 293 LEELEREieELEEELEGLRALLEELEELLEKLKSLEERLEKLEEKLekLESELEELAEEKNELAKLLEERLKELEERLEE 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 263 STDETSQIVELQELLEKQnyeMAQMKERLAALSSRVGEVEQEAETARKDLikteemnTKYQRDIREAMAQKEDMEERITT 342
Cdd:COG0419 373 LEKELEKALERLKQLEEA---IQELKEELAELSAALEEIQEELEELEKEL-------EELERELEELEEEIKKLEEQINQ 442
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 343 LEKRYLSAqRESTSIHDMNDKLENELANkeailrqmeEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTK 422
Cdd:COG0419 443 LESKELMI-AELAGAGEKCPVCGQELPE---------EHEKELLELYELELEELEEELSREKEEAELREEIEELEKELRE 512
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 423 AEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEhnkrlsdtvdRLLTESNERLQLHLKERMAALEEknvliqese 502
Cdd:COG0419 513 LEEELIELLELEEALKEELEEKLEKLENLLEELEELKE----------KLQLQQLKEELRQLEDRLQELKE--------- 573
|
490 500 510
....*....|....*....|....*....|.
gi 333805618 503 tfrknLEESLHDKERLAEEIEKLRSELDQLK 533
Cdd:COG0419 574 -----LLEELRLLRTRKEELEELRERLKELK 599
|
|
| SAM_liprin-beta1,2_repeat1 |
cd09563 |
SAM domain of liprin-beta1,2 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of ... |
895-959 |
1.65e-12 |
|
SAM domain of liprin-beta1,2 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of liprin-beta1,2 proteins is a protein-protein interaction domain. Liprin-beta protein contain three copies (repeats) of SAM domain. They may form heterodimers with liprins-alpha through their SAM domains. It was suggested based on bioinformatic approaches that the second SAM domain of liprin-beta is potentially able to form polymers. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development, in axon guidance, and in the maintenance of lymphatic vessel integrity.
Pssm-ID: 188962 Cd Length: 64 Bit Score: 63.40 E-value: 1.65e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 333805618 895 FAQWDGPTVVAWL-ELWLGMpawYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQ 959
Cdd:cd09563 1 FAEWSTEQVCDWLaELGLGQ---YVDECRRWVKSGQTLLKASPQELEKELGIKHPLHRKKLQLALQ 63
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
32-541 |
1.86e-12 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 223496 [Multi-domain] Cd Length: 908 Bit Score: 72.10 E-value: 1.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 32 EQLMVNMLDERDRLLDTLRETQESLSLAQQRLQDVIYDRDSLQRQLNSALpQDIESLTGGLAGSKGADPPEFAALTKELN 111
Cdd:COG0419 192 GQLSELLEDIEDLLEALEEELKELKKLEEIQEEQEEEELEQEIEALEERL-AELEEEKERLEELKARLLEIESLELEALK 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 112 ACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHER-----SLRMTVVKRQAQSPSGVSSEVEVLKALKSLFEHHKA 186
Cdd:COG0419 271 IREEELRELERLLEELEEKIERLEELEREIEELEEELEGlrallEELEELLEKLKSLEERLEKLEEKLEKLESELEELAE 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 187 LDEKVRERLRvslERVSALEEELAAANQEIVALRE--QNVHIQRKMASSEGSTESEHLEGMEPGQKVHEKRLSngsiDST 264
Cdd:COG0419 351 EKNELAKLLE---ERLKELEERLEELEKELEKALErlKQLEEAIQELKEELAELSAALEEIQEELEELEKELE----ELE 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 265 DETSQIVELQELLEKQNYEMAQMKERLAALSSRVG-------EVEQEAETARKDLIKTEEMNTKYQRDIREamaQKEDME 337
Cdd:COG0419 424 RELEELEEEIKKLEEQINQLESKELMIAELAGAGEkcpvcgqELPEEHEKELLELYELELEELEEELSREK---EEAELR 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 338 ERITTLEKRYLSAQRESTSIHDMNDKLENEL-ANKEAILRQMEE----KNRQLQERLELAEQKLQQTMRKAETLPEVEAE 412
Cdd:COG0419 501 EEIEELEKELRELEEELIELLELEEALKEELeEKLEKLENLLEEleelKEKLQLQQLKEELRQLEDRLQELKELLEELRL 580
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 413 LAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHN--KRLSDTVDRL-----LTESNERLQLHLK 485
Cdd:COG0419 581 LRTRKEELEELRERLKELKKKLKELEERLSQLEELLQSLELSEAENELEEaeEELESELEKLnlqaeLEELLQAALEELE 660
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 333805618 486 ERMAALEEK-NVLIQESETfRKNLEESLHDKERLAEEIEKLRSELDQLKMRTGSLIE 541
Cdd:COG0419 661 EKVEELEAEiRRELQRIEN-EEQLEEKLEELEQLEEELEQLREELEELLKKLGEIEQ 716
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning]; |
40-533 |
2.91e-12 |
|
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 224117 [Multi-domain] Cd Length: 1163 Bit Score: 71.28 E-value: 2.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 40 DERDRLLDTLRETQESLSLAQQRLQDVIYDRDSLQRQLNsalpqDIESLTGGLAGSKGADPPEFAALTKELNACREQLLE 119
Cdd:COG1196 383 EELAELEAELAEIRNELEELKREIESLEERLERLSERLE-----DLKEELKELEAELEELQTELEELNEELEELEEQLEE 457
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 120 KEEEISELKAERNNTRLLLEHLECLVSRHERSLRMTvvKRQAQSPSGVSsevEVLKALKSLFEHHKALdekVRERLRVSL 199
Cdd:COG1196 458 LRDRLKELERELAELQEELQRLEKELSSLEARLDRL--EAEQRASQGVR---AVLEALESGLPGVYGP---VAELIKVKE 529
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 200 ERVSALEEELAAANQEIVALREQ-NVHIQRKMASSEGSTESE-HLEGMEPGqKVHEKRLSNGSIDSTdetSQIVELQELL 277
Cdd:COG1196 530 KYETALEAALGNRLQAVVVENEEvAKKAIEFLKENKAGRATFlPLDRIKPL-RSLKSDAAPGFLGLA---SDLIDFDPKY 605
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 278 EKQNY----------EMAQMKERLAALSSRVGEVEQEAETARKDLIKTEemNTKYQRDIREAMAQKEDMEERITTLEKRY 347
Cdd:COG1196 606 EPAVRfvlgdtlvvdDLEQARRLARKLRIKYRIVTLDGDLVEPSGSITG--GSRNKRSSLAQKRELKELEEELAELEAQL 683
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 348 LSAQRESTSIHDMNDKLENELANKEAILRQM--------------EEKNRQLQERLELAEQKLQQTMRKAETLPEVEAEL 413
Cdd:COG1196 684 EKLEEELKSLKNELRSLEDLLEELRRQLEELerqleelkrelaalEEELEQLQSRLEELEEELEELEEELEELQERLEEL 763
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 414 AQRIAALTKA----EERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQ--LHLKER 487
Cdd:COG1196 764 EEELESLEEAlaklKEEIEELEEKRQALQEELEELEEELEEAERRLDALERELESLEQRRERLEQEIEELEEeiEELEEK 843
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 333805618 488 MAALEEKNVLIQES-ETFRKNLEESLHDKERLAEEIEKLRSELDQLK 533
Cdd:COG1196 844 LDELEEELEELEKElEELKEELEELEAEKEELEDELKELEEEKEELE 890
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
108-534 |
2.99e-12 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 223496 [Multi-domain] Cd Length: 908 Bit Score: 71.33 E-value: 2.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 108 KELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQspsgVSSEVEVLKALKSLFEHHKAL 187
Cdd:COG0419 322 EKLKSLEERLEKLEEKLEKLESELEELAEEKNELAKLLEERLKELEERLEELEKE----LEKALERLKQLEEAIQELKEE 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 188 DEKVRERLRVSLERVSALEEELAAANQEIVALREQNVHIQR-KMASSEGSTESEHLEGME--------PGQKVHEKRLS- 257
Cdd:COG0419 398 LAELSAALEEIQEELEELEKELEELERELEELEEEIKKLEEqINQLESKELMIAELAGAGekcpvcgqELPEEHEKELLe 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 258 ---------NGSIDSTDETSQIVELQELLEKQNYEMAQMKERLAALSS-RVGEVEQEAETARKDLIKTEEMNTKYQR-DI 326
Cdd:COG0419 478 lyeleleelEEELSREKEEAELREEIEELEKELRELEEELIELLELEEaLKEELEEKLEKLENLLEELEELKEKLQLqQL 557
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 327 REAMAQKEDMEERITTLEKRYLsaqrestsihdmndkLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETL 406
Cdd:COG0419 558 KEELRQLEDRLQELKELLEELR---------------LLRTRKEELEELRERLKELKKKLKELEERLSQLEELLQSLELS 622
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 407 pEVEAELAQRIAALTKAEERHG-------NIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTvdrlltesnER 479
Cdd:COG0419 623 -EAENELEEAEEELESELEKLNlqaeleeLLQAALEELEEKVEELEAEIRRELQRIENEEQLEEKLEEL---------EQ 692
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 333805618 480 LQLHLKERMAALEEKNVLIQESETFRKNLEESLHDKERLAEEIEKLRSELDQLKM 534
Cdd:COG0419 693 LEEELEQLREELEELLKKLGEIEQLIEELESRKAELEELKKELEKLEKALELLEE 747
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
255-539 |
4.95e-12 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 70.87 E-value: 4.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 255 RLSNGSIDSTDETSQIVELQELLEKqnyemaqMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKE 334
Cdd:TIGR02169 661 APRGGILFSRSEPAELQRLRERLEG-------LKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEE 733
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 335 DMEERITTLEKRYLSAQRESTSIHDMNDKLENELAnkeailrQMEEKNRQLQERLELAEQKLQQtmrkaETLPEVEAEla 414
Cdd:TIGR02169 734 KLKERLEELEEDLSSLEQEIENVKSELKELEARIE-------ELEEDLHKLEEALNDLEARLSH-----SRIPEIQAE-- 799
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 415 qriaaLTKAEERHGNIEERMRHLEGQLEEKNQELQRArqREKMNEEHNKRlsdtvdRLLTESNERLQLHLKERMAALEEK 494
Cdd:TIGR02169 800 -----LSKLEEEVSRIEARLREIEQKLNRLTLEKEYL--EKEIQELQEQR------IDLKEQIKSIEKEIENLNGKKEEL 866
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 333805618 495 NVLIQESETFRKNLEESLHDkerLAEEIEKLRSELDQLKMRTGSL 539
Cdd:TIGR02169 867 EEELEELEAALRDLESRLGD---LKKERDELEAQLRELERKIEEL 908
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
169-460 |
8.50e-12 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 70.10 E-value: 8.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 169 SEVEVLKALKSLFEHHKALDEKVRERLrvslERVSALEEELAAANQEIVAL-REQNVHIQRKMASSEGSTES--EHLEGM 245
Cdd:TIGR02169 238 QKEAIERQLASLEEELEKLTEEISELE----KRLEEIEQLLEELNKKIKDLgEEEQLRVKEKIGELEAEIASleRSIAEK 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 246 EPGQKVHEKRLSNGSIDSTDETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRD 325
Cdd:TIGR02169 314 ERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREK 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 326 IREAmaqKEDMEERITTLEKRYLSAQRESTSIHDMNdkleNELANKEAILRQMEEKNRQLQERLELAEQKLQQTmrkaet 405
Cdd:TIGR02169 394 LEKL---KREINELKRELDRLQEELQRLSEELADLN----AAIAGIEAKINELEEEKEDKALEIKKQEWKLEQL------ 460
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 333805618 406 lpeveaelaqrIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEE 460
Cdd:TIGR02169 461 -----------AADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEE 504
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
265-541 |
8.83e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 70.09 E-value: 8.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 265 DETSQIVELQELLEKQNYEMAQMKERLA-------ALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDME 337
Cdd:TIGR02168 257 ELTAELQELEEKLEELRLEVSELEEEIEelqkelyALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELA 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 338 ERITTLEKRYLSAQRESTSihdmndkLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLpevEAELAQRI 417
Cdd:TIGR02168 337 EELAELEEKLEELKEELES-------LEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASL---NNEIERLE 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 418 AALTKAEERHGNIEERMRHLEGQLEEKNQELQRAR--QREKMNEEHNKRLSDTVDRLLTESNERLQlhLKERMAALEEKN 495
Cdd:TIGR02168 407 ARLERLEDRRERLQQEIEELLKKLEEAELKELQAEleELEEELEELQEELERLEEALEELREELEE--AEQALDAAEREL 484
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 333805618 496 VLIQESETFRKNLEESLHDKERLAEEIEKLRSELDQLKMRTGSLIE 541
Cdd:TIGR02168 485 AQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELIS 530
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
102-535 |
6.16e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 67.01 E-value: 6.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 102 EFAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLEclvsRHERSLRMTVvkRQAQSPSGVSSEVEVLKALKSLF 181
Cdd:PRK03918 232 ELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELK----KEIEELEEKV--KELKELKEKAEEYIKLSEFYEEY 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 182 EHHKALDEKVRERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMASSEGSTES-EHLEGMEPGQKVHEKRLSNGS 260
Cdd:PRK03918 306 LDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELyEEAKAKKEELERLKKRLTGLT 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 261 IDSTDETSQIV-----ELQELLEKQNYEMAQMKERLAALSSRVGEVEQE-----------AETARKDLIK--TEEMNtKY 322
Cdd:PRK03918 386 PEKLEKELEELekakeEIEEEISKITARIGELKKEIKELKKAIEELKKAkgkcpvcgrelTEEHRKELLEeyTAELK-RI 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 323 QRDIREAMAQKEDMEERITTLEKrYLSAQRESTSIHDMNDKLEN-ELANKEAILRQMEEKNRQ---LQERLELAEQKLQQ 398
Cdd:PRK03918 465 EKELKEIEEKERKLRKELRELEK-VLKKESELIKLKELAEQLKElEEKLKKYNLEELEKKAEEyekLKEKLIKLKGEIKS 543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 399 TMRKAETLPEVEAELAQRIAALTKAEERHGNIEERMRHL----EGQLEEKNQELqrarqrEKMNEEHNkRLSDTVDRL-- 472
Cdd:PRK03918 544 LKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELgfesVEELEERLKEL------EPFYNEYL-ELKDAEKELer 616
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 333805618 473 LTESNERLQLHLKERMAALEEKNVLIQESETFRKNLEESLHDKE---------RLAEEIEKLRSELDQLKMR 535
Cdd:PRK03918 617 EEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEyeelreeylELSRELAGLRAELEELEKR 688
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
49-427 |
7.09e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 67.00 E-value: 7.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 49 LRETQESLslaqQRLQDVIYDR----DSLQRQLNSA-----------------LPQDIESLTGGLAGSKGadppEFAALT 107
Cdd:TIGR02168 181 LERTRENL----DRLEDILNELerqlKSLERQAEKAerykelkaelrelelalLVLRLEELREELEELQE----ELKEAE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 108 KELNACREQLLEKEEEISELKAERNNTRLLLEHLEclvsrherslrmtvvkrqaqspsgvsSEVEVLKALKSLFEHHKal 187
Cdd:TIGR02168 253 EELEELTAELQELEEKLEELRLEVSELEEEIEELQ--------------------------KELYALANEISRLEQQK-- 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 188 dekvrERLRVSLERvsaLEEELAAANQEIVALREQNVHIQRKMASSEgstesehlegmepgqkvhekrlsngsidstdet 267
Cdd:TIGR02168 305 -----QILRERLAN---LERQLEELEAQLEELESKLDELAEELAELE--------------------------------- 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 268 SQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRy 347
Cdd:TIGR02168 344 EKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQE- 422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 348 LSAQRESTSIHDMnDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERH 427
Cdd:TIGR02168 423 IEELLKKLEEAEL-KELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENL 501
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
104-540 |
8.15e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 66.63 E-value: 8.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 104 AALTKELNACREQL---LEKEEEISELKAERNNTRLLLEHLECLVSRHERSLRMTVvkrqaqspSGVSSEVEVLKALKSL 180
Cdd:PRK03918 168 GEVIKEIKRRIERLekfIKRTENIEELIKEKEKELEEVLREINEISSELPELREEL--------EKLEKEVKELEELKEE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 181 FEHHKALDEKVRERLRVSLERVSALEEELAAANQEIVALREQnvhIQRKMASSEGSTESEHLEGMepgQKVHEKRLSNGS 260
Cdd:PRK03918 240 IEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEK---VKELKELKEKAEEYIKLSEF---YEEYLDELREIE 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 261 IDSTDETSQIVELQELLEKqnyemaqmkerLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRdIREAMAQKEDMEERI 340
Cdd:PRK03918 314 KRLSRLEEEINGIEERIKE-----------LEEKEERLEELKKKLKELEKRLEELEERHELYEE-AKAKKEELERLKKRL 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 341 T-----TLEKRYLSAQRESTSIHDMNDKLENELANkeaiLRQMEEKNRQLQERLELAEQKLQQTMR------KAETLPEV 409
Cdd:PRK03918 382 TgltpeKLEKELEELEKAKEEIEEEISKITARIGE----LKKEIKELKKAIEELKKAKGKCPVCGRelteehRKELLEEY 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 410 EAELAQRIAALTKAEERHGNIEERMRHLEGQLEeKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLhLKERMA 489
Cdd:PRK03918 458 TAELKRIEKELKEIEEKERKLRKELRELEKVLK-KESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEK-LKEKLI 535
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 333805618 490 ALEEKnvliqesetfRKNLEESLHDKERLAEEIEKLRSELDQLKMRTGSLI 540
Cdd:PRK03918 536 KLKGE----------IKSLKKELEKLEELKKKLAELEKKLDELEEELAELL 576
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
266-541 |
8.29e-11 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 223496 [Multi-domain] Cd Length: 908 Bit Score: 66.71 E-value: 8.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 266 ETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQK--EDMEERITTL 343
Cdd:COG0419 165 GLEKYEKLSELLKEVIKEAKAKIEELEGQLSELLEDIEDLLEALEEELKELKKLEEIQEEQEEEELEQeiEALEERLAEL 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 344 EKRYLSAQRESTSIHDMN-------DKLENELANKEAILRQMEEKNRQLQE---RLELAEQKLQQTMRKAETLPEVEAEL 413
Cdd:COG0419 245 EEEKERLEELKARLLEIEslelealKIREEELRELERLLEELEEKIERLEElerEIEELEEELEGLRALLEELEELLEKL 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 414 AQRIAALTKAEERHGNIEERMRHLEgqlEEKNQELQRARQREKMNEEHNKRLSDTVDRLL------TESNERLQLHLKER 487
Cdd:COG0419 325 KSLEERLEKLEEKLEKLESELEELA---EEKNELAKLLEERLKELEERLEELEKELEKALerlkqlEEAIQELKEELAEL 401
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 333805618 488 MAALEEKNVLIQESETFRKNLEESLhdkERLAEEIEKLRSELDQLKMRTGSLIE 541
Cdd:COG0419 402 SAALEEIQEELEELEKELEELEREL---EELEEEIKKLEEQINQLESKELMIAE 452
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
39-532 |
1.71e-10 |
|
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: 65.76 E-value: 1.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 39 LDERDRLLDTLRETQESLSLAQQRLQDVIYDRDSLQRQLNSALPQDIE--SLTGGLAGSKGADPPEFAALTKELNACREQ 116
Cdd:TIGR00618 371 SCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAfrDLQGQLAHAKKQQELQQRYAELCAAAITCT 450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 117 LLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLRM-TVVKRQAQSPSGVSSEVEvlKALKSLFEHHKALDEK--VRE 193
Cdd:TIGR00618 451 AQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKkAVVLARLLELQEEPCPLC--GSCIHPNPARQDIDNPgpLTR 528
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 194 RLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMASSEGSTE------SEHLEGMEPGQKVHEKRLSNGSIDSTDET 267
Cdd:TIGR00618 529 RMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSiltqcdNRSKEDIPNLQNITVRLQDLTEKLSEAED 608
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 268 SQIVELQELLEKQNYEMAqmKERLAALSSRVGEVEQEAETArkdliKTEEMNTKYQRDIREAMAQKEDMEERitTLEKRY 347
Cdd:TIGR00618 609 MLACEQHALLRKLQPEQD--LQDVRLHLQQCSQELALKLTA-----LHALQLTLTQERVREHALSIRVLPKE--LLASRQ 679
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 348 LSAQRESTSIHDMNDKLEnELANKEAILRQMEE---KNRQLQERLELAEQKLQQTMR-KAETLPEVEAEL-AQRIAALTK 422
Cdd:TIGR00618 680 LALQKMQSEKEQLTYWKE-MLAQCQTLLRELEThieEYDREFNEIENASSSLGSDLAaREDALNQSLKELmHQARTVLKA 758
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 423 AEERHGNIEER----------MRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAALE 492
Cdd:TIGR00618 759 RTEAHFNNNEEvtaalqtgaeLSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLE 838
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 333805618 493 EKNVLIQESETFRKNLEESLHDKERLAEEIEKLRSELDQL 532
Cdd:TIGR00618 839 EKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKL 878
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
265-530 |
2.81e-10 |
|
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 characteristic 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: 63.93 E-value: 2.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 265 DETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLE 344
Cdd:pfam19220 45 QAKSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVARLAKLEAALREAEAAKEELRIELRDKTAQAEALE 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 345 KRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAE 424
Cdd:pfam19220 125 RQLAAETEQNRALEEENKALREEAQAAEKALQRAEGELATARERLALLEQENRRLQALSEEQAAELAELTRRLAELETQL 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 425 ERHgniEERMRHLEGQLEEKNQELQRA-RQREKMNEEHNKRLSD-------------TVDRLLTESNERLQlHLKERMAA 490
Cdd:pfam19220 205 DAT---RARLRALEGQLAAEQAERERAeAQLEEAVEAHRAERASlrmklealtaraaATEQLLAEARNQLR-DRDEAIRA 280
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 333805618 491 LEEKNV-LIQESETFRKNLEESLHDKERLAE---EIEKLRSELD 530
Cdd:pfam19220 281 AERRLKeASIERDTLERRLAGLEADLERRTQqfqEMQRARAELE 324
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
109-514 |
3.50e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 64.78 E-value: 3.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 109 ELNACREQLLEKEEEISELKAERNNTRLLLEHLEcLVSRHERSLRMTVVKRQAQSPSGVSSEVEVLKALKSLFEHHKALD 188
Cdd:PTZ00121 1395 EAKKKAEEDKKKADELKKAAAAKKKADEAKKKAE-EKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKAD 1473
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 189 E--KVRERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMAssEGSTESEHLEGMEPGQKVHEKRLSNgSIDSTDE 266
Cdd:PTZ00121 1474 EakKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKA--EEAKKADEAKKAEEAKKADEAKKAE-EKKKADE 1550
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 267 TSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDliktEEMNTKYQRDIREAMAQKEDMEERITTLEKR 346
Cdd:PTZ00121 1551 LKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIE----EVMKLYEEEKKMKAEEAKKAEEAKIKAEELK 1626
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 347 ylSAQRESTSIHDMNDKLENEL--------ANKEAILRQMEEKNRQLQERLELAE-QKLQQTMRKAETLPEVEAELAQRI 417
Cdd:PTZ00121 1627 --KAEEEKKKVEQLKKKEAEEKkkaeelkkAEEENKIKAAEEAKKAEEDKKKAEEaKKAEEDEKKAAEALKKEAEEAKKA 1704
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 418 AALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKR---LSDTVDRLLTESNERLQLHLKERMAALEEK 494
Cdd:PTZ00121 1705 EELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKdeeEKKKIAHLKKEEEKKAEEIRKEKEAVIEEE 1784
|
410 420
....*....|....*....|
gi 333805618 495 nvLIQESETFRKNLEESLHD 514
Cdd:PTZ00121 1785 --LDEEDEKRRMEVDKKIKD 1802
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
192-539 |
4.98e-10 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 64.21 E-value: 4.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 192 RERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMA---SSEGSTESEHLEGMEPGQKVHEKRLSNGSIDSTDEts 268
Cdd:PRK04863 278 ANERRVHLEEALELRRELYTSRRQLAAEQYRLVEMARELAelnEAESDLEQDYQAASDHLNLVQTALRQQEKIERYQA-- 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 269 QIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLikteemntkyqrdireamaqkEDMEERITTLEKR-- 346
Cdd:PRK04863 356 DLEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQL---------------------ADYQQALDVQQTRai 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 347 -YLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTmRKAETLPEVEAELAQRIAALTKAEE 425
Cdd:PRK04863 415 qYQQAVQALERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVA-QAAHSQFEQAYQLVRKIAGEVSRSE 493
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 426 RHgnieERMRHLEGQLEEKNQELQRARQ-REKMNE-EHNKRLSDTVDRLLTESNERLQLHLkERMAALEEknvLIQESET 503
Cdd:PRK04863 494 AW----DVARELLRRLREQRHLAEQLQQlRMRLSElEQRLRQQQRAERLLAEFCKRLGKNL-DDEDELEQ---LQEELEA 565
|
330 340 350
....*....|....*....|....*....|....*.
gi 333805618 504 FRKNLEESlhdKERLAEEIEKLRSELDQLKMRTGSL 539
Cdd:PRK04863 566 RLESLSES---VSEARERRMALRQQLEQLQARIQRL 598
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
175-539 |
8.80e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 63.16 E-value: 8.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 175 KALKSLFEHHKALDEKvRERLRVSLERVSALEEELAAANQEIvalrEQNVHIQRKMASSEGSTESEhLEGMEPGQKVHEK 254
Cdd:PRK03918 162 NAYKNLGEVIKEIKRR-IERLEKFIKRTENIEELIKEKEKEL----EEVLREINEISSELPELREE-LEKLEKEVKELEE 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 255 RlsngsidstdeTSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVE---QEAETARKDLIKTEEMNTKYQRDIR---E 328
Cdd:PRK03918 236 L-----------KEEIEELEKELESLEGSKRKLEEKIRELEERIEELKkeiEELEEKVKELKELKEKAEEYIKLSEfyeE 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 329 AMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQME---------EKNRQLQERLELAEQKLqqt 399
Cdd:PRK03918 305 YLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEeleerhelyEEAKAKKEELERLKKRL--- 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 400 mrKAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQ---ELQRARQR-----EKMNEEHNKRLSDTVDR 471
Cdd:PRK03918 382 --TGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKaieELKKAKGKcpvcgRELTEEHRKELLEEYTA 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 472 LLTESNERLQ-LHLKERMAALEEKNV---LIQESETFR--------KNLEESL--HDKERL---AEEIEKLRSELDQLKM 534
Cdd:PRK03918 460 ELKRIEKELKeIEEKERKLRKELRELekvLKKESELIKlkelaeqlKELEEKLkkYNLEELekkAEEYEKLKEKLIKLKG 539
|
....*
gi 333805618 535 RTGSL 539
Cdd:PRK03918 540 EIKSL 544
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
115-533 |
1.18e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 62.77 E-value: 1.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 115 EQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLRmtVVKRQAQSPSGVSSEV-EVLKALKSLFEHHKALDEKVR- 192
Cdd:PRK03918 286 KELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEIN--GIEERIKELEEKEERLeELKKKLKELEKRLEELEERHEl 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 193 -ERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMASSEGSTESEHLEGMEpgQKVHEKRLSNGSIDSTDETSQIV 271
Cdd:PRK03918 364 yEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELK--KEIKELKKAIEELKKAKGKCPVC 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 272 -------ELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQ-----------------RDIR 327
Cdd:PRK03918 442 grelteeHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKElaeqlkeleeklkkynlEELE 521
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 328 EAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDK---LENELANKEA----ILRQMEEKNRQLQERLELAEQKLQQTM 400
Cdd:PRK03918 522 KKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKlaeLEKKLDELEEelaeLLKELEELGFESVEELEERLKELEPFY 601
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 401 RKAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQreKMNEEHNKRLSDTVDRLltesnERL 480
Cdd:PRK03918 602 NEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEK--KYSEEEYEELREEYLEL-----SRE 674
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 333805618 481 QLHLKERMAALEEknvLIQESETFRKNLEESLHDKERLAEEIEKLRSELDQLK 533
Cdd:PRK03918 675 LAGLRAELEELEK---RREEIKKTLEKLKEELEEREKAKKELEKLEKALERVE 724
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
265-685 |
1.96e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 62.39 E-value: 1.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 265 DETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEemntKYQrdirEAMAQKEDMEERITTLE 344
Cdd:TIGR02169 160 DEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAE----RYQ----ALLKEKREYEGYELLKE 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 345 KRYLSAQREstsihdmndKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAelaqrIAALTKAE 424
Cdd:TIGR02169 232 KEALERQKE---------AIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQ-----LRVKEKIG 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 425 ERHGNIEErmrhLEGQLEEKNQELQRA-RQREKMNEEHNKrlsdtvdrlltesnerlqlhLKERMAALEEKnvliqeset 503
Cdd:TIGR02169 298 ELEAEIAS----LERSIAEKERELEDAeERLAKLEAEIDK--------------------LLAEIEELERE--------- 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 504 frknLEESLHDKERLAEEIEKLRSELDQLKMRTGSLieptiprthldtSAELRYSVGSLVDSQSDYRTTKVIRRPRRGRM 583
Cdd:TIGR02169 345 ----IEEERKRRDKLTEEYAELKEELEDLRAELEEV------------DKEFAETRDELKDYREKLEKLKREINELKREL 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 584 GVRRDEPKVKS--LGDHEwnrtQQIGVLSSHPFESDTEMSDIDDDDRETIFSSMDLLSPSGHSDAQTLAmmLQEQLDAIN 661
Cdd:TIGR02169 409 DRLQEELQRLSeeLADLN----AAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYD--LKEEYDRVE 482
|
410 420
....*....|....*....|....
gi 333805618 662 KEIRLIQEEKESTELRAEEIENRV 685
Cdd:TIGR02169 483 KELSKLQRELAEAEAQARASEERV 506
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
102-529 |
2.40e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 61.62 E-value: 2.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 102 EFAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSPSGVSSEVEVLKALKSLF 181
Cdd:PRK03918 315 RLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELE 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 182 EHHKAlDEKVRERLRVSLERVSALEEELAAANQEIVALRE---------------------QNVHIQRKMASSEGSTESE 240
Cdd:PRK03918 395 ELEKA-KEEIEEEISKITARIGELKKEIKELKKAIEELKKakgkcpvcgrelteehrkellEEYTAELKRIEKELKEIEE 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 241 HLEGMEPGQKVHEKRLSNGSIDSTDET--SQIVELQELLEKQNYEMAQMKERLA-ALSSRVGEVEQEAETARKDLIKTEE 317
Cdd:PRK03918 474 KERKLRKELRELEKVLKKESELIKLKElaEQLKELEEKLKKYNLEELEKKAEEYeKLKEKLIKLKGEIKSLKKELEKLEE 553
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 318 MNTKyqrdIREAMAQKEDMEERITTLEKRYLSAQREStsIHDMNDKLE---------NELANKEAILRQMEEKNRQLQER 388
Cdd:PRK03918 554 LKKK----LAELEKKLDELEEELAELLKELEELGFES--VEELEERLKelepfyneyLELKDAEKELEREEKELKKLEEE 627
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 389 LELAEQKLQQTMRKAEtlpeveaELAQRIAALTK--AEERHGNIEERMRHLEGQLEEKNQELqrarqrekmneEHNKRLS 466
Cdd:PRK03918 628 LDKAFEELAETEKRLE-------ELRKELEELEKkySEEEYEELREEYLELSRELAGLRAEL-----------EELEKRR 689
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 333805618 467 DTVDRLLTEsnerlqlhLKERMAALEEKnvlIQESEtfrkNLEESLHDKERLAEEIEKLRSEL 529
Cdd:PRK03918 690 EEIKKTLEK--------LKEELEEREKA---KKELE----KLEKALERVEELREKVKKYKALL 737
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
30-541 |
3.25e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 61.70 E-value: 3.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 30 HFEQLMVNMLDERDRLLDTLRETQESLSLAQQRLQDVIYDRDSLQRQLNSALPQDiESLTGGLAGSKGADP----PEFAA 105
Cdd:PTZ00121 1264 HFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKAD-EAKKKAEEAKKKADAakkkAEEAK 1342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 106 LTKELNACREQLLEKEEEISELKAERNNTRLLLEH--LECLVSRHERSLRMTVVKRQAQSPSGVSSEVEVLKALKSLFEH 183
Cdd:PTZ00121 1343 KAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKkkADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADE 1422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 184 HKALDEKVR--ERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMASSEGSTESEHLEGMEPGQKVHE-KRLSNGS 260
Cdd:PTZ00121 1423 AKKKAEEKKkaDEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEaKKKADEA 1502
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 261 IDSTDETSQIVELQELLEKQNYEMAQMKERlaalsSRVGEVEQEAETARK--DLIKTEEMntKYQRDIREAMAQKEDMEE 338
Cdd:PTZ00121 1503 KKAAEAKKKADEAKKAEEAKKADEAKKAEE-----AKKADEAKKAEEKKKadELKKAEEL--KKAEEKKKAEEAKKAEED 1575
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 339 RITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEE---------KNRQLQERLELAEQKLQQTMRKAETLPEV 409
Cdd:PTZ00121 1576 KNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEakikaeelkKAEEEKKKVEQLKKKEAEEKKKAEELKKA 1655
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 410 EAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLltesnERLQLHLKERMA 489
Cdd:PTZ00121 1656 EEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKA-----EELKKAEEENKI 1730
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 333805618 490 ALEEknvLIQESETFRKNLEESLHD---KERLAEEIEKLRSELDQLKMRTGSLIE 541
Cdd:PTZ00121 1731 KAEE---AKKEAEEDKKKAEEAKKDeeeKKKIAHLKKEEEKKAEEIRKEKEAVIE 1782
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
284-695 |
5.36e-09 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 435022 [Multi-domain] Cd Length: 1112 Bit Score: 60.89 E-value: 5.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 284 MAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEerITTLEKRYLSAQRESTSIHDMNDK 363
Cdd:pfam15921 226 LRELDTEISYLKGRIFPVEDQLEALKSESQNKIELLLQQHQDRIEQLISEHEVE--ITGLTEKASSARSQANSIQSQLEI 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 364 LENELANKEAI-LRQMEEknrqlqerLELAEQKLQQTMRKA-----ETLPEVEAELAQRIAALTKAEERHGNIEERMRHL 437
Cdd:pfam15921 304 IQEQARNQNSMyMRQLSD--------LESTVSQLRSELREAkrmyeDKIEELEKQLVLANSELTEARTERDQFSQESGNL 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 438 EGQLEEKNQELQRARQREKMNEEHNKRLSD-------TVDRLLTESNER-----------------LQLHLKERMAALEE 493
Cdd:pfam15921 376 DDQLQKLLADLHKREKELSLEKEQNKRLWDrdtgnsiTIDHLRRELDDRnmevqrleallkamkseCQGQMERQMAAIQG 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 494 KNVLIQESETFRKNLEESlhdKERLAEEIEKLRSELDQLKmrtgsliepTIPRTHLDTSAELRYSVGSLVDSQSDyrTTK 573
Cdd:pfam15921 456 KNESLEKVSSLTAQLEST---KEMLRKVVEELTAKKMTLE---------SSERTVSDLTASLQEKERAIEATNAE--ITK 521
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 574 VirrprRGRMGVRRDEPK-VKSLGDHEWNRTQQIGVLSSHPFESDTEMSDIddddRETIFSSMDLLSPSGHSDA--QTLA 650
Cdd:pfam15921 522 L-----RSRVDLKLQELQhLKNEGDHLRNVQTECEALKLQMAEKDKVIEIL----RQQIENMTQLVGQHGRTAGamQVEK 592
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 333805618 651 MMLQEQLDAINKEIRLIQEEKESTELRAEEIENRVASVSLEGLNL 695
Cdd:pfam15921 593 AQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKL 637
|
|
| SAM |
smart00454 |
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ... |
895-961 |
5.73e-09 |
|
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related tyrosine kinases, appears to mediate cell-cell initiated signal transduction via the binding of SH2-containing proteins to a conserved tyrosine that is phosphorylated. In many cases mediates homodimerisation.
Pssm-ID: 197735 Cd Length: 68 Bit Score: 53.45 E-value: 5.73e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 333805618 895 FAQWDGPTVVAWLELwLGMPAwYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEM 961
Cdd:smart00454 1 VSQWSPESVADWLES-IGLEQ-YADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKL 65
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
33-539 |
7.79e-09 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 435022 [Multi-domain] Cd Length: 1112 Bit Score: 60.12 E-value: 7.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 33 QLMVNMLDERDRLLDTLRETQESLSLAQQRLQDVIYDRDSLQrQLNSALPQDIESLTGGLAGSKgadppefaaltKELNA 112
Cdd:pfam15921 328 QLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFS-QESGNLDDQLQKLLADLHKRE-----------KELSL 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 113 CREQ---LLEKEE----EISELKAERNNTRLLLEHLECLVsRHERSLRMTVVKRQAQSPSGVSSEVEVLKALKSLFEHHK 185
Cdd:pfam15921 396 EKEQnkrLWDRDTgnsiTIDHLRRELDDRNMEVQRLEALL-KAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTK 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 186 ALDEKVRERL---RVSLER----VSAL-------EEELAAANQEIVALREQnvhIQRKMASSEG-STESEHLEGMEPGQK 250
Cdd:pfam15921 475 EMLRKVVEELtakKMTLESsertVSDLtaslqekERAIEATNAEITKLRSR---VDLKLQELQHlKNEGDHLRNVQTECE 551
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 251 VHEKRLSngsidstdETSQIVE-LQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREA 329
Cdd:pfam15921 552 ALKLQMA--------EKDKVIEiLRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIREL 623
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 330 MAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAET-LPE 408
Cdd:pfam15921 624 EARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMqLKS 703
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 409 VEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEhnkrlsdtvdrLLTESNerlqlhlKERM 488
Cdd:pfam15921 704 AQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEE-----------AMTNAN-------KEKH 765
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 333805618 489 AALEEKNVLIQESETFRKnleeslhDKERLAEEIEKLRSELDQLKMRTGSL 539
Cdd:pfam15921 766 FLKEEKNKLSQELSTVAT-------EKNKMAGELEVLRSQERRLKEKVANM 809
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
275-556 |
9.23e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 60.07 E-value: 9.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 275 ELLEKQnyemAQMKERLAALSSRVGEVE-----QEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRYLS 349
Cdd:TIGR02168 203 KSLERQ----AEKAERYKELKAELRELElallvLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSE 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 350 AQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALtkaeerhgn 429
Cdd:TIGR02168 279 LEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEEL--------- 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 430 iEERMRHLEGQLEEKNQELQRARQREKMNEEHnkrlsdtvdrLLTESNERLQLhlkermaaLEEKNVLIQESETFRKNLE 509
Cdd:TIGR02168 350 -KEELESLEAELEELEAELEELESRLEELEEQ----------LETLRSKVAQL--------ELQIASLNNEIERLEARLE 410
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 333805618 510 ESLHDKERLAEEIEKLRSELDQLKMRTGSLIEPTIPRTHLDTSAELR 556
Cdd:TIGR02168 411 RLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELE 457
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
291-539 |
1.12e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 59.69 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 291 LAALSSRVGEVEQ--EAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKrYLSAQREstsIHDMNDKLENEL 368
Cdd:PRK03918 127 LNAIYIRQGEIDAilESDESREKVVRQILGLDDYENAYKNLGEVIKEIKRRIERLEK-FIKRTEN---IEELIKEKEKEL 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 369 ANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQ---LEEKN 445
Cdd:PRK03918 203 EEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEieeLEEKV 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 446 QELQRARQREKMNEEHNKRLSDTVDRL-----LTESNERLQLHLKERMAALEEKNVLIQESETFRKNLE---ESLHDKER 517
Cdd:PRK03918 283 KELKELKEKAEEYIKLSEFYEEYLDELreiekRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEkrlEELEERHE 362
|
250 260
....*....|....*....|..
gi 333805618 518 LAEEIEKLRSELDQLKMRTGSL 539
Cdd:PRK03918 363 LYEEAKAKKEELERLKKRLTGL 384
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
106-540 |
3.33e-08 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 58.11 E-value: 3.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 106 LTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHeRSLrmtvvkrqaqspsgvSSEVEVLKALKSLFEhhK 185
Cdd:TIGR04523 171 LENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKN-KSL---------------ESQISELKKQNNQLK--D 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 186 ALDEKVRErlrvslerVSALEEELAAANQEIVALREQNVHIQRKMA--SSEGSTESEHLEGMEPGQKVHEKRLSNgsIDS 263
Cdd:TIGR04523 233 NIEKKQQE--------INEKTTEISNTQTQLNQLKDEQNKIKKQLSekQKELEQNNKKIKELEKQLNQLKSEISD--LNN 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 264 TDETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREamaqKEDMEERIttl 343
Cdd:TIGR04523 303 QKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEE----KQNEIEKL--- 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 344 ekrylsaQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKA 423
Cdd:TIGR04523 376 -------KKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQ 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 424 ----EERHGNIEERMRHLEGQ--------------LEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNErlqlhLK 485
Cdd:TIGR04523 449 dsvkELIIKNLDNTRESLETQlkvlsrsinkikqnLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISS-----LK 523
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 333805618 486 ERMAALE----EKNVLIQESETFRKNLEESLhDKERLAEEIEKLRSELDQLKMRTGSLI 540
Cdd:TIGR04523 524 EKIEKLEsekkEKESKISDLEDELNKDDFEL-KKENLEKEIDEKNKEIEELKQTQKSLK 581
|
|
| COG4372 |
COG4372 |
Uncharacterized conserved protein, contains DUF3084 domain [Function unknown]; |
269-472 |
4.41e-08 |
|
Uncharacterized conserved protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 226809 [Multi-domain] Cd Length: 499 Bit Score: 57.34 E-value: 4.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 269 QIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMN-------TKYQRDIREAMAQKEDMEERIT 341
Cdd:COG4372 75 QLDDIRPQLRALRTELGTAQGEKRAAETEREAARSELQKARQEREAVRQELaaarqnlAKAQQELARLTKQAQDLQTRLK 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 342 TL--EKRYLSAQREStsihdmndkLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAA 419
Cdd:COG4372 155 TLaeQRRQLEAQAQS---------LQASQKQLQASATQLKSQVLDLKLRSAQIEQEAQNLATRANAAQARTEELARRAAA 225
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 333805618 420 LTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRL 472
Cdd:COG4372 226 AQQTAQAIQQRDAQISQKAQQIAARAEQIRERERQLQRLETAQARLEQEVAQL 278
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
35-481 |
4.55e-08 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 57.60 E-value: 4.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 35 MVNMLDERDRLLDTLRETQESLSLAQQRLQDVIYDRDSLQRQLNSA-------------LPQDIESLTGGLAGSKGADPP 101
Cdd:PRK01156 244 LSSLEDMKNRYESEIKTAESDLSMELEKNNYYKELEERHMKIINDPvyknrnyindyfkYKNDIENKKQILSNIDAEINK 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 102 EFAALTK--ELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHErSLRMtvvKRQAQSPSGVSSEVEVLKALKS 179
Cdd:PRK01156 324 YHAIIKKlsVLQKDYNDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIE-SLKK---KIEEYSKNIERMSAFISEILKI 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 180 LFEHHKALDeKVRERLRVSLERVSAleeELAAANQEIVALREQNVHIQRKMASSEGSTESEhLEGMEPGQKVHEKRLSNG 259
Cdd:PRK01156 400 QEIDPDAIK-KELNEINVKLQDISS---KVSSLNQRIRALRENLDELSRNMEMLNGQSVCP-VCGTTLGEEKSNHIINHY 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 260 SIDSTDETSQIVELQELLEKQNYEMAQMKERLAALSSrvGEVEQ------EAETARKDL--IKTEEMNTKYQRDIREAMA 331
Cdd:PRK01156 475 NEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLES--EEINKsineynKIESARADLedIKIKINELKDKHDKYEEIK 552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 332 QK------EDMEERITTLEKryLSAQRESTSIhDMNDKLENELANK----------------------EAILRQMEEKNR 383
Cdd:PRK01156 553 NRykslklEDLDSKRTSWLN--ALAVISLIDI-ETNRSRSNEIKKQlndlesrlqeieigfpddksyiDKSIREIENEAN 629
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 384 QLQERLELAEQK--LQQTMR-KAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEE 460
Cdd:PRK01156 630 NLNNKYNEIQENkiLIEKLRgKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRT 709
|
490 500
....*....|....*....|.
gi 333805618 461 HNKRLSDTVdrllTESNERLQ 481
Cdd:PRK01156 710 RINELSDRI----NDINETLE 726
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
324-533 |
7.92e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 56.99 E-value: 7.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 324 RDIREAMAQKED----MEERITTLEKRYLSAQRestsIHDMNDKLENelANKEAILRQMEEKNRQLqERLELAEQKLQQT 399
Cdd:TIGR02168 182 ERTRENLDRLEDilneLERQLKSLERQAEKAER----YKELKAELRE--LELALLVLRLEELREEL-EELQEELKEAEEE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 400 MRKAET-LPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRL------ 472
Cdd:TIGR02168 255 LEELTAeLQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELesklde 334
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 333805618 473 ----LTESNERLQLhLKERMAALEEKnvlIQESETFRKNLEESLHDKErlaEEIEKLRSELDQLK 533
Cdd:TIGR02168 335 laeeLAELEEKLEE-LKEELESLEAE---LEELEAELEELESRLEELE---EQLETLRSKVAQLE 392
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
38-538 |
8.20e-08 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 435022 [Multi-domain] Cd Length: 1112 Bit Score: 57.03 E-value: 8.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 38 MLDERDRLLDTLRETQESLSLAQQRLQDVIYD-------RDSLQRQLNSALPQ--------------------DIESLTG 90
Cdd:pfam15921 122 MQMERDAMADIRRRESQSQEDLRNQLQNTVHEleaakclKEDMLNDSNTQIEQlrkmmlshegvlqeirsilvDFEEASG 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 91 -----------------GLAGSKgadppEFAALTKELNACREQLLEKEEEISELKAE-RNNTRLLLEH----LECLVSRH 148
Cdd:pfam15921 202 kkiyehdsmstihfrslGSAISK-----ILRELDTEISYLKGRIFPVEDQLEALKSEsQNKIELLLQQhqdrIEQLISEH 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 149 ERSL-----RMTVVKRQAQSpsgVSSEVEV------------LKALKSLFEHHKALDEKVRERLRVSLERVSALEEELAA 211
Cdd:pfam15921 277 EVEItglteKASSARSQANS---IQSQLEIiqeqarnqnsmyMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVL 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 212 ANQEIVALReqnvhIQRKMASSEGSTESEHLEGMEPGQKVHEKRLS-----NGSIDSTDETSQIV--ELQELLEKQNYEM 284
Cdd:pfam15921 354 ANSELTEAR-----TERDQFSQESGNLDDQLQKLLADLHKREKELSlekeqNKRLWDRDTGNSITidHLRRELDDRNMEV 428
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 285 AQMKERLAALSSRV-GEVEQEAETARKdliKTEEMNtKYQRDIREAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDK 363
Cdd:pfam15921 429 QRLEALLKAMKSECqGQMERQMAAIQG---KNESLE-KVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTAS 504
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 364 LEnelaNKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAE-----------------LAQRIAALTKAEER 426
Cdd:pfam15921 505 LQ----EKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTEcealklqmaekdkvieiLRQQIENMTQLVGQ 580
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 427 HGNIEERMR----HLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTEsNERLQLHLKERMAAL----EEKNVLI 498
Cdd:pfam15921 581 HGRTAGAMQvekaQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELE-KVKLVNAGSERLRAVkdikQERDQLL 659
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 333805618 499 QESETFRKNLEESLHDKERLAEEI----EKLRSELDQLKMRTGS 538
Cdd:pfam15921 660 NEVKTSRNELNSLSEDYEVLKRNFrnksEEMETTTNKLKMQLKS 703
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
115-520 |
8.63e-08 |
|
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: 56.98 E-value: 8.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 115 EQLLEKEEEISELKAERNNTRLL----LEHLECLVSRHERSLRMTVVKRQAQSpsgvsSEVE-VLKALKSLFEHHKALDE 189
Cdd:TIGR00606 684 QRVFQTEAELQEFISDLQSKLRLapdkLKSTESELKKKEKRRDEMLGLAPGRQ-----SIIDlKEKEIPELRNKLQKVNR 758
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 190 KVrERLRVSLERVSAL------EEELAAANQEIVA----LREQNVHIQRKMASSEGSTESEHLEG--MEPGQKVHEKRLS 257
Cdd:TIGR00606 759 DI-QRLKNDIEEQETLlgtimpEEESAKVCLTDVTimerFQMELKDVERKIAQQAAKLQGSDLDRtvQQVNQEKQEKQHE 837
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 258 NGSIdstdeTSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDME 337
Cdd:TIGR00606 838 LDTV-----VSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDS 912
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 338 ERITTLEKrylSAQRESTSIHDMNDklENELANKEaiLRQMEEKNRQLQERLELAEQKLQQTmrKAETLPEVEAELAQRI 417
Cdd:TIGR00606 913 PLETFLEK---DQQEKEELISSKET--SNKKAQDK--VNDIKEKVKNIHGYMKDIENKIQDG--KDDYLKQKETELNTVN 983
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 418 AALTKAEERHGNIEERMRHLEGQLEEKNQE---LQRARQREKMNEEHnKRLSDTVDRLLTESNERLQLHLKERMAALEEK 494
Cdd:TIGR00606 984 AQLEECEKHQEKINEDMRLMRQDIDTQKIQerwLQDNLTLRKRENEL-KEVEEELKQHLKEMGQMQVLQMKQEHQKLEEN 1062
|
410 420 430
....*....|....*....|....*....|.
gi 333805618 495 NVLIQESETF-----RKNLEESLHDKERLAE 520
Cdd:TIGR00606 1063 IDLIKRNHVLalgrqKGYEKEIKHFKKELRE 1093
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
36-494 |
8.95e-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: 56.65 E-value: 8.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 36 VNMLDERDRLLD-TLRETQESLSLAQQRLQDViydRDSLQRQLNS--ALPQDIESLTGGLAgskgadppefaALTKELNA 112
Cdd:pfam05483 270 ANQLEEKTKLQDeNLKELIEKKDHLTKELEDI---KMSLQRSMSTqkALEEDLQIATKTIC-----------QLTEEKEA 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 113 CREQLLEKEEE----ISELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSpsgvsSEVEVLKALKS-----LFEH 183
Cdd:pfam05483 336 QMEELNKAKAAhsfvVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKS-----SELEEMTKFKNnkeveLEEL 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 184 HKALDEKvrERLRVSLERVSALEEELAAANQEIVAL---REQNVH---IQ------------RKMASSEGSTESEHLEGM 245
Cdd:pfam05483 411 KKILAED--EKLLDEKKQFEKIAEELKGKEQELIFLlqaREKEIHdleIQltaiktseehylKEVEDLKTELEKEKLKNI 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 246 EPGQKVHEKRLSNGSI--DSTDETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLI---------- 313
Cdd:pfam05483 489 ELTAHCDKLLLENKELtqEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIqkgdevkckl 568
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 314 -KTEEMNTKYQRDIREAMAQKEDMEERITTLEKRYLSAQRESTSIHDMN---------------------DKLENELANK 371
Cdd:pfam05483 569 dKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENkalkkkgsaenkqlnayeikvNKLELELASA 648
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 372 EAILRQMEEKNRQLQERLELAEQKLQQTMRKAETL--------PEVEAELAQRIAALTKAEERHGN-----IEERMRHLe 438
Cdd:pfam05483 649 KQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIadeavklqKEIDKRCQHKIAEMVALMEKHKHqydkiIEERDSEL- 727
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 333805618 439 GQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLT---ESNERLQLHLKERMAALEEK 494
Cdd:pfam05483 728 GLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEiekEEKEKLKMEAKENTAILKDK 786
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
169-533 |
1.18e-07 |
|
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: 56.29 E-value: 1.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 169 SEVEVLKALKSLFEHHKALDEKVRERL--RVSLERVSALEEELAAANQEIVALREQNVHIQRKMASSEGSTESEHLEGME 246
Cdd:pfam17380 266 TENEFLNQLLHIVQHQKAVSERQQQEKfeKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAME 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 247 PGQKV-----HEKRLSNGSIDSTDETSQIVELQELlEKQNYEMAQMKERlaalssrvgeVEQEAETARKDLIKTEEMntk 321
Cdd:pfam17380 346 RERELerirqEERKRELERIRQEEIAMEISRMREL-ERLQMERQQKNER----------VRQELEAARKVKILEEER--- 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 322 yQRDIREAMAQKEDMeerittlekrylsaqrestsihdmndKLENELANKEAILRQMEEKNRQLqERLELAEQKLQQTMr 401
Cdd:pfam17380 412 -QRKIQQQKVEMEQI--------------------------RAEQEEARQREVRRLEEERAREM-ERVRLEEQERQQQV- 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 402 kaETLPEVEAELAQRIAALTKAEERHGNIEERMRH-LEGQLEEKnqelqrarqREKMNEEHNKRlsdtvdrlltesnERL 480
Cdd:pfam17380 463 --ERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKiLEKELEER---------KQAMIEEERKR-------------KLL 518
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 333805618 481 QLHLKERMAALEEKNVLIQESETFRKNLEesLHDKERLAEEIEKLRSELDQLK 533
Cdd:pfam17380 519 EKEMEERQKAIYEEERRREAEEERRKQQE--MEERRRIQEQMRKATEERSRLE 569
|
|
| SAM |
smart00454 |
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ... |
1021-1076 |
1.18e-07 |
|
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: 49.99 E-value: 1.18e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 333805618 1021 EWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLK 1076
Cdd:smart00454 11 DWLESIGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKLK 66
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
193-541 |
1.57e-07 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 56.13 E-value: 1.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 193 ERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMASSEGSTESEHLEGMepgQKVHEKRLSNgsidstdetsQIVE 272
Cdd:TIGR00618 212 CMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQ---LRARIEELRA----------QEAV 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 273 LQELLEKQNYemAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEkrylSAQR 352
Cdd:TIGR00618 279 LEETQERINR--ARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQ----TLHS 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 353 ESTSIHDMNDKlenELANKEAILRQMEEKN--RQLQERLELAEQKLQQTMRKAETLPE----VEAELAQRIAALTKAEER 426
Cdd:TIGR00618 353 QEIHIRDAHEV---ATSIREISCQQHTLTQhiHTLQQQKTTLTQKLQSLCKELDILQReqatIDTRTSAFRDLQGQLAHA 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 427 HGNIEERMRHLEGQ----------LEEKNQELQRARQR---EKMNEEHNKRLSDTVDRLLTESNERLQLH------LKER 487
Cdd:TIGR00618 430 KKQQELQQRYAELCaaaitctaqcEKLEKIHLQESAQSlkeREQQLQTKEQIHLQETRKKAVVLARLLELqeepcpLCGS 509
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 333805618 488 MAALEEKNVLIQESETFRKNLEESLHDKERLAEEIEKLRSELDQLKMRTGSLIE 541
Cdd:TIGR00618 510 CIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKE 563
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
309-532 |
1.81e-07 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 55.75 E-value: 1.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 309 RKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRY----LSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQ 384
Cdd:TIGR00618 165 KKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSqlltLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAY 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 385 LQERLELAEQK------LQQTMRKAETLPEVEAELAQRIAALTKA--EERHGNIEERMRHLEGQLEEKNQELQ-RARQRE 455
Cdd:TIGR00618 245 LTQKREAQEEQlkkqqlLKQLRARIEELRAQEAVLEETQERINRArkAAPLAAHIKAVTQIEQQAQRIHTELQsKMRSRA 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 456 KMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAALEEKNVLIQESETFRKNLEESLH----DKERLAEEIEKLRSELDQ 531
Cdd:TIGR00618 325 KLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHtlqqQKTTLTQKLQSLCKELDI 404
|
.
gi 333805618 532 L 532
Cdd:TIGR00618 405 L 405
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
220-532 |
1.89e-07 |
|
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: 426331 [Multi-domain] Cd Length: 1081 Bit Score: 55.55 E-value: 1.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 220 REQNVHIQRKMASSEGSTESEHLEGMEPG-QKVH-EKRLSNGSIDSTDETSQIVELQEllEKQNYEMAQMKERLAALSSR 297
Cdd:pfam01576 90 RSQQLQNEKKKMQQHIQDLEEQLEEEEAArQKLQlEKVTTEAKIKKMEEDILLLEDQN--NKLQKERKLLEERISEFTSN 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 298 VGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEErittlEKRYLSAqrESTSIHDMNDKLENELANKEAILRQ 377
Cdd:pfam01576 168 LAEEEEKSKSLNKLKNKHEAMISDLEDRLKKEEKGRQELEK-----AKRKLEG--ESSDLQEQIAELQAQIAELRAQLAK 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 378 MEEKNRQLQERLE---LAEQKLQQTMRKAET-LPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEK------NQE 447
Cdd:pfam01576 241 KEEELQAALARLEeetAQKNAALKKLRELEAqLSELQEDLESERAARAKAEKQRRDLGEELEALKTELEDTldttaaQQE 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 448 LQRARQRE--------------------KMNEEHNKRLSDTVDRLltESNERLQLHLKERMAALEEKNVLI--------- 498
Cdd:pfam01576 321 LRSKREQEvtelkkaleeetrsheaqlqEMRQKHTQALEELTEQL--EQAKRNKASLEKAKQALESENAELqaelrslqq 398
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 333805618 499 --QESETFRKNLEESLHD-----------KERLAEEIEKLRSELDQL 532
Cdd:pfam01576 399 akQDSEHKRKKLEGQLQElqsrlseserqRAELAEKLSKLQSELESV 445
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
38-422 |
2.30e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 55.46 E-value: 2.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 38 MLDERDRLLDTLRETQESLSLAQQRLQDviydrdsLQRQLnSALPQDIESLTGglagskgadppEFAALTKELNACREQL 117
Cdd:TIGR02169 686 LKRELSSLQSELRRIENRLDELSQELSD-------ASRKI-GEIEKEIEQLEQ-----------EEEKLKERLEELEEDL 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 118 LEKEEEISELKAErnntrllLEHLECLVSRHERSLrmtvvkrqaqspSGVSSEVEVLKA--LKSLFEHHKALDEKVRERL 195
Cdd:TIGR02169 747 SSLEQEIENVKSE-------LKELEARIEELEEDL------------HKLEEALNDLEArlSHSRIPEIQAELSKLEEEV 807
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 196 RVSLERVSALEEELAAANQEIVALREQNVHIQRKMASSEGSTESEhlegmepGQKVHEKRLsngsidstdetsQIVELQE 275
Cdd:TIGR02169 808 SRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSI-------EKEIENLNG------------KKEELEE 868
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 276 LLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKdliKTEEMNTKYQRD---IREAMAQKEDMEERITTLEKRYLSAQR 352
Cdd:TIGR02169 869 ELEELEAALRDLESRLGDLKKERDELEAQLRELER---KIEELEAQIEKKrkrLSELKAKLEALEEELSEIEDPKGEDEE 945
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 353 ESTSIHDMnDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTK 422
Cdd:TIGR02169 946 IPEEELSL-EDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEK 1014
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
114-538 |
2.30e-07 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 55.21 E-value: 2.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 114 REQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLRmtvvkRQAQSPSGVSSEVEVLKAL------KSLFEHHK-- 185
Cdd:pfam10174 330 KESLTAKEQRAAILQTEVDALRLRLEEKESFLNKKTKQLQ-----DLTEEKSTLAGEIRDLKDMldvkerKINVLQKKie 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 186 ALDEKVRERLRV---------SLERVSA--------LEEELAAANQEIVALREQNvhiqrkmaSSEGSTESEHLEGMEPG 248
Cdd:pfam10174 405 NLQEQLRDKDKQlaglkervkSLQTDSSntdtalttLEEALSEKERIIERLKEQR--------EREDRERLEELESLKKE 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 249 QKVHEKRLSNGSIDSTDETSQIVELQELLEKQNYEMAQMKERLAALssrvgevEQEAETARKDLIKTEEMNTKYQrDIRE 328
Cdd:pfam10174 477 NKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSL-------EIAVEQKKEECSKLENQLKKAH-NAEE 548
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 329 AMAQKEDMEERITTLEKRYLSAQRESTsihdmndKLENELANKEAILRQME----EKNRQLQERLELAEQKLQQTMRKAE 404
Cdd:pfam10174 549 AVRTNPEINDRIRLLEQEVARYKEESG-------KAQAEVERLLGILREVEneknDKDKKIAELESLTLRQMKEQNKKVA 621
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 405 TLPEVEAELAQRIAALTkaEERHGNIEERMR-HLEGQLEEKNQELQRARQREkmnEEHNKRLSDTV------DRLLTESN 477
Cdd:pfam10174 622 NIKHGQQEMKKKGAQLL--EEARRREDNLADnSQQLQLEELMGALEKTRQEL---DATKARLSSTQqslaekDGHLTNLR 696
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 333805618 478 ERLQLHLKERM--------AALEEKNVLIQEsetfrknLEESLHDKERLAEEIEKLRSELD----QLKMRTGS 538
Cdd:pfam10174 697 AERRKQLEEILemkqeallAAISEKDANIAL-------LELSSSKKKKTQEEVMALKREKDrlvhQLKQQTQN 762
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
30-451 |
2.38e-07 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 435022 [Multi-domain] Cd Length: 1112 Bit Score: 55.49 E-value: 2.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 30 HFEQLMVNMLDERDRLLDTLRETQESLSLAQQRlQDVIYDRDS--------LQRQLN---------SALPQDIESLTGG- 91
Cdd:pfam15921 367 QFSQESGNLDDQLQKLLADLHKREKELSLEKEQ-NKRLWDRDTgnsitidhLRRELDdrnmevqrlEALLKAMKSECQGq 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 92 ----LAGSKGADPP--EFAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLRMTVVKrQAQSPS 165
Cdd:pfam15921 446 merqMAAIQGKNESleKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAE-ITKLRS 524
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 166 GVSSEVEVLKALKSLFEHhkaldekvrerLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMASSEGSTESEHLEGM 245
Cdd:pfam15921 525 RVDLKLQELQHLKNEGDH-----------LRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKA 593
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 246 EPGQKVHEKR--LSNGSIDSTDETSQIVELQELLEKQNYEMAQM----KERLAALSSRVGEVEQ---EAETARKDLIKTE 316
Cdd:pfam15921 594 QLEKEINDRRleLQEFKILKDKKDAKIRELEARVSDLELEKVKLvnagSERLRAVKDIKQERDQllnEVKTSRNELNSLS 673
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 317 EMNTKYQRDIREamaQKEDMEERITTLEKRYLSAQRE----STSIHDMNDKLENELANKEAILRQMEEKNRQ---LQERL 389
Cdd:pfam15921 674 EDYEVLKRNFRN---KSEEMETTTNKLKMQLKSAQSEleqtRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQidaLQSKI 750
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 333805618 390 ELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRA 451
Cdd:pfam15921 751 QFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVA 812
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
350-537 |
3.01e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 55.05 E-value: 3.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 350 AQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGN 429
Cdd:PRK02224 197 EEKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETEREREE 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 430 IEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRL---LTESNERLQLH-------------LKERMAALEE 493
Cdd:PRK02224 277 LAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELedrDEELRDRLEECrvaaqahneeaesLREDADDLEE 356
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 333805618 494 KNVLIQE-SETFRKNLEESLHDKERLAEEIEKLRSELDQLKMRTG 537
Cdd:PRK02224 357 RAEELREeAAELESELEEAREAVEDRREEIEELEEEIEELRERFG 401
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
102-533 |
3.03e-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: 55.23 E-value: 3.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 102 EFAALTKELNacrEQLLEKEEEISELKAERNNTRLLL--------EHLECLVSRHERSLRMTVVKR---QAQSPSgVSSE 170
Cdd:pfam12128 280 ERQETSAELN---QLLRTLDDQWKEKRDELNGELSAAdaavakdrSELEALEDQHGAFLDADIETAaadQEQLPS-WQSE 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 171 VEVL-KALKSLFEHHKALDEKVrERLRvsLERVSALEEELAAANQEIVALREQnvhIQRKMASSEGsteseHLEGME-PG 248
Cdd:pfam12128 356 LENLeERLKALTGKHQDVTAKY-NRRR--SKIKEQNNRDIAGIKDKLAKIREA---RDRQLAVAED-----DLQALEsEL 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 249 QKVHEKRLSNGSIDSTDETSQIVELQELLEKQNYEmAQMKERLAALSSRVGEVEQEAETARKDLikteemnTKYQRDIRE 328
Cdd:pfam12128 425 REQLEAGKLEFNEEEYRLKSRLGELKLRLNQATAT-PELLLQLENFDERIERAREEQEAANAEV-------ERLQSELRQ 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 329 AMAQKEDMEERITTLEKRYLSAQRESTSIHDMND----KLENELANKEAILRQMEEK--NRQLQERLELAEQKLQQTMRK 402
Cdd:pfam12128 497 ARKRRDQASEALRQASRRLEERQSALDELELQLFpqagTLLHFLRKEAPDWEQSIGKviSPELLHRTDLDPEVWDGSVGG 576
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 403 AETL-------------------PEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNK 463
Cdd:pfam12128 577 ELNLygvkldlkridvpewaaseEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLR 656
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 333805618 464 RLSDTVDRL---LTESNERLQLHLKERMAALE-EKNVLIQESETF-----RKNLEESLHDKERLAEEIEKLRSELDQLK 533
Cdd:pfam12128 657 RLFDEKQSEkdkKNKALAERKDSANERLNSLEaQLKQLDKKHQAWleeqkEQKREARTEKQAYWQVVEGALDAQLALLK 735
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
106-524 |
4.03e-07 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 54.26 E-value: 4.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 106 LTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLRMTvvKRQAQSpsgVSSEVEVLKALKSlfehhK 185
Cdd:TIGR04523 237 KQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKEL--EKQLNQ---LKSEISDLNNQKE-----Q 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 186 ALDEKVRERLRVSLERVSALEEELAAANQEIVALREQNVHIqrkmassegstesehlegmepgqkvhEKRLSNGSIDSTD 265
Cdd:TIGR04523 307 DWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQL--------------------------KKELTNSESENSE 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 266 ETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAEtarkdliKTEEMNTKYQRDIREAMAQKEDMEERITTLEK 345
Cdd:TIGR04523 361 KQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQ-------NQEKLNQQKDEQIKKLQQEKELLEKEIERLKE 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 346 RYLSAQREstsIHDmndkLENELANKEAILRQMEEKNRQLQERLEL-------AEQKLQQTMR-------KAETLPEVEA 411
Cdd:TIGR04523 434 TIIKNNSE---IKD----LTNQDSVKELIIKNLDNTRESLETQLKVlsrsinkIKQNLEQKQKelkskekELKKLNEEKK 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 412 ELAQRIAALTKaeeRHGNIEERMRHLEGQLEEKNQEL-QRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAA 490
Cdd:TIGR04523 507 ELEEKVKDLTK---KISSLKEKIEKLESEKKEKESKIsDLEDELNKDDFELKKENLEKEIDEKNKEIEELKQTQKSLKKK 583
|
410 420 430
....*....|....*....|....*....|....
gi 333805618 491 LEEKNVLIQESETFRKNLEESLHDKERLAEEIEK 524
Cdd:TIGR04523 584 QEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEK 617
|
|
| SAM |
smart00454 |
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ... |
1099-1170 |
7.15e-07 |
|
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: 47.68 E-value: 7.15e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 333805618 1099 VLVWSNDRVIRWIQAIGLREYANNILESGVHGSLIALDEnfdysSLALLLQIPTQNTQARQILEREYNNLLA 1170
Cdd:smart00454 1 VSQWSPESVADWLESIGLEQYADNFRKNGIDGALLLLLT-----SEEDLKELGITKLGHRKKILKAIQKLKE 67
|
|
| COG4372 |
COG4372 |
Uncharacterized conserved protein, contains DUF3084 domain [Function unknown]; |
273-606 |
7.88e-07 |
|
Uncharacterized conserved protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 226809 [Multi-domain] Cd Length: 499 Bit Score: 53.10 E-value: 7.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 273 LQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDlikteemNTKYQRDIREAMAQKEDMEERITTLEKRYLSAQR 352
Cdd:COG4372 65 LNRNLRSGVFQLDDIRPQLRALRTELGTAQGEKRAAETE-------REAARSELQKARQEREAVRQELAAARQNLAKAQQ 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 353 ESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEE 432
Cdd:COG4372 138 ELARLTKQAQDLQTRLKTLAEQRRQLEAQAQSLQASQKQLQASATQLKSQVLDLKLRSAQIEQEAQNLATRANAAQARTE 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 433 RMRHLEGQLEEKNQEL-QRARQREKMNEEHNKRlsdtvdrlltesnerlqlhlKERMAALEEKnvlIQESETFRKNLEES 511
Cdd:COG4372 218 ELARRAAAAQQTAQAIqQRDAQISQKAQQIAAR--------------------AEQIRERERQ---LQRLETAQARLEQE 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 512 LHDKERLAEEIEKLRseLDQLKMRTGSLIEPTIPRThlDTSAELRYSVGSLVDSQSDYRTTKVIRRPRRGrmgvRRDEPK 591
Cdd:COG4372 275 VAQLEAYYQAYVRLR--QQAAATQRGQVLAGAAQRV--AQAQAQAQAQAQLLSSANRPAALRLRRSPRRG----RRQRPV 346
|
330
....*....|....*
gi 333805618 592 VKSLGDHEWNRTQQI 606
Cdd:COG4372 347 TRHTTRRRRPATRQS 361
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
367-524 |
1.32e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 52.47 E-value: 1.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 367 ELANKEAIlRQMEEKNRQLQERLELAEQKLQQTMRKAETlpEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQ 446
Cdd:PRK12704 34 KEAEEEAK-RILEEAKKEAEAIKKEALLEAKEEIHKLRN--EFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 447 ELQRARQREKMNEEHNKRLSDTVDRLLTESNERLqlhlkERMAAL---EEKNVLIQESEtfrknlEESLHDKERLAEEIE 523
Cdd:PRK12704 111 ELEKKEKELEQKQQELEKKEEELEELIEEQLQEL-----ERISGLtaeEAKEILLEKVE------EEARHEAAVLIKEIE 179
|
.
gi 333805618 524 K 524
Cdd:PRK12704 180 E 180
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
240-524 |
1.75e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.84 E-value: 1.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 240 EHLEGMEPGQKVHEKRLSNGSIDSTDET-----SQIVELQELL-EKQNYEMAQMKErlaalsSRVGEVEQEAETARKDLI 313
Cdd:PTZ00121 1031 ELTEYGNNDDVLKEKDIIDEDIDGNHEGkaeakAHVGQDEGLKpSYKDFDFDAKED------NRADEATEEAFGKAEEAK 1104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 314 KTEEMNTKYQRDIREAMAQKEDMeerittlekRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKnRQLQERLELAE 393
Cdd:PTZ00121 1105 KTETGKAEEARKAEEAKKKAEDA---------RKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDA-RKAEEARKAED 1174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 394 QKLQQTMRKAETLPEVE----AELAQRIAALTKAEERHgNIEERMRHLEgqlEEKNQELQRARQREKMNEEHNKRLSDTV 469
Cdd:PTZ00121 1175 AKKAEAARKAEEVRKAEelrkAEDARKAEAARKAEEER-KAEEARKAED---AKKAEAVKKAEEAKKDAEEAKKAEEERN 1250
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 333805618 470 DRLLTESNERLQLHLKERMAAL--EEKnvliQESETFRKNLEESLHDKERLAEEIEK 524
Cdd:PTZ00121 1251 NEEIRKFEEARMAHFARRQAAIkaEEA----RKADELKKAEEKKKADEAKKAEEKKK 1303
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
63-532 |
1.93e-06 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 426331 [Multi-domain] Cd Length: 1081 Bit Score: 52.47 E-value: 1.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 63 LQDVIYDRDSLQRQLNSALPQDIESLTGGLAGSKgadpPEFAALTKELNACRE---QLLEKEEEISELKAERNNT----R 135
Cdd:pfam01576 220 LQEQIAELQAQIAELRAQLAKKEEELQAALARLE----EETAQKNAALKKLREleaQLSELQEDLESERAARAKAekqrR 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 136 LLLEHLECLVSRHERSLRMTVVKRQAQSpsgvSSEVEVLKALKSLFEHHKALDEKVRERLRVSLERVSALEEELAAANQE 215
Cdd:pfam01576 296 DLGEELEALKTELEDTLDTTAAQQELRS----KREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRN 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 216 IV-------ALREQNVHIQRKMAS-SEGSTESEHlegmepGQKVHEKRLSNGSIDSTDETSQIVELQELLEKqnyemaqM 287
Cdd:pfam01576 372 KAslekakqALESENAELQAELRSlQQAKQDSEH------KRKKLEGQLQELQSRLSESERQRAELAEKLSK-------L 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 288 KERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKrylsaqrESTSIHDMndkLENE 367
Cdd:pfam01576 439 QSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSSRLRQLED-------EKNSLQEQ---LEEE 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 368 LANKEAILRQMEEKNRQLQErlelAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEERM----RHLEGQLEE 443
Cdd:pfam01576 509 EEAKRNVERQLQTLQAQLSD----LKKKLEEDAGAVEALEEGRKRLQRELEALTQRLEEKAAAYDKLektkNRLQQELDD 584
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 444 KNQELQRARQREKMNEEHNKRLsdtvDRLLTESNERLQLHLKERMAALEEKNVLIQESETFRKNLEESLHDKERLAEEIE 523
Cdd:pfam01576 585 LLVDLDHQRQLVSNLEKKQKKF----DQMLAEEKAISARYAEERDRAEAEAREKETKALSLARALEEALDAKEELERQNK 660
|
....*....
gi 333805618 524 KLRSELDQL 532
Cdd:pfam01576 661 QLRAEMEDL 669
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
41-383 |
2.14e-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: 52.38 E-value: 2.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 41 ERDRLLDTLRETQESLSLAQQRLQDVIYDRDSLQRQLNSALPQDIESLTGG------LAGSKGADPPEFAALTKELNACR 114
Cdd:TIGR02169 171 KKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKReyegyeLLKEKEALERQKEAIERQLASLE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 115 EQLLEKEEEISELKAERNNTRLLLEHLECLVSRhERSLRMTVVKRQAQSpsgVSSEVEVLK-ALKSLFEHHKALDEKVR- 192
Cdd:TIGR02169 251 EELEKLTEEISELEKRLEEIEQLLEELNKKIKD-LGEEEQLRVKEKIGE---LEAEIASLErSIAEKERELEDAEERLAk 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 193 --ERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMASSEGSTESEHLEGMEPGQKV--HEKRLSNGSIDSTDETS 268
Cdd:TIGR02169 327 leAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELkdYREKLEKLKREINELKR 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 269 QIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRYL 348
Cdd:TIGR02169 407 ELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELS 486
|
330 340 350
....*....|....*....|....*....|....*
gi 333805618 349 SAQREstsihdmndkleneLANKEAILRQMEEKNR 383
Cdd:TIGR02169 487 KLQRE--------------LAEAEAQARASEERVR 507
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning]; |
39-329 |
2.32e-06 |
|
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 224117 [Multi-domain] Cd Length: 1163 Bit Score: 52.02 E-value: 2.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 39 LDERDRLLDTLRETQESLSLAQQRLQDVIYDRDSLQRQLNSaLPQDIESLTGGLAgskgadppefaALTKELNACREQLL 118
Cdd:COG1196 736 QSRLEELEEELEELEEELEELQERLEELEEELESLEEALAK-LKEEIEELEEKRQ-----------ALQEELEELEEELE 803
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 119 EKEEEISELKAERNNTRLLLEHLEclVSRHERSLRMTVVKRQAQSPSGVSSEVE-VLKALKSLFEHHKALDEKVRERLRV 197
Cdd:COG1196 804 EAERRLDALERELESLEQRRERLE--QEIEELEEEIEELEEKLDELEEELEELEkELEELKEELEELEAEKEELEDELKE 881
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 198 SLERVSALEEELAAANQEIVALREQNVHIQRKMASSEGSTESEHLEGMEPGQKVHEKRLSNGSIDSTDETSQIVELQELL 277
Cdd:COG1196 882 LEEEKEELEEELRELESELAELKEEIEKLRERLEELEAKLERLEVELPELEEELEEEYEDTLETELEREIERLEEEIEAL 961
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 333805618 278 EKQNY----EMAQMKERLAALSSRVGEVEQEAETARKdliKTEEMNTKYQRDIREA 329
Cdd:COG1196 962 GPVNLraieEYEEVEERYEELKSQREDLEEAKEKLLE---VIEELDKEKRERFKET 1014
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
43-457 |
3.70e-06 |
|
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 characteristic 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: 50.84 E-value: 3.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 43 DRLLDTLRETQESLSLAQQRLQDViydRDSLQRQL--NSALPQDIESLTGGLAGSKGadppEFAALTKELNACREQLLEK 120
Cdd:pfam19220 30 SQLIEPIEAILRELPQAKSRLLEL---EALLAQERaaYGKLRRELAGLTRRLSAAEG----ELEELVARLAKLEAALREA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 121 EEEISELKAERNNTRLLLEHLEclvsrherslrmtvvKRQAQspsgvssEVEVLKALKslfEHHKALdekvRERLRVSLE 200
Cdd:pfam19220 103 EAAKEELRIELRDKTAQAEALE---------------RQLAA-------ETEQNRALE---EENKAL----REEAQAAEK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 201 RVSALEEELAAAnQEIVALREQNVHIQRKMASSEGSTESEHLEGMEPgqkvHEKRLSNGSIDSTDETSQIVELQELLEK- 279
Cdd:pfam19220 154 ALQRAEGELATA-RERLALLEQENRRLQALSEEQAAELAELTRRLAE----LETQLDATRARLRALEGQLAAEQAERERa 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 280 ---QNYEMAQMKERLAALSSRVgeveqEAETARkdLIKTEEMNTkyqrdirEAMAQKEDMEERITTLEKRYLSAQRESTS 356
Cdd:pfam19220 229 eaqLEEAVEAHRAERASLRMKL-----EALTAR--AAATEQLLA-------EARNQLRDRDEAIRAAERRLKEASIERDT 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 357 IHDMNDKLENELANKEAILRQMEEKNRQLQERLElaeqklqqTMRKAetlpeveaeLAQRIAALTKAEERHGNIEERMRH 436
Cdd:pfam19220 295 LERRLAGLEADLERRTQQFQEMQRARAELEERAE--------MLTKA---------LAAKDAALERAEERIASLSDRIAE 357
|
410 420
....*....|....*....|....*...
gi 333805618 437 LEGQ-------LEEKNQELQRARQREKM 457
Cdd:pfam19220 358 LTKRfeveraaLEQANRRLKEELQRERA 385
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
260-463 |
4.36e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 227278 [Multi-domain] Cd Length: 420 Bit Score: 50.49 E-value: 4.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 260 SIDSTDETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEER 339
Cdd:COG4942 30 AFSAAADDKQLKQIQKEIAALEKKIREQQDQRAKLEKQLKSLETEIASLEAQLIETADDLKKLRKQIADLNARLNALEVQ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 340 -------------------------ITTLEKRYLSAQRESTSIHDMN-------DKLENELANKEAILRQMEEKNRQLQE 387
Cdd:COG4942 110 ereqrrrlaeqlaalqrsgrnpppaLLVSPEDAQRSVRLAIYYGALNparaeriDALKATLKQLAAVRAEIAAEQAELTT 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 333805618 388 -RLELAEQKLQQTMRKAETlPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNK 463
Cdd:COG4942 190 lLSEQRAQQAKLAQLLEER-KKTLAQLNSELSADQKKLEELRANESRLKNEIASAEAAAAKAREAAAAAEAAAARAR 265
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
264-532 |
4.63e-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: 4.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 264 TDETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKT-----------EEMNTKYQRDIReamaQ 332
Cdd:TIGR04523 92 KKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFlteikkkekelEKLNNKYNDLKK----Q 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 333 KEDMEERITTLEKrylsaqrESTSIHDMNDKLENELANKE---AILRQMEEKNRQLQ-ERLELAEQKLQQTmrkaETLPE 408
Cdd:TIGR04523 168 KEELENELNLLEK-------EKLNIQKNIDKIKNKLLKLElllSNLKKKIQKNKSLEsQISELKKQNNQLK----DNIEK 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 409 VEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRArqrEKMNEEHNKRLSDTVDRLLTESNERLQLHLKERM 488
Cdd:TIGR04523 237 KQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQN---NKKIKELEKQLNQLKSEISDLNNQKEQDWNKELK 313
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 333805618 489 AALEEKNVLIQESETFRKNLEESLhdkERLAEEIEKLRSELDQL 532
Cdd:TIGR04523 314 SELKNQEKKLEEIQNQISQNNKII---SQLNEQISQLKKELTNS 354
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N-terminus of SMC proteins. The ... |
265-529 |
8.46e-06 |
|
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: 50.36 E-value: 8.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 265 DETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVE----QEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERI 340
Cdd:pfam02463 159 EEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKlqelKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEER 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 341 TTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAA- 419
Cdd:pfam02463 239 IDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKe 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 420 ----LTKAEERHGNIEERMRHLEGQLEEKN---QELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAALE 492
Cdd:pfam02463 319 sekeKKKAEKELKKEKEEIEELEKELKELEikrEAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELE 398
|
250 260 270
....*....|....*....|....*....|....*..
gi 333805618 493 EKNVLIQESETFRKNLEESLHDKERLAEEIEKLRSEL 529
Cdd:pfam02463 399 LKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEE 435
|
|
| SAM_superfamily |
cd09487 |
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ... |
1021-1072 |
8.72e-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: 44.15 E-value: 8.72e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 333805618 1021 EWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRvHLKMVDSFHRTSLQYGI 1072
Cdd:cd09487 4 EWLESLGLEQYADLFRKNEIDGDALLLLTDEDLK-ELGITSPGHRKKILRAI 54
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
269-541 |
1.14e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 49.63 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 269 QIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQK----------EDMEE 338
Cdd:TIGR04523 132 QKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLlklelllsnlKKKIQ 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 339 RITTLEKRYLSAQRESTSIHDMNDKLENELANKEAI-------LRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEA 411
Cdd:TIGR04523 212 KNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEisntqtqLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLN 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 412 ELAQRIAALTKAEERH---------GNIEERMRHLEGQLEEKNQELQRARQ------REKMNEEHNKRlsdTVDRLLTES 476
Cdd:TIGR04523 292 QLKSEISDLNNQKEQDwnkelkselKNQEKKLEEIQNQISQNNKIISQLNEqisqlkKELTNSESENS---EKQRELEEK 368
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 333805618 477 NERLQLHLKERMAALEEKNVL----------IQESETFRKNLEESLH----DKERLAEEIEKLRSELDQLKMRTGSLIE 541
Cdd:TIGR04523 369 QNEIEKLKKENQSYKQEIKNLesqindleskIQNQEKLNQQKDEQIKklqqEKELLEKEIERLKETIIKNNSEIKDLTN 447
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
102-448 |
1.23e-05 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 49.44 E-value: 1.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 102 EFAALTKELNACREQLLEKEEEISELKAERNNtrlLLEHLEclvsrhERSLRMTVVKRQAQSPSGVSSEVEVlkALKSLF 181
Cdd:pfam10174 374 EKSTLAGEIRDLKDMLDVKERKINVLQKKIEN---LQEQLR------DKDKQLAGLKERVKSLQTDSSNTDT--ALTTLE 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 182 EhhkALDEKVR--ERLRVSLERVS-ALEEELAAANQEIVALREQNVHIQRKMASSEGSTES--EHLEGMEPGQKVHEKRL 256
Cdd:pfam10174 443 E---ALSEKERiiERLKEQREREDrERLEELESLKKENKDLKEKVSALQPELTEKESSLIDlkEHASSLASSGLKKDSKL 519
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 257 SNGSIDSTDETSQIVELQELLEK-QNYEMAQMKErlAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKED 335
Cdd:pfam10174 520 KSLEIAVEQKKEECSKLENQLKKaHNAEEAVRTN--PEINDRIRLLEQEVARYKEESGKAQAEVERLLGILREVENEKND 597
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 336 MEERITTLEKRYLSaQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQ 415
Cdd:pfam10174 598 KDKKIAELESLTLR-QMKEQNKKVANIKHGQQEMKKKGAQLLEEARRREDNLADNSQQLQLEELMGALEKTRQELDATKA 676
|
330 340 350
....*....|....*....|....*....|....*...
gi 333805618 416 RIAALTKA-EERHGNIE----ERMRHLEGQLEEKNQEL 448
Cdd:pfam10174 677 RLSSTQQSlAEKDGHLTnlraERRKQLEEILEMKQEAL 714
|
|
| EzrA |
COG4477 |
Septation ring formation regulator EzrA [Cell cycle control, cell division, chromosome ... |
184-520 |
2.52e-05 |
|
Septation ring formation regulator EzrA [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 226883 [Multi-domain] Cd Length: 570 Bit Score: 48.53 E-value: 2.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 184 HKALDEKVrERLRVSLERVSALEEELaaanqEIVALREQNVHIQRKMASSegsteSEHLEGMEPGQKVHEKRLSNgsids 263
Cdd:COG4477 250 HVNIDSRL-ERLKEQLVENSELLTQL-----ELDEAEEELGLIQEKIESL-----YDLLEREVEAKNVVEENLPI----- 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 264 tdetsqiveLQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKdlikteemntkYQRDIREAMAQKEDMEERITTL 343
Cdd:COG4477 314 ---------LPDYLEKAKENNEHLKEEIERVKESYRLAETELGSVRK-----------FEKELKELESVLDEILENIEAQ 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 344 EKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAET--LPEVEAELAQRIAalt 421
Cdd:COG4477 374 EVAYSELQDNLEEIEKALTDIEDEQEKVQEHLTSLRKDELEARENLERLKSKLHEIKRYMEKsnLPGLPETFLSLFF--- 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 422 kaeerhgNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDtvdrlltESNERLQlhlkerMAALEEKnvLIQES 501
Cdd:COG4477 451 -------TAGHEIQDLMKELSEVPINMEAVSALVDIATEDMNTLED-------ETEEVVE------NAVLAEQ--LIQYG 508
|
330 340
....*....|....*....|..
gi 333805618 502 ETFRK---NLEESLHDKERLAE 520
Cdd:COG4477 509 NRYRSrnaEVAKSLNEAERLFE 530
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
186-529 |
2.53e-05 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 48.68 E-value: 2.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 186 ALDEKVRERLRV-------SLERVSALEEELAAANqeiVALREQNVHIQRKMASSEGSTES-EHLEGMEPGQKVHEKRLS 257
Cdd:pfam12128 597 ASEEELRERLDKaeealqsAREKQAAAEEQLVQAN---GELEKASREETFARTALKNARLDlRRLFDEKQSEKDKKNKAL 673
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 258 NGSIDSTDETSQIVELQE--LLEKQNYEMAQMKERLAALSSRVGEVEQEAETARK---DLIKTEEMNTKYQRDiREAMAQ 332
Cdd:pfam12128 674 AERKDSANERLNSLEAQLkqLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGALDaqlALLKAAIAARRSGAK-AELKAL 752
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 333 KEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQmeekNRQLQERLELAEQKLQQTMRKAET-LPEVEA 411
Cdd:pfam12128 753 ETWYKRDLASLGVDPDVIAKLKREIRTLERKIERIAVRRQEVLRY----FDWYQETWLQRRPRLATQLSNIERaISELQQ 828
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 412 ELAQRIAaltKAEERHGNIEERMRHLEGQLEEKNQELQRARQR-EKMNEEHnkrlsdtvdrlLTESNERLQLHLKERMAA 490
Cdd:pfam12128 829 QLARLIA---DTKLRRAKLEMERKASEKQQVRLSENLRGLRCEmSKLATLK-----------EDANSEQAQGSIGERLAQ 894
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 333805618 491 LEE-KNVLIQESETFRKNLEE-----SLHDKERLAEEIEKLRSEL 529
Cdd:pfam12128 895 LEDlKLKRDYLSESVKKYVEHfknviADHSGSGLAETWESLREED 939
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
285-533 |
2.54e-05 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 428520 [Multi-domain] Cd Length: 660 Bit Score: 48.57 E-value: 2.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 285 AQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRylsaqrestsihdmndkl 364
Cdd:pfam05557 2 AELIESKARLSQLQNEKKQMELEHKRARIELERKASALARQLERESDRNQELQKRIRLLEKR------------------ 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 365 eneLANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHgnieermrhlEGQLEEK 444
Cdd:pfam05557 64 ---EAEAEEALREQAELNRLKKKNLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRQ----------ELELSST 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 445 NQELQRARQRekmNEEHNKRLSDtvdrlLTESNERLQLHLKERMAALEEKNVLIQESETFRKNLEESLHDKERLAeEIEK 524
Cdd:pfam05557 131 NSELEELQER---LDLQKAKAQE-----AEQLRQNLEAQQSSLAEAEQRIKELEFEIQSQEQDSEIVKNSKSELA-RIPE 201
|
....*....
gi 333805618 525 LRSELDQLK 533
Cdd:pfam05557 202 LERELERLR 210
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
190-533 |
2.66e-05 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 48.31 E-value: 2.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 190 KVRERLRVSLERVSALEEELAAANQEIVALREQNvhiqrkmasSEGSTESEHLEGM--EPGQKVHEKRLSNG-SIDSTDE 266
Cdd:pfam06160 83 KAKKALDEIEELLDDIEEDIKQILEELDELLESE---------EKNREEVEELKDKyrELRKTLLANRFSYGpAIDELEK 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 267 T-----SQIVELQELLEKQNYEMA-----QMKERLAALSSRVGEVEQEAETARKDLikTEEMNtkyqrDIREAMAQkedM 336
Cdd:pfam06160 154 QlaeieEEFSQFEELTESGDYLEArevleKLEEETDALEELMEDIPPLYEELKTEL--PDQLE-----ELKEGYRE---M 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 337 EERITTLEkrYLSAQRESTSIHDMNDKLENELANKEaiLRQMEEKNRQLQERLElaeqKLQQTMRKaetlpEVEAELaqr 416
Cdd:pfam06160 224 EEEGYALE--HLNVDKEIQQLEEQLEENLALLENLE--LDEAEEALEEIEERID----QLYDLLEK-----EVDAKK--- 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 417 iaaltKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEH-------NKRLsDTVDRLLTESNERLQLH------ 483
Cdd:pfam06160 288 -----YVEKNLPEIEDYLEHAEEQNKELKEELERVQQSYTLNENElervrglEKQL-EELEKRYDEIVERLEEKevayse 361
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 333805618 484 LKERMAALEEKNVLIQES-ETFRKNLeESLHDKERLA-EEIEKLRSELDQLK 533
Cdd:pfam06160 362 LQEELEEILEQLEEIEEEqEEFKESL-QSLRKDELEArEKLDEFKLELREIK 412
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
355-465 |
2.76e-05 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 48.67 E-value: 2.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 355 TSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAEL---AQRIA--ALTKAEERHGN 429
Cdd:PRK00409 509 KLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLleeAEKEAqqAIKEAKKEADE 588
|
90 100 110
....*....|....*....|....*....|....*....
gi 333805618 430 IEERMRHLE--GQLEEKNQELQRARQR-EKMNEEHNKRL 465
Cdd:PRK00409 589 IIKELRQLQkgGYASVKAHELIEARKRlNKANEKKEKKK 627
|
|
| COG5281 |
COG5281 |
Phage-related minor tail protein [Mobilome: prophages, transposons]; |
255-494 |
3.07e-05 |
|
Phage-related minor tail protein [Mobilome: prophages, transposons];
Pssm-ID: 227606 [Multi-domain] Cd Length: 833 Bit Score: 48.48 E-value: 3.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 255 RLSNGSIDSTDETSQIVElqELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQrdirEAMAQKE 334
Cdd:COG5281 244 RFASASGESIDKTIKAFS--KLTDDPVNGAKALNRQFHYLTAAQLEQIAALQRAGDTAAAAAAAAEAAA----AMDDRTA 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 335 DMEERITTLEKrylSAQRESTSIHDMNDKLENELANKE--AILRQMEEKNRQLQERLELAEQKLQQTMRKAETLpeveAE 412
Cdd:COG5281 318 RVKENMGTLET---AWDALADAAKKMWDAVLGIGREDKqaALLAAKLAAEKLARVTAQGALNARLKLAQDDLTQ----AE 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 413 LAQRIAALTKAEERHGNieERMRHLEGQLEEKNQELQR------ARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKE 486
Cdd:COG5281 391 LNYAAADQAANQEGALN--AREDEAEVLSTQEERRDILknlladAEKRTARQEELNKALAKAKILQADKAAKAYQEDILQ 468
|
....*...
gi 333805618 487 RMAALEEK 494
Cdd:COG5281 469 REAQSRGK 476
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
45-538 |
3.72e-05 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 47.89 E-value: 3.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 45 LLDTLRETQES---LSLAQQRLQDVIydrdSLQRQLNSALPQDIESlTGGLAGSKGADPP-----------EFAALTKEL 110
Cdd:pfam10174 58 LKEQYRVTQEEnqhLQLTIQALQDEL----RAQRDLNQLLQQDFTT-SPVDGEDKFSTPElteenfrrlqsEHERQAKEL 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 111 NACREQLLEKEEEISE----LKAERNNTRLLLEHLEC-------LVSRHERSLRMTVVKRQAQspsgvssEVEVLKALKS 179
Cdd:pfam10174 133 FLLRKTLEEMELRIETqkqtLGARDESIKKLLEMLQSkglpkksGEEDWERTRRIAEAEMQLG-------HLEVLLDQKE 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 180 LFEHHKALDEKVRERLRVSLERVSALEEELAAANQEIVAL----REQNVHIQRKMASSEGSTE--SEHLEGMEPgQKVHE 253
Cdd:pfam10174 206 KENIHLREELHRRNQLQPDPAKTKALQTVIEMKDTKISSLerniRDLEDEVQMLKTNGLLHTEdrEEEIKQMEV-YKSHS 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 254 KRLSNgSIDSTDE-----TSQIVELQ---ELLEKQNYEMAQ----MKERLAALSSRVGEVEQEAETARKDLIKTEEMNTK 321
Cdd:pfam10174 285 KFMKN-KIDQLKQelskkESELLALQtklETLTNQNSDCKQhievLKESLTAKEQRAAILQTEVDALRLRLEEKESFLNK 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 322 YQ-----------------RDIREAMAQKE------------------DMEERITTLEKRYLSAQRESTSIHDMNDKLEN 366
Cdd:pfam10174 364 KTkqlqdlteekstlageiRDLKDMLDVKErkinvlqkkienlqeqlrDKDKQLAGLKERVKSLQTDSSNTDTALTTLEE 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 367 ELANKEAIL-RQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGN-------IEERMRHLE 438
Cdd:pfam10174 444 ALSEKERIIeRLKEQREREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSlassglkKDSKLKSLE 523
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 439 GQLEEKNQE-------LQRARQRE---KMNEEHNKRLS---DTVDRLLTESN------ERLQLHLKE----------RMA 489
Cdd:pfam10174 524 IAVEQKKEEcsklenqLKKAHNAEeavRTNPEINDRIRlleQEVARYKEESGkaqaevERLLGILREvenekndkdkKIA 603
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 333805618 490 ALEE-------------KNVLIQESETFRKN---LEESLHDK------------ERLAEEIEKLRSELDQLKMRTGS 538
Cdd:pfam10174 604 ELESltlrqmkeqnkkvANIKHGQQEMKKKGaqlLEEARRREdnladnsqqlqlEELMGALEKTRQELDATKARLSS 680
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning]; |
384-541 |
5.93e-05 |
|
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 224117 [Multi-domain] Cd Length: 1163 Bit Score: 47.40 E-value: 5.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 384 QLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTK---AEERHGNIEERMRHLEG-----QLEEKNQELQRARQRE 455
Cdd:COG1196 169 KYKERKEEAERKLERTEENLERLEDLLEELEKQLEKLERqaeKAERYQELKAELRELELalllaKLKELRKELEELEEEL 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 456 KMNEEHNKRLSDTVDRLLTEsNERLQLHLKERMAALEEKNVLIQESETFRKNLEEslhDKERLAEEIEKLRSELDQLKMR 535
Cdd:COG1196 249 SRLEEELEELQEELEEAEKE-IEELKSELEELREELEELQEELLELKEEIEELEG---EISLLRERLEELENELEELEER 324
|
....*.
gi 333805618 536 TGSLIE 541
Cdd:COG1196 325 LEELKE 330
|
|
| COG1579 |
COG1579 |
Predicted nucleic acid-binding protein, contains Zn-ribbon domain [General function ... |
269-419 |
6.42e-05 |
|
Predicted nucleic acid-binding protein, contains Zn-ribbon domain [General function prediction only];
Pssm-ID: 224495 [Multi-domain] Cd Length: 239 Bit Score: 45.82 E-value: 6.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 269 QIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTE----EMNTKYQRDiREAMAQKEDMEE------ 338
Cdd:COG1579 18 EKDRLEPRIKEIRKALKKAKAELEALNKALEALEIELEDLENQVSQLEseiqEIRERIKRA-EEKLSAVKDERElralni 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 339 RITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAET-LPEVEAELAQRI 417
Cdd:COG1579 97 EIQIAKERINSLEDELAELMEEIEKLEKEIEDLKERLERLEKNLAEAEARLEEEVAEIREEGQELSSkREELKEKLDPEL 176
|
..
gi 333805618 418 AA 419
Cdd:COG1579 177 LS 178
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
383-580 |
7.09e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 47.01 E-value: 7.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 383 RQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEERmrhlegqlEEKNQELQRARQREKMNEEHN 462
Cdd:PRK12705 26 KKRQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARRER--------EELQREEERLVQKEEQLDARA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 463 KRLSDTVDRLLTESN----ERLQLHLKERMAALEEKNVLIQESETFRKNLEESLHD--KERLAEEIEKLRSELD-QLKMR 535
Cdd:PRK12705 98 EKLDNLENQLEEREKalsaRELELEELEKQLDNELYRVAGLTPEQARKLLLKLLDAelEEEKAQRVKKIEEEADlEAERK 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 333805618 536 TGSLIEPTIPRTHLDTSAELRYSVgslVDSQSDYRTTKVIRRPRR 580
Cdd:PRK12705 178 AQNILAQAMQRIASETASDLSVSV---VPIPSDAMKGRIIGREGR 219
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Escherichia coli str. K-12 ... |
196-541 |
9.24e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Escherichia coli str. K-12 substr. MG1655 [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 225638 [Multi-domain] Cd Length: 1480 Bit Score: 46.80 E-value: 9.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 196 RVSLERVSALEEELAAANQEIVALREQNVHIQRKMA---SSEGSTESEHLEGMEPGQKVHEKRLSNGSIDSTDEtsQIVE 272
Cdd:COG3096 282 RVHLDQALEFRRELYTSRQQLAAEQYRHVDMSRELAelnGAEGDLEADYQAASDHLNLVQTALRQQEKIERYQA--DLEE 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 273 LQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLikteemnTKYQRDIREAMAQKEDMEERITTLEKRYLSAQR 352
Cdd:COG3096 360 LTIRLEEQNEVVEEANERQEENEARAEAAELEVDELKSQL-------ADYQQALDVQQTRAIQYQQAIAALERAKELCHL 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 353 ESTSIHDMNDKLENELANKEAILRQMeeknRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAE-----ERH 427
Cdd:COG3096 433 PDLTADSAEEWLETFQAKEEEATEKL----LSLEQKMSMAQAAHSQFEQAYQLVVAIAGELARSEAWDVAREllregPDQ 508
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 428 GNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMA-----ALEEKNVLIQEse 502
Cdd:COG3096 509 RHLAEQVQPLRMRLSELEQRLRQQQSAERLLADFCKRQGKNLDAEELEALHQELEALIESLSdsvsnAREQRMALRQE-- 586
|
330 340 350
....*....|....*....|....*....|....*....
gi 333805618 503 tfRKNLEESLHDKERLAEEIEKLRSELDQLKMRTGSLIE 541
Cdd:COG3096 587 --QEQLQSRIQSLMQRAPVWLAAQNALEQLSEQSGEEFT 623
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
333-532 |
1.20e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 46.44 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 333 KEDMEERITTLEKRYLSAQRESTSIHDmndkLENELANKEAILRQmEEKNRQLQERLELAEQKLQQTMRKAETLPEVEA- 411
Cdd:PRK11281 38 EADVQAQLDALNKQKLLEAEDKLVQQD----LEQTLALLDKIDRQ-KEETEQLKQQLAQAPAKLRQAQAELEALKDDNDe 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 412 ELAQRIAALTkaeerhgnieerMRHLEGQLEEKNQELQRARqrekmneehnKRLSDTVDRLLTESN--ERLQlhlkermA 489
Cdd:PRK11281 113 ETRETLSTLS------------LRQLESRLAQTLDQLQNAQ----------NDLAEYNSQLVSLQTqpERAQ-------A 163
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 333805618 490 ALEEKNVLIQESETFRKNLEESlhDKERLAEEIEKLRSELDQL 532
Cdd:PRK11281 164 ALYANSQRLQQIRNLLKGGKVG--GKALRPSQRVLLQAEQALL 204
|
|
| SAM_1 |
pfam00536 |
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ... |
897-961 |
1.26e-04 |
|
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily conserved protein binding domain that is involved in the regulation of numerous developmental processes in diverse eukaryotes. The SAM domain can potentially function as a protein interaction module through its ability to homo- and heterooligomerize with other SAM domains.
Pssm-ID: 425739 Cd Length: 64 Bit Score: 41.10 E-value: 1.26e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 333805618 897 QWDGPTVVAWLElWLGMPAwYVAACRANVKSGAIMSALSDTEIqREIGISNPLHRLKLRLAIQEM 961
Cdd:pfam00536 2 GWSVEDVGEWLE-SIGLGQ-YIDSFRAGYIDGDALLQLTEDDL-LKLGVTLLGHRKKILYAIQRL 63
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
188-468 |
1.40e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 227278 [Multi-domain] Cd Length: 420 Bit Score: 45.87 E-value: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 188 DEKVRERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMASSEGS-TESEHLEGMEPGQKVHEKRLSNGSIDSTDE 266
Cdd:COG4942 47 IAALEKKIREQQDQRAKLEKQLKSLETEIASLEAQLIETADDLKKLRKQiADLNARLNALEVQEREQRRRLAEQLAALQR 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 267 TSQIVELQELLekqNYEMAQMKERLAALssrvgevEQEAETARKDLIKTEEMNTKYQRDIREAMAQKedmeerittlekr 346
Cdd:COG4942 127 SGRNPPPALLV---SPEDAQRSVRLAIY-------YGALNPARAERIDALKATLKQLAAVRAEIAAE------------- 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 347 ylsaQRESTSihdmndkLENELANKEAILRQMEEKNRQLQERLelaEQKLQQTMRKAETLPEVEAELAQRIAALTKAEER 426
Cdd:COG4942 184 ----QAELTT-------LLSEQRAQQAKLAQLLEERKKTLAQL---NSELSADQKKLEELRANESRLKNEIASAEAAAAK 249
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 333805618 427 HGNIEERMRHLEgqLEEKNQELQRARQREKMNEEHNKRLSDT 468
Cdd:COG4942 250 AREAAAAAEAAA--ARARAAEAKRTGETYKPTAPEKMLISST 289
|
|
| SAM_2 |
pfam07647 |
SAM domain (Sterile alpha motif); |
1099-1169 |
1.48e-04 |
|
SAM domain (Sterile alpha motif);
Pssm-ID: 429573 Cd Length: 66 Bit Score: 41.10 E-value: 1.48e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 333805618 1099 VLVWSNDRVIRWIQAIGLREYANNILESGVHG--SLIALDENFdysslalLLQIPTQNTQARQILEREYNNLL 1169
Cdd:pfam07647 1 VESWSLESVADWLRSIGLEQYTDNFRDQGITGaeLLLRLTLED-------LKRLGITSVGHRRKILKKIQELK 66
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
179-465 |
1.63e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 46.10 E-value: 1.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 179 SLFEHHKALDEKVR--ERLRVSLERVSALEEELAAA---NQEIVALREQNVHIQRKMASSEGSTE--SEHLEGMEPGQKV 251
Cdd:PRK04863 797 ELAERYATLSFDVQklQRLHQAFSRFIGSHLAVAFEadpEAELRQLNRRRVELERALADHESQEQqqRSQLEQAKEGLSA 876
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 252 HEKRLsnGSIDSTDETSQIVELQELLEkQNYEMAQMKERLAALSSRVGEVEQEAETARKDliktEEMNTKYQRDIREAMA 331
Cdd:PRK04863 877 LNRLL--PRLNLLADETLADRVEEIRE-QLDEAEEAKRFVQQHGNALAQLEPIVSVLQSD----PEQFEQLKQDYQQAQQ 949
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 332 QKEDMEERITTL----EKR----YLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKA 403
Cdd:PRK04863 950 TQRDAKQQAFALtevvQRRahfsYEDAAEMLAKNSDLNEKLRQRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSY 1029
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 333805618 404 ETLPEVEAELAQRIAALT---------KAEERHGNIEERMRHLEGQleeKNQ-ELQRARQREKMNEEhNKRL 465
Cdd:PRK04863 1030 DAKRQMLQELKQELQDLGvpadsgaeeRARARRDELHARLSANRSR---RNQlEKQLTFCEAEMDNL-TKKL 1097
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
290-549 |
1.65e-04 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 45.62 E-value: 1.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 290 RLAALSSRVGEVEQEAET-----ARKDLIKTEEMNTKYQRDIR-------EAMAQKEDMEERITTLEKRY------LSAQ 351
Cdd:pfam06160 61 SLPDIEELLFEAEELNDKyrfkkAKKALDEIEELLDDIEEDIKqileeldELLESEEKNREEVEELKDKYrelrktLLAN 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 352 RES--TSIhdmnDKLENELANKEAILRQMEEKN--------RQLQERLELAEQKLQQTMRK--------AETLPEVEAEL 413
Cdd:pfam06160 141 RFSygPAI----DELEKQLAEIEEEFSQFEELTesgdyleaREVLEKLEEETDALEELMEDipplyeelKTELPDQLEEL 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 414 AQRIAALTKAEER--HGNIEERMRHLEGQLEE-----KNQELQRArqrEKMNEEHNKRLSDTVDRLLTESNERLQLH--- 483
Cdd:pfam06160 217 KEGYREMEEEGYAleHLNVDKEIQQLEEQLEEnlallENLELDEA---EEALEEIEERIDQLYDLLEKEVDAKKYVEknl 293
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 333805618 484 --LKERMAALEEKNVLIQE-----SETFRKNlEESLHDKERLAEEIEKLRSELDQLKMRtgsLIEPTIPRTHL 549
Cdd:pfam06160 294 peIEDYLEHAEEQNKELKEelervQQSYTLN-ENELERVRGLEKQLEELEKRYDEIVER---LEEKEVAYSEL 362
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
273-535 |
1.66e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 429718 [Multi-domain] Cd Length: 488 Bit Score: 45.65 E-value: 1.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 273 LQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLiktEEMNTKYQRDIREAMAQKEDMEERITTLEKRYLSAQR 352
Cdd:pfam07888 32 LQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQW---ERQRRELESRVAELKEELRQSREKVEELEEKYKELSR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 353 ESTSIHdmndklenelANKEAILRQMEEKNRQLQErLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEE-RHGNIE 431
Cdd:pfam07888 109 SGEELA----------EEKDALLAQRAESEARIRE-LEEDIKTLTQRVLERETELERMKERVKKAGAQRKEEEaERKQLQ 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 432 ERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRL---LTESNERLQLH--LKERMAALEEK-NVLIQESETFR 505
Cdd:pfam07888 178 AKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLtqkLTTAHRKEAENeaLLEELRSLQERlNASERKVEGLG 257
|
250 260 270
....*....|....*....|....*....|
gi 333805618 506 KNLEESLHDKERLAEEIEKLRSELDQLKMR 535
Cdd:pfam07888 258 EELSSMAAQRDRTQAELHQARLQAAQLTLQ 287
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
278-491 |
1.75e-04 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 225177 [Multi-domain] Cd Length: 548 Bit Score: 45.59 E-value: 1.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 278 EKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQ-RDIREAMAQKEDMEERITTLEKRYLSAqrESTS 356
Cdd:COG2268 246 KLVELEVEQQPAGKTAEQTREVKIILAETEAEVAAWKAETRREAEQaEILAEQAIQEEKAQAEQEVQHAKALEA--REMR 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 357 IHDMNDKLENELANKE---AILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEV-EAELAQRIAALTKAE-------- 424
Cdd:COG2268 324 VGLIERQKETELEPQErsyFINAAQRQAQEEAKAAANIAEAIGAQAEAAVETARETeEAERAEQAALVAAAEaaeqeqve 403
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 333805618 425 --ERHGNIEERMRH------LEGQLEEKNQELQRARQReKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAAL 491
Cdd:COG2268 404 iaVRAEAAKAEAEAqaaeikAEAEAIREKGKAEAEAKR-ALAEAIQVLGDAAAAELFKALVQALPEVAEEAAQPM 477
|
|
| GumC |
COG3206 |
Uncharacterized protein involved in exopolysaccharide biosynthesis [Cell wall/membrane ... |
189-453 |
2.07e-04 |
|
Uncharacterized protein involved in exopolysaccharide biosynthesis [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 225747 [Multi-domain] Cd Length: 458 Bit Score: 45.13 E-value: 2.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 189 EKVRERLRVSLERVSALEEE---------LAAANQEIVALREQNvHIQRKMASSEGSTESehLEGMEPgQKVHEKRLSNG 259
Cdd:COG3206 141 DDLLESLKVLRAGRSRVIELsytsndpklAAKLANALAQAYLAD-QLEAQLEAFRRASDS--LDERLE-ELRARLQEAEA 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 260 SIDSTDETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTeemntkyqrdiREAMAQKEDMEER 339
Cdd:COG3206 217 QVEDFRAQHGLTDAARGQLLSEQQLSALNTQLQSARARLAQAEARLASLLQLLPLG-----------REAAALREVLESP 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 340 -ITTLEKRYLSAQREstsIHDMNDKLENELANKEAILRQMEEKNRQLQERLelaeQKLQQTMRKAETLPEV-EAELAQRI 417
Cdd:COG3206 286 tIQDLRQQYAQVRQQ---IADLSTELGAKHPQLVALEAQLAELRQQIAAEL----RQILASLPNELALLEQqEAALEKEL 358
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 333805618 418 AALTKAEERHGNIEERMRHLEGQLEEK----NQELQRARQ 453
Cdd:COG3206 359 AQLKGRLSKLPKLQVQLRELEREAEAArslyETLLQRYQE 398
|
|
| pepcterm_ChnLen |
TIGR03007 |
polysaccharide chain length determinant protein, PEP-CTERM locus subfamily; Members of this ... |
200-415 |
2.36e-04 |
|
polysaccharide chain length determinant protein, PEP-CTERM locus subfamily; Members of this protein family belong to the family of polysaccharide chain length determinant proteins (pfam02706). All are found in species that encode the PEP-CTERM/exosortase system predicted to act in protein sorting in a number of Gram-negative bacteria, and are found near the epsH homolog that is the putative exosortase gene. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]
Pssm-ID: 274386 [Multi-domain] Cd Length: 498 Bit Score: 45.04 E-value: 2.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 200 ERVSALEEELAAANQEIVALREQNVhiqrkmassegstesehleGMEPGQkvhekrlsngsidSTDETSQIVELQELLEK 279
Cdd:TIGR03007 168 EQIKTYEKKLEAAENRLKAFKQENG-------------------GILPDQ-------------EGDYYSEISEAQEELEA 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 280 QNYEMAQMKERLAALSSRVGEVEQEAETARKDL-----IKTEEMNTKYQR----------DIREAMAQKEDMEERITTLE 344
Cdd:TIGR03007 216 ARLELNEAIAQRDALKRQLGGEEPVLLAGSSVAnseldGRIEALEKQLDAlrlrytdkhpDVIATKREIAQLEEQKEEEG 295
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 333805618 345 KRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLElaeqklqQTMRKAETLPEVEAELAQ 415
Cdd:TIGR03007 296 SAKNGGPERGEIANPVYQQLQIELAEAEAEIASLEARVAELTARIE-------RLESLLRTIPEVEAELTQ 359
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
272-503 |
2.42e-04 |
|
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
Pssm-ID: 310534 [Multi-domain] Cd Length: 258 Bit Score: 44.33 E-value: 2.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 272 ELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKryLSAQ 351
Cdd:pfam06008 27 QLQEYLSPENAHKIQIEILEKELSSLAQETEELQKKATQTLAKAQQVNAESERTLGHAKELAEAIKNLIDNIKE--INEK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 352 RESTSIHDM---NDKLENELANKEAILRQMeeKNRQLQERLELAEQKLqqtmRKAETLPEVEAELAQRIAALTKAeerhg 428
Cdd:pfam06008 105 VATLGENDFalpSSDLSRMLAEAQRMLGEI--RSRDFGTQLQNAEAEL----KAAQDLLSRIQTWFQSPQEENKA----- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 429 nIEERMRHLEGQLEEKNQELQ--------RARQREKMNEEHNKRLSDTVDRLLT--ESNERLQLHLKERMAALEEKNVLI 498
Cdd:pfam06008 174 -LANALRDSLAEYEAKLSDLRellreaaaKTRDANRLNLANQANLREFQRKKEEvsEQKNQLEETLKTARDSLDAANLLL 252
|
....*
gi 333805618 499 QESET 503
Cdd:pfam06008 253 QEIDD 257
|
|
| RmuC |
COG1322 |
DNA anti-recombination protein (rearrangement mutator) RmuC [Replication, recombination and ... |
372-533 |
3.19e-04 |
|
DNA anti-recombination protein (rearrangement mutator) RmuC [Replication, recombination and repair];
Pssm-ID: 224241 [Multi-domain] Cd Length: 448 Bit Score: 44.69 E-value: 3.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 372 EAILRQMEEKNRQLQERLELAEqKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLE-------EK 444
Cdd:COG1322 14 LVNLAFIRQLLLRLGRLEQMLG-ELAAVLEQLLLLLAFRAEAEQLRTFARSLQALNLELIQELNELKARLQqqllqsrEQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 445 NQELQRARQR---------EKMNEEHNKRLSDTVDrlltESNERLQLHLKERMAALEEKnVLIQESETFRKNLEEsLHDK 515
Cdd:COG1322 93 LQLLIESLAQlssefqelaNEIFEELNRRLAELNQ----QNLKQLLKPLREVLEKFREQ-LEQRIHESAEERSTL-LEEI 166
|
170
....*....|....*...
gi 333805618 516 ERLAEEIEKLRSELDQLK 533
Cdd:COG1322 167 DRLLGEIQQLAQEAGNLT 184
|
|
| COG4487 |
COG4487 |
Uncharacterized protein, contains DUF2130 domain [Function unknown]; |
364-535 |
4.35e-04 |
|
Uncharacterized protein, contains DUF2130 domain [Function unknown];
Pssm-ID: 226889 [Multi-domain] Cd Length: 438 Bit Score: 44.42 E-value: 4.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 364 LENELANKEAILRQMEEKNRQLQERlELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEE 443
Cdd:COG4487 47 FEKEANEKRAQYRSAKKKELSQLEE-QLINQKKEQKNLFNEQIKQFELALQDEIAKLEALELLNLEKDKELELLEKELDE 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 444 KNQELQRARQReKMNEEHNKRLSDTVDRLLTESNERlqlhlkermaalEEKNVLIQESETFRKNLEESLHDKE--RLAEE 521
Cdd:COG4487 126 LSKELQKQLQN-TAEIIEKKRENNKNEERLKFENEK------------KLEESLELEREKFEEQLHEANLDLEfkENEEQ 192
|
170
....*....|....
gi 333805618 522 IEKLRSELDQLKMR 535
Cdd:COG4487 193 RESKWAILKKLKRR 206
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
41-568 |
4.53e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 44.51 E-value: 4.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 41 ERDRLLDTLRETqESLSLAQQRLQDVI-----------YDRDSLQRQLNsalpqDIESLTGGLAgskgADPPEFAALTKE 109
Cdd:PRK01156 150 QRKKILDEILEI-NSLERNYDKLKDVIdmlraeisnidYLEEKLKSSNL-----ELENIKKQIA----DDEKSHSITLKE 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 110 LNACREQLLEKEEEISELKAERNNtrllLEHLECLVSRHERSLRmtvvkrqaQSPSGVSSEVEVLKALKSLFEHHKALDE 189
Cdd:PRK01156 220 IERLSIEYNNAMDDYNNLKSALNE----LSSLEDMKNRYESEIK--------TAESDLSMELEKNNYYKELEERHMKIIN 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 190 ----KVRERLRVSLERVSALE---EELAAANQEIvalreQNVHIQRKMASSEGSTESEHLEgMEPGQKVHEKRLSNGSID 262
Cdd:PRK01156 288 dpvyKNRNYINDYFKYKNDIEnkkQILSNIDAEI-----NKYHAIIKKLSVLQKDYNDYIK-KKSRYDDLNNQILELEGY 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 263 STDETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDL----IKTEEMNTK---YQRDIREAMAQKED 335
Cdd:PRK01156 362 EMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELneinVKLQDISSKvssLNQRIRALRENLDE 441
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 336 MEERITTLEKR--------YLSAQRESTSIHDMNDK---LENELANKEAILRQMEEKNRQLQERLE-LAEQKLQQTMRKA 403
Cdd:PRK01156 442 LSRNMEMLNGQsvcpvcgtTLGEEKSNHIINHYNEKksrLEEKIREIEIEVKDIDEKIVDLKKRKEyLESEEINKSINEY 521
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 404 ETLPEVEAELAQ---RIAALTKAEERHGNIEERMRHLE-GQLEEKNQELQRA-RQREKMNEEHNKRLSDTVDRLLTESNE 478
Cdd:PRK01156 522 NKIESARADLEDikiKINELKDKHDKYEEIKNRYKSLKlEDLDSKRTSWLNAlAVISLIDIETNRSRSNEIKKQLNDLES 601
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 479 RLQlhlkERMAALEEKNVLIQESETFRKNLEESLHDKERLAEE----IEKLRSELDQLKMRTGSL--IEP---TIPRTHL 549
Cdd:PRK01156 602 RLQ----EIEIGFPDDKSYIDKSIREIENEANNLNNKYNEIQEnkilIEKLRGKIDNYKKQIAEIdsIIPdlkEITSRIN 677
|
570
....*....|....*....
gi 333805618 550 DTSAELRYSVGSLVDSQSD 568
Cdd:PRK01156 678 DIEDNLKKSRKALDDAKAN 696
|
|
| COG4372 |
COG4372 |
Uncharacterized conserved protein, contains DUF3084 domain [Function unknown]; |
150-453 |
4.73e-04 |
|
Uncharacterized conserved protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 226809 [Multi-domain] Cd Length: 499 Bit Score: 44.25 E-value: 4.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 150 RSLRMTVVK--------RQAQSPSGVSSEVevLKALKSLFEHHKALDEKVRERLRVSLERVSALEEELAAANQEIVALRE 221
Cdd:COG4372 67 RNLRSGVFQlddirpqlRALRTELGTAQGE--KRAAETEREAARSELQKARQEREAVRQELAAARQNLAKAQQELARLTK 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 222 QNVHIQRKMassegstesehlegmepGQKVHEKRLSNGSIDSTDETSQivELQELLEkqnyemaQMKERLAALSSRVGEV 301
Cdd:COG4372 145 QAQDLQTRL-----------------KTLAEQRRQLEAQAQSLQASQK--QLQASAT-------QLKSQVLDLKLRSAQI 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 302 EQEAetarkdlikteemntkyqrdiREAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEK 381
Cdd:COG4372 199 EQEA---------------------QNLATRANAAQARTEELARRAAAAQQTAQAIQQRDAQISQKAQQIAARAEQIRER 257
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 333805618 382 NRQLQeRLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIeERMRHLEGQLEEKNQELQRARQ 453
Cdd:COG4372 258 ERQLQ-RLETAQARLEQEVAQLEAYYQAYVRLRQQAAATQRGQVLAGAA-QRVAQAQAQAQAQAQLLSSANR 327
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
300-526 |
4.80e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 44.44 E-value: 4.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 300 EVEQEAET-----ARKDLIKTEEMNTKYQRD---IREAMA----QKEDMEERITTLEKRYLSAQRE----STSIHDMNDK 363
Cdd:PRK04778 90 EAEELNDKfrfrkAKHEINEIESLLDLIEEDieqILEELQelleSEEKNREEVEQLKDLYRELRKSllanRFSFGPALDE 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 364 LENELANKEAILRQMEEKN-----RQLQERLELAEQKLQQTMRKAETLPEVEAELAQRI-AALTKAEE------------ 425
Cdd:PRK04778 170 LEKQLENLEEEFSQFVELTesgdyVEAREILDQLEEELAALEQIMEEIPELLKELQTELpDQLQELKAgyrelveegyhl 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 426 RHGNIEERMRHLEGQLEEKNQELQR---ARQREKmNEEHNKRLSDTVDRLLTEsnerlqlhlkerMAAleeKNVLIQESE 502
Cdd:PRK04778 250 DHLDIEKEIQDLKEQIDENLALLEEldlDEAEEK-NEEIQERIDQLYDILERE------------VKA---RKYVEKNSD 313
|
250 260
....*....|....*....|....
gi 333805618 503 TFRKNLEESLHDKERLAEEIEKLR 526
Cdd:PRK04778 314 TLPDFLEHAKEQNKELKEEIDRVK 337
|
|
| BMS1 |
COG5192 |
GTP-binding protein required for 40S ribosome biogenesis [Translation, ribosomal structure and ... |
193-620 |
4.90e-04 |
|
GTP-binding protein required for 40S ribosome biogenesis [Translation, ribosomal structure and biogenesis];
Pssm-ID: 227519 [Multi-domain] Cd Length: 1077 Bit Score: 44.35 E-value: 4.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 193 ERLRVSLERVsalEEELAAANQEIVALREQNVHIQRKMASSEGSTESEHLEGMEPGQKVHEK--RLSNGSID----STDE 266
Cdd:COG5192 363 EKMKMQLQEI---EQDPGVDGVGLQLFSNSDAIDTVDRESSEIDNVGRKTRRQPTGKAIAEEtsREDELSFDdsdvSTSD 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 267 TSQIVELQELLEKQNYEMAQMKERLAALSSRVGEvEQEAETARKDLIKTEEMNTkyQRDIREAMAQKEDMEERITTlEKR 346
Cdd:COG5192 440 ENEDVDFTGKKGAINNEDESDNEEVAFDSDSQFD-ESEGNLRWKEGLASKLAYS--QSGKRGRNIQKIFYDESLSP-EEC 515
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 347 YLSAQRESTSIHDMNDKLENElanKEAILRQMEEKNRQLQERLE-LAEQKLQQTMRKAETLPEVEAELAQriAALTKAEE 425
Cdd:COG5192 516 IEEYKGESAKSSESDLVVQDE---PEDFFDVSKVANESISSNHEkLMESEFEELKKKWSSLAQLKSRFQK--DATLDSIE 590
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 426 RHgniEErmrhLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAALEEK---NVLIQESE 502
Cdd:COG5192 591 GE---EE----LIQDDEKGNFEDLEDEENSSDNEMEESRGSSVTAENEESADEVDYETEREENARKKEElrgNFELEERG 663
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 503 TFRKN-LEESLHDKERLAEEIEKLRSELDQLKMRTGSLIEPT------------IPRTHLDTSaELRYSV--GSLVDSQS 567
Cdd:COG5192 664 DPEKKdVDWYTEEKRKIEEQLKINRSEFETMVPESRVVIEGYragryvrivlshVPLEFVDEF-NSRYPIvlGGLLPAEK 742
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 333805618 568 DYRTTKV-IRRPRRGRMGVRRDEPKVKSLGdheWNRTQQIGVLSSHPFESDTEM 620
Cdd:COG5192 743 EMGIVQGrIKRHRWHKKILKTNDPLIFSVG---WRRFQSIPVYSMKDSRTRNRM 793
|
|
| SAM_STIM-1,2-like |
cd09504 |
SAM domain of STIM-1,2-like proteins; SAM (sterile alpha motif) domain of STIM-1,2-like ... |
898-956 |
5.02e-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: 5.02e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 333805618 898 WDGPTVVAWLELWLGMPAwYVAACRANVKSGAIMSALSDTE---IQREIGISNPLHRLKLRL 956
Cdd:cd09504 5 WTVEDTVEWLVNSVELPQ-YVEAFKENGVDGSALPRLAVNNpsfLTSVLGIKDPIHRQKLSL 65
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
272-535 |
5.78e-04 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 433539 [Multi-domain] Cd Length: 341 Bit Score: 43.75 E-value: 5.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 272 ELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIRE--AMAQKEDMEERITTLE--KRY 347
Cdd:pfam13868 56 ALEEEEEKEEERKEERKQYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQEedQAEAEEKLEKQRQLREeiDEF 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 348 LSAQRESTSIHDMNDKLENElANKEAILRQMEEKNRQLQERLELAEQK----------LQQTMRKAETLPEVEAELAQ-- 415
Cdd:pfam13868 136 NEEQAKWKELEKEEEKEEDL-RILEYLKEKAEREEEREAERREIKEEKereiarlraqQEKAQDEKAERDELRAKLYQee 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 416 -----RIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAA 490
Cdd:pfam13868 215 qerkwRQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRREKRLEHRRE 294
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 333805618 491 LEEknvLIQE-SETFRKNLEESLHDKERLAEEIEKLRSELDQLKMR 535
Cdd:pfam13868 295 LEK---QIEErERQRAAEREEELEEGERLREEEAERRERIEEERQK 337
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
182-529 |
5.84e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.36 E-value: 5.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 182 EHHKALDEKVRERLRVSLERVSALEEELAAANQEIVALRE-QNVHIQRKMASSEGSTESEHLEGMEPGQKVHEKRLSNGS 260
Cdd:PTZ00121 1168 EARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKaEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEE 1247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 261 IDSTDETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARK--DLIKTEEMNTKYQ--RDIREAMAQKEDM 336
Cdd:PTZ00121 1248 ERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKaeEKKKADEAKKKAEeaKKADEAKKKAEEA 1327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 337 EERITTLEKRYLSAQREStsihdmndklenELANKEAilRQMEEKNRQLQERLELAEQKLQQTMRKAEtlpeveaELAQR 416
Cdd:PTZ00121 1328 KKKADAAKKKAEEAKKAA------------EAAKAEA--EAAADEAEAAEEKAEAAEKKKEEAKKKAD-------AAKKK 1386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 417 IAALTKAEERHGNIEERMRHLEgQLEEKNQELQRARQREKMNEEhnKRLSDTVDRLLTESN--ERLQLHLKERMAA--LE 492
Cdd:PTZ00121 1387 AEEKKKADEAKKKAEEDKKKAD-ELKKAAAAKKKADEAKKKAEE--KKKADEAKKKAEEAKkaDEAKKKAEEAKKAeeAK 1463
|
330 340 350
....*....|....*....|....*....|....*....
gi 333805618 493 EKNVLIQESETFRKNLEESLHDKE--RLAEEIEKLRSEL 529
Cdd:PTZ00121 1464 KKAEEAKKADEAKKKAEEAKKADEakKKAEEAKKKADEA 1502
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
267-532 |
6.31e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 44.06 E-value: 6.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 267 TSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLE-- 344
Cdd:PRK04778 111 ESLLDLIEEDIEQILEELQELLESEEKNREEVEQLKDLYRELRKSLLANRFSFGPALDELEKQLENLEEEFSQFVELTes 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 345 ------KRYLSAQRESTS------------IHDMNDKLENELANKEAILRQMEEKN-----RQLQERLELAEQKLQQTMR 401
Cdd:PRK04778 191 gdyveaREILDQLEEELAaleqimeeipelLKELQTELPDQLQELKAGYRELVEEGyhldhLDIEKEIQDLKEQIDENLA 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 402 KAETLpeveaelaqriaALTKAEERHGNIEERMRHLEGQLE---------EKNQElqRARQREKMNEEHNKRLSDTVDRL 472
Cdd:PRK04778 271 LLEEL------------DLDEAEEKNEEIQERIDQLYDILErevkarkyvEKNSD--TLPDFLEHAKEQNKELKEEIDRV 336
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 333805618 473 -----LTESNERLQLHLKERMAALEEKNVLIQE---------SETfRKNLEESLHDKERLAEEIEKLRSELDQL 532
Cdd:PRK04778 337 kqsytLNESELESVRQLEKQLESLEKQYDEITEriaeqeiaySEL-QEELEEILKQLEEIEKEQEKLSEMLQGL 409
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
362-536 |
6.73e-04 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 42.43 E-value: 6.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 362 DKLENELANKEAILRQME------------EKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIaaltkaEERHGN 429
Cdd:cd00176 10 DELEAWLSEKEELLSSTDygddlesveallKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEI------QERLEE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 430 IEERMRHLEGQLEEKNQELQRARQREKMNEEH---NKRLSDTVDRLLTESN-------ERLQLHLKERMAALEEKNVLIQ 499
Cdd:cd00176 84 LNQRWEELRELAEERRQRLEEALDLQQFFRDAddlEQWLEEKEAALASEDLgkdlesvEELLKKHKELEEELEAHEPRLK 163
|
170 180 190
....*....|....*....|....*....|....*....
gi 333805618 500 ESETFRKNLEESLH--DKERLAEEIEKLRSELDQLKMRT 536
Cdd:cd00176 164 SLNELAEELLEEGHpdADEEIEEKLEELNERWEELLELA 202
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
177-448 |
7.52e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 44.06 E-value: 7.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 177 LKSLFEHHKALDEKVRERLRVSLERVSALEEELAAANQEIVALREQnVHIQRKMASSEGSTESEHLEGMEPGQKVHEKrl 256
Cdd:pfam12128 260 LSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDE-LNGELSAADAAVAKDRSELEALEDQHGAFLD-- 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 257 sngsidstDETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETaRKDLIKtEEMNTKYQRDIREAMAQKEDM 336
Cdd:pfam12128 337 --------ADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNR-RRSKIK-EQNNRDIAGIKDKLAKIREAR 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 337 EERITTLEKRYlsAQRESTSIHDMN-DKLENELANKEAILRQMEEKNR---------------QLQERLELAEQKLQQTM 400
Cdd:pfam12128 407 DRQLAVAEDDL--QALESELREQLEaGKLEFNEEEYRLKSRLGELKLRlnqatatpelllqleNFDERIERAREEQEAAN 484
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 333805618 401 RKAETLpevEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQEL 448
Cdd:pfam12128 485 AEVERL---QSELRQARKRRDQASEALRQASRRLEERQSALDELELQL 529
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
300-533 |
8.89e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 43.56 E-value: 8.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 300 EVEQEAETARKdlikteEMNTKYQRDIREAMAQKEDMEERITTLEKRYLSAQRESTsihdmndKLENELANKEAILRQME 379
Cdd:pfam05483 201 ELRVQAENARL------EMHFKLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQIT-------EKENKMKDLTFLLEESR 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 380 EKNRQLQERLELAEQKLQQTMRK----AETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQRE 455
Cdd:pfam05483 268 DKANQLEEKTKLQDENLKELIEKkdhlTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAH 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 456 KMNEEHNKRLSDTVDRLLTESNERLQLH---LKERMAALEEKNVLIQESETFRKNLEESLHDKERLAEEIEKLRSELDQL 532
Cdd:pfam05483 348 SFVVTEFEATTCSLEELLRTEQQRLEKNedqLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQF 427
|
.
gi 333805618 533 K 533
Cdd:pfam05483 428 E 428
|
|
| Tropomyosin_1 |
pfam12718 |
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ... |
386-524 |
9.77e-04 |
|
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and Tpm2, biochemical and sequence analyses indicate that Tpm2p spans four actin monomers along a filament, whereas Tpm1p spans five. Despite its shorter length, Tpm2p can compete with Tpm1p for binding to F-actin. Over-expression of Tpm2p in vivo alters the axial budding of haploids to a bipolar pattern, and this can be partially suppressed by co-over-expression of Tpm1p. This suggests distinct functions for the two tropomyosins, and indicates that the ratio between them is important for correct morphogenesis. The family also contains higher eukaryote Tpm3 members.
Pssm-ID: 403808 [Multi-domain] Cd Length: 142 Bit Score: 40.75 E-value: 9.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 386 QERLELAEQKLQQtmrkaetLPEVEAELAQRIAALTKaeeRHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRL 465
Cdd:pfam12718 13 QERAEELEEKVKE-------LEQENLEKEQEIKSLTH---KNQQLEEEVEKLEEQLKEAKEKAEESEKLKTNNENLTRKI 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 333805618 466 sdtvdRLLTESNERLQLHLKERMAALEEKNVLIQESETFRKNLEESLHDKERLAEEIEK 524
Cdd:pfam12718 83 -----QLLEEELEESDKRLKETTEKLRETDVKAEHLERKVQALEQERDEWEKKYEELEE 136
|
|
| PRK03992 |
PRK03992 |
proteasome-activating nucleotidase; Provisional |
486-544 |
1.14e-03 |
|
proteasome-activating nucleotidase; Provisional
Pssm-ID: 179699 [Multi-domain] Cd Length: 389 Bit Score: 42.90 E-value: 1.14e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 486 ERMAALEEKNV-LIQESETFRKNLEESLHDKERLAEEIEKLRSELDQLKmrTGSLIEPTI 544
Cdd:PRK03992 1 ERLEALEERNSeLEEQIRQLELKLRDLEAENEKLERELERLKSELEKLK--SPPLIVATV 58
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N-terminus of SMC proteins. The ... |
320-533 |
1.19e-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: 43.42 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 320 TKYQRDIREAMAQKEDMEERITTLEKRYLSAQRESTSIhDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQK---- 395
Cdd:pfam02463 165 SRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKL-KEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIdllq 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 396 -----LQQTMRKAETLPEVEAELAQRIAALTKAEERhgnIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRlsdtVD 470
Cdd:pfam02463 244 ellrdEQEEIESSKQEIEKEEEKLAQVLKENKEEEK---EKKLQEEELKLLAKEEEELKSELLKLERRKVDDEE----KL 316
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 333805618 471 RLLTESNERLQLHLKERMAALEEKNVLIQESETFRKNLEESLHDKERLAEEIEKLRSELDQLK 533
Cdd:pfam02463 317 KESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKK 379
|
|
| YhaN |
COG4717 |
Uncharacterized protein YhaN, contains AAA domain [Function unknown]; |
122-455 |
1.21e-03 |
|
Uncharacterized protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 227061 [Multi-domain] Cd Length: 984 Bit Score: 43.29 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 122 EEISELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSPSG----VSSEVEVLKALKSLFEHHKALDEKVRERL-- 195
Cdd:COG4717 134 QEIHELNSKGILGYLLFSGTSGSPASTKLLEVLNKEADSLYKPSGrnpqINQLLEKLKQERNEIDEAEKEYATYHKLLes 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 196 -RVSLERVSALEEELAAANQEIVALR---EQNVHIQRKMASSEGSTESEHLEGMEPGQKVH--EKRLSNGSIDSTDETSQ 269
Cdd:COG4717 214 rRAEHARLAELRSELRADRDHIRALRdavELWPRLQEWKQLEQELTRRREELATFPRDGVLrlEKREAHLQKTEAEIDAL 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 270 IVELQELLEKQNyEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNtkyQRDIREAMAQKEDMEERITTLEKRYLS 349
Cdd:COG4717 294 LVRLAELKDLAS-QLIPAKEAVLQALVRLHQQLSEIKASAFELTETLAGI---EADLRDKEEAAGNGFEAERVHDLRSLE 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 350 AQRESTSIHDMNDKLENELANK--EAILRQME-EKNRQLQERLELAEQKLQQtmrkaETLPEVEAELAQRIAALTKAEER 426
Cdd:COG4717 370 CMLRYQSSQRELKQTEAAYCKRldEKRLFEDEaEEEARQRLADDEEEVRAGD-----EAREEKIAANSQVIDKEEVCNLY 444
|
330 340
....*....|....*....|....*....
gi 333805618 427 HGNIEERMRHLEGQLEEKNQELQRARQRE 455
Cdd:COG4717 445 DRRDTAWQKQRFLREKQTAFERQKTEHTK 473
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
268-420 |
1.28e-03 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 433526 [Multi-domain] Cd Length: 200 Bit Score: 41.43 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 268 SQIVELQELLEKQNYEMA-------QMKERLAALSSRVGEVEQEAETARKD---LIKTEEMNTKYQRDIREAMAQKEDME 337
Cdd:pfam13851 33 EEIAEMKKKEERNEKLMSeiqqenkRLTEPLQKAQEEVEELRKQLENYEKDkqsLKNLKARLKVLEKELKDLKWEHEVLE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 338 ERITTLEKRY--LSAQREStSIHDMNDKLENE---LANK-EAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEA 411
Cdd:pfam13851 113 QRFEKVERERdeLYDKFEA-AIQDVQQKTGLKnllLEKKlQALGETLEKKEAQLNEVLAAANLDPDALQAVTEKLEDVLE 191
|
....*....
gi 333805618 412 ELAQRIAAL 420
Cdd:pfam13851 192 SKNQLIKDL 200
|
|
| ERM |
pfam00769 |
Ezrin/radixin/moesin family; This family of proteins contain a band 4.1 domain (pfam00373), at ... |
333-536 |
1.38e-03 |
|
Ezrin/radixin/moesin family; This family of proteins contain a band 4.1 domain (pfam00373), at their amino terminus. This family represents the rest of these proteins.
Pssm-ID: 425860 [Multi-domain] Cd Length: 247 Bit Score: 41.85 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 333 KEDMEERITTLEKRYLSAQrestsihDMNDKLENELANKEAILRQMEEKNRQLQE---RLELAEQKLQQTMRKAETLPEV 409
Cdd:pfam00769 1 REEAEREKQELEERLKQYE-------EETRKAQEELEESEETAELLEEKLRVAEEeaeLLEQKAQEAEEEKERLEESAEM 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 410 EAE----LAQRIAALTKAEERhgnIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLK 485
Cdd:pfam00769 74 EAEekeqLERELREAQEEVAR---LEEESERKEEEAERLQEELEEAREEEEEAKEKLLAASTSPSHHHSEESENEDDEEE 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 333805618 486 ERM-----AALEEKNVLIQESETFRKNLEESLHDKERLAEEIEKLRSELDQLKMRT 536
Cdd:pfam00769 151 EESyeggsAELSNDGDMDQLSDRIEEERVTEAEKNERLQKQLKALKSELAQARDET 206
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
152-691 |
1.45e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 43.11 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 152 LRMTVVKRQAQspsgVSSEVEVLKALKSLFEHHKALDEKVRErlrvSLERVSALEEELAAANQEIVALREQNVHIQRKMA 231
Cdd:TIGR00606 222 IRDQITSKEAQ----LESSREIVKSYENELDPLKNRLKEIEH----NLSKIMKLDNEIKALKSRKKQMEKDNSELELKME 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 232 SSEGSTESEHLEgmepgqkVHEKRLSNGSidstDETSQIVELQELLEKQNYEMAQMKERLAALSSRVG------EVEQEA 305
Cdd:TIGR00606 294 KVFQGTDEQLND-------LYHNHQRTVR----EKERELVDCQRELEKLNKERRLLNQEKTELLVEQGrlqlqaDRHQEH 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 306 ETARKDLIKTEEMNTKY---------QRDIREAMA-QKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAIL 375
Cdd:TIGR00606 363 IRARDSLIQSLATRLELdgfergpfsERQIKNFHTlVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTI 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 376 RQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEErHGNIEERMRHLEGQLEEKNQELQRARQRE 455
Cdd:TIGR00606 443 ELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEK-NSLTETLKKEVKSLQNEKADLDRKLRKLD 521
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 456 KMNEEHNkRLSDTVDRLLTESNERLQLHLKERMAALEEKNVLIQESETF--RKNLEESLH----DKERLAEEIEKLRSEL 529
Cdd:TIGR00606 522 QEMEQLN-HHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYFpnKKQLEDWLHskskEINQTRDRLAKLNKEL 600
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 530 DQLKMRTGSLIEPTIPRTHLDTSAELR-YSVGSLVDSQSDY-RTTKVIRRPRRGRMGVRRDEPKVKSLGDHEWNRTQQIG 607
Cdd:TIGR00606 601 ASLEQNKNHINNELESKEEQLSSYEDKlFDVCGSQDEESDLeRLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCC 680
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 608 VLSSHPFESDTEMSDIDDDdretiFSSMDLLSPSGHSDAQTLAMMLQEQLDAINKEIRLIQEEKESTELRAEEIENRVAS 687
Cdd:TIGR00606 681 PVCQRVFQTEAELQEFISD-----LQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQK 755
|
....
gi 333805618 688 VSLE 691
Cdd:TIGR00606 756 VNRD 759
|
|
| HOOK |
pfam05622 |
HOOK protein; This family consists of several HOOK1, 2 and 3 proteins from different ... |
169-290 |
1.61e-03 |
|
HOOK protein; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organisms. 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 the 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.
Pssm-ID: 428548 [Multi-domain] Cd Length: 526 Bit Score: 42.35 E-value: 1.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 169 SEVEVLKALKSLFEHHKALDEKVRERLRVSLERVSALE---EELAAANQEIVALREQNVHIQRKM---------ASSEGS 236
Cdd:pfam05622 300 SEREKLTELQALLEDANRRKNELETQNRLANQRILELQqqvEELQKALQEQGSKAEDSSLLKQKLeehleklheAQEELQ 379
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 333805618 237 TESEHLEGMEPGQkvhekrlsngsidsTDETSQIVELQELLEKQNYEMAQMKER 290
Cdd:pfam05622 380 KKKEQLEELEPKV--------------DSNLQKIDELQEALRKKDEDMKAMEER 419
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
309-532 |
1.74e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 42.76 E-value: 1.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 309 RKDLIKTEEMNTKYQRDIREAMAQKEdMEERITTLEkrylsaqreSTSIHdmNDKLENELANKEAILRQMEEKNRQLQER 388
Cdd:COG5022 809 RKEYRSYLACIIKLQKTIKREKKLRE-TEEVEFSLK---------AEVLI--QKFGRSLKAKKRFSLLKKETIYLQSAQR 876
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 389 LELAEQK---LQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIE-----ERMRHLEGQLEEKNQELQRARQREKmNEE 460
Cdd:COG5022 877 VELAERQlqeLKIDVKSISSLKLVNLELESEIIELKKSLSSDLIENlefktELIARLKKLLNNIDLEEGPSIEYVK-LPE 955
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 333805618 461 HNKRLsdTVDRLLTESNERLQLHLKERMAALEEKNVLIQESETFRKNLEESLHDKERLAEEIEKLRSELDQL 532
Cdd:COG5022 956 LNKLH--EVESKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQYGALQESTKQLKELPVEV 1025
|
|
| TolA |
COG3064 |
Membrane protein involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
299-514 |
2.26e-03 |
|
Membrane protein involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 225606 [Multi-domain] Cd Length: 387 Bit Score: 41.86 E-value: 2.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 299 GEVEQEAETARKdliKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRYLSAQREStsihdmndklenELANKEAILRQM 378
Cdd:COG3064 65 GRIQSQQSSAKK---GEQQRKKKEEQVAEELKPKQAAEQERLKQLEKERLKAQEQQ------------KQAEEAEKQAQL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 379 EEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMN 458
Cdd:COG3064 130 EQKQQEEQARKAAAEQKKKAEAAKAKAAAEAAKLKAAAEAKKKAEEAAKAAEEAKAKAEAAAAKKKAEAEAKAAAEKAKA 209
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 333805618 459 EEHNKRLSDTVDRLLTESNERLQLHLKERMAALEEKNVLIQESEtfRKNLEESLHD 514
Cdd:COG3064 210 EAEAKAKAEKKAEAAAEEKAAAEKKKAAAKAKADKAAAAAKAAE--RKAAAAALDD 263
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
259-442 |
2.43e-03 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 41.59 E-value: 2.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 259 GSIDSTDETSQIVELQELLEKQNYEMAQM---------KERLAALSSRVGEVEQEAETARKDLikteemnTKYQRDIrea 329
Cdd:cd22656 82 AQNAGGTIDSYYAEILELIDDLADATDDEeleeakktiKALLDDLLKEAKKYQDKAAKVVDKL-------TDFENQT--- 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 330 MAQKEDMEERITTLEKRYlsaQRESTSIHDMN-DKLENELAN-KEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLP 407
Cdd:cd22656 152 EKDQTALETLEKALKDLL---TDEGGAIARKEiKDLQKELEKlNEEYAAKLKAKIDELKALIADDEAKLAAALRLIADLT 228
|
170 180 190
....*....|....*....|....*....|....*
gi 333805618 408 EVEAELAQRIAALTKAEERHGNIEERMRHLEGQLE 442
Cdd:cd22656 229 AADTDLDNLLALIGPAIPALEKLQGAWQAIATDLD 263
|
|
| ERM |
pfam00769 |
Ezrin/radixin/moesin family; This family of proteins contain a band 4.1 domain (pfam00373), at ... |
278-486 |
2.59e-03 |
|
Ezrin/radixin/moesin family; This family of proteins contain a band 4.1 domain (pfam00373), at their amino terminus. This family represents the rest of these proteins.
Pssm-ID: 425860 [Multi-domain] Cd Length: 247 Bit Score: 41.08 E-value: 2.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 278 EKQNYEMAQmkerlaalssRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRYLSAQRESTSI 357
Cdd:pfam00769 5 EREKQELEE----------RLKQYEEETRKAQEELEESEETAELLEEKLRVAEEEAELLEQKAQEAEEEKERLEESAEME 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 358 HDMNDKLENELANKEA-ILRQMEEKNR------QLQERLELAEQKLQQTMRKAETLPEVEaelaqriaaltkaeerHGNI 430
Cdd:pfam00769 75 AEEKEQLERELREAQEeVARLEEESERkeeeaeRLQEELEEAREEEEEAKEKLLAASTSP----------------SHHH 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 333805618 431 EErmrHLEGQLEEKNQELQRARQREKMNEEHNKRLSDT--VDRL-LTESNERLQLHLKE 486
Cdd:pfam00769 139 SE---ESENEDDEEEEESYEGGSAELSNDGDMDQLSDRieEERVtEAEKNERLQKQLKA 194
|
|
| SAM_2 |
pfam07647 |
SAM domain (Sterile alpha motif); |
1021-1076 |
2.69e-03 |
|
SAM domain (Sterile alpha motif);
Pssm-ID: 429573 Cd Length: 66 Bit Score: 37.63 E-value: 2.69e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 333805618 1021 EWLPSLGLPQYRSYFMECLVD-ARMLDHLTKKDLRvHLKMVDSFHRTSLQYGIMCLK 1076
Cdd:pfam07647 11 DWLRSIGLEQYTDNFRDQGITgAELLLRLTLEDLK-RLGITSVGHRRKILKKIQELK 66
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
383-531 |
2.75e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.69 E-value: 2.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 383 RQLQERLELAEQKLQQTMRKAETlpevEAELAQRIAALTKAEERHgnieERMRHLEGQLEEKNQELQRARQREKMNEEHn 462
Cdd:PRK12704 27 KIAEAKIKEAEEEAKRILEEAKK----EAEAIKKEALLEAKEEIH----KLRNEFEKELRERRNELQKLEKRLLQKEEN- 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 333805618 463 krlsdtvdrlltesnerlqlhLKERMAALEEKNvliQESETFRKNLEESLHDKERLAEEIEKLRSELDQ 531
Cdd:PRK12704 98 ---------------------LDRKLELLEKRE---EELEKKEKELEQKQQELEKKEEELEELIEEQLQ 142
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal domain of peptidoglycan hydrolase CwlO [Function unknown]; |
253-434 |
3.42e-03 |
|
Uncharacterized N-terminal domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 226400 [Multi-domain] Cd Length: 265 Bit Score: 40.86 E-value: 3.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 253 EKRLSNGSIDSTDetSQIVELQEllEKQNYEmaqmkERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAmaq 332
Cdd:COG3883 25 FAALLSDKIQNQD--SKLSELQK--EKKNIQ-----NEIESLDNQIEEIQSKIDELQKEIDQSKAEIKKLQKEIAEL--- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 333 KEDMEERITTLEKR------------YLSAQRESTSIHDMNDKL--------------------ENELANKEAILrqmEE 380
Cdd:COG3883 93 KENIVERQELLKKRaramqvngtatsYIDVILNSKSFSDLISRVtaisvivdadkkileqqkedKKSLEEKQAAL---ED 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 333805618 381 KNRQLQERLELAEQKLQQ---------------TMRKAETLPEVEAELAQR-----IAALTKAEERHGNIEERM 434
Cdd:COG3883 170 KLETLVALQNELETQLNSlnsqkaeknaliaalAAKEASALGEKAALEEQKalaeaAAAEAAKQEAAAKAAAQE 243
|
|
| HEC1 |
COG5185 |
Protein involved in chromosome segregation, interacts with SMC proteins [Cell cycle control, ... |
171-534 |
3.68e-03 |
|
Protein involved in chromosome segregation, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 227512 [Multi-domain] Cd Length: 622 Bit Score: 41.51 E-value: 3.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 171 VEVLKALKSLFEHHKALDEKVRERLRV----------SLERVSALEEELAAANQEIVALREQNVHIQRKMASSEGSTESE 240
Cdd:COG5185 203 VRLIIKLDMCLQPLKTLDQQDRYELMVekllfdyfteSYKSFLKLEDNYEPSEQELKLGFEKFVHIINTDIANLKTQNDN 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 241 HLEGMEPGQKVHEKrlsngsIDSTDETSQivELQELLEKQNYEMAQMKERLaalSSRVGEVEQEAEtarkDLIKTEEMNT 320
Cdd:COG5185 283 LYEKIQEAMKISQK------IKTLREKWR--ALKSDSNKYENYVNAMKQKS---QEWPGKLEKLKS----EIELKEEEIK 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 321 KYQRDIREAMAQKEdmEERITTLEKRYLSAQREstsihDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTM 400
Cdd:COG5185 348 ALQSNIDELHKQLR--KQGISTEQFELMNQERE-----KLTRELDKINIQSDKLTKSVKSRKLEAQGIFKSLEKTLRQYD 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 401 RKAETLPEVEAEL------AQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKrlsDTVDRLLT 474
Cdd:COG5185 421 SLIQNITRSRSQIghnvndSSLKINIEQLFPKGSGINESIKKSILELNDEIQERIKTEENKSITLEEDI---KNLKHDIN 497
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 475 ESNERLQLHLKERMAALEEKNVLIQESEtfrknleeslHDKERLAEEIEKLRSELDQLKM 534
Cdd:COG5185 498 ELTQILEKLELELSEANSKFELSKEENE----------RELVAQRIEIEKLEKELNDLNL 547
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
274-452 |
3.72e-03 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 40.12 E-value: 3.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 274 QELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLikteEMNTKYQRDIREAmaqkEDMEERITTLEKRYLSaqre 353
Cdd:cd00176 64 EQLIEEGHPDAEEIQERLEELNQRWEELRELAEERRQRL----EEALDLQQFFRDA----DDLEQWLEEKEAALAS---- 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 354 stsihdmnDKLENELANKEAILRQMEEknrqLQERLELAEQKLQQTMRKAETLPEveaelAQRIAALTKAEERHGNIEER 433
Cdd:cd00176 132 --------EDLGKDLESVEELLKKHKE----LEEELEAHEPRLKSLNELAEELLE-----EGHPDADEEIEEKLEELNER 194
|
170
....*....|....*....
gi 333805618 434 MRHLEGQLEEKNQELQRAR 452
Cdd:cd00176 195 WEELLELAEERQKKLEEAL 213
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
269-480 |
3.89e-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: 426331 [Multi-domain] Cd Length: 1081 Bit Score: 41.68 E-value: 3.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 269 QIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTlekryl 348
Cdd:pfam01576 890 RIAQLEEELEEEQSNTELLNDRLRKLTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMEGTVKS------ 963
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 349 saqrestsihdmndKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRK-AETLPEVEAElaQRIAALTKAEERH 427
Cdd:pfam01576 964 --------------KYKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKlKEVLLQVEDE--RRNADQYKDQAEK 1027
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 333805618 428 GNIeeRMRHLEGQLEEKNQELQRAR-QREKMNEEhnkrLSDTvdrllTESNERL 480
Cdd:pfam01576 1028 GNS--RLKQLKRQLEEAEEEASRANaARRKLQRE----LDDA-----TESAEAM 1070
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
303-460 |
4.14e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.30 E-value: 4.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 303 QEAETARKDLIKTEEmntkyqrdiREAMAQKEDMEerittlekryLSAQREstsIHDMNDKLENELANKEAILRQMEEKN 382
Cdd:PRK12704 34 KEAEEEAKRILEEAK---------KEAEAIKKEAL----------LEAKEE---IHKLRNEFEKELRERRNELQKLEKRL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 383 RQLQERLElaeqklqqtmRKAETLPEVEAELAQRIAALTKAEErhgNIEERmrhlEGQLEEK----NQELQR-------- 450
Cdd:PRK12704 92 LQKEENLD----------RKLELLEKREEELEKKEKELEQKQQ---ELEKK----EEELEELieeqLQELERisgltaee 154
|
170
....*....|..
gi 333805618 451 ARQR--EKMNEE 460
Cdd:PRK12704 155 AKEIllEKVEEE 166
|
|
| BAR_SNX7 |
cd07666 |
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexin 7; BAR domains are dimerization, lipid ... |
277-468 |
4.37e-03 |
|
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexin 7; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. The specific function of SNX7 is still unknown. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.
Pssm-ID: 153350 Cd Length: 243 Bit Score: 40.27 E-value: 4.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 277 LEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQrDIREAMAQK----EDMEERITTLEKRYLSAQR 352
Cdd:cd07666 14 LTAQAWELSSHKKQGPGLLSRMGQTVKAVASSVRGVKNRPEEFTEMN-EYVEAFSQKinvlDKISQRIYKEQREYFEELK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 353 ESTSIHDMNDKLENELANK--------EAILRQMEEKNRQLQERLE-------LAEQKLQQTMRKAEtlpEVEAELAQRI 417
Cdd:cd07666 93 EYGPIYTLWSASEEELADSlkgmasciDRCCKATDKRMKGLSEQLLpviheyvLYSETLMGVIKRRD---QIQAELDSKV 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 333805618 418 AALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDT 468
Cdd:cd07666 170 EALANKKADRDLLKEEIEKLEDKVECANNALKADWERWKQNMQTDLRSAFT 220
|
|
| COG1579 |
COG1579 |
Predicted nucleic acid-binding protein, contains Zn-ribbon domain [General function ... |
386-533 |
5.68e-03 |
|
Predicted nucleic acid-binding protein, contains Zn-ribbon domain [General function prediction only];
Pssm-ID: 224495 [Multi-domain] Cd Length: 239 Bit Score: 40.04 E-value: 5.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 386 QERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRL 465
Cdd:COG1579 6 LKSLLAIQKLDLEKDRLEPRIKEIRKALKKAKAELEALNKALEALEIELEDLENQVSQLESEIQEIRERIKRAEEKLSAV 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 333805618 466 SDtvdrlltesnerlqlhLKERMAALEEKNVLIQESETFRKNLEESLHDKERLAEEIEKLRSELDQLK 533
Cdd:COG1579 86 KD----------------ERELRALNIEIQIAKERINSLEDELAELMEEIEKLEKEIEDLKERLERLE 137
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
43-682 |
5.83e-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: 40.82 E-value: 5.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 43 DRLLDTLRETQESLSLAQqrLQDVIYDRDSLQRQLnSALPQDIESLTGgLAGSKGADPPEFAALTKELNACREQLLEKE- 121
Cdd:TIGR02169 214 QALLKEKREYEGYELLKE--KEALERQKEAIERQL-ASLEEELEKLTE-EISELEKRLEEIEQLLEELNKKIKDLGEEEq 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 122 ----EEISELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSP--SGVSSEVEVLKALKSLFEHHKALDEKVRERL 195
Cdd:TIGR02169 290 lrvkEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAeiEELEREIEEERKRRDKLTEEYAELKEELEDL 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 196 RVSLErvsALEEELAAANQEIVALREQNVHIQRKMASSEGstesEHLEGMEPGQKVHEkRLSNGSIDSTDETSQIVELQE 275
Cdd:TIGR02169 370 RAELE---EVDKEFAETRDELKDYREKLEKLKREINELKR----ELDRLQEELQRLSE-ELADLNAAIAGIEAKINELEE 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 276 LLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERIT-------------- 341
Cdd:TIGR02169 442 EKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRggraveevlkasiq 521
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 342 ----------TLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEK---------NRQLQERLELAEQKLQQTMRK 402
Cdd:TIGR02169 522 gvhgtvaqlgSVGERYATAIEVAAGNRLNNVVVEDDAVAKEAIELLKRRKagratflplNKMRDERRDLSILSEDGVIGF 601
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 403 AETLPEVEAELA-------------QRIAAltkAEERHGNIeeRMRHLEGQLEEKN---------------------QEL 448
Cdd:TIGR02169 602 AVDLVEFDPKYEpafkyvfgdtlvvEDIEA---ARRLMGKY--RMVTLEGELFEKSgamtggsraprggilfsrsepAEL 676
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 449 QRARQREKMNEEHNKRLSDTVDRLLTESNERLQL--HLKERMAALE-EKNVLIQESETFRKNLEESLHDKERLAEEIEKL 525
Cdd:TIGR02169 677 QRLRERLEGLKRELSSLQSELRRIENRLDELSQElsDASRKIGEIEkEIEQLEQEEEKLKERLEELEEDLSSLEQEIENV 756
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 526 RSELDQLKMRTGSLIEptiprthldTSAELRYSVGSLVDSQSDYRTTKVIRRPRRGRMGVRRDEPKVKSLGDHEWNRTQQ 605
Cdd:TIGR02169 757 KSELKELEARIEELEE---------DLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLE 827
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 606 IGVLSShpfESDTEMSDIDD--DDRETIFSSMDLLSPSGHSDAQTLAMM------LQEQLDAINKEIRLIQEEKESTELR 677
Cdd:TIGR02169 828 KEYLEK---EIQELQEQRIDlkEQIKSIEKEIENLNGKKEELEEELEELeaalrdLESRLGDLKKERDELEAQLRELERK 904
|
....*
gi 333805618 678 AEEIE 682
Cdd:TIGR02169 905 IEELE 909
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
189-487 |
5.87e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 428520 [Multi-domain] Cd Length: 660 Bit Score: 40.87 E-value: 5.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 189 EKVRERLRVSLERVSALEEELAAANQeivALREQNVHIQRKMASSEGSTESEHlegmEPGQKVHEKRLSNGSI-DSTDET 267
Cdd:pfam05557 44 ERESDRNQELQKRIRLLEKREAEAEE---ALREQAELNRLKKKNLEALNKKLN----EKESQLADAREVISCLkNELSEL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 268 SQIVELQEL-LEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEE-------- 338
Cdd:pfam05557 117 RRQIQRQELeLSSTNSELEELQERLDLQKAKAQEAEQLRQNLEAQQSSLAEAEQRIKELEFEIQSQEQDSEIvknsksel 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 339 -RITTLEKRyLSAQRE-----STSIHDmNDKLENELANKEAILRQME---EKNRQLQERLELAEQKLQQ----------T 399
Cdd:pfam05557 197 aRIPELERE-LERLREhnkhlNENIEN-KLLLKEEVEDLKRKLEREEgyrEELATLELEKEKLEQELKSweklaqdtglN 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 400 MRKAETLPEVEAELAQRIAALTkaeERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLltesNER 479
Cdd:pfam05557 275 LRSPEDLSRRIEQLQQREITLK---EENSSLTSSARQLEKAQRELEQELAQYLKNIEDLNKKLKRHKALVRRL----QRR 347
|
....*...
gi 333805618 480 LQLHLKER 487
Cdd:pfam05557 348 VLLLTKER 355
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
362-529 |
6.00e-03 |
|
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: 281941 [Multi-domain] Cd Length: 218 Bit Score: 39.67 E-value: 6.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 362 DKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAEtlPEVEAELAQRIAALTKAEERHG-----------NI 430
Cdd:pfam04012 40 GKARQALAQVIARQKQLERKLEEQKEQAKKLENKARAALTKGN--EELAREALAEIATLEKLAEALEtqltqqrsaveQL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 431 EERMRHLEGQLEEKNQE-------LQRARQREKMNEehnkrlsdTVDRLLTESNERLQLHLKERMAALEEKNVLIQESEt 503
Cdd:pfam04012 118 RKQLAALETKIQQLKAKktalkarLKAAKAQEAVNT--------SLGSASTESATDSFERIEEKIEEREARADAAAELA- 188
|
170 180
....*....|....*....|....*.
gi 333805618 504 FRKNLEESLHDKERLAEEIEKLRSEL 529
Cdd:pfam04012 189 SAQDLDAKLEAAGIQMEVSEDVLARL 214
|
|
| SAM_superfamily |
cd09487 |
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ... |
903-960 |
6.29e-03 |
|
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of approximately 70 amino acids. This domain is found in the Fungi/Metazoa group and in a restricted number of bacteria. Proteins with SAM domains are represented by a wide variety of domain architectures and have different intracellular localization, including nucleus, cytoplasm and membranes. SAM domains have diverse functions. They can interact with proteins, RNAs and membrane lipids, contain site of phosphorylation and/or kinase docking site, and play a role in protein homo and hetero dimerization/oligomerization in processes ranging from signal transduction to regulation of transcription. Mutations in SAM domains have been linked to several diseases.
Pssm-ID: 188886 [Multi-domain] Cd Length: 56 Bit Score: 36.06 E-value: 6.29e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 333805618 903 VVAWLElWLGMPaWYVAACRANVKSGAIMSALSDTEIQrEIGISNPLHRLKLRLAIQE 960
Cdd:cd09487 2 VAEWLE-SLGLE-QYADLFRKNEIDGDALLLLTDEDLK-ELGITSPGHRKKILRAIQR 56
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
178-467 |
6.92e-03 |
|
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: 40.51 E-value: 6.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 178 KSLFEHHKALDEKVRERLRvSLERVSALEEELAAANQEIVALREQNVH--IQRKMASSEGSTESEHLEGMEPGQKVHEKR 255
Cdd:pfam09731 121 KSEQEKEKALEEVLKEAIS-KAESATAVAKEAKDDAIQAVKAHTDSLKeaSDTAEISREKATDSALQKAEALAEKLKEVI 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 256 LSNGSIDSTDETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAE-TARKDLIKTEEM---------------- 318
Cdd:pfam09731 200 NLAKQSEEEAAPPLLDAAPETPPKLPEHLDNVEEKVEKAQSLAKLVDQYKElVASERIVFQQELvsifpdiipvlkednl 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 319 --NTKYQRDIREAMAQKEDMEERITTLEKR-YLSAQRESTSIHDMNDKLENELAnkEAILRQMEEKNRQLQERLELAEQK 395
Cdd:pfam09731 280 lsNDDLNSLIAHAHREIDQLSKKLAELKKReEKHIERALEKQKEELDKLAEELS--ARLEEVRAADEAQLRLEFEREREE 357
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 333805618 396 LQQTMRKaetlpEVEAELAQRIAALTKaeerhgnieermrHLEGQLEEKNQELQRARQR---EKMNEEHNKRLSD 467
Cdd:pfam09731 358 IRESYEE-----KLRTELERQAEAHEE-------------HLKDVLVEQEIELQREFLQdikEKVEEERAGRLLK 414
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
212-427 |
7.97e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 40.38 E-value: 7.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 212 ANQEIVALREQNVHIQRKMAssegsTESEHLEGMEPGQKVHEKRLSNgSIDSTDET-----SQIVELQELL-------EK 279
Cdd:PHA02562 179 LNQQIQTLDMKIDHIQQQIK-----TYNKNIEEQRKKNGENIARKQN-KYDELVEEaktikAEIEELTDELlnlvmdiED 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 280 QNYEMAQMKERLAALSSRVGEVEQEAE---------TARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRYLSA 350
Cdd:PHA02562 253 PSAALNKLNTAAAKIKSKIEQFQKVIKmyekggvcpTCTQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEF 332
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 333805618 351 QRESTSIHDMNDKLENelaNKEAILRqMEEKNRQLQERLELAEqklQQTMRKAETLPEVEAELAQRIAALTK-AEERH 427
Cdd:PHA02562 333 NEQSKKLLELKNKIST---NKQSLIT-LVDKAKKVKAAIEELQ---AEFVDNAEELAKLQDELDKIVKTKSElVKEKY 403
|
|
| SAM_SARM1-like_repeat1 |
cd09501 |
SAM domain ot SARM1-like proteins, repeat 1; SAM (sterile alpha motif) domain repeat 1 of ... |
1021-1065 |
8.71e-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 Cd Length: 69 Bit Score: 36.13 E-value: 8.71e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 333805618 1021 EWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHR 1065
Cdd:cd09501 11 TWLKQIGFEDYAEKFSESQVDGDLLLQLTEDELKQDLGMSSGLLR 55
|
|
| RmuC |
COG1322 |
DNA anti-recombination protein (rearrangement mutator) RmuC [Replication, recombination and ... |
269-423 |
9.22e-03 |
|
DNA anti-recombination protein (rearrangement mutator) RmuC [Replication, recombination and repair];
Pssm-ID: 224241 [Multi-domain] Cd Length: 448 Bit Score: 40.07 E-value: 9.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 269 QIVELQELLEKQNYEMAQMKERLAALSsrvgEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKE----DMEERITTLE 344
Cdd:COG1322 22 QLLLRLGRLEQMLGELAAVLEQLLLLL----AFRAEAEQLRTFARSLQALNLELIQELNELKARLQqqllQSREQLQLLI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 345 KRYLSAQREST-SIHDMNDKLENELA--NKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEV-------EAELA 414
Cdd:COG1322 98 ESLAQLSSEFQeLANEIFEELNRRLAelNQQNLKQLLKPLREVLEKFREQLEQRIHESAEERSTLLEEidrllgeIQQLA 177
|
....*....
gi 333805618 415 QRIAALTKA 423
Cdd:COG1322 178 QEAGNLTAA 186
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
372-541 |
9.25e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.43 E-value: 9.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 372 EAILRQMEEKNRQLQERLELAEQKlqqtmRKAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRA 451
Cdd:PRK03918 138 DAILESDESREKVVRQILGLDDYE-----NAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEI 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 452 RQREKmneehnkRLSDTVDRLltesnERLQLHLKERMAALEEKNVLIQESETFRKNLEESLHDKErlaEEIEKLRSELDQ 531
Cdd:PRK03918 213 SSELP-------ELREELEKL-----EKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELE---ERIEELKKEIEE 277
|
170
....*....|
gi 333805618 532 LKMRTGSLIE 541
Cdd:PRK03918 278 LEEKVKELKE 287
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
392-533 |
9.56e-03 |
|
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.
Pssm-ID: 397124 [Multi-domain] Cd Length: 297 Bit Score: 39.58 E-value: 9.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 392 AEQKLQQTMRKAETlpeVEAELAQRIAALTKAE----ERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSD 467
Cdd:pfam02841 174 AEEVLQEFLKSKEA---VEEAILQTDQALTAKEkaieAERAKAEAAEAEQELLREKQKEEEQMMEAQERSYQEHVKQLIE 250
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 333805618 468 TVdrlltESNERLQLHLKERMAALEEknvliQESETFRKnleeslhdkERLAEEIEKLRSELDQLK 533
Cdd:pfam02841 251 KM-----EAEREQLLAEQERMLEHKL-----QEQEELLK---------EGFKTEAESLQKEIQDLK 297
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
294-533 |
9.61e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 40.00 E-value: 9.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 294 LSSRVGEVEQEAET--ARKDLIKTE-EMNTKYQRDIREAMAQkedmeeRITTLEKRYLSAQRESTSIHDMNDKLENELAN 370
Cdd:PHA02562 172 NKDKIRELNQQIQTldMKIDHIQQQiKTYNKNIEEQRKKNGE------NIARKQNKYDELVEEAKTIKAEIEELTDELLN 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 371 keaILRQMEEKNRQLQE-RLELAEQKLQ-QTMRKAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQEL 448
Cdd:PHA02562 246 ---LVMDIEDPSAALNKlNTAAAKIKSKiEQFQKVIKMYEKGGVCPTCTQQISEGPDRITKIKDKLKELQHSLEKLDTAI 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 449 QRARQREKMNEEHNKRLSDTvdrlltesneRLQLHLKERMAALEEKNVLIQESETfrKNLEESLHDKErlaEEIEKLRSE 528
Cdd:PHA02562 323 DELEEIMDEFNEQSKKLLEL----------KNKISTNKQSLITLVDKAKKVKAAI--EELQAEFVDNA---EELAKLQDE 387
|
....*
gi 333805618 529 LDQLK 533
Cdd:PHA02562 388 LDKIV 392
|
|
| MscK |
COG3264 |
Small-conductance mechanosensitive channel [Cell wall/membrane/envelope biogenesis]; |
273-455 |
9.82e-03 |
|
Small-conductance mechanosensitive channel [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 225803 [Multi-domain] Cd Length: 835 Bit Score: 40.05 E-value: 9.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 273 LQELLEKQ----NYEMAQMKERLAALSSRVGEVEQ-EAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRy 347
Cdd:COG3264 9 LQELLQSRrellTAESAQLEAALQLLQEAVNSKRQeEAEPAAEEAELQAELIQQELAINDQLSQALNQQTERLNALASD- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 348 lsaqrestsihdmNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTmrkaETLPEVEAElaQRIAALTkaEERH 427
Cdd:COG3264 88 -------------DRQLANLLLQLLQSSRTIREQIAVLRGSLLLSRILLQQL----GPLPEAGQP--QEQFEVT--QERD 146
|
170 180 190
....*....|....*....|....*....|....*.
gi 333805618 428 GNIEER--MRHLEGQLEEKNQELQR------ARQRE 455
Cdd:COG3264 147 ALQAEKayINALEGQAEQLTAEVRDildqilDTRRE 182
|
|
|