|
Name |
Accession |
Description |
Interval |
E-value |
| SAM_liprin-alpha1,2,3,4_repeat2 |
cd09565 |
SAM domain of liprin-alpha1,2,3,4 proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 ... |
1066-1131 |
9.52e-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: 149.93 E-value: 9.52e-43
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578821804 1066 MNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRGQLKMVDSFHRNSFQCGIMCLRRL 1131
Cdd:cd09565 1 MNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRTHLKMVDSFHRTSLQYGILCLKRL 66
|
|
| SAM_liprin-alpha1,2,3,4_repeat1 |
cd09562 |
SAM domain of liprin-alpha1,2,3,4 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 ... |
949-1019 |
1.30e-42 |
|
SAM domain of liprin-alpha1,2,3,4 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of liprin-alpha1,2,3,4 proteins is a protein-protein interaction domain. Liprin-alpha proteins contain three copies (repeats) of SAM domain. They may form heterodimers with liprin-beta proteins through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development and in axon guidance; in particular, liprin-alpha is involved in formation of the presynaptic active zone.
Pssm-ID: 188961 Cd Length: 71 Bit Score: 149.64 E-value: 1.30e-42
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578821804 949 FAQWDGPTVVVWLELWVGMPAWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEIMSLT 1019
Cdd:cd09562 1 FALWNGPTVVAWLELWVGMPAWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEMVSLT 71
|
|
| SAM_liprin-alpha1,2,3,4_repeat3 |
cd09568 |
SAM domain of liprin-alpha1,2,3,4 proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 ... |
1151-1222 |
3.10e-42 |
|
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: 148.62 E-value: 3.10e-42
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578821804 1151 DVLVWSNDRVIRWILSIGLKEYANNLIESGVHGALLALDETFDFSALALLLQIPTQNTQARAVLEREFNNLL 1222
Cdd:cd09568 1 DVLVWSNERVIRWVQSIGLREYANNLLESGVHGALIALDETFDANSFALALQIPTQNTQARQILEREFNNLL 72
|
|
| SAM_liprin-kazrin_repeat2 |
cd09495 |
SAM domain of liprin/kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of ... |
1070-1129 |
1.17e-28 |
|
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: 109.55 E-value: 1.17e-28
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 1070 WIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRGQLKMVDSFHRNSFQCGIMCLR 1129
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 ... |
956-1014 |
1.69e-26 |
|
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: 103.07 E-value: 1.69e-26
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 578821804 956 TVVVWLELWVGMPaWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQE 1014
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 ... |
1159-1220 |
2.12e-24 |
|
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: 97.23 E-value: 2.12e-24
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578821804 1159 RVIRWILSIGLKEYANNLIESGVHGALLALDETFDFSALALLLQIPTQNTQARAVLEREFNN 1220
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 ... |
1151-1222 |
7.63e-22 |
|
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: 90.58 E-value: 7.63e-22
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578821804 1151 DVLVWSNDRVIRWILSIGLKEYANNLIESGVHGALLALDETFDFSALALLLQIPTQNTQARAVLEREFNNLL 1222
Cdd:cd09570 1 DPVVWTNQRVIKWARSIDLKEYADNLRDSGVHGALMVLEPSFNSDTMATALGIPSSKNIIRRHLTTEMEALV 72
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
266-548 |
5.37e-18 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 90.38 E-value: 5.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 266 QSQMKERLASLSSHvteleeDLDTARKDLIKSEEMNTKLQRDVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDK 345
Cdd:COG1196 219 KEELKELEAELLLL------KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYE 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 346 LENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKSDLLSSGSSAAKEAKLLELTS 425
Cdd:COG1196 293 LLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 426 KLRKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSESNERLQLHLKERMAALEDKNSLL 505
Cdd:COG1196 373 ELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEA 452
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 578821804 506 REvESAKKQLEETQHDKDQLVLNIEALRAELDHMRLRGASLHH 548
Cdd:COG1196 453 EL-EEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLL 494
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
272-546 |
1.08e-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: 86.26 E-value: 1.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 272 RLASLSSHVTELEEDLDTARKDLIKSEEMNTKLQRDVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIA 351
Cdd:TIGR02168 226 ELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQ 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 352 NKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKsdllssgSSAAKEAKLLELTSKLRKAE 431
Cdd:TIGR02168 306 ILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEA-------ELEELEAELEELESRLEELE 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 432 ERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSESNERLQLHLKERMAALE-DKNSLLREVES 510
Cdd:TIGR02168 379 EQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEeELEELQEELER 458
|
250 260 270
....*....|....*....|....*....|....*.
gi 578821804 511 AKKQLEETQHDKDQLVLNIEALRAELDHMRLRGASL 546
Cdd:TIGR02168 459 LEEALEELREELEEAEQALDAAERELAQLQARLDSL 494
|
|
| SAM_kazrin_repeat1 |
cd09564 |
SAM domain of kazrin proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of kazrin ... |
950-1014 |
2.26e-16 |
|
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: 74.80 E-value: 2.26e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578821804 950 AQWDGPTVVVWLELWVGMPAwYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQE 1014
Cdd:cd09564 2 SRWKADMVLAWLEVVMHMPM-YSKACAENVKSGKVLLGLSDSELESGLGISNVLHRRKLRLAIEE 65
|
|
| SAM_liprin-beta1,2_repeat3 |
cd09569 |
SAM domain of liprin-beta proteins repeat 3; SAM (sterile alpha motif) domain repea t3 of ... |
1151-1222 |
1.30e-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: 72.49 E-value: 1.30e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578821804 1151 DVLVWSNDRVIRWILSIGLKEYANNLIESGVHGALLALDETFDFSALALLLQIPTQNTQARAVLEREFNNLL 1222
Cdd:cd09569 1 EVVLWTNHRVMEWLRSVDLAEYAPNLRGSGVHGALMVLEPRFTAETLAALLNIPPNKTLLRRHLATHFNQLL 72
|
|
| SAM_kazrin_repeat2 |
cd09567 |
SAM domain of kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of kazrin ... |
1065-1129 |
4.06e-15 |
|
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: 70.90 E-value: 4.06e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578821804 1065 DMNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRGQLKMVDSFHRNSFQCGIMCLR 1129
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 ... |
1065-1129 |
5.00e-15 |
|
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: 70.80 E-value: 5.00e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578821804 1065 DMNHEWIgNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRgQLKMVDSFHRNSFQCGIMCLR 1129
Cdd:cd09566 1 KLDTHWV-LRWLDDIGLPQYKDAFSEAKVDGRMLHYLTVDDLL-HLKVTSALHHASIRRGIQVLR 63
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
246-467 |
3.55e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 74.59 E-value: 3.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 246 EEDLAKVIELQEIISKQSREQSQMKERLASLSSHVTELEEDLDTARKDLIKSEEMNTKLQRDVREAMAQKEDMEERITTL 325
Cdd:COG1196 284 EEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEA 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 326 EKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKS 405
Cdd:COG1196 364 EEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEA 443
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578821804 406 DllssgssAAKEAKLLELTSKLRKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEE 467
Cdd:COG1196 444 L-------EEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLE 498
|
|
| SAM_1 |
pfam00536 |
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ... |
1065-1129 |
8.14e-13 |
|
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily conserved protein binding domain that is involved in the regulation of numerous developmental processes in diverse eukaryotes. The SAM domain can potentially function as a protein interaction module through its ability to homo- and heterooligomerise with other SAM domains.
Pssm-ID: 425739 Cd Length: 64 Bit Score: 64.60 E-value: 8.14e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578821804 1065 DMNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRgQLKMVDSFHRNSFQCGIMCLR 1129
Cdd:pfam00536 1 DGWSVEDVGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDDLL-KLGVTLLGHRKKILYAIQRLK 64
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
233-536 |
1.06e-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: 73.18 E-value: 1.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 233 TSGKRSSDG-SLSHEEDLAKVIELQEIISKqsreqsqMKERLASLSSHVTELEEDLDTARKDLIKSEEMNTKLQRDVREA 311
Cdd:TIGR02169 656 TGGSRAPRGgILFSRSEPAELQRLRERLEG-------LKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQL 728
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 312 MAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIAnkdsmhRQTEDKNrQLQERLE-----LAEQKLQQTLRKAE 386
Cdd:TIGR02169 729 EQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIE------ELEEDLH-KLEEALNdlearLSHSRIPEIQAELS 801
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 387 TLPEVEAELAQRVAALSKSDLLSSGSSAAKEAKLLELTSKLRKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNE 466
Cdd:TIGR02169 802 KLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLE 881
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 467 EHNKRLSDTVDKL-------------LSESNERLQLHLKERMAALEDKNSLLREVESAKKQLEE---TQHDKDQLVLNIE 530
Cdd:TIGR02169 882 SRLGDLKKERDELeaqlrelerkieeLEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEipeEELSLEDVQAELQ 961
|
....*.
gi 578821804 531 ALRAEL 536
Cdd:TIGR02169 962 RVEEEI 967
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
45-687 |
1.08e-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: 73.17 E-value: 1.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 45 EERDRLLDTLRETQETLALTQGKLHEVGHERDSLQRQLNTALPQEFAALTKELNvCREQLLEREEEIAELKAE----RNN 120
Cdd:TIGR02168 323 AQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEE-LEEQLETLRSKVAQLELQiaslNNE 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 121 TRLLLEHLECLVSRHER------SLRMTVVKRQAQSPAGVSSEVE-VLKALKSLFEHHKALDEKVRERLRVALERCSLLE 193
Cdd:TIGR02168 402 IERLEARLERLEDRRERlqqeieELLKKLEEAELKELQAELEELEeELEELQEELERLEEALEELREELEEAEQALDAAE 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 194 EELGATHKELMILKEQNNQKKTLTDGVLDINHEQENTPSTSGKRSSdgSLSHEEDLAKVIE------LQEIISKqsREQS 267
Cdd:TIGR02168 482 RELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSE--LISVDEGYEAAIEaalggrLQAVVVE--NLNA 557
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 268 QMKErLASLSSH----VTELEEDLDTAR--------------------KDLIKSEE-----MNTKLQR-----DVREAMA 313
Cdd:TIGR02168 558 AKKA-IAFLKQNelgrVTFLPLDSIKGTeiqgndreilkniegflgvaKDLVKFDPklrkaLSYLLGGvlvvdDLDNALE 636
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 314 Q--KEDMEERITTLE-----KRYLAA-QREATSVHDLNdkLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKA 385
Cdd:TIGR02168 637 LakKLRPGYRIVTLDgdlvrPGGVITgGSAKTNSSILE--RRREIEELEEKIEELEEKIAELEKALAELRKELEELEEEL 714
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 386 ETLPEVEAELAQRVAALSKSdllssgssaakeakLLELTSKLRKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMN 465
Cdd:TIGR02168 715 EQLRKELEELSRQISALRKD--------------LARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEA 780
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 466 EEHNKRLSDTVDKL----------LSESNERLQLHLKERMAALEDKNSLLREVESAKKQLEETQHDKDQLVLNIEALRAE 535
Cdd:TIGR02168 781 EAEIEELEAQIEQLkeelkalreaLDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAE 860
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 536 LDHMRLRGASLHHGRPHLGSVPDFRFPMADGHTDSYSTSAVLRRPQKGRLAALRDEPSKVQTLNEQDWERAQQASV-LAN 614
Cdd:TIGR02168 861 IEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVrIDN 940
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578821804 615 VAQAFESDAdvSDGEDDRDTLLSSVDLLSPSGQADAHTLAMMLQE----QLDAInkeirliqEEKENTEQRAEEIES 687
Cdd:TIGR02168 941 LQERLSEEY--SLTLEEAEALENKIEDDEEEARRRLKRLENKIKElgpvNLAAI--------EEYEELKERYDFLTA 1007
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
192-490 |
5.29e-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: 70.86 E-value: 5.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 192 LEEELGATHKELMI--LKEQNNQKKTLTDGVLDINHEQENTPST--------SGKRSSDGSLSHEEDLA--KVIELQEII 259
Cdd:TIGR02168 218 LKAELRELELALLVlrLEELREELEELQEELKEAEEELEELTAElqeleeklEELRLEVSELEEEIEELqkELYALANEI 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 260 SKQSREQSQMKERLASLSSHVTELEEDLDTARKDLIKSEEMNTKLQRDVREAMAQKEDMEERITTLEKRYLAAQREATSV 339
Cdd:TIGR02168 298 SRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEEL 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 340 HDLNDKLENEIAnkdsmhrQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKSDLlsSGSSAAKEAK 419
Cdd:TIGR02168 378 EEQLETLRSKVA-------QLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKEL--QAELEELEEE 448
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578821804 420 LLELTSKLRKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSESNERLQLH 490
Cdd:TIGR02168 449 LEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLS 519
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
305-517 |
2.08e-11 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 67.48 E-value: 2.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 305 QRDVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRK 384
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 385 AETLpevEAELAQRVAALSKS------DLLSSGSSAAKEAKLLELTSKLrkAEERHGNIEE------RLRQMEAQLEEKN 452
Cdd:COG4942 99 LEAQ---KEELAELLRALYRLgrqpplALLLSPEDFLDAVRRLQYLKYL--APARREQAEElradlaELAALRAELEAER 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578821804 453 QELQRARQREKMNEEHNKRLSDTVDKLLSESNERLQLHLKERMAALEDKNSLLREVESAKKQLEE 517
Cdd:COG4942 174 AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
74-488 |
2.35e-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: 68.54 E-value: 2.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 74 ERDSLQRQLNtALPQEFAALTKELNVCREQLLEREEEIAELKAERNNTRLLLEHLECLVSRHERSLRmTVVKRQAQSPAG 153
Cdd:TIGR02168 678 EIEELEEKIE-ELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVE-QLEERIAQLSKE 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 154 VSS----EVEVLKALKSLFEHHKALDEK---VRERLRVALERCSLLEEELGATHKELMILK-EQNNQKKTLTdgvldinh 225
Cdd:TIGR02168 756 LTEleaeIEELEERLEEAEEELAEAEAEieeLEAQIEQLKEELKALREALDELRAELTLLNeEAANLRERLE-------- 827
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 226 eqentpstsgkrssdgslSHEEDLAKVIELQEIISKQSReqsQMKERLASLSSHVTELEEDLDTARKDLIKSEEMNTKLQ 305
Cdd:TIGR02168 828 ------------------SLERRIAATERRLEDLEEQIE---ELSEDIESLAAEIEELEELIEELESELEALLNERASLE 886
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 306 RDVREAMAQKEDMEERITTLEKRYLAAQREAtsvHDLNDKLEneiankdsmhrqtedknrQLQERLELAEQKLQQTLRKA 385
Cdd:TIGR02168 887 EALALLRSELEELSEELRELESKRSELRREL---EELREKLA------------------QLELRLEGLEVRIDNLQERL 945
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 386 ETLPEVEAELAQRVAALSKSDllssgsSAAKEAKLLELTSKLRK-------AEERHGNIEERLRQMEAQLEeknqELQRA 458
Cdd:TIGR02168 946 SEEYSLTLEEAEALENKIEDD------EEEARRRLKRLENKIKElgpvnlaAIEEYEELKERYDFLTAQKE----DLTEA 1015
|
410 420 430
....*....|....*....|....*....|....*
gi 578821804 459 RQR-----EKMNEEHNKRLSDTVDKLlsesNERLQ 488
Cdd:TIGR02168 1016 KETleeaiEEIDREARERFKDTFDQV----NENFQ 1046
|
|
| SAM_liprin-beta1,2_repeat1 |
cd09563 |
SAM domain of liprin-beta1,2 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of ... |
949-1013 |
4.13e-11 |
|
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: 59.55 E-value: 4.13e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578821804 949 FAQWDGPTVVVWL-ELWVGMpawYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQ 1013
Cdd:cd09563 1 FAEWSTEQVCDWLaELGLGQ---YVDECRRWVKSGQTLLKASPQELEKELGIKHPLHRKKLQLALQ 63
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
54-402 |
2.88e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 65.08 E-value: 2.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 54 LRETQETLALTQGKLHEVGHERDSLQRQLNTAlpQEFAALTKELNvcREQLLEREEEIAELKAERNNTRLLLEHLECLVS 133
Cdd:TIGR02168 181 LERTRENLDRLEDILNELERQLKSLERQAEKA--ERYKELKAELR--ELELALLVLRLEELREELEELQEELKEAEEELE 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 134 RHERSlrmtvvkrqaqspagvssevevLKALKSLFEHHKALDEKVRERLRVALERCSLLEEELGATHKELMILKEQNNQk 213
Cdd:TIGR02168 257 ELTAE----------------------LQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLAN- 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 214 ktltdgvLDINHEQENTPSTSGKRSSDGSLSHEEDLAKVI-ELQEIISKQSREQSQMKERLASLSSHVTELEEDLDTARK 292
Cdd:TIGR02168 314 -------LERQLEELEAQLEELESKLDELAEELAELEEKLeELKEELESLEAELEELEAELEELESRLEELEEQLETLRS 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 293 DLIKSEEMNTKLQRDVREAMAQKEDMEERITTLEKRYLAAQREATSVHdlNDKLENEIANKDSMHRQTEDKNRQLQERLE 372
Cdd:TIGR02168 387 KVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAE--LKELQAELEELEEELEELQEELERLEEALE 464
|
330 340 350
....*....|....*....|....*....|
gi 578821804 373 LAEQKLQQTLRKAETLPEVEAELAQRVAAL 402
Cdd:TIGR02168 465 ELREELEEAEQALDAAERELAQLQARLDSL 494
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
45-517 |
1.12e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 63.03 E-value: 1.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 45 EERDRLLDTLRETQETLALTQGKLHEVGHERDSLQRQLNTALPQEFAALTKELNVCREQLLEREEEIAELKAERNNTRLL 124
Cdd:COG1196 323 EELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQL 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 125 LEHLECLVSRHERSLRMTVVKRQAQSpagvssevEVLKALKSLFEHHKALDEKVRERLRVALERCSLLEEELGATHKELM 204
Cdd:COG1196 403 EELEEAEEALLERLERLEEELEELEE--------ALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAAL 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 205 ILKEQNNQKKTLTDGVLDINHEQENTPSTSGKRSSDGSLSHEEDLAKVI-ELQEIISKQSREQSQMKERLASLSSH-VTE 282
Cdd:COG1196 475 LEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAgAVAVLIGVEAAYEAALEAALAAALQNiVVE 554
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 283 LEEDLDTARKDLikseemntKLQRDVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIANKDsmhRQTED 362
Cdd:COG1196 555 DDEVAAAAIEYL--------KAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVL---GDTLL 623
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 363 KNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKSDLLSSGSSAAKEAKLLELTSKLRKAEERHGNIEERLR 442
Cdd:COG1196 624 GRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEE 703
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578821804 443 QMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSESNERLQLHLKERMAALEDKNSLLREVESAKKQLEE 517
Cdd:COG1196 704 EEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEA 778
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
152-537 |
1.42e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 62.77 E-value: 1.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 152 AGVSSEVEVLKALKSLFEHHKALDEKVRERLRVALERCSLLEEELGATHKELMILKEQNNQKKTL---TDGVLDINHEQE 228
Cdd:PRK03918 224 EKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELkekAEEYIKLSEFYE 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 229 NTpstsgkrsSDGSLSHEEDLAKVIELQEIISKQSREQSQMKERLASLSSHVTELEEDLDTARKDLIKSEEMNTKLQR-- 306
Cdd:PRK03918 304 EY--------LDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEEle 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 307 --DVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIAN-KDSMHRQTEDK------NRQLQE--RLELAE 375
Cdd:PRK03918 376 rlKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKElKKAIEELKKAKgkcpvcGRELTEehRKELLE 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 376 Q------KLQQTLRKA-ETLPEVEAELAQRVAALSKSDLLSSGSSAAKEAKLLE--LTS----KLRKAEERHGNIEERLR 442
Cdd:PRK03918 456 EytaelkRIEKELKEIeEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEekLKKynleELEKKAEEYEKLKEKLI 535
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 443 QMEAQLEEKNQELQRARQREKMNEEHNKRLsDTVDKLLSESNERLQL-------HLKERMAALEDKNSLLREVESAKKQL 515
Cdd:PRK03918 536 KLKGEIKSLKKELEKLEELKKKLAELEKKL-DELEEELAELLKELEElgfesveELEERLKELEPFYNEYLELKDAEKEL 614
|
410 420
....*....|....*....|..
gi 578821804 516 EETQHDKDQLVLNIEALRAELD 537
Cdd:PRK03918 615 EREEKELKKLEEELDKAFEELA 636
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
158-525 |
2.25e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 61.98 E-value: 2.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 158 VEVLKALKSLFEHHkaldEKVRERLRVALERCSLLEEELGATHKELMILKEQnnqKKTLTDGVLDINHEQENTPSTSGKR 237
Cdd:PRK02224 233 RETRDEADEVLEEH----EERREELETLEAEIEDLRETIAETEREREELAEE---VRDLRERLEELEEERDDLLAEAGLD 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 238 SSDGS--LSHEEDLAKVI-ELQEIISKQSREQSQMKERLASLSSHVTELEEDLDTARKDLIKSEEMNTKLQRDVREAMAQ 314
Cdd:PRK02224 306 DADAEavEARREELEDRDeELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREE 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 315 KEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQ--------QTLRK-- 384
Cdd:PRK02224 386 IEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEagkcpecgQPVEGsp 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 385 -AETLPEVE---AELAQRVAAL-SKSDLLSSGSSAAKEAKllELTSKLRKAEERHGNIEERLRQMEAQLEEKNQELQRAR 459
Cdd:PRK02224 466 hVETIEEDRervEELEAELEDLeEEVEEVEERLERAEDLV--EAEDRIERLEERREDLEELIAERRETIEEKRERAEELR 543
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578821804 460 ------------QREKMNEEHNKrlSDTVDKLLSESNERLQlHLKERMAALEDKNSLLREVESAKKQLEETQHDKDQL 525
Cdd:PRK02224 544 eraaeleaeaeeKREAAAEAEEE--AEEAREEVAELNSKLA-ELKERIESLERIRTLLAAIADAEDEIERLREKREAL 618
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
44-537 |
2.89e-09 |
|
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: 61.91 E-value: 2.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 44 LEERDRLLDTLR-ETQETLALTQGKLHEVGHERDSLQRQLNTALPQEFAALTKELNVCREQLLEREEEIAELKAERNNTR 122
Cdd:TIGR00618 417 SAFRDLQGQLAHaKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARL 496
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 123 LLLEHLECLVSRHERSLRMTVVkrQAQSPAGVSSEVEvlkALKSLFEHHKALDEKVRERLRVALERCSLLEEELGATHKE 202
Cdd:TIGR00618 497 LELQEEPCPLCGSCIHPNPARQ--DIDNPGPLTRRMQ---RGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQS 571
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 203 LMILKEQNNQKKTLTDGVLDINHE-QENTPSTSGKRSSDGSLSHEEDLakviELQEIISKQ--SREQSQMKERLASLSSH 279
Cdd:TIGR00618 572 FSILTQCDNRSKEDIPNLQNITVRlQDLTEKLSEAEDMLACEQHALLR----KLQPEQDLQdvRLHLQQCSQELALKLTA 647
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 280 VTELEEDLdtarkdlikseemntkLQRDVREAMAQKEDMEERitTLEKRYLAAQREATSVHDLNDKLEnEIANKDSMHR- 358
Cdd:TIGR00618 648 LHALQLTL----------------TQERVREHALSIRVLPKE--LLASRQLALQKMQSEKEQLTYWKE-MLAQCQTLLRe 708
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 359 --QTEDKNRQLQERLELAEQKLQQTLR-KAETLPEVEAEL-AQRVAALSKSDLlssgssaAKEAKLLELTSKLRKAEErh 434
Cdd:TIGR00618 709 leTHIEEYDREFNEIENASSSLGSDLAaREDALNQSLKELmHQARTVLKARTE-------AHFNNNEEVTAALQTGAE-- 779
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 435 gnieerLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSESNERLQLHLKERMAALEDKNSLLREVESAKKQ 514
Cdd:TIGR00618 780 ------LSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLK 853
|
490 500
....*....|....*....|...
gi 578821804 515 LEETQHDKDQLVLNIEALRAELD 537
Cdd:TIGR00618 854 YEECSKQLAQLTQEQAKIIQLSD 876
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
249-534 |
4.57e-09 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 61.13 E-value: 4.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 249 LAKVIE---LQEIISKQSREQSQMKERLASLSSHVTELEEDLDTARKDLIKSEEmntklqrDVREAMAQKEDMEERITTL 325
Cdd:PRK04863 337 LNLVQTalrQQEKIERYQADLEELEERLEEQNEVVEEADEQQEENEARAEAAEE-------EVDELKSQLADYQQALDVQ 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 326 EKR---YLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTlRKAETLPEVEAELAQRVAA- 401
Cdd:PRK04863 410 QTRaiqYQQAVQALERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVA-QAAHSQFEQAYQLVRKIAGe 488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 402 LSKSDllssgssAAKEAKlleltSKLRKAEErHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDklls 481
Cdd:PRK04863 489 VSRSE-------AWDVAR-----ELLRRLRE-QRHLAEQLQQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLD---- 551
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 578821804 482 eSNERLQLHLKERMAALEDKNSllrEVESAKKQLEETQHDKDQLVLNIEALRA 534
Cdd:PRK04863 552 -DEDELEQLQEELEARLESLSE---SVSEARERRMALRQQLEQLQARIQRLAA 600
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
285-546 |
4.95e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 60.85 E-value: 4.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 285 EDLDTARKDLIKSEEMNTKLQRDVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTED-- 362
Cdd:PRK03918 158 DDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEElk 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 363 --------KNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKSDLLSSGSSAAKEAKLlELTSKLRKAEERH 434
Cdd:PRK03918 238 eeieelekELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYE-EYLDELREIEKRL 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 435 GNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDtvdklLSESNERLQ--LHLKERMAALEDKNSLLrEVESAK 512
Cdd:PRK03918 317 SRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEE-----LEERHELYEeaKAKKEELERLKKRLTGL-TPEKLE 390
|
250 260 270
....*....|....*....|....*....|....
gi 578821804 513 KQLEETQHDKDQLVLNIEALRAELDHMRLRGASL 546
Cdd:PRK03918 391 KELEELEKAKEEIEEEISKITARIGELKKEIKEL 424
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
246-450 |
5.68e-09 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 58.01 E-value: 5.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 246 EEDLAKVIELQEIISkqsrEQSQMKERLASLSSHVTELEEDLDTARKDLIKSEEMNTKLQRDVREAMAQKEDMEERITTL 325
Cdd:COG1579 3 PEDLRALLDLQELDS----ELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 326 EKRylaaQREATSVHDLNDkLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQqtlrkaetlpEVEAELAQRVAALsks 405
Cdd:COG1579 79 EEQ----LGNVRNNKEYEA-LQKEIESLKRRISDLEDEILELMERIEELEEELA----------ELEAELAELEAEL--- 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 578821804 406 dllssgssAAKEAKLLELTSKLRKAEERhgnIEERLRQMEAQLEE 450
Cdd:COG1579 141 --------EEKKAELDEELAELEAELEE---LEAEREELAAKIPP 174
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
256-486 |
7.77e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 59.39 E-value: 7.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 256 QEIISKQSREQSQMKERLASLSSHVTELEEDLDTARKDLIKSEEMNTKLQRDVREAMAQKEDMEERITTLEKRYLAAQRE 335
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 336 AtsvhdlnDKLENEIANkdsMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKSDLLSSGSSAA 415
Cdd:COG4942 99 L-------EAQKEELAE---LLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAE 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578821804 416 KEAKLLELTSKLRKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSESNER 486
Cdd:COG4942 169 LEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
268-521 |
1.22e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 59.97 E-value: 1.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 268 QMKERLASLSSHVTELEEDLDTARKDLIKSEEMNTKLQRDVREAMA-QKEDMEERITTLEKRYLAAQREATSVhDLNDKL 346
Cdd:PRK04863 841 QLNRRRVELERALADHESQEQQQRSQLEQAKEGLSALNRLLPRLNLlADETLADRVEEIREQLDEAEEAKRFV-QQHGNA 919
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 347 ENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLpeveAELAQRVAALSKSDllsSGSSAAKEAKLLE-LTS 425
Cdd:PRK04863 920 LAQLEPIVSVLQSDPEQFEQLKQDYQQAQQTQRDAKQQAFAL----TEVVQRRAHFSYED---AAEMLAKNSDLNEkLRQ 992
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 426 KLRKAEERHGNIEERLRQMEAQLEEKNQ---ELQRARQR-EKMNEEHNKRLSDTVDKLLSESNERLQLHLKERMAAL--- 498
Cdd:PRK04863 993 RLEQAEQERTRAREQLRQAQAQLAQYNQvlaSLKSSYDAkRQMLQELKQELQDLGVPADSGAEERARARRDELHARLsan 1072
|
250 260 270
....*....|....*....|....*....|.
gi 578821804 499 -EDKNSLLR-------EVESAKKQLEETQHD 521
Cdd:PRK04863 1073 rSRRNQLEKqltfceaEMDNLTKKLRKLERD 1103
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
68-680 |
1.29e-08 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 59.75 E-value: 1.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 68 LHEVGHERDSLQRQLNTA-----------------LPQEFAALTKELNVCREQLLEREEEIAELKAERNNTRLLLEHLEC 130
Cdd:pfam15921 80 LEEYSHQVKDLQRRLNESnelhekqkfylrqsvidLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEAAKC 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 131 LVSR--HERSLRMTVVKRQAQSPAGVSSEVEVL------KALKSLFEHH-------KALDEKVRERLRVALERCSLLEEE 195
Cdd:pfam15921 160 LKEDmlEDSNTQIEQLRKMMLSHEGVLQEIRSIlvdfeeASGKKIYEHDsmstmhfRSLGSAISKILRELDTEISYLKGR 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 196 LGATHKELMILKEQNNQKKTL-----TDGV--LDINHEQENTPST---SGKRSSDGSLSHEedlakvielQEIISKQSRE 265
Cdd:pfam15921 240 IFPVEDQLEALKSESQNKIELllqqhQDRIeqLISEHEVEITGLTekaSSARSQANSIQSQ---------LEIIQEQARN 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 266 QSQMKER-LASLSSHVTELEEDLDTARKD-------------LIKSEEMNTKLQRD--VREAMAQKEDMEERITTLEKRY 329
Cdd:pfam15921 311 QNSMYMRqLSDLESTVSQLRSELREAKRMyedkieelekqlvLANSELTEARTERDqfSQESGNLDDQLQKLLADLHKRE 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 330 LAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQeRLELAEQKLqqtlrKAETLPEVEAELAQ---RVAALSKSD 406
Cdd:pfam15921 391 KELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQ-RLEALLKAM-----KSECQGQMERQMAAiqgKNESLEKVS 464
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 407 LLSSGSSAAKEA--KLLE-LTSK---LRKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLL 480
Cdd:pfam15921 465 SLTAQLESTKEMlrKVVEeLTAKkmtLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLR 544
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 481 SESNE----RLQLHLKERM-----------------------AALEDKNSLLREVESAKKQLEETQHDKDQLVLNIEALR 533
Cdd:pfam15921 545 NVQTEcealKLQMAEKDKVieilrqqienmtqlvgqhgrtagAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELE 624
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 534 AELDHMRLRGASL-HHGRPHLGSVPDF---RFPMADGHTDSYSTSAVLRRPQKGRLAALRDEPSKVQ-TLNEQDWERAQQ 608
Cdd:pfam15921 625 ARVSDLELEKVKLvNAGSERLRAVKDIkqeRDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMEtTTNKLKMQLKSA 704
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578821804 609 ASVLANVAQAFESdADVSDGEDDRDTLLSSVDLLSPSGQADA-HTLAMMLQEQLDAINKEIRLIQEEKENTEQ 680
Cdd:pfam15921 705 QSELEQTRNTLKS-MEGSDGHAMKVAMGMQKQITAKRGQIDAlQSKIQFLEEAMTNANKEKHFLKEEKNKLSQ 776
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
45-525 |
1.44e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.57 E-value: 1.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 45 EERDRLLDTLRETQETLALTQGKLHEVGHERDSLQRQLNtALPQEFAALTKELNVCREQLLEREEEIAELKAERNNTRLL 124
Cdd:COG1196 274 LELEELELELEEAQAEEYELLAELARLEQDIARLEERRR-ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEE 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 125 LEHLECLVSRHERSLRMTVVKRQAQSPAGVSSEVEVLKALKSLFEHHKALDEKVRERLRVALERCSLLEEELGATHKELM 204
Cdd:COG1196 353 LEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAE 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 205 ILKEQNNQKKTLTDGVLDINHEQENTPSTSGKRSSDGSLSHEEDLAKVIELQEIISKQSRE--QSQMKERLASLSSHVTE 282
Cdd:COG1196 433 LEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLllLLEAEADYEGFLEGVKA 512
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 283 LEEDLDTARKDLIKSEEMNTK--------------LQRDVREAMAQ--------KEDMEERITTLEKRyLAAQREATSVH 340
Cdd:COG1196 513 ALLLAGLRGLAGAVAVLIGVEaayeaaleaalaaaLQNIVVEDDEVaaaaieylKAAKAGRATFLPLD-KIRARAALAAA 591
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 341 DLNDKLENEIANKDSMHRQTEDKNRQLQERLE---LAEQKLQQTLRKAETLPEVEAELAQRVAALSKSDLLSSGSSAAKE 417
Cdd:COG1196 592 LARGAIGAAVDLVASDLREADARYYVLGDTLLgrtLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELL 671
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 418 AKLLELTSKLRKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSESNERLQLHLKERMAA 497
Cdd:COG1196 672 AALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEE 751
|
490 500
....*....|....*....|....*...
gi 578821804 498 LEDKNSLLREVESAKKQLEETQHDKDQL 525
Cdd:COG1196 752 ALEELPEPPDLEELERELERLEREIEAL 779
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
37-540 |
2.06e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.92 E-value: 2.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 37 EQLMVSMLEERDRLLDTLRETQETLALTQGKLHEVGHERDSLqrqlnTALPQEFAALTKELNVCREQLLEREEEIAELKA 116
Cdd:PRK03918 199 EKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEI-----EELEKELESLEGSKRKLEEKIRELEERIEELKK 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 117 ERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSpagVSSEVEvlKALKSLFEHHKALDEKVRErLRVALERCSLLEEEL 196
Cdd:PRK03918 274 EIEELEEKVKELKELKEKAEEYIKLSEFYEEYLD---ELREIE--KRLSRLEEEINGIEERIKE-LEEKEERLEELKKKL 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 197 GATHKELMILKEqnnqKKTLTDGVLDINHEQENTPSTSGKRSSDGSLSHEEDLAKV-IELQEIISKQSREQSQMKERLAS 275
Cdd:PRK03918 348 KELEKRLEELEE----RHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAkEEIEEEISKITARIGELKKEIKE 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 276 LSSHVTELE-----------EDLDTARKDLIK--SEEMNtKLQRDVREAMAQKEDMEERITTLEKrYLAAQREATSVHDL 342
Cdd:PRK03918 424 LKKAIEELKkakgkcpvcgrELTEEHRKELLEeyTAELK-RIEKELKEIEEKERKLRKELRELEK-VLKKESELIKLKEL 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 343 NDKLENeiankdsmhrqtedknrqLQERLE-LAEQKLQQTLRKAETLPEVEAELAQRVAALsKSDLlssGSSAAKEAKLL 421
Cdd:PRK03918 502 AEQLKE------------------LEEKLKkYNLEELEKKAEEYEKLKEKLIKLKGEIKSL-KKEL---EKLEELKKKLA 559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 422 ELTSKLRKAEERHGNIEERLRQM----EAQLEEKNQELQR----------ARQREKMNEEHNKRLSDTVDKL---LSESN 484
Cdd:PRK03918 560 ELEKKLDELEEELAELLKELEELgfesVEELEERLKELEPfyneylelkdAEKELEREEKELKKLEEELDKAfeeLAETE 639
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578821804 485 ERLQlHLKERMAALEDKNS-------------LLREVESAKKQLEETQHDKDQLVLNIEALRAELDHMR 540
Cdd:PRK03918 640 KRLE-ELRKELEELEKKYSeeeyeelreeyleLSRELAGLRAELEELEKRREEIKKTLEKLKEELEERE 707
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
38-533 |
2.98e-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: 58.52 E-value: 2.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 38 QLMVSMLEERDRLLDTLRETQETLALTQGKLHEVGHER--DSLQRQLNTALPQEFAALTKELNVCREQLLEREEEIAELK 115
Cdd:TIGR00606 353 QLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERqiKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIR 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 116 AERNNTRLLLEHLECLVSRHERSLRMtvVKRQAQSPAGVSSEV-----EVLKALK--SLFEHHKALDEKVRERLRVALER 188
Cdd:TIGR00606 433 DEKKGLGRTIELKKEILEKKQEELKF--VIKELQQLEGSSDRIleldqELRKAERelSKAEKNSLTETLKKEVKSLQNEK 510
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 189 CSLLEE--ELGATHKELMILKEQNNQKKTLTDGVLDINHEQENTPStsgkRSSDGSLSHEEDLAKVIELQEIISKQSREQ 266
Cdd:TIGR00606 511 ADLDRKlrKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKS----RHSDELTSLLGYFPNKKQLEDWLHSKSKEI 586
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 267 SQMKERLASLSSHVTELEEDLDTARKDLIKSEEMNTKLQRDVREAMAQkEDMEERITTLEKRYLAAQREA---TSVHDLN 343
Cdd:TIGR00606 587 NQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGS-QDEESDLERLKEEIEKSSKQRamlAGATAVY 665
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 344 DKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAET-LPEVEAELAQrvaalsksdllssgssaaKEAKLLE 422
Cdd:TIGR00606 666 SQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDkLKSTESELKK------------------KEKRRDE 727
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 423 LtskLRKAEERHGNIEERLRQMEaQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSESN---------ERLQLHLKE 493
Cdd:TIGR00606 728 M---LGLAPGRQSIIDLKEKEIP-ELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKvcltdvtimERFQMELKD 803
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 578821804 494 ------RMAALEDKNSLLREVESAKKQLEETQHDKDQLVLNIEALR 533
Cdd:TIGR00606 804 verkiaQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNR 849
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
254-540 |
4.19e-08 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 57.88 E-value: 4.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 254 ELQEIISKQSREQSQMKE---RLASLSSHVTELEEDLDTARKDLIKSEemntKLQRDVREAM-AQKEDMEERI-TTLEKR 328
Cdd:pfam01576 244 ELQAALARLEEETAQKNNalkKIRELEAQISELQEDLESERAARNKAE----KQRRDLGEELeALKTELEDTLdTTAAQQ 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 329 YLAAQREaTSVHDLNDKLENEIANKDSMHRQTEDKNRQ----LQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSK 404
Cdd:pfam01576 320 ELRSKRE-QEVTELKKALEEETRSHEAQLQEMRQKHTQaleeLTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQ 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 405 SDLLSSGSSAAKEAKLLELTSKLRKAEERHGNIEERLRQMEAQLEEKNQELQRArqrEKMNEEHNKRLSdTVDKLLSESN 484
Cdd:pfam01576 399 AKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEA---EGKNIKLSKDVS-SLESQLQDTQ 474
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578821804 485 ERLQ------LHLKERMAALEDKNSLLREvesakkQLEETQHDKDQLVLNIEALRAELDHMR 540
Cdd:pfam01576 475 ELLQeetrqkLNLSTRLRQLEDERNSLQE------QLEEEEEAKRNVERQLSTLQAQLSDMK 530
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
254-526 |
5.12e-08 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 57.65 E-value: 5.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 254 ELQEIiskqSREQSQMKERLASLSSHVTELEEDLDTARKDLikseemnTKLQRDVREAMA-QKEDMEERITTLEKRYLAA 332
Cdd:COG3096 837 ELAAL----RQRRSELERELAQHRAQEQQLRQQLDQLKEQL-------QLLNKLLPQANLlADETLADRLEELREELDAA 905
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 333 QREATSVHDLNDKLEnEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLpeveAELAQRVAALSKSDL--LSS 410
Cdd:COG3096 906 QEAQAFIQQHGKALA-QLEPLVAVLQSDPEQFEQLQADYLQAKEQQRRLKQQIFAL----SEVVQRRPHFSYEDAvgLLG 980
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 411 GSSAAKEAklleLTSKLRKAEERHGNIEERLRQMEAQLEEKNQELQ----RARQREKMNEEHNKRLSDTVDKLLSESNER 486
Cdd:COG3096 981 ENSDLNEK----LRARLEQAEEARREAREQLRQAQAQYSQYNQVLAslksSRDAKQQTLQELEQELEELGVQADAEAEER 1056
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 578821804 487 LQLHLKERMAALEDKNSLLREVEsakKQLEETQHDKDQLV 526
Cdd:COG3096 1057 ARIRRDELHEELSQNRSRRSQLE---KQLTRCEAEMDSLQ 1093
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
257-462 |
5.99e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 57.39 E-value: 5.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 257 EIISKQSREQSQMKERLASLSSHVTELEEDLDTARKDLIKSEEMNTKLQRDVREAMAQKEDMEERITTLEKRYLAAQREA 336
Cdd:TIGR02169 280 KIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEY 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 337 TSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELA----------EQKLQQTLRKA---------------ETLPEV 391
Cdd:TIGR02169 360 AELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLkreinelkreLDRLQEELQRLseeladlnaaiagieAKINEL 439
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578821804 392 EAELAQRVAALSKSDLLSSGSSAAK---EAKLLELTSKLRKaeerhgnIEERLRQMEAQLEEKNQELQRARQRE 462
Cdd:TIGR02169 440 EEEKEDKALEIKKQEWKLEQLAADLskyEQELYDLKEEYDR-------VEKELSKLQRELAEAEAQARASEERV 506
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
282-475 |
7.31e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 56.70 E-value: 7.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 282 ELEEDLD-----TARKDLIKSEEMNtKLQRDVREAMAQKED---MEERITTLEKRYLAAQREATSVHDLNDKLENEIANK 353
Cdd:COG4717 50 RLEKEADelfkpQGRKPELNLKELK-ELEEELKEAEEKEEEyaeLQEELEELEEELEELEAELEELREELEKLEKLLQLL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 354 DSMHRQTEDKNR--QLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALsksDLLSSGSSAAKEAKLLELTSKLRKAE 431
Cdd:COG4717 129 PLYQELEALEAElaELPERLEELEERLEELRELEEELEELEAELAELQEEL---EELLEQLSLATEEELQDLAEELEELQ 205
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 578821804 432 ERHGNIEERLRQMEAQLEEKNQELQRArQREKMNEEHNKRLSDT 475
Cdd:COG4717 206 QRLAELEEELEEAQEELEELEEELEQL-ENELEAAALEERLKEA 248
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
32-560 |
8.08e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.85 E-value: 8.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 32 ADSHFEQLMVSMLEER-DRLLDTLRETQETLALTQGKLHEVGHERDSLQRQLNTA-------LPQEFAALTKELNVCREQ 103
Cdd:COG4913 281 LRLWFAQRRLELLEAElEELRAELARLEAELERLEARLDALREELDELEAQIRGNggdrleqLEREIERLERELEERERR 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 104 LLEREEEIA-----------ELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSP--AGVSSEVEVLKALKSLFEH 170
Cdd:COG4913 361 RARLEALLAalglplpasaeEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRelRELEAEIASLERRKSNIPA 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 171 HkalDEKVRERLRvalERCSLLEEEL---GathkELMILKEQ------------NNQKKTL------------------T 217
Cdd:COG4913 441 R---LLALRDALA---EALGLDEAELpfvG----ELIEVRPEeerwrgaiervlGGFALTLlvppehyaaalrwvnrlhL 510
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 218 DGVLDINHEQENTPSTSGKRSSDGSLSHeedlakvielqEIISKQSREQSQMKERLASLSSHVT-ELEEDLDTARKD--- 293
Cdd:COG4913 511 RGRLVYERVRTGLPDPERPRLDPDSLAG-----------KLDFKPHPFRAWLEAELGRRFDYVCvDSPEELRRHPRAitr 579
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 294 --LIKSEemNTKLQRDVREAMAQK----EDMEERITTLEKRYLAAQREATSVHDLNDKLENEIankdsmhrqtedknRQL 367
Cdd:COG4913 580 agQVKGN--GTRHEKDDRRRIRSRyvlgFDNRAKLAALEAELAELEEELAEAEERLEALEAEL--------------DAL 643
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 368 QERLElAEQKLQQTLRKAETLPEVEAELAQRVAALSKsdlLSSGSSaakeaKLLELTSKLRKAEERHGNIEERLRQMEAQ 447
Cdd:COG4913 644 QERRE-ALQRLAEYSWDEIDVASAEREIAELEAELER---LDASSD-----DLAALEEQLEELEAELEELEEELDELKGE 714
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 448 LEEKNQELQRARQREkmneehnKRLSDTVDKLLSESNERLQLHLKERMAALEDKNSLLREVESAKKQLEETQHDKDQLVL 527
Cdd:COG4913 715 IGRLEKELEQAEEEL-------DELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEE 787
|
570 580 590
....*....|....*....|....*....|...
gi 578821804 528 NIEALRAEldHMRLRGASLHHGRPHLGSVPDFR 560
Cdd:COG4913 788 ELERAMRA--FNREWPAETADLDADLESLPEYL 818
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
250-541 |
1.19e-07 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 55.46 E-value: 1.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 250 AKVIELQEIISKQSREQSQMKERLASLSSHVTELEEDLDTARKDLIKSEEMNTKLQRDVREAMAQKEDMEERITTLEKRY 329
Cdd:pfam19220 48 SRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVARLAKLEAALREAEAAKEELRIELRDKTAQAEALERQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 330 LAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALsksdlls 409
Cdd:pfam19220 128 AAETEQNRALEEENKALREEAQAAEKALQRAEGELATARERLALLEQENRRLQALSEEQAAELAELTRRLAEL------- 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 410 SGSSAAKEAKLLELTSKLrkAEERhgniEERLRQMEAQLEEKN-QELQRARQREKMnEEHNKRLSDTvDKLLSESNErlq 488
Cdd:pfam19220 201 ETQLDATRARLRALEGQL--AAEQ----AERERAEAQLEEAVEaHRAERASLRMKL-EALTARAAAT-EQLLAEARN--- 269
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 578821804 489 lHLKERMAALEDKNSLLREVESAKKQLEETQHDKDQLVLNIEALRAELDHMRL 541
Cdd:pfam19220 270 -QLRDRDEAIRAAERRLKEASIERDTLERRLAGLEADLERRTQQFQEMQRARA 321
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
251-467 |
1.29e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 55.61 E-value: 1.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 251 KVIELQEIISKQSREQSQMKERLASLSSHVTELEEDLDTARKDLIKSEEMNTKLQRDVREAmaqKEDMEERITTLEKRYL 330
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEA---EAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 331 AAQR------------EATSVHDLNDKLE--NEI--ANKDSMHRQTEDKnrqlqERLELAEQKLQQTLRKAETLpevEAE 394
Cdd:COG3883 94 ALYRsggsvsyldvllGSESFSDFLDRLSalSKIadADADLLEELKADK-----AELEAKKAELEAKLAELEAL---KAE 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578821804 395 LAQRVAALsksdllssgssaakEAKLLELTSKLRKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEE 467
Cdd:COG3883 166 LEAAKAEL--------------EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAA 224
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
55-550 |
1.59e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.10 E-value: 1.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 55 RETQETLALTQGKLHevGHERDSLQRQLNTALpQEFAALTKELNVCREQLLEREEEIAELKAERNNTRLLLEHLeclvsr 134
Cdd:COG1196 216 RELKEELKELEAELL--LLKLRELEAELEELE-AELEELEAELEELEAELAELEAELEELRLELEELELELEEA------ 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 135 heRSLRMTVVKRQAQSPAGVSSEVEVLKALKSLFEHHKALDEKVRERLRVALERCSLLEEELGATHKELMILKEQNNQKK 214
Cdd:COG1196 287 --QAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAE 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 215 TLTDGVLDINHEQENTPSTSGKRSSDGSLSHEEDLAKVIELQEIISKQSREQSQMKERLASLSSHVTELEEDLDTARKDL 294
Cdd:COG1196 365 EALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEAL 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 295 IKSEEMNTKLQRDVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQT-EDKNRQLQERLEL 373
Cdd:COG1196 445 EEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVkAALLLAGLRGLAG 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 374 AEQKLQQTLRKAETLPEVEAEL------------AQRVAALSKSDLLSSGS----SAAKEAKLLELTSKLRKAEERHGNI 437
Cdd:COG1196 525 AVAVLIGVEAAYEAALEAALAAalqnivveddevAAAAIEYLKAAKAGRATflplDKIRARAALAAALARGAIGAAVDLV 604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 438 EERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSESNERLQLHLKERMAALEDKNSLLREVESAKKQLEE 517
Cdd:COG1196 605 ASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEEL 684
|
490 500 510
....*....|....*....|....*....|...
gi 578821804 518 TQHDKDQLVLNIEALRAELDHMRLRGASLHHGR 550
Cdd:COG1196 685 AERLAEEELELEEALLAEEEEERELAEAEEERL 717
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
303-519 |
1.77e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 54.84 E-value: 1.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 303 KLQRDVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIAnkdsmhrqtedknrQLQERLELAEQKLQQTl 382
Cdd:COG3883 20 AKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEID--------------KLQAEIAEAEAEIEER- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 383 rkaetlpevEAELAQRVAALSKSDLLSSGSSAAKEAK----LLELTSKLRKAEERHGNIEERLRQMEAQLEEKNQELQRA 458
Cdd:COG3883 85 ---------REELGERARALYRSGGSVSYLDVLLGSEsfsdFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAK 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578821804 459 RQREKMNEEHNKRLSDTVDKLLSESNERLQLHLKERMAALEDKNSLLREVESAKKQLEETQ 519
Cdd:COG3883 156 LAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAA 216
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
365-535 |
1.85e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.54 E-value: 1.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 365 RQLQERLELAEQKLQQTLRKAETLPEVEAELAQrvAALSKSDLLSSGSSAAKEAKLLELTSKLRKAEERHGNIEERLRQM 444
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEE--LEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEEL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 445 EAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSESNERLQLHLKERMAALEDKNSLLREVESAKKQLEETQHDKDQ 524
Cdd:COG4717 152 EERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQ 231
|
170
....*....|.
gi 578821804 525 LVLNIEALRAE 535
Cdd:COG4717 232 LENELEAAALE 242
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
244-539 |
1.99e-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: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 55.57 E-value: 1.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 244 SHEEDLAKVIELQEIIS--KQSREQSQMKERLAS--LSSHVTELEEDLDTARKdlikSEEMNTKLQRDVREAmaqKEDME 319
Cdd:pfam01576 265 KIRELEAQISELQEDLEseRAARNKAEKQRRDLGeeLEALKTELEDTLDTTAA----QQELRSKREQEVTEL---KKALE 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 320 ERITTLEKRYLA-AQREATSVHDLNDKLENEIANKDSMHRQT---EDKNRQLQERLEL--------------AEQKLQQT 381
Cdd:pfam01576 338 EETRSHEAQLQEmRQKHTQALEELTEQLEQAKRNKANLEKAKqalESENAELQAELRTlqqakqdsehkrkkLEGQLQEL 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 382 LRKAETLPEVEAELAQRVAAL-----SKSDLLSS----GSSAAKEAKLLEL----TSKLRKAEERHG-NIEERLRQMEaq 447
Cdd:pfam01576 418 QARLSESERQRAELAEKLSKLqseleSVSSLLNEaegkNIKLSKDVSSLESqlqdTQELLQEETRQKlNLSTRLRQLE-- 495
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 448 lEEKNQELQRARQREKMNEEHNKRLSdTVDKLLSESNERLQLHLKERMAALEDKNSLLREVESAKKQLEETQHDKDQLVL 527
Cdd:pfam01576 496 -DERNSLQEQLEEEEEAKRNVERQLS-TLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEK 573
|
330
....*....|..
gi 578821804 528 NIEALRAELDHM 539
Cdd:pfam01576 574 TKNRLQQELDDL 585
|
|
| SAM |
smart00454 |
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ... |
1152-1222 |
2.14e-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: 49.22 E-value: 2.14e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578821804 1152 VLVWSNDRVIRWILSIGLKEYANNLIESGVHGALLALDETFDfsalaLLLQIPTQNTQARAVLEREFNNLL 1222
Cdd:smart00454 1 VSQWSPESVADWLESIGLEQYADNFRKNGIDGALLLLLTSEE-----DLKELGITKLGHRKKILKAIQKLK 66
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
40-689 |
2.15e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 55.83 E-value: 2.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 40 MVSMLEERDRLLDTLRETQETLALTQGKLHEVGHERDSLQRQLNtALPQEFAALTKELNVCREQLLEREEEIAELKAERN 119
Cdd:TIGR02168 234 LEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVS-ELEEEIEELQKELYALANEISRLEQQKQILRERLA 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 120 NTRLLLEHLECLVSRHERSLrmtvvKRQAQSPAGVSSEVEVLKALKSLFEhhKALDEKvRERLRVALERCSLLEEELGAT 199
Cdd:TIGR02168 313 NLERQLEELEAQLEELESKL-----DELAEELAELEEKLEELKEELESLE--AELEEL-EAELEELESRLEELEEQLETL 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 200 HKELMILKEQ----NNQKKTLTDGVLDINHEQENTPSTSGKRSSDGSLSHEEDL-AKVIELQEIISKQSREQSQMKERLA 274
Cdd:TIGR02168 385 RSKVAQLELQiaslNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELqAELEELEEELEELQEELERLEEALE 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 275 SLSSHVTELEEDLDTARKDLIKS----------EEMNTKLQRDVREAMAQKEDME-------ERITTLEK------RYLA 331
Cdd:TIGR02168 465 ELREELEEAEQALDAAERELAQLqarldslerlQENLEGFSEGVKALLKNQSGLSgilgvlsELISVDEGyeaaieAALG 544
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 332 AQREATSVHDLNDKLE-----------------------NEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTL------ 382
Cdd:TIGR02168 545 GRLQAVVVENLNAAKKaiaflkqnelgrvtflpldsikgTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALsyllgg 624
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 383 -----------------RKAETLPEVEAELAQRVAALSKSDLLSSGSSAAKEAKLLELTSKLRKAEE------------- 432
Cdd:TIGR02168 625 vlvvddldnalelakklRPGYRIVTLDGDLVRPGGVITGGSAKTNSSILERRREIEELEEKIEELEEkiaelekalaelr 704
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 433 -RHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSESNErLQLHLKERMAALEDKNSLLREVESA 511
Cdd:TIGR02168 705 kELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTE-LEAEIEELEERLEEAEEELAEAEAE 783
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 512 KKQLEET-QHDKDQLVLNIE---ALRAELDHMRLRGASLHHGRPHLgsvpdfRFPMADGHTDSYSTSAVLRRpQKGRLAA 587
Cdd:TIGR02168 784 IEELEAQiEQLKEELKALREaldELRAELTLLNEEAANLRERLESL------ERRIAATERRLEDLEEQIEE-LSEDIES 856
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 588 LRDEPSKVQTLNEQdwERAQQASVLANVAQAFESDADVSDGEDDRDTllssvDLLSPSGQADAhtlammLQEQLDAINKE 667
Cdd:TIGR02168 857 LAAEIEELEELIEE--LESELEALLNERASLEEALALLRSELEELSE-----ELRELESKRSE------LRRELEELREK 923
|
730 740
....*....|....*....|..
gi 578821804 668 IRLIQEEKENTEQRAEEIESRV 689
Cdd:TIGR02168 924 LAQLELRLEGLEVRIDNLQERL 945
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
236-535 |
3.45e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 55.15 E-value: 3.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 236 KRSSDGSLSHEEDLAKVIELQEIiSKQSREQSQMKERlASLSSHVTELEEDLDTARK--DLIKSEEMNTKLQRDVREAMA 313
Cdd:PTZ00121 1430 KKKADEAKKKAEEAKKADEAKKK-AEEAKKAEEAKKK-AEEAKKADEAKKKAEEAKKadEAKKKAEEAKKKADEAKKAAE 1507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 314 QKEDMEERITTLEKRYLAAQREATSVHDLND-KLENEIANKDSMHRQTEDKNRQLQERLE---LAEQKLQQTLRKAETLP 389
Cdd:PTZ00121 1508 AKKKADEAKKAEEAKKADEAKKAEEAKKADEaKKAEEKKKADELKKAEELKKAEEKKKAEeakKAEEDKNMALRKAEEAK 1587
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 390 EVEAELAQRVAALSKSDLLSSGSSAAKEAKLLELTSKLRKAEERHGNIEErLRQMEAQLEEKNQELQRARQREKMNEEHN 469
Cdd:PTZ00121 1588 KAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQ-LKKKEAEEKKKAEELKKAEEENKIKAAEE 1666
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578821804 470 KRLSDTVDKLLSESNerlqlhlKERMAALEDKNSLLREVESAKKqLEETQHDKDQLVLNIEALRAE 535
Cdd:PTZ00121 1667 AKKAEEDKKKAEEAK-------KAEEDEKKAAEALKKEAEEAKK-AEELKKKEAEEKKKAEELKKA 1724
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
45-548 |
4.74e-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: 4.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 45 EERDRLLDTLRETQETLALTQGKLHEVGHERDSLQRQLNTaLPQEFAALTKELNVCREQLLEREEEIAELKAERNNTRLL 124
Cdd:TIGR04523 124 VELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYND-LKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELL 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 125 LEHLECLVSRHeRSLRMTVVKRQAQSpagvSSEVEVLKALKSLFEHHKALDEKVRERLRVALERCSLLEEELGATHKELm 204
Cdd:TIGR04523 203 LSNLKKKIQKN-KSLESQISELKKQN----NQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKEL- 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 205 ilkEQNNQK-KTLTDGVLDINHEQENTPStsgKRSSDGSLSHEEDLA----KVIELQEIISKQSREQSQMKERLASLSSH 279
Cdd:TIGR04523 277 ---EQNNKKiKELEKQLNQLKSEISDLNN---QKEQDWNKELKSELKnqekKLEEIQNQISQNNKIISQLNEQISQLKKE 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 280 VTELEEDLDTARKDLIKSEEMNTKLQRDVREAMAQKEDMEERITtlekrylaaqreatsvhDLNDKLENEiankdsmhrq 359
Cdd:TIGR04523 351 LTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQIN-----------------DLESKIQNQ---------- 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 360 tEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKSDllssgssAAKEAKLLELTSKLRKAEERHGNIEE 439
Cdd:TIGR04523 404 -EKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQD-------SVKELIIKNLDNTRESLETQLKVLSR 475
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 440 RLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSESNErlqlhLKERMAALEdknSLLREVESAKKQLEEtQ 519
Cdd:TIGR04523 476 SINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISS-----LKEKIEKLE---SEKKEKESKISDLED-E 546
|
490 500
....*....|....*....|....*....
gi 578821804 520 HDKDQLVLNIEALRAELDHMRLRGASLHH 548
Cdd:TIGR04523 547 LNKDDFELKKENLEKEIDEKNKEIEELKQ 575
|
|
| SAM |
smart00454 |
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ... |
1074-1129 |
5.16e-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: 48.06 E-value: 5.16e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 578821804 1074 EWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRGQLKMVDSFHRNSFQCGIMCLR 1129
Cdd:smart00454 11 DWLESIGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKLK 66
|
|
| SAM |
smart00454 |
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ... |
949-1015 |
5.21e-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: 48.06 E-value: 5.21e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578821804 949 FAQWDGPTVVVWLELWvGMPAwYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEI 1015
Cdd:smart00454 1 VSQWSPESVADWLESI-GLEQ-YADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKL 65
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
113-543 |
6.36e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.91 E-value: 6.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 113 ELKAERNNTRLLLEHLECLVSRHERSLRmtVVKRQAQSPAGVSSEV-EVLKALKSLFEHHKALDEKVR--ERLRVALERC 189
Cdd:PRK03918 297 KLSEFYEEYLDELREIEKRLSRLEEEIN--GIEERIKELEEKEERLeELKKKLKELEKRLEELEERHElyEEAKAKKEEL 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 190 SLLEEELGATHKELMI--LKEQNNQKKTLTDGVLDINHEQENTPSTSGKRSSD--------------GSLSHEEDLAkvi 253
Cdd:PRK03918 375 ERLKKRLTGLTPEKLEkeLEELEKAKEEIEEEISKITARIGELKKEIKELKKAieelkkakgkcpvcGRELTEEHRK--- 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 254 elqEIISKQSREQSQMKERLASLSSHVTELEEDLDTARKDLIKSEEMntklqRDVREAMAQKEDMEERITTLEKRYL-AA 332
Cdd:PRK03918 452 ---ELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESEL-----IKLKELAEQLKELEEKLKKYNLEELeKK 523
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 333 QREATSVHDLNDKLENEIAN-KDSMHRQTEDKNR--QLQERLELAEQKLQQTLRKAETLP-EVEAELAQRVAALSKSdll 408
Cdd:PRK03918 524 AEEYEKLKEKLIKLKGEIKSlKKELEKLEELKKKlaELEKKLDELEEELAELLKELEELGfESVEELEERLKELEPF--- 600
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 409 ssgssAAKEAKLLELTSKLRKAEERHGNIEERLRQMEAQLEEKNQELQRARQREkmnEEHNKRLSDTVDKLLSESNERLQ 488
Cdd:PRK03918 601 -----YNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKEL---EELEKKYSEEEYEELREEYLELS 672
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 578821804 489 LHLKERMAALEDKNSLLREVESAKKQLEETQHDKDQLVLNIEALRAELDHM-RLRG 543
Cdd:PRK03918 673 RELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERVeELRE 728
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
45-456 |
7.14e-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: 53.92 E-value: 7.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 45 EERDRLLDTLRETQETLALTQGKLHEVGHERDSLQRQLNTALpqEFAALTKElnvcreqllereeeiaelKAERNNTRLL 124
Cdd:TIGR02169 170 RKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAE--RYQALLKE------------------KREYEGYELL 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 125 LEHLEclvsrHERSLRmtvvkrqaqspagvssevEVLKALKSLFEHHKALDEKVRERLrvalERCSLLEEELGATHKELM 204
Cdd:TIGR02169 230 KEKEA-----LERQKE------------------AIERQLASLEEELEKLTEEISELE----KRLEEIEQLLEELNKKIK 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 205 ILKEqnNQKKTLTDGVLDINHEQENTpstsgKRSSDGSLSHEEDLA-KVIELQEIISKQ-------SREQSQMKERLASL 276
Cdd:TIGR02169 283 DLGE--EEQLRVKEKIGELEAEIASL-----ERSIAEKERELEDAEeRLAKLEAEIDKLlaeieelEREIEEERKRRDKL 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 277 SSHVTELEEDLDTARKDLiksEEMNTKLQRDVREAMAQKEDME---ERITTLEKRYLAAQREATSVHDLNDKLENEIANK 353
Cdd:TIGR02169 356 TEEYAELKEELEDLRAEL---EEVDKEFAETRDELKDYREKLEklkREINELKRELDRLQEELQRLSEELADLNAAIAGI 432
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 354 DSMHRQTEDKNRQLQERLELAEQKLQQTlrkAETLPEVEAELAQRVAALSKSdllssgssaakEAKLLELTSKLRKAEER 433
Cdd:TIGR02169 433 EAKINELEEEKEDKALEIKKQEWKLEQL---AADLSKYEQELYDLKEEYDRV-----------EKELSKLQRELAEAEAQ 498
|
410 420
....*....|....*....|...
gi 578821804 434 HGNIEERLRQMEAQLEEKNQELQ 456
Cdd:TIGR02169 499 ARASEERVRGGRAVEEVLKASIQ 521
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
44-488 |
7.45e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 53.62 E-value: 7.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 44 LEERDRLLDTLRETQETLALTQGKLHEVGHERDSLQRQLNTA-LPQEFAALTKELNVCREQLLEREEEIAELKAERNNTR 122
Cdd:COG4717 87 EEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLpLYQELEALEAELAELPERLEELEERLEELRELEEELE 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 123 LLLEHLECLVSRHERSLRmtvvkrqaqspagvSSEVEVLKALKSLFEHHKALDEKV---RERLRVALERCSLLEEELGAT 199
Cdd:COG4717 167 ELEAELAELQEELEELLE--------------QLSLATEEELQDLAEELEELQQRLaelEEELEEAQEELEELEEELEQL 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 200 HKELMILKEQNNQKKT-----LTDGVLDINHEQENTPSTSGKRSSDGSLsheedLAKVIELQEIISKQSREQSQMKERLA 274
Cdd:COG4717 233 ENELEAAALEERLKEArllllIAAALLALLGLGGSLLSLILTIAGVLFL-----VLGLLALLFLLLAREKASLGKEAEEL 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 275 SLSSHVTELE-EDLDTARKDLIKSEEMNTKLQRDVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIANK 353
Cdd:COG4717 308 QALPALEELEeEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEEL 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 354 DSMHRQTEDKnRQLQERLELAEQKLQQTLRKAETLPEV--EAELAQRVAALsksdllssgssaakEAKLLELTSKLRKAE 431
Cdd:COG4717 388 RAALEQAEEY-QELKEELEELEEQLEELLGELEELLEAldEEELEEELEEL--------------EEELEELEEELEELR 452
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 578821804 432 ERHGNIEERLRQMEAQ--LEEKNQELQRARQREKMNEEHNKRLsDTVDKLLSESNERLQ 488
Cdd:COG4717 453 EELAELEAELEQLEEDgeLAELLQELEELKAELRELAEEWAAL-KLALELLEEAREEYR 510
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
362-540 |
8.13e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.84 E-value: 8.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 362 DKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALsksdllssgssaakEAKLLELTSKLRKAEERHGNIEERL 441
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAAL--------------ERRIAALARRIRALEQELAALEAEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 442 RQMEAQLEEKNQELQRARQR--EKMNEEHNKRLSDTVDKLLSESN--------ERLQLHLKERMAALEDKNSLLREVESA 511
Cdd:COG4942 86 AELEKEIAELRAELEAQKEElaELLRALYRLGRQPPLALLLSPEDfldavrrlQYLKYLAPARREQAEELRADLAELAAL 165
|
170 180
....*....|....*....|....*....
gi 578821804 512 KKQLEETQHDKDQLVLNIEALRAELDHMR 540
Cdd:COG4942 166 RAELEAERAELEALLAELEEERAALEALK 194
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
335-548 |
8.50e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.77 E-value: 8.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 335 EATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQ--ERLELAEQKLQQTLRKAETLPEVEAEL----AQRVAALSKSDLL 408
Cdd:COG4913 219 EEPDTFEAADALVEHFDDLERAHEALEDAREQIEllEPIRELAERYAAARERLAELEYLRAALrlwfAQRRLELLEAELE 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 409 SSGSSAAK-EAKLLELTSKLRKAEERHGNIEERLRQ--------MEAQLEEKNQELQRARQREKmneehnkRLSDTVDKL 479
Cdd:COG4913 299 ELRAELARlEAELERLEARLDALREELDELEAQIRGnggdrleqLEREIERLERELEERERRRA-------RLEALLAAL 371
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578821804 480 ---LSESNERLQLHLKERMAALEDKNSLLREVESAKKQLEETQHDKDQlvlNIEALRAELDHMRLRGASLHH 548
Cdd:COG4913 372 glpLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRR---ELRELEAEIASLERRKSNIPA 440
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
264-457 |
1.19e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.38 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 264 REQSQMKERLASLSSHVTELEEDLDTARKDLIKSEEMNTKLQRDVREAMAQKEDMEERITTLEKRYLAAQREATSVH--D 341
Cdd:COG4913 671 AELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELraL 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 342 LNDKLENEIANK--DSMHRQTEDKNRQLQERLELAEQKLQQTLRK---------------AETLPEVEAELAQrvaaLSK 404
Cdd:COG4913 751 LEERFAAALGDAveRELRENLEERIDALRARLNRAEEELERAMRAfnrewpaetadldadLESLPEYLALLDR----LEE 826
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 578821804 405 SDLlssgssAAKEAKLLELtskLRKAEER-----HGNIEERLRQMEAQLEEKNQELQR 457
Cdd:COG4913 827 DGL------PEYEERFKEL---LNENSIEfvadlLSKLRRAIREIKERIDPLNDSLKR 875
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
44-536 |
1.55e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 52.73 E-value: 1.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 44 LEERDRLLDTLRETQETLALTQGKLHEVGHERDSLQRQLNTaLPQEFAALTKELNVCREQLLEREEEIAELKAERNNTRL 123
Cdd:PRK02224 250 REELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEE-LEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRD 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 124 LLEHLECLVSRH--------ERSLRMTVVKRQAQSPAGVsSEVEVLKALKSLFEHHKALDEkVRERLRVALERCSLLEEE 195
Cdd:PRK02224 329 RLEECRVAAQAHneeaeslrEDADDLEERAEELREEAAE-LESELEEAREAVEDRREEIEE-LEEEIEELRERFGDAPVD 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 196 LGATHKELMILKEQnnqkktltdgvLDINHEQENTPSTSGKrssdgslSHEEDLAKVIELQEI----ISKQSREQSQMKE 271
Cdd:PRK02224 407 LGNAEDFLEELREE-----------RDELREREAELEATLR-------TARERVEEAEALLEAgkcpECGQPVEGSPHVE 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 272 RLASLSSHVTELEEDLDTARKDLiksEEMNTKLQR--DVREAMAQKEDMEERITTLEKRylAAQREATsVHDLNDKLENE 349
Cdd:PRK02224 469 TIEEDRERVEELEAELEDLEEEV---EEVEERLERaeDLVEAEDRIERLEERREDLEEL--IAERRET-IEEKRERAEEL 542
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 350 IANKDSMHRQTEDKNRQLQErlelAEQKLQQTLRKAETLPEVEAELAQRVAALSK-SDLLSSGSSAAKEA-----KLLEL 423
Cdd:PRK02224 543 RERAAELEAEAEEKREAAAE----AEEEAEEAREEVAELNSKLAELKERIESLERiRTLLAAIADAEDEIerlreKREAL 618
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 424 TSKLRKAEERHGNIEERLRQMEAQ-----LEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSE----SNERLQLH-LKE 493
Cdd:PRK02224 619 AELNDERRERLAEKRERKRELEAEfdearIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEigavENELEELEeLRE 698
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 578821804 494 RMAALEDKNSLLREVESAKKQLEETQHDkdqlvlnieaLRAEL 536
Cdd:PRK02224 699 RREALENRVEALEALYDEAEELESMYGD----------LRAEL 731
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
247-521 |
1.61e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.84 E-value: 1.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 247 EDLAKVIELQEIISKQSREQSQMKERLASLSSHVTELEEDLDTARKDliksEEMNTKLQRDVREAMAQKEDMEERITTLE 326
Cdd:PTZ00121 1549 DELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIE----EVMKLYEEEKKMKAEEAKKAEEAKIKAEE 1624
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 327 KRylAAQREATSVHDLNDKLENEIANKDSMHRQTED-KNRQLQERLELAEQKlqqtlRKAETLPEVEAELAQRVAALSKS 405
Cdd:PTZ00121 1625 LK--KAEEEKKKVEQLKKKEAEEKKKAEELKKAEEEnKIKAAEEAKKAEEDK-----KKAEEAKKAEEDEKKAAEALKKE 1697
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 406 dllssgssaAKEAKLLELTSK-----LRKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKrlsdtVDKLL 480
Cdd:PTZ00121 1698 ---------AEEAKKAEELKKkeaeeKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKK-----IAHLK 1763
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 578821804 481 SESNERLQLHLKERMAALEDKnsLLREVESAKKQLEETQHD 521
Cdd:PTZ00121 1764 KEEEKKAEEIRKEKEAVIEEE--LDEEDEKRRMEVDKKIKD 1802
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
304-517 |
1.70e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 52.33 E-value: 1.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 304 LQRDVREAMAQKEDMEERITTLEKRYLAAQREatsvhdLND-KLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTL 382
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELEEAEAA------LEEfRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 383 RKAETLPEVEAELAQRVAALSKSDLLSSGSS--AAKEAKLLELTSKLRkaeERHGNIEERLRQMEAQLEEKNQELQRARQ 460
Cdd:COG3206 240 ARLAALRAQLGSGPDALPELLQSPVIQQLRAqlAELEAELAELSARYT---PNHPDVIALRAQIAALRAQLQQEAQRILA 316
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 578821804 461 REKMNEEHNKRLSDTVDKLLSESNERLQlhlkeRMAALEDK-NSLLREVESAKKQLEE 517
Cdd:COG3206 317 SLEAELEALQAREASLQAQLAQLEARLA-----ELPELEAElRRLEREVEVARELYES 369
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
46-536 |
1.83e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 52.75 E-value: 1.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 46 ERDRLLDTLRETQETLALTQGKLHEVGHERDSLQRQLNtalpqefaALTKELNVCREQLLEREEEIAELKAERNNTRLLL 125
Cdd:TIGR02168 226 ELALLVLRLEELREELEELQEELKEAEEELEELTAELQ--------ELEEKLEELRLEVSELEEEIEELQKELYALANEI 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 126 EHLECLVSRH---ERSLRMTVVKRQAQSPAGVSSEVEVLKALK-------SLFEHHKALDEKV---RERLRVALERCSLL 192
Cdd:TIGR02168 298 SRLEQQKQILrerLANLERQLEELEAQLEELESKLDELAEELAeleekleELKEELESLEAELeelEAELEELESRLEEL 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 193 EEELGATHKELMILKEQ----NNQKKTLTDGVLDINHEQENTPSTSGKRSSDGSLSHEEDL-AKVIELQEIISKQSREQS 267
Cdd:TIGR02168 378 EEQLETLRSKVAQLELQiaslNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELqAELEELEEELEELQEELE 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 268 QMKERLASLSSHVTELEEDLDTARKDLIKS----------EEMNTKLQRDVREAMAQKEDME-------ERITTLEK--- 327
Cdd:TIGR02168 458 RLEEALEELREELEEAEQALDAAERELAQLqarldslerlQENLEGFSEGVKALLKNQSGLSgilgvlsELISVDEGyea 537
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 328 ---RYLAAQREATSVHDLNDK------LENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAEL--- 395
Cdd:TIGR02168 538 aieAALGGRLQAVVVENLNAAkkaiafLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLrka 617
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 396 ----------------AQRVAALSKSDL--------------LSSGSSAAKEAKLLELTSKLRkaeerhgNIEERLRQME 445
Cdd:TIGR02168 618 lsyllggvlvvddldnALELAKKLRPGYrivtldgdlvrpggVITGGSAKTNSSILERRREIE-------ELEEKIEELE 690
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 446 AQLEEKNQELQRAR-QREKMNEEHNK--RLSDTVDKLLSESNERLQLHLKERMAALEDKNSLLREVESAKKQLEETQHDK 522
Cdd:TIGR02168 691 EKIAELEKALAELRkELEELEEELEQlrKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERL 770
|
570
....*....|....
gi 578821804 523 DQLVLNIEALRAEL 536
Cdd:TIGR02168 771 EEAEEELAEAEAEI 784
|
|
| SAM_superfamily |
cd09487 |
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ... |
1074-1125 |
1.92e-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: 46.08 E-value: 1.92e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 578821804 1074 EWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRgQLKMVDSFHRNSFQCGI 1125
Cdd:cd09487 4 EWLESLGLEQYADLFRKNEIDGDALLLLTDEDLK-ELGITSPGHRKKILRAI 54
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
34-525 |
1.96e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 52.42 E-value: 1.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 34 SHFEQLMVSMleerDRLLDTLRETQETLALTQGKLHEVGHERDSLQRQLNTALPQEFAALTK-ELNVCREQLLEREEeia 112
Cdd:pfam05483 296 KELEDIKMSL----QRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEfEATTCSLEELLRTE--- 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 113 ELKAERNNTRLLLEHLEcLVSRHERSLRMTVVKRqaqspagvSSEVEVLKALKSLFEHHKALDEKvrerlrvalERCSLL 192
Cdd:pfam05483 369 QQRLEKNEDQLKIITME-LQKKSSELEEMTKFKN--------NKEVELEELKKILAEDEKLLDEK---------KQFEKI 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 193 EEELGATHKELMILKEQNNQKktltdgVLDInhEQENTPSTSgkrssdgslSHEEDLAKVIELQEIISKQSREQSQMKER 272
Cdd:pfam05483 431 AEELKGKEQELIFLLQAREKE------IHDL--EIQLTAIKT---------SEEHYLKEVEDLKTELEKEKLKNIELTAH 493
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 273 LASLSSHVTELEEDLDTARKDLIKSEEmntklqrDVREAMAQKEDMEERITTLEKRYLAAQREATSVHD----LNDKLEN 348
Cdd:pfam05483 494 CDKLLLENKELTQEASDMTLELKKHQE-------DIINCKKQEERMLKQIENLEEKEMNLRDELESVREefiqKGDEVKC 566
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 349 EIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKSDLLSSGSSAAKEAKL----LELT 424
Cdd:pfam05483 567 KLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVnkleLELA 646
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 425 SKLRKAEERHGNIEERLRQMEAQLEEKNQELQRAR----QREKMNEEHNKRLSDTV--------------DKLLSESNER 486
Cdd:pfam05483 647 SAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKaiadEAVKLQKEIDKRCQHKIaemvalmekhkhqyDKIIEERDSE 726
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 578821804 487 LQLHLKERM------AALEDKNSLLR-EVESAKKQLEETQHDKDQL 525
Cdd:pfam05483 727 LGLYKNKEQeqssakAALEIELSNIKaELLSLKKQLEIEKEEKEKL 772
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
247-546 |
2.42e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.45 E-value: 2.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 247 EDLAKVIELQEIISKQSREQSQMKERLASLSSHVTELEEDLDTARKDLIKSEEMNTKLQRDVREAMAQKEDMEERITTLE 326
Cdd:PTZ00121 1357 DEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEA 1436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 327 KRylaAQREATSVHDLNDKLEnEIANKDSMHRQTEDKnRQLQERLELAEQ--KLQQTLRKAETLPEVEAELAQRVAALSK 404
Cdd:PTZ00121 1437 KK---KAEEAKKADEAKKKAE-EAKKAEEAKKKAEEA-KKADEAKKKAEEakKADEAKKKAEEAKKKADEAKKAAEAKKK 1511
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 405 SDLLSSGSSA--AKEAKLLELTSK---LRKAEERHGNIE----ERLRQMEA---------QLEEKNQELQRARQREKMNE 466
Cdd:PTZ00121 1512 ADEAKKAEEAkkADEAKKAEEAKKadeAKKAEEKKKADElkkaEELKKAEEkkkaeeakkAEEDKNMALRKAEEAKKAEE 1591
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 467 EHNKRLSDTVDKLLSESNERLQLHLKERMAALEdknslLREVESAKKQLEETQHDKDQLVLNIEALRAELDHMRLRGASL 546
Cdd:PTZ00121 1592 ARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEE-----LKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEE 1666
|
|
| Lebercilin |
pfam15619 |
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ... |
254-384 |
2.52e-06 |
|
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of eukaryotic ciliary proteins. Mutations in the gene, LCA5, are implicated in the disease Leber congenital amaurosis. In photoreceptors, lebercilin is uniquely localized at the cilium that bridges the inner and outer segments. Lebercilin functions as an integral element of selective protein transport through photoreceptor cilia. Lebercilin specifically interacts with the intraflagellar transport (IFT), and disruption of IFT can lead to Leber congenital amaurosis.
Pssm-ID: 464776 [Multi-domain] Cd Length: 193 Bit Score: 49.52 E-value: 2.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 254 ELQEIISKQSREQSQMKERLASLSSHVTELEEDLDTARKDLIKSEEMNTKLQRDVREA-MAQKEDMEERITTLEKRYLAA 332
Cdd:pfam15619 57 ELPQLIARHNEEVRVLRERLRRLQEKERDLERKLKEKEAELLRLRDQLKRLEKLSEDKnLAEREELQKKLEQLEAKLEDK 136
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 578821804 333 QREatsVHDLNDKLEN-------EIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRK 384
Cdd:pfam15619 137 DEK---IQDLERKLELenksfrrQLAAEKKKHKEAQEEVKILQEEIERLQQKLKEKERE 192
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
236-534 |
3.00e-06 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 51.88 E-value: 3.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 236 KRSSDGSLSHEEDLAKviELQEIISKQSREQSQMKErLASLSSHVTELEEDLDTARKDLIKseemntklqrdVREAMAQK 315
Cdd:COG3096 281 RELSERALELRRELFG--ARRQLAEEQYRLVEMARE-LEELSARESDLEQDYQAASDHLNL-----------VQTALRQQ 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 316 EDME---ERITTLEKRyLAAQREAtsVHDLNDKLENEIANK-------DSMHRQTEDKNRQL--QERLELAEQKLQQTLR 383
Cdd:COG3096 347 EKIEryqEDLEELTER-LEEQEEV--VEEAAEQLAEAEARLeaaeeevDSLKSQLADYQQALdvQQTRAIQYQQAVQALE 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 384 KAETL---PEVEAE-LAQRVAAL-SKSDLLSSG----------SSAAKE--AKLLELTSKLRKAEER------------- 433
Cdd:COG3096 424 KARALcglPDLTPEnAEDYLAAFrAKEQQATEEvleleqklsvADAARRqfEKAYELVCKIAGEVERsqawqtarellrr 503
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 434 ---HGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDkllseSNERLQLHLKERMAALEDknsLLREVES 510
Cdd:COG3096 504 yrsQQALAQRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLD-----AAEELEELLAELEAQLEE---LEEQAAE 575
|
330 340
....*....|....*....|....
gi 578821804 511 AKKQLEETQHDKDQLVLNIEALRA 534
Cdd:COG3096 576 AVEQRSELRQQLEQLRARIKELAA 599
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
365-530 |
3.97e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 50.93 E-value: 3.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 365 RQLQERLELAEQKLQQTLRKAETlpevEAELAQRVAALsksdllssgssAAKEaKLLELTSKL-RKAEERHGNI---EER 440
Cdd:PRK12704 27 KIAEAKIKEAEEEAKRILEEAKK----EAEAIKKEALL-----------EAKE-EIHKLRNEFeKELRERRNELqklEKR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 441 LRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSESNERLQLHLK--ERMAAL---EDKNSLLREVEsakkql 515
Cdd:PRK12704 91 LLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQelERISGLtaeEAKEILLEKVE------ 164
|
170
....*....|....*
gi 578821804 516 EETQHDKDQLVLNIE 530
Cdd:PRK12704 165 EEARHEAAVLIKEIE 179
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
321-542 |
4.54e-06 |
|
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.
Pssm-ID: 432790 [Multi-domain] Cd Length: 238 Bit Score: 49.61 E-value: 4.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 321 RITTLEKRYLAAQREATSVHDLNDKLENeIANKDSmhrqTEDKNRQLQERLELAEQKLQQTLRKAETL-PEVEAELAQRV 399
Cdd:pfam12795 1 KLDELEKAKLDEAAKKKLLQDLQQALSL-LDKIDA----SKQRAAAYQKALDDAPAELRELRQELAALqAKAEAAPKEIL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 400 AALSKSDLlssgssaakEAKLLELTSKLRKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTvDKL 479
Cdd:pfam12795 76 ASLSLEEL---------EQRLLQTSAQLQELQNQLAQLNSQLIELQTRPERAQQQLSEARQRLQQIRNRLNGPAPP-GEP 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578821804 480 LSESnerLQLHLKERMAALEDKNSLLRE--------VESAKKQLEETQHDKDQLVLNIEALRAELDHMRLR 542
Cdd:pfam12795 146 LSEA---QRWALQAELAALKAQIDMLEQellsnnnrQDLLKARRDLLTLRIQRLEQQLQALQELLNEKRLQ 213
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
44-335 |
8.73e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 50.45 E-value: 8.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 44 LEERDRLLDTLRETQETLALTQGKLHE-----VGHERDSLQRQLnTALPQEFAALTKELNVCREQLLEREEEIAELKAER 118
Cdd:TIGR02169 210 AERYQALLKEKREYEGYELLKEKEALErqkeaIERQLASLEEEL-EKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEE 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 119 NNT-RLLLEHLECLVSRHERSLRmtVVKRQAQSPAGVSSEVEV--------LKALKSLFEHHKALDEKVRERLRVALERC 189
Cdd:TIGR02169 289 QLRvKEKIGELEAEIASLERSIA--EKERELEDAEERLAKLEAeidkllaeIEELEREIEEERKRRDKLTEEYAELKEEL 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 190 SLLEEELGATHKELMILKEQNNQKKTLTDgvlDINHEQEntpstsgkrssdgSLSHEEDlakviELQEIISKQSREQSQM 269
Cdd:TIGR02169 367 EDLRAELEEVDKEFAETRDELKDYREKLE---KLKREIN-------------ELKRELD-----RLQEELQRLSEELADL 425
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578821804 270 KERLASLSSHVTELEEDLDTARKDLIKSEEMNTKLQRDVREAMAQKEDMEERITTLEKRYLAAQRE 335
Cdd:TIGR02169 426 NAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRE 491
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
249-533 |
9.06e-06 |
|
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: 50.21 E-value: 9.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 249 LAKVIE-LQEIISKQSREQSQMKERLASLS-------SHVTELEEDLdtARKDLIkSEEMNTKLQRDVREAMAQKEDMEE 320
Cdd:pfam10174 399 LQKKIEnLQEQLRDKDKQLAGLKERVKSLQtdssntdTALTTLEEAL--SEKERI-IERLKEQREREDRERLEELESLKK 475
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 321 RITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQ---KLQQTLRKAETLPEVE---AE 394
Cdd:pfam10174 476 ENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEecsKLENQLKKAHNAEEAVrtnPE 555
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 395 LAQRVAALSKSDLLSSGSSAAKEAKLLELTSKLRKAEERHGNIEERLRQME--AQLEEKNQELQRARQREKMNEEHNKRL 472
Cdd:pfam10174 556 INDRIRLLEQEVARYKEESGKAQAEVERLLGILREVENEKNDKDKKIAELEslTLRQMKEQNKKVANIKHGQQEMKKKGA 635
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578821804 473 SDTVDKLLSESNER---LQLHLKERMAALEDKNSllrEVESAKKQLEETQ---HDKDQLVLNIEALR 533
Cdd:pfam10174 636 QLLEEARRREDNLAdnsQQLQLEELMGALEKTRQ---ELDATKARLSSTQqslAEKDGHLTNLRAER 699
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
156-489 |
9.69e-06 |
|
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: 50.12 E-value: 9.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 156 SEVEVLKALKSLFEHHKALDEKVRERL--RVALERCSLLEEELGATHKELMILKEQNNQKKTLTDGVLDINHEQENTPST 233
Cdd:pfam17380 266 TENEFLNQLLHIVQHQKAVSERQQQEKfeKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAME 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 234 SGK---------RSSDGSLSHEEDLAKVIELQEIISKQSREQSQMKERLaslsshvtelEEDLDTARKDLIKSEEMNTKL 304
Cdd:pfam17380 346 RERelerirqeeRKRELERIRQEEIAMEISRMRELERLQMERQQKNERV----------RQELEAARKVKILEEERQRKI 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 305 QRDVREaMAQKEDMEERITTLEKRYLAAQREatsvHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRK 384
Cdd:pfam17380 416 QQQKVE-MEQIRAEQEEARQREVRRLEEERA----REMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAE 490
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 385 AETLPEVEAELAQRVAALsksdLLSSGSSAAKEAKLLELTSKLRKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKM 464
Cdd:pfam17380 491 EQRRKILEKELEERKQAM----IEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERS 566
|
330 340
....*....|....*....|....*
gi 578821804 465 NEEHNKRLSDTVDKLLSESNERLQL 489
Cdd:pfam17380 567 RLEAMEREREMMRQIVESEKARAEY 591
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
422-542 |
1.02e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 50.07 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 422 ELTSKLRKAEERHGNIEERLRQMEAQLEEKNQELQR-ARQREKMNEehnkrlsdtVDKLLSESNE-RLQLHLKERMAALE 499
Cdd:TIGR02169 167 EFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERlRREREKAER---------YQALLKEKREyEGYELLKEKEALER 237
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 578821804 500 DKNSLLREVESAKKQLEETQHDKDQLVLNIEALRAELDHMRLR 542
Cdd:TIGR02169 238 QKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKK 280
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
270-538 |
1.02e-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: 50.02 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 270 KERLASLSSHVTELEEDLDTARKDLIKSEEMNTKLQRDVREAMAQKEDMEERITTLEK-------RYLAAQREATSVHDL 342
Cdd:TIGR04523 95 KDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKeleklnnKYNDLKKQKEELENE 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 343 NDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQqtlrKAETLPEVEAELAQRVAALSKSDLLssgssaaKEAKLLE 422
Cdd:TIGR04523 175 LNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQ----KNKSLESQISELKKQNNQLKDNIEK-------KQQEINE 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 423 LTSKLRKAEERHGNIEERLRQMEAQLEEKNQELQRArqrEKMNEEHNKRLSDTVDKLLSESNERLQLHLKERMAALEDKN 502
Cdd:TIGR04523 244 KTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQN---NKKIKELEKQLNQLKSEISDLNNQKEQDWNKELKSELKNQE 320
|
250 260 270
....*....|....*....|....*....|....*.
gi 578821804 503 SLLREVESakkQLEETQHDKDQLVLNIEALRAELDH 538
Cdd:TIGR04523 321 KKLEEIQN---QISQNNKIISQLNEQISQLKKELTN 353
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
266-460 |
1.31e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 49.63 E-value: 1.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 266 QSQMKERLASLSSHVTELEEDLDTARKDLIKSEE--MNTKLQRDVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLN 343
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEEAEAalEEFRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 344 DKLENEIA-NKDSMHRQTEDKN-RQLQERLELAEQKLQQTLRK-AETLPEVEAELAQRVAALSKSDLLSSGSSAAKEAKL 420
Cdd:COG3206 243 AALRAQLGsGPDALPELLQSPViQQLRAQLAELEAELAELSARyTPNHPDVIALRAQIAALRAQLQQEAQRILASLEAEL 322
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 578821804 421 LELTSKLRKAEERHGNIEERLRQM---EAQLEEKNQELQRARQ 460
Cdd:COG3206 323 EALQAREASLQAQLAQLEARLAELpelEAELRRLEREVEVARE 365
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
38-521 |
1.45e-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: 49.84 E-value: 1.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 38 QLMVSMLEERDR--LLDTLRETQETLALTQGKLHE--VGHERDSLQRQ-----LNTALPQEFAALTKELNvcreqlLERE 108
Cdd:pfam12128 231 QAIAGIMKIRPEftKLQQEFNTLESAELRLSHLHFgyKSDETLIASRQeerqeTSAELNQLLRTLDDQWK------EKRD 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 109 EEIAELKAERNNTRLLLEHLECLVSRHERSLRMTVVKR---QAQSPAgVSSEVEVL-KALKSLFEHHKALDEKVRERLRV 184
Cdd:pfam12128 305 ELNGELSAADAAVAKDRSELEALEDQHGAFLDADIETAaadQEQLPS-WQSELENLeERLKALTGKHQDVTAKYNRRRSK 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 185 ALERCSlleEELGATHKELMILKEQNNQKKTLTDGVLDINHEQENTPSTSGKRS-SDGSLSHEEDL--AKVIELQEIISK 261
Cdd:pfam12128 384 IKEQNN---RDIAGIKDKLAKIREARDRQLAVAEDDLQALESELREQLEAGKLEfNEEEYRLKSRLgeLKLRLNQATATP 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 262 QSREQ--------SQMKERLASLSSHVTELEEDLDTARKdliKSEEMNTKLQRDVREAMAQKEDMEERITTLEKRylaaq 333
Cdd:pfam12128 461 ELLLQlenfderiERAREEQEAANAEVERLQSELRQARK---RRDQASEALRQASRRLEERQSALDELELQLFPQ----- 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 334 reatsVHDLNDKLENEIAN-KDSMHRQTedkNRQLQERLELAEQKLQQTLRKAETLPEVEAELaQRVAALSKSDllssgS 412
Cdd:pfam12128 533 -----AGTLLHFLRKEAPDwEQSIGKVI---SPELLHRTDLDPEVWDGSVGGELNLYGVKLDL-KRIDVPEWAA-----S 598
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 413 SAAKEAKLLELTSKLRKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDtvdkllSESNERLQLHlK 492
Cdd:pfam12128 599 EEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFD------EKQSEKDKKN-K 671
|
490 500
....*....|....*....|....*....
gi 578821804 493 ERMAALEDKNSLLREVESAKKQLEETQHD 521
Cdd:pfam12128 672 ALAERKDSANERLNSLEAQLKQLDKKHQA 700
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
245-537 |
1.55e-05 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 49.30 E-value: 1.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 245 HEEDLAK-VIELQ---EIISKQSREQSQMKERLASL---SSHVTELEEDLDTARKDLiksEEMNtKLQRDVR-------E 310
Cdd:pfam05622 88 KCEELEKeVLELQhrnEELTSLAEEAQALKDEMDILresSDKVKKLEATVETYKKKL---EDLG-DLRRQVKlleernaE 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 311 AMAQKEDMEERIttleKRY--LAAQREATS--VHDLNDKLENEIANKDsmhrQTEDKNRQLQERLELAEQKLQQTLRKAE 386
Cdd:pfam05622 164 YMQRTLQLEEEL----KKAnaLRGQLETYKrqVQELHGKLSEESKKAD----KLEFEYKKLEEKLEALQKEKERLIIERD 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 387 TLPE----------VEAELAQRVAALSKSDllSSGSSAAKEAKLLELTSKLRK--------AEERHGNIEERLRQMEAQL 448
Cdd:pfam05622 236 TLREtneelrcaqlQQAELSQADALLSPSS--DPGDNLAAEIMPAEIREKLIRlqhenkmlRLGQEGSYRERLTELQQLL 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 449 EEKNQELQRARQREKMNeehNKRLSdtvdkLLSESNERLQLHLKERMAALEDKNSLLREVESAKKQLEETQHDKDQLVLN 528
Cdd:pfam05622 314 EDANRRKNELETQNRLA---NQRIL-----ELQQQVEELQKALQEQGSKAEDSSLLKQKLEEHLEKLHEAQSELQKKKEQ 385
|
....*....
gi 578821804 529 IEALRAELD 537
Cdd:pfam05622 386 IEELEPKQD 394
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
145-524 |
1.74e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 49.37 E-value: 1.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 145 KRQAQSPAGVSSEVEVLKALKSLFEHHKALDE--KVRERLRVALERCSLLEEELGATHkelmiLKEQNNQKKtltdgvld 222
Cdd:PTZ00121 1417 KKKADEAKKKAEEKKKADEAKKKAEEAKKADEakKKAEEAKKAEEAKKKAEEAKKADE-----AKKKAEEAK-------- 1483
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 223 iNHEQENTPSTSGKRSSDGSLSHEEDLAKVIELQEIISKQSREQSQMKERlASLSSHVTELEEdldtARK--DLIKSEEM 300
Cdd:PTZ00121 1484 -KADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEE-AKKADEAKKAEE----KKKadELKKAEEL 1557
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 301 ntKLQRDVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQErlelaeqklqq 380
Cdd:PTZ00121 1558 --KKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEE----------- 1624
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 381 tLRKAEtlpeveaELAQRVAALSKsdllssgssaaKEAKLLELTSKLRKAEERHGNIEERLRQMEAQLEEKNQELQRARQ 460
Cdd:PTZ00121 1625 -LKKAE-------EEKKKVEQLKK-----------KEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEE 1685
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 461 REKMNEE------HNKRLSDTVDKLLSESNERLQLHLKERMAALEDKNSLLREVESAKKQLEETQHDKDQ 524
Cdd:PTZ00121 1686 DEKKAAEalkkeaEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEE 1755
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
344-500 |
2.11e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 47.23 E-value: 2.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 344 DKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAEtlpEVEAELAQRVAALSKSDLLSSGSSAAKEAKllEL 423
Cdd:COG1579 20 DRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIK---RLELEIEEVEARIKKYEEQLGNVRNNKEYE--AL 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578821804 424 TSKLRKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSESNERLQLHLKERMAALED 500
Cdd:COG1579 95 QKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAK 171
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
47-538 |
2.30e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.61 E-value: 2.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 47 RDRLLDTLRETQETLALTQGKLHEVG-HERDSLQRQLNTA--LPQEFAALTKELNvcreqllEREEEIAELKAERNNTRL 123
Cdd:COG4717 44 RAMLLERLEKEADELFKPQGRKPELNlKELKELEEELKEAeeKEEEYAELQEELE-------ELEEELEELEAELEELRE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 124 LLEHLECLVSRHERSLRMTVVKRQaqspagvssevevlkaLKSLFEHHKALDEKVRERLRvALERCSLLEEELGATHKEL 203
Cdd:COG4717 117 ELEKLEKLLQLLPLYQELEALEAE----------------LAELPERLEELEERLEELRE-LEEELEELEAELAELQEEL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 204 milkeqnnqkktltdgvldiNHEQENTPSTSGKRSSDGSLSHEEDLAKVIELQEIISKQSREQSQMKERLASLSSHVTEL 283
Cdd:COG4717 180 --------------------EELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 284 EED------------------LDTARKDLIKSEEMNTKLQRDVREAMAqkedMEERITTLEKRYLAAQREATSVHDLNDK 345
Cdd:COG4717 240 ALEerlkearlllliaaallaLLGLGGSLLSLILTIAGVLFLVLGLLA----LLFLLLAREKASLGKEAEELQALPALEE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 346 LENEIAN--KDSMHRQTEDKNRQLQERLELAEQkLQQTLRKAETLpevEAELAQRVAALSKSDLLSSGSSAAKEakllEL 423
Cdd:COG4717 316 LEEEELEelLAALGLPPDLSPEELLELLDRIEE-LQELLREAEEL---EEELQLEELEQEIAALLAEAGVEDEE----EL 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 424 TSKLRKAEERHgNIEERLRQMEAQLEEKNQELQRARQREKmNEEHNKRLSDTVDKLLSESNERLQLH-----LKERMAAL 498
Cdd:COG4717 388 RAALEQAEEYQ-ELKEELEELEEQLEELLGELEELLEALD-EEELEEELEELEEELEELEEELEELReelaeLEAELEQL 465
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 578821804 499 EDKNSL---LREVESAKKQLEETQHDKDQLVLNIEALRAELDH 538
Cdd:COG4717 466 EEDGELaelLQELEELKAELRELAEEWAALKLALELLEEAREE 508
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
418-537 |
2.38e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 47.23 E-value: 2.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 418 AKLLELTSKLRKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEhnkrlsdtvdKLLSESNER----LQL---H 490
Cdd:COG1579 31 AELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEE----------QLGNVRNNKeyeaLQKeieS 100
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 578821804 491 LKERMAALEDK-NSLLREVESAKKQLEETQHDKDQLVLNIEALRAELD 537
Cdd:COG1579 101 LKRRISDLEDEiLELMERIEELEEELAELEAELAELEAELEEKKAELD 148
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
255-467 |
2.60e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.97 E-value: 2.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 255 LQEIISKQSREQSQMKERLASLSSHVTELEEDLDTARKDLIKSEEMNTKLQRDVREAMAQKEDMEERITTLEKRYLAAQR 334
Cdd:COG4372 29 LSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 335 EATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKSDLLSSGSSA 414
Cdd:COG4372 109 EAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDEL 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 578821804 415 AKEAKLLELTSKLRKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEE 467
Cdd:COG4372 189 LKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDA 241
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
169-540 |
3.24e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.60 E-value: 3.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 169 EHHKALDEKVRERLRVALERCSLLEEELGATHKELMILKEQNNQKKTLTDgvLDINHEQENTPSTSGKRSSDGSLSHEED 248
Cdd:PTZ00121 1346 EAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADE--AKKKAEEDKKKADELKKAAAAKKKADEA 1423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 249 LAKVIELQEIISKQSREQSQMKERLASLSSHVTELEEDLDTARKDLIKSEEMNTKLQ--RDVREAMAQKEDMEERITTLE 326
Cdd:PTZ00121 1424 KKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEeaKKADEAKKKAEEAKKKADEAK 1503
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 327 KRYlAAQREATSVHDLNDKLENEIANKDSMHRQTEDKnRQLQERLELAEQKLQQTLRKAETLPEVEA---ELAQRVAALS 403
Cdd:PTZ00121 1504 KAA-EAKKKADEAKKAEEAKKADEAKKAEEAKKADEA-KKAEEKKKADELKKAEELKKAEEKKKAEEakkAEEDKNMALR 1581
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 404 KSDLLSSGSSA-AKEAKLLELTSKLRKAEERHGNIEERLRQMEAQLEEknqELQRARQREKMNEEHNKRLSDTVDKLLSE 482
Cdd:PTZ00121 1582 KAEEAKKAEEArIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAE---EEKKKVEQLKKKEAEEKKKAEELKKAEEE 1658
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 578821804 483 SNERlqlhlkermaaledKNSLLREVESAKKQLEETQHDKDQLVLNIEALRAELDHMR 540
Cdd:PTZ00121 1659 NKIK--------------AAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAK 1702
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
31-460 |
3.91e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 48.19 E-value: 3.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 31 DADSHFEQLMVSMLEERDRLLDTLRETQETLALTQGKLHEVGHERDSLQRQ---LNTALPQEFAAL---TKELNVCREQL 104
Cdd:pfam15921 321 DLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQEsgnLDDQLQKLLADLhkrEKELSLEKEQN 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 105 LE-------REEEIAELKAERNNTRLLLEHLECLVsRHERSLRMTVVKRQAQSPAGVSSEVEVLKALKSLFEHHKALDEK 177
Cdd:pfam15921 401 KRlwdrdtgNSITIDHLRRELDDRNMEVQRLEALL-KAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRK 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 178 VRERL---RVALER---------CSLLEEE--LGATHKELMILKE-------------------QNNQKK--------TL 216
Cdd:pfam15921 480 VVEELtakKMTLESsertvsdltASLQEKEraIEATNAEITKLRSrvdlklqelqhlknegdhlRNVQTEcealklqmAE 559
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 217 TDGVLDINHEQ-ENTPSTSGK--RSSDGSLSHEEDLAKVI-----ELQEIISKQSREQSQMKERLASLSS---------- 278
Cdd:pfam15921 560 KDKVIEILRQQiENMTQLVGQhgRTAGAMQVEKAQLEKEIndrrlELQEFKILKDKKDAKIRELEARVSDlelekvklvn 639
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 279 -------HVTELEEDLD-------TARKDLIKSEEMNTKLQRDVREamaQKEDMEERITTLEKRYLAAQREATSVHDLND 344
Cdd:pfam15921 640 agserlrAVKDIKQERDqllnevkTSRNELNSLSEDYEVLKRNFRN---KSEEMETTTNKLKMQLKSAQSELEQTRNTLK 716
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 345 KLE----NEIANKDSMHRQTEDKNRQ---LQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSksdllssgSSAAKE 417
Cdd:pfam15921 717 SMEgsdgHAMKVAMGMQKQITAKRGQidaLQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVA--------TEKNKM 788
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 578821804 418 AKLLE-LTSKLRKAEERHGNIEERLRQMEAQLEEKNQELQRARQ 460
Cdd:pfam15921 789 AGELEvLRSQERRLKEKVANMEVALDKASLQFAECQDIIQRQEQ 832
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
86-516 |
3.99e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.14 E-value: 3.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 86 LPQEFAALTKELNVCREQLLEREEEIAELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSPAGVSSEVEVLKALK 165
Cdd:PRK03918 312 IEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEK 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 166 SLFEHHKAlDEKVRERLRVALERCSLLEEELGATHKELMILKeqnnqkktltdgvldinheqentpSTSGKRSSDGSLSH 245
Cdd:PRK03918 392 ELEELEKA-KEEIEEEISKITARIGELKKEIKELKKAIEELK------------------------KAKGKCPVCGRELT 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 246 EEDLAkvielqEIISKQSREQSQMKERLASLSSHVTELEEDLDTARKDLIKSEEMntklqRDVREAMAQKEDMEERITTL 325
Cdd:PRK03918 447 EEHRK------ELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESEL-----IKLKELAEQLKELEEKLKKY 515
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 326 EKRYL-AAQREATSVHDLNDKLENEIAN-KDSMHRQTEDKNR--QLQERLELAEQKLQQTLRKAETLP-EVEAELAQRVA 400
Cdd:PRK03918 516 NLEELeKKAEEYEKLKEKLIKLKGEIKSlKKELEKLEELKKKlaELEKKLDELEEELAELLKELEELGfESVEELEERLK 595
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 401 ALSKS-----DLLSSGSSAAKEAKLLE-LTSKLRKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEehNKRLSD 474
Cdd:PRK03918 596 ELEPFyneylELKDAEKELEREEKELKkLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREE--YLELSR 673
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 578821804 475 TVDKLLSESnERLQLHLKERMAALEDKNSLLREVESAKKQLE 516
Cdd:PRK03918 674 ELAGLRAEL-EELEKRREEIKKTLEKLKEELEEREKAKKELE 714
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
207-524 |
4.31e-05 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 47.11 E-value: 4.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 207 KEQNNQKKTLTDGVLDINHEQENTPSTSGKRSSDGSLSHE-----EDLAKVIELQEIISKQSREQSQMKERLASLsshvt 281
Cdd:pfam15905 25 KSQRFRKQKAAESQPNLNNSKDASTPATARKVKSLELKKKsqknlKESKDQKELEKEIRALVQERGEQDKRLQAL----- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 282 elEEDLdtarkdliksEEMNTKLQRDVREamaqKEDMEERITTLEKRylaaQREATSVHDLNDKLENEIANKDSM----- 356
Cdd:pfam15905 100 --EEEL----------EKVEAKLNAAVRE----KTSLSASVASLEKQ----LLELTRVNELLKAKFSEDGTQKKMsslsm 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 357 -----HRQTEDKNRQLQERLELAEQKLQQTLRKaetLPEVEAELAQRVAALSKSDLLSSGSSAAKEaKLLELTSKLRKAE 431
Cdd:pfam15905 160 elmklRNKLEAKMKEVMAKQEGMEGKLQVTQKN---LEHSKGKVAQLEEKLVSTEKEKIEEKSETE-KLLEYITELSCVS 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 432 ERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVD---KLLSESNERLQLHLKERmaaledKNSLLREV 508
Cdd:pfam15905 236 EQVEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQELSKQIKDLNekcKLLESEKEELLREYEEK------EQTLNAEL 309
|
330
....*....|....*...
gi 578821804 509 ESAKKQL--EETQHDKDQ 524
Cdd:pfam15905 310 EELKEKLtlEEQEHQKLQ 327
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
344-517 |
4.63e-05 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 46.21 E-value: 4.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 344 DKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAEtlPEVEAELAQRVAALSKSdllssgsSAAKEAKLLEL 423
Cdd:pfam04012 39 VKARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQAALTKGN--EELAREALAEKKSLEKQ-------AEALETQLAQQ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 424 TSKLRKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEehnkrlsdTVDKLLSESNERLQLHLKERMAALEDKNS 503
Cdd:pfam04012 110 RSAVEQLRKQLAALETKIQQLKAKKNLLKARLKAAKAQEAVQT--------SLGSLSTSSATDSFERIEEKIEEREARAD 181
|
170
....*....|....
gi 578821804 504 LLREVESAKKQLEE 517
Cdd:pfam04012 182 AAAELASAVDLDAK 195
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
129-541 |
4.94e-05 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 47.58 E-value: 4.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 129 ECLVSRHErslrmtVVKRQAQSPAGVSSEVEVLKALKSLFEH-HKALDEKVrERLRVALERCSLLEEELGATHKELMILK 207
Cdd:pfam07888 38 ECLQERAE------LLQAQEAANRQREKEKERYKRDREQWERqRRELESRV-AELKEELRQSREKHEELEEKYKELSASS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 208 EQNNQKKTLTdgvldinheqentpstsgkrssdgSLSHEEDLAKVIELQEIIskqsreqsqmkerlASLSSHVTELEEDL 287
Cdd:pfam07888 111 EELSEEKDAL------------------------LAQRAAHEARIRELEEDI--------------KTLTQRVLERETEL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 288 DtarkdlikseemntKLQRDVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQL 367
Cdd:pfam07888 153 E--------------RMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTL 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 368 QERLELAEQK---LQQTLRKAETLPEVeAELAQRVAALSKSDLLSSGSsaAKEAKLLEL-TSKLRKAEerhgnIEERLRQ 443
Cdd:pfam07888 219 TQKLTTAHRKeaeNEALLEELRSLQER-LNASERKVEGLGEELSSMAA--QRDRTQAELhQARLQAAQ-----LTLQLAD 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 444 MEAQLEEKN----QELQRARQREKMNEEHNKRLSDTVDKLlsesNERLQlhlKERMAALEDKNSLLREVESAKKQLEETQ 519
Cdd:pfam07888 291 ASLALREGRarwaQERETLQQSAEADKDRIEKLSAELQRL----EERLQ---EERMEREKLEVELGREKDCNRVQLSESR 363
|
410 420
....*....|....*....|..
gi 578821804 520 HDKDQLVLNIEALRAELDHMRL 541
Cdd:pfam07888 364 RELQELKASLRVAQKEKEQLQA 385
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
391-540 |
5.05e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.13 E-value: 5.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 391 VEAELAQRVAALSKSDLLSSGSSAakEAKLLELTSKLRKAEERHGNIEERLRQMEAQLEEKNQELQRARQR-EKMNEEHN 469
Cdd:COG3883 12 AFADPQIQAKQKELSELQAELEAA--QAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEiEERREELG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 470 KRLSD---------TVDKLL-SESNERL--QLHLKERMAalEDKNSLLREVESAKKQLEETQHDKDQLVLNIEALRAELD 537
Cdd:COG3883 90 ERARAlyrsggsvsYLDVLLgSESFSDFldRLSALSKIA--DADADLLEELKADKAELEAKKAELEAKLAELEALKAELE 167
|
...
gi 578821804 538 HMR 540
Cdd:COG3883 168 AAK 170
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
250-461 |
5.11e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.07 E-value: 5.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 250 AKVIELQEIISKQSREQSQMKERLASLSSHVTELEEDLDTARKDLIKSEEMNTKLQRDVREamaQKEDMEERITTLEKR- 328
Cdd:COG4942 41 KELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEA---QKEELAELLRALYRLg 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 329 ---YLAAQREATSVHDLNDKLENEiankDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKs 405
Cdd:COG4942 118 rqpPLALLLSPEDFLDAVRRLQYL----KYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEA- 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 578821804 406 dllssgSSAAKEAKLLELTSKLRKAEERHGNIEERLRQMEAQLEEKNQELQRARQR 461
Cdd:COG4942 193 ------LKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| SAM_2 |
pfam07647 |
SAM domain (Sterile alpha motif); |
1152-1222 |
6.10e-05 |
|
SAM domain (Sterile alpha motif);
Pssm-ID: 429573 Cd Length: 66 Bit Score: 42.26 E-value: 6.10e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578821804 1152 VLVWSNDRVIRWILSIGLKEYANNLIESGVHGALLALDETFDFsalalLLQIPTQNTQARAVLEREFNNLL 1222
Cdd:pfam07647 1 VESWSLESVADWLRSIGLEQYTDNFRDQGITGAELLLRLTLED-----LKRLGITSVGHRRKILKKIQELK 66
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
192-519 |
6.68e-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: 47.32 E-value: 6.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 192 LEEELGATHKELMILKEQNNQK----KTLTDGVLDINHEQENTPSTSGKRSSDGSLSHEEDLAKVIELQEIISKQSREQS 267
Cdd:TIGR04523 389 LESQINDLESKIQNQEKLNQQKdeqiKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLET 468
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 268 QMKERLASLSSHVTELEE---DLDTARKDLIKSEEMNTKLQRDVREAMAQKEDMEERITTLEKRYLAAQREatsVHDLND 344
Cdd:TIGR04523 469 QLKVLSRSINKIKQNLEQkqkELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESK---ISDLED 545
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 345 KLENEIANKDSmhRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKSdllssgsSAAKEAKLLELT 424
Cdd:TIGR04523 546 ELNKDDFELKK--ENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKE-------IEEKEKKISSLE 616
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 425 SKLRKAEERHGNIEERLRQMEAQLEEKNQELQRARQ-----REKMNE--EHNKRLSDTVD---KLLSESNERLQLHLKER 494
Cdd:TIGR04523 617 KELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKEtikeiRNKWPEiiKKIKESKTKIDdiiELMKDWLKELSLHYKKY 696
|
330 340
....*....|....*....|....*
gi 578821804 495 MAALEDKNSLLREVESAKKQLEETQ 519
Cdd:TIGR04523 697 ITRMIRIKDLPKLEEKYKEIEKELK 721
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
358-550 |
6.99e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.60 E-value: 6.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 358 RQTEDKNRQLQE---RLELAEQKLQQTLRKAETL---PEVEAELAQRVAALSKSDLLSSGSSA-AKEAKLLELTSKLRKA 430
Cdd:COG4913 221 PDTFEAADALVEhfdDLERAHEALEDAREQIELLepiRELAERYAAARERLAELEYLRAALRLwFAQRRLELLEAELEEL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 431 EERHGNIEERLRQMEAQLEEKNQELQRARQR------------EKMNEEHNKRLSDTVDKL--LSESNERLQLHLKERMA 496
Cdd:COG4913 301 RAELARLEAELERLEARLDALREELDELEAQirgnggdrleqlEREIERLERELEERERRRarLEALLAALGLPLPASAE 380
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 578821804 497 ALEDKNSLLRE-VESAKKQLEETQHDKDQLVLNIEALRAELDHMRLRGASLHHGR 550
Cdd:COG4913 381 EFAALRAEAAAlLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRK 435
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
37-478 |
8.04e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 47.24 E-value: 8.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 37 EQLMVSMLEERDRLLDTLRETQETLALTQGKLHEVGHERDSLQRQLNTALPQEFAALTKELNVCREQLLEREEEIAELKA 116
Cdd:COG1196 371 EAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEE 450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 117 ERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSPAGV-SSEVEVLKALKSLFEHH-----KALDEKVRERLRVALERCS 190
Cdd:COG1196 451 EAELEEEEEALLELLAELLEEAALLEAALAELLEELAEaAARLLLLLEAEADYEGFlegvkAALLLAGLRGLAGAVAVLI 530
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 191 LLEEELGATHKELMILKEQNNQKKTLTDGVLDINHEQEN-----TPSTSGKRSSDGSLSHEEDLAKVIELQEIISKQSRE 265
Cdd:COG1196 531 GVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAkagraTFLPLDKIRARAALAAALARGAIGAAVDLVASDLRE 610
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 266 QSQMKERLASLSSHVTELEEDLDTARKDLIKSEEMNTKLQRDVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDK 345
Cdd:COG1196 611 ADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAE 690
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 346 LENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKSDLLSSGSSAAKEAKLLELTS 425
Cdd:COG1196 691 EELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELE 770
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578821804 426 KLRKAEERHGNI-----------EERLRQMEAQLEeknqELQRARQR-----EKMNEEHNKRLSDTVDK 478
Cdd:COG1196 771 RLEREIEALGPVnllaieeyeelEERYDFLSEQRE----DLEEARETleeaiEEIDRETRERFLETFDA 835
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
423-542 |
9.51e-05 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 45.20 E-value: 9.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 423 LTSKLRKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLlsesNERLQLHLK---ERMA--A 497
Cdd:COG1842 14 INALLDKAEDPEKMLDQAIRDMEEDLVEARQALAQVIANQKRLERQLEELEAEAEKW----EEKARLALEkgrEDLAreA 89
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 578821804 498 LEDKNSLLREVESAKKQLEETQHDKDQLVLNIEALRAELDHMRLR 542
Cdd:COG1842 90 LERKAELEAQAEALEAQLAQLEEQVEKLKEALRQLESKLEELKAK 134
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
366-536 |
1.27e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.92 E-value: 1.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 366 QLQERLELAE--QKLQQTLRKAETLPEVEAELAQRVAALSKSdllssgsSAAKEAKLLELTSKLRKAEERHGNIEERLRQ 443
Cdd:COG1579 5 DLRALLDLQEldSELDRLEHRLKELPAELAELEDELAALEAR-------LEAAKTELEDLEKEIKRLELEIEEVEARIKK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 444 MEAQLEE-KNQELQRARQREKmnEEHNKRLSDTVDKLLsESNERLQlHLKERMAALEDK-NSLLREVESAKKQLEETQHD 521
Cdd:COG1579 78 YEEQLGNvRNNKEYEALQKEI--ESLKRRISDLEDEIL-ELMERIE-ELEEELAELEAElAELEAELEEKKAELDEELAE 153
|
170
....*....|....*
gi 578821804 522 KDQLVLNIEALRAEL 536
Cdd:COG1579 154 LEAELEELEAEREEL 168
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
154-542 |
1.67e-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: 46.25 E-value: 1.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 154 VSSEVEVLKALKSLFEHHKALD--EKVRERLRVALERCSLLEEELGATHKELMilkEQNNQKKTLTDGVldinheqENTP 231
Cdd:pfam05483 95 VSIEAELKQKENKLQENRKIIEaqRKAIQELQFENEKVSLKLEEEIQENKDLI---KENNATRHLCNLL-------KETC 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 232 STSGKRSSDGSLSHEEDLAKVIELQEIISKqsreqsqmkerlasLSSHVTELEEDLDTARKdlikseEMNTKLQRDVREA 311
Cdd:pfam05483 165 ARSAEKTKKYEYEREETRQVYMDLNNNIEK--------------MILAFEELRVQAENARL------EMHFKLKEDHEKI 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 312 MAQKEDMEERITTLEKRYLAAQREATsvhdlndKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRK----AET 387
Cdd:pfam05483 225 QHLEEEYKKEINDKEKQVSLLLIQIT-------EKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKkdhlTKE 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 388 LPEVEAELAQRVA---ALSKSDLLSSGS----SAAKEAKLLELTsklrKAEERHGNIEERLRQMEAQLEEKnqeLQRARQ 460
Cdd:pfam05483 298 LEDIKMSLQRSMStqkALEEDLQIATKTicqlTEEKEAQMEELN----KAKAAHSFVVTEFEATTCSLEEL---LRTEQQ 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 461 REKMNEEHNKRLSDTVDKLLSESNERLQL------HLKERMAALEDKNSLLREVESAKKQLEETQHDKDQLVLNIEALRA 534
Cdd:pfam05483 371 RLEKNEDQLKIITMELQKKSSELEEMTKFknnkevELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREK 450
|
....*...
gi 578821804 535 ELDHMRLR 542
Cdd:pfam05483 451 EIHDLEIQ 458
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
193-517 |
1.89e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 45.94 E-value: 1.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 193 EEELGATHKELMILKEQNNQ-KKTLTDgvldinHEQENTPSTSGKRSSDGSLSHEEDL------------AKVIELQEII 259
Cdd:pfam01576 4 EEEMQAKEEELQKVKERQQKaESELKE------LEKKHQQLCEEKNALQEQLQAETELcaeaeemrarlaARKQELEEIL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 260 --------SKQSREQSQMKERlASLSSHVTELEEDLDtarkdliKSEEMNTKLQRDVREAMAQKEDMEERITTLEKRYLA 331
Cdd:pfam01576 78 helesrleEEEERSQQLQNEK-KKMQQHIQDLEEQLD-------EEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 332 AQREATSVHDLNDKLENEIANKDSMHRQ-TEDKNRQ------LQERLElAEQKLQQTLRKAETLPEVEA-ELAQRVAALS 403
Cdd:pfam01576 150 LSKERKLLEERISEFTSNLAEEEEKAKSlSKLKNKHeamisdLEERLK-KEEKGRQELEKAKRKLEGEStDLQEQIAELQ 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 404 KSDLLSSGSSAAKEAKLLELTSKLRKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSEs 483
Cdd:pfam01576 229 AQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTE- 307
|
330 340 350
....*....|....*....|....*....|....
gi 578821804 484 nerLQLHLKERMAALEDKNSLLREVESAKKQLEE 517
Cdd:pfam01576 308 ---LEDTLDTTAAQQELRSKREQEVTELKKALEE 338
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
160-688 |
1.93e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 46.12 E-value: 1.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 160 VLKALKSLFEHHKALDEK--VRERLRVALERCSLLEEELGATHKELMILKEQNNQKKTLTDGVLDINHEQENTPSTSGKR 237
Cdd:pfam02463 228 YLDYLKLNEERIDLLQELlrDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLER 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 238 SSDGSLS----HEEDLAKVIELQEIISKQSREQSQMKERL----ASLSSHVTELEEDLDTARKDLIKSEEMNTKLQRDVR 309
Cdd:pfam02463 308 RKVDDEEklkeSEKEKKKAEKELKKEKEEIEELEKELKELeikrEAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLS 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 310 EAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIANKDSM--HRQTEDKNRQLQERLELAEQKL-QQTLRKAE 386
Cdd:pfam02463 388 SAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEeeESIELKQGKLTEEKEELEKQELkLLKDELEL 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 387 TLPEVEAELAQRVAALSKSDLLSSgssaakEAKLLELTSKLRKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNE 466
Cdd:pfam02463 468 KKSEDLLKETQLVKLQEQLELLLS------RQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENY 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 467 EHNKRLSDTVDkllsESNERLQLHLKERMAALEDKNSLLREVESAKKQLEETQHDKDQLVLNIEALRAELDHMRLRGASL 546
Cdd:pfam02463 542 KVAISTAVIVE----VSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADE 617
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 547 HHGRPHLGSVPDFRFPMADGHTDSYSTSAVLRRPQ---KGRLAALRDEPSKVQTLNEQDWERAQQASVLANVAQAFESDA 623
Cdd:pfam02463 618 DDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVsleEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRR 697
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578821804 624 DVSDGEDDRDTLLSSVDLLspsgQADAHTLAMMLQEQLDAINKEIRLIQEEKENTEQRAEEIESR 688
Cdd:pfam02463 698 QLEIKKKEQREKEELKKLK----LEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLK 758
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
315-546 |
1.96e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 46.06 E-value: 1.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 315 KEDMEERITTLEKRYLAAQREATSVHDLNDKLEnEIANKDsmhrQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEA- 393
Cdd:PRK11281 38 EADVQAQLDALNKQKLLEAEDKLVQQDLEQTLA-LLDKID----RQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDe 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 394 ELAQRVAALSksdllssgssaakeaklleltsklrkaeerhgnieerLRQMEAQLEEKNQELQRARqrekmneehnKRLS 473
Cdd:PRK11281 113 ETRETLSTLS-------------------------------------LRQLESRLAQTLDQLQNAQ----------NDLA 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578821804 474 DTVDKLLSESN--ERLQLHLKERMAALEDKNSLLREVESAKKQLEETQhdKDQLVLNIEALRAELDHMR--LRGASL 546
Cdd:PRK11281 146 EYNSQLVSLQTqpERAQAALYANSQRLQQIRNLLKGGKVGGKALRPSQ--RVLLQAEQALLNAQNDLQRksLEGNTQ 220
|
|
| SAM_STIM-1,2-like |
cd09504 |
SAM domain of STIM-1,2-like proteins; SAM (sterile alpha motif) domain of STIM-1,2-like ... |
952-1010 |
2.15e-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: 40.78 E-value: 2.15e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578821804 952 WDGPTVVVWLELWVGMPAwYVAACRANVKSGAIMSALSDTE---IQREIGISNPLHRLKLRL 1010
Cdd:cd09504 5 WTVEDTVEWLVNSVELPQ-YVEAFKENGVDGSALPRLAVNNpsfLTSVLGIKDPIHRQKLSL 65
|
|
| RNase_Y_N |
pfam12072 |
RNase Y N-terminal region; |
365-531 |
2.36e-04 |
|
RNase Y N-terminal region;
Pssm-ID: 463456 [Multi-domain] Cd Length: 201 Bit Score: 43.72 E-value: 2.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 365 RQLQERLELAEQKLQQTLRKAETLPEvEAEL-AQRVAALSKSDLlssgssaakEAKLLELTSKLRKAEERHGNIEERLRQ 443
Cdd:pfam12072 27 AKIGSAEELAKRIIEEAKKEAETKKK-EALLeAKEEIHKLRAEA---------ERELKERRNELQRQERRLLQKEETLDR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 444 MEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSESNERLqlhlkERMAAL---EDKNSLLREVEsakkqlEETQH 520
Cdd:pfam12072 97 KDESLEKKEESLEKKEKELEAQQQQLEEKEEELEELIEEQRQEL-----ERISGLtseEAKEILLDEVE------EELRH 165
|
170
....*....|.
gi 578821804 521 DKDQLVLNIEA 531
Cdd:pfam12072 166 EAAVMIKEIEE 176
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
244-510 |
2.50e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 45.55 E-value: 2.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 244 SHEEDLakvIELQEIISKQSREQSQMKERLASLSSHVTELEEDLDTARKDLIKSEEMNT--------------------- 302
Cdd:pfam01576 135 KLEEDI---LLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISdleerlkkeekgrqelekakr 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 303 KLQRDVREAMAQKEDMEERITTL-------EKRYLAAQ-----------------REATS-VHDLNDKLENEIAnkdsMH 357
Cdd:pfam01576 212 KLEGESTDLQEQIAELQAQIAELraqlakkEEELQAALarleeetaqknnalkkiRELEAqISELQEDLESERA----AR 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 358 RQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKSDLLSSGSSAAK--------EAKLLELTSKLRK 429
Cdd:pfam01576 288 NKAEKQRRDLGEELEALKTELEDTLDTTAAQQELRSKREQEVTELKKALEEETRSHEAQlqemrqkhTQALEELTEQLEQ 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 430 AEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSESN--ERLQLHLKERMAA----LEDKNS 503
Cdd:pfam01576 368 AKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSesERQRAELAEKLSKlqseLESVSS 447
|
....*..
gi 578821804 504 LLREVES 510
Cdd:pfam01576 448 LLNEAEG 454
|
|
| SAM_2 |
pfam07647 |
SAM domain (Sterile alpha motif); |
1074-1129 |
2.51e-04 |
|
SAM domain (Sterile alpha motif);
Pssm-ID: 429573 Cd Length: 66 Bit Score: 40.33 E-value: 2.51e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 578821804 1074 EWLPSLGLPQYRSYFMECLVD-ARMLDHLTKKDLrGQLKMVDSFHRNSFQCGIMCLR 1129
Cdd:pfam07647 11 DWLRSIGLEQYTDNFRDQGITgAELLLRLTLEDL-KRLGITSVGHRRKILKKIQELK 66
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
172-546 |
2.70e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.14 E-value: 2.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 172 KALDEKVRErLRVALERCSLLEEELGATHKELMILKEQnnqKKTLTDGVLDINHEQENTPSTSGKRSSDGSLSH------ 245
Cdd:COG4717 74 KELEEELKE-AEEKEEEYAELQEELEELEEELEELEAE---LEELREELEKLEKLLQLLPLYQELEALEAELAElperle 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 246 --EEDLAKVIELQEIISKQSREQSQMKERLASLSSHVT-ELEEDLDTARKDLIKSEEMNTKLQRDVREAMAQKEDMEERI 322
Cdd:COG4717 150 elEERLEELRELEEELEELEAELAELQEELEELLEQLSlATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEEL 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 323 TTLEKRYLAAQREAT------------------SVHDLNDKLENEIA------------------NKDSMHRQTEDKNRQ 366
Cdd:COG4717 230 EQLENELEAAALEERlkearlllliaaallallGLGGSLLSLILTIAgvlflvlgllallflllaREKASLGKEAEELQA 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 367 LQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKS--DLLSSGSSAAKEAKLLELTSKLRK-AEERHGNIEERLRQ 443
Cdd:COG4717 310 LPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEElqELLREAEELEEELQLEELEQEIAAlLAEAGVEDEEELRA 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 444 MEAQLEEKNQELQRARQREKMNEEHNK----RLSDTVDKLLSESNERLQLHLKERMAALEDKNSLLREVESAKKQLEEtQ 519
Cdd:COG4717 390 ALEQAEEYQELKEELEELEEQLEELLGeleeLLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEE-D 468
|
410 420
....*....|....*....|....*..
gi 578821804 520 HDKDQLVLNIEALRAELDHMRLRGASL 546
Cdd:COG4717 469 GELAELLQELEELKAELRELAEEWAAL 495
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
245-485 |
4.05e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 44.53 E-value: 4.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 245 HEEDLAKVIELQEI-----ISKQSREQSQMKERLASLSSHVTELEEDLDTARK-------DLIKSEEMNT-KLQRDVREA 311
Cdd:PRK05771 26 HELGVVHIEDLKEElsnerLRKLRSLLTKLSEALDKLRSYLPKLNPLREEKKKvsvksleELIKDVEEELeKIEKEIKEL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 312 MAQKEDMEERITTLEKRylaaQREATSVHDLNDKLENEIANKdSMHRQTEDKNRQLQERLELAEqklqqTLRKAETLPEV 391
Cdd:PRK05771 106 EEEISELENEIKELEQE----IERLEPWGNFDLDLSLLLGFK-YVSVFVGTVPEDKLEELKLES-----DVENVEYISTD 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 392 EAELAqrVAALSKSDLLSSgssAAKEAKLLELtskLRKAEERHGNIEERLRQMEAQLEEKNQELQRARQR-EKMNEEHNK 470
Cdd:PRK05771 176 KGYVY--VVVVVLKELSDE---VEEELKKLGF---ERLELEEEGTPSELIREIKEELEEIEKERESLLEElKELAKKYLE 247
|
250
....*....|....*
gi 578821804 471 RLSDTVDKLLSESNE 485
Cdd:PRK05771 248 ELLALYEYLEIELER 262
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
134-484 |
4.45e-04 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 44.47 E-value: 4.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 134 RHERSLRMTVvkRQAQSPAGVSSEVEVLKAlKSLFEHHKALDEKVRERLRvalERCSLLEEELGATHKELMILKEQNNQK 213
Cdd:pfam02029 13 RRAREERRRQ--KEEEEPSGQVTESVEPNE-HNSYEEDSELKPSGQGGLD---EEEAFLDRTAKREERRQKRLQEALERQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 214 K----TLTDGVLDINHEQENTPSTSGKRSSDGSLSHEEDLAKVIELQEIISKQSREQ--SQMKERLASLSSHVTELEEDL 287
Cdd:pfam02029 87 KefdpTIADEKESVAERKENNEEEENSSWEKEEKRDSRLGRYKEEETEIREKEYQENkwSTEVRQAEEEGEEEEDKSEEA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 288 DTARKDLIKSEEM---NTKLQRDVREAMAQKEDMEERITTLekrylAAQREATSVHDLNDKLENEIANKDSMHRQTEDKN 364
Cdd:pfam02029 167 EEVPTENFAKEEVkdeKIKKEKKVKYESKVFLDQKRGHPEV-----KSQNGEEEVTKLKVTTKRRQGGLSQSQEREEEAE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 365 RQLQerlelAEQKLQQTLRKAETLPEVEAE-LAQRVAalsksdllssgssaakEAKLlELTSKLRKAEERHGNIEERLRQ 443
Cdd:pfam02029 242 VFLE-----AEQKLEELRRRRQEKESEEFEkLRQKQQ----------------EAEL-ELEELKKKREERRKLLEEEEQR 299
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 578821804 444 MEAqlEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSESN 484
Cdd:pfam02029 300 RKQ--EEAERKLREEEEKRRMKEEIERRRAEAAEKRQKLPE 338
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
163-455 |
4.59e-04 |
|
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: 44.81 E-value: 4.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 163 ALKSLFEhhkALDEKVR--ERLRVALER-CSLLEEELGATHKELMILKEQ-NNQKKTLTDGVLDINHEQENTPS------ 232
Cdd:pfam10174 437 ALTTLEE---ALSEKERiiERLKEQREReDRERLEELESLKKENKDLKEKvSALQPELTEKESSLIDLKEHASSlassgl 513
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 233 --TSGKRSSDGSLSHEEDLAKVIELQEIISKQSREQSQMKErlaSLSSHVTELEEDLDTARKDLIKSEEMNTKLQRDVRE 310
Cdd:pfam10174 514 kkDSKLKSLEIAVEQKKEECSKLENQLKKAHNAEEAVRTNP---EINDRIRLLEQEVARYKEESGKAQAEVERLLGILRE 590
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 311 AMAQKEDMEERITTLEKRYLAAQREATSvhdlndklenEIANKDSMhrQTEDKNRQLQErlelaeqkLQQTLRKAETLPE 390
Cdd:pfam10174 591 VENEKNDKDKKIAELESLTLRQMKEQNK----------KVANIKHG--QQEMKKKGAQL--------LEEARRREDNLAD 650
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578821804 391 VEAE--LAQRVAALSKSDLlssgssaAKEAKLLELTSKLRKAEERHGNIE----ERLRQMEAQLEEKNQEL 455
Cdd:pfam10174 651 NSQQlqLEELMGALEKTRQ-------ELDATKARLSSTQQSLAEKDGHLTnlraERRKQLEEILEMKQEAL 714
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
44-450 |
4.62e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.37 E-value: 4.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 44 LEERDRLLDTLRETQETLALTQGKLHEVGHERDSLQRQLNTALPQEFAALTKELNVCREQLLEREEEIAELKAERNNTRL 123
Cdd:COG4717 148 LEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEE 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 124 LLEHLECLVSRHERSLRmtvVKRQAQSPAGVSSEVEVLKALKSLFEHHKALDEKVRERLRVALERCSLLEEELGATHKEL 203
Cdd:COG4717 228 ELEQLENELEAAALEER---LKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEA 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 204 MILKEQNNQKKTltdgvldinhEQENTPSTSGKRSSDGSLSHEEDLAKVIELQEIISKQSREQSQMKErlASLSSHVTEL 283
Cdd:COG4717 305 EELQALPALEEL----------EEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEE--LQLEELEQEI 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 284 EEDLDTARKDLIKSEEMNTKLQRDVREAMAQKEDMEERITTLEKRYLAAQREATSvhdlnDKLENEIANKDSMHRQTEDK 363
Cdd:COG4717 373 AALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDE-----EELEEELEELEEELEELEEE 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 364 NRQLQERLELAEQKLQQtLRKAETLPEVEAELAQRVAALsksdllssgSSAAKEAKLLELTSK-LRKAEERHgnIEERLR 442
Cdd:COG4717 448 LEELREELAELEAELEQ-LEEDGELAELLQELEELKAEL---------RELAEEWAALKLALElLEEAREEY--REERLP 515
|
....*...
gi 578821804 443 QMEAQLEE 450
Cdd:COG4717 516 PVLERASE 523
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
222-501 |
4.65e-04 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 44.51 E-value: 4.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 222 DINHEQENTPSTSGKRSSDGSLSHEED--LAKVIELQEIISKQSREQSQMKERLASLSSHVTELEEDLDTARKDLIKSEE 299
Cdd:PLN02939 70 DENGQLENTSLRTVMELPQKSTSSDDDhnRASMQRDEAIAAIDNEQQTNSKDGEQLSDFQLEDLVGMIQNAEKNILLLNQ 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 300 MNTKLQRDVREAMAQKEDMEERITTLEKRY--------LAAQrEATSVHDLNDKLENeiANKDSMHRQTEDKNRQLQERL 371
Cdd:PLN02939 150 ARLQALEDLEKILTEKEALQGKINILEMRLsetdarikLAAQ-EKIHVEILEEQLEK--LRNELLIRGATEGLCVHSLSK 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 372 ELAEQKLQQTLRKA------ETLPEVeAELAQRVAALSKsdllssgSSAAKEAKLLELTSKLRKAEERHGNIEErlRQME 445
Cdd:PLN02939 227 ELDVLKEENMLLKDdiqflkAELIEV-AETEERVFKLEK-------ERSLLDASLRELESKFIVAQEDVSKLSP--LQYD 296
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578821804 446 AqLEEKNQELQRARQREKMNEEH-------NKRLSDTVDKL---LSESN------ERLQLhLKERMAALEDK 501
Cdd:PLN02939 297 C-WWEKVENLQDLLDRATNQVEKaalvldqNQDLRDKVDKLeasLKEANvskfssYKVEL-LQQKLKLLEER 366
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
176-353 |
4.68e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.98 E-value: 4.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 176 EKVRERLRVALERCSLLEEELGATHKELMILKEQNNQKKTLTDGVLDINHEQENTPSTSGKRSSDGSLSHEEDLAKVIEL 255
Cdd:COG4942 58 AALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRR 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 256 QEIISKQSREQSQMKERLASLSSHVTELEEDLDTARKDLIKSEEMNTKLQRDVREAMAQKEDM----EERITTLEKRYLA 331
Cdd:COG4942 138 LQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLlarlEKELAELAAELAE 217
|
170 180
....*....|....*....|..
gi 578821804 332 AQREATSVHDLNDKLENEIANK 353
Cdd:COG4942 218 LQQEAEELEALIARLEAEAAAA 239
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
177-564 |
5.00e-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: 44.83 E-value: 5.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 177 KVRERLRVALERCSLLEEELGATHKEL------MILKEQNNQKKTLTDGVLDINHEQE----NTPSTSGKRSSDGSLSHE 246
Cdd:pfam12128 608 KAEEALQSAREKQAAAEEQLVQANGELekasreETFARTALKNARLDLRRLFDEKQSEkdkkNKALAERKDSANERLNSL 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 247 EDLAKVIELQEIISKQSrEQSQMKERLASLSSHVTELEEDLDtARKDLIKSEEMNTKLQRDVReamaQKEDMEERITTLE 326
Cdd:pfam12128 688 EAQLKQLDKKHQAWLEE-QKEQKREARTEKQAYWQVVEGALD-AQLALLKAAIAARRSGAKAE----LKALETWYKRDLA 761
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 327 KRYLAAQREAtsvhdlndKLENEIANkdsMHRQTEDKNRQLQERLE----LAEQKLQQTLRKAETLPEVEAELaqrvaal 402
Cdd:pfam12128 762 SLGVDPDVIA--------KLKREIRT---LERKIERIAVRRQEVLRyfdwYQETWLQRRPRLATQLSNIERAI------- 823
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 403 skSDLLSsgssaakeakllELTSKLRKAEERHGNIEERLRQMEAQLEEKNQELQRARQR-EKMNEEHnkrlsdtvdklLS 481
Cdd:pfam12128 824 --SELQQ------------QLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEmSKLATLK-----------ED 878
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 482 ESNERLQLHLKERMAALED-KNSLLREVESAKKQLEE-----TQHDKDQLVLNIEALRAELDHMRLRGASLHHGRPHLGS 555
Cdd:pfam12128 879 ANSEQAQGSIGERLAQLEDlKLKRDYLSESVKKYVEHfknviADHSGSGLAETWESLREEDHYQNDKGIRLLDYRKLVPY 958
|
....*....
gi 578821804 556 VPDFRFPMA 564
Cdd:pfam12128 959 LEQWFDVRV 967
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
268-539 |
5.87e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 44.40 E-value: 5.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 268 QMKERLASLSSHVTELEEDLDTARKDLIKSEEMNTKLQRDVREAMAQKEDM-------EERITTLEKRYL-------AAQ 333
Cdd:pfam01576 774 KLELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARASRDEIlaqskesEKKLKNLEAELLqlqedlaASE 853
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 334 REATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSkSDLLSSGSS 413
Cdd:pfam01576 854 RARRQAQQERDELADEIASGASGKSALQDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLT-TELAAERST 932
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 414 AAK---------------EAKLLELTSKLR-KAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEehnKRLSDTVd 477
Cdd:pfam01576 933 SQKsesarqqlerqnkelKAKLQEMEGTVKsKFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTE---KKLKEVL- 1008
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578821804 478 kLLSESNERLQLHLKERMaalEDKNSLLREVesaKKQLEETQHDKDQLVLNIEALRAELDHM 539
Cdd:pfam01576 1009 -LQVEDERRHADQYKDQA---EKGNSRMKQL---KRQLEEAEEEASRANAARRKLQRELDDA 1063
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
297-531 |
6.42e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.74 E-value: 6.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 297 SEEMNTKLQRDVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQ 376
Cdd:COG4372 1 GDRLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 377 KLQQTLRKAETLPEVEAELAQRVAALSKsdllssgSSAAKEAKLLELTSKLRKAEERHGNIEERLRQMEAQLEEKNQELQ 456
Cdd:COG4372 81 ELEELNEQLQAAQAELAQAQEELESLQE-------EAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELK 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578821804 457 RARQREKMNEEHNKRLSDTVDKL-LSESNERLQLHLKERMAALEDKNSLLREVESAKKQLEETQHDKDQLVLNIEA 531
Cdd:COG4372 154 ELEEQLESLQEELAALEQELQALsEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEA 229
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
260-519 |
6.68e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.36 E-value: 6.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 260 SKQSREQSQMKERLAslsshvTELEEDLDTARKDLIKSEEMNTKLQRDVREAMAQKED---MEERITTLEKRYLAAQREA 336
Cdd:PTZ00121 1075 SYKDFDFDAKEDNRA------DEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDarkAEEARKAEDARKAEEARKA 1148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 337 TSVHDLNDKLENEIANKDSMHRQTEDKnRQLQERLELAEQKLQQTLRKAETLPEVEAelAQRVAALSKsdllssgssaAK 416
Cdd:PTZ00121 1149 EDAKRVEIARKAEDARKAEEARKAEDA-KKAEAARKAEEVRKAEELRKAEDARKAEA--ARKAEEERK----------AE 1215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 417 EAKLLEltsKLRKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSESNERLQLHLKERMA 496
Cdd:PTZ00121 1216 EARKAE---DAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKA 1292
|
250 260
....*....|....*....|...
gi 578821804 497 ALEDKNSLLREVESAKKQLEETQ 519
Cdd:PTZ00121 1293 DEAKKAEEKKKADEAKKKAEEAK 1315
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
113-462 |
8.07e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 43.81 E-value: 8.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 113 ELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSPAGVSSEVEVLKALKSLFEHHKALDEKVRERLRVALERCSLL 192
Cdd:pfam02463 674 ELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEE 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 193 EEELGATHKELMILKEQNNQKKTLTDGVLDINHEQEntpstsgKRSSDGSLSHEEDLAKVIELQEIISKQSREQSQMKER 272
Cdd:pfam02463 754 KSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVE-------EEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQ 826
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 273 LASLSSHVTELEEDLDTARKDLIKSEEMNTKLQRD---VREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKL--- 346
Cdd:pfam02463 827 EEKIKEEELEELALELKEEQKLEKLAEEELERLEEeitKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEees 906
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 347 ---------ENEIANKDSMHRQTEDKNRQLQERLELAEQKLQqtlRKAETLPEVEAELAQRvaALSKSDLLSSGSSAAKE 417
Cdd:pfam02463 907 qklnlleekENEIEERIKEEAEILLKYEEEPEELLLEEADEK---EKEENNKEEEEERNKR--LLLAKEELGKVNLMAIE 981
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 578821804 418 AKLLELTSKLRKAEERHGNIEERLRQMEAQLEEKNQELQRARQRE 462
Cdd:pfam02463 982 EFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLELF 1026
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
256-472 |
1.01e-03 |
|
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.
Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 43.10 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 256 QEIISKQSREQSQMKERLASLSShvtELEEDLDTARKDLIKSEEmntKLQRDVREAMAQKEDMEERittleKRYLAAQRE 335
Cdd:pfam15558 54 LLLQQSQEQWQAEKEQRKARLGR---EERRRADRREKQVIEKES---RWREQAEDQENQRQEKLER-----ARQEAEQRK 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 336 ATSVHDLNDKLENEiankdsmHRQTEDKNRQLQERLELAEQKLQqtLRKAETLPEVEAE-LAQRVAALSKSDLLSSGSSA 414
Cdd:pfam15558 123 QCQEQRLKEKEEEL-------QALREQNSLQLQERLEEACHKRQ--LKEREEQKKVQENnLSELLNHQARKVLVDCQAKA 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 415 AKEAKLLELTSKLRKAEERH-GNIEERLRQMEAQLEEKNQELQRARQR-EKMNEEHNKRL 472
Cdd:pfam15558 194 EELLRRLSLEQSLQRSQENYeQLVEERHRELREKAQKEEEQFQRAKWRaEEKEEERQEHK 253
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
206-683 |
1.20e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 43.42 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 206 LKEQNNQKKTLTDGVLDIN-HEQENTPSTSGKRSSDGSLSHEEDLAKVIEL---QEIISKQSREQSQMKErLASLSSHVT 281
Cdd:TIGR00618 158 LKAKSKEKKELLMNLFPLDqYTQLALMEFAKKKSLHGKAELLTLRSQLLTLctpCMPDTYHERKQVLEKE-LKHLREALQ 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 282 ELEEDLDTARKDLIKSEEmNTKLQRDVREAMAQkedmEERITTLEKRyLAAQREATSVHDLNDKLENEIANKDSMHRQTE 361
Cdd:TIGR00618 237 QTQQSHAYLTQKREAQEE-QLKKQQLLKQLRAR----IEELRAQEAV-LEETQERINRARKAAPLAAHIKAVTQIEQQAQ 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 362 DKNRQLQERLELAEQKLQQTlrkaetlpevEAELAQRVAALSKSDLLSSGSSAAKEAKLLELTSKLRKAE-ERHGNIEER 440
Cdd:TIGR00618 311 RIHTELQSKMRSRAKLLMKR----------AAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREIsCQQHTLTQH 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 441 LRQMEAQLEEKNQELQRARQR-EKMNEEHNKRLSDTVD---------------KLLSESNERLQLHLKERMAALEDKNSL 504
Cdd:TIGR00618 381 IHTLQQQKTTLTQKLQSLCKElDILQREQATIDTRTSAfrdlqgqlahakkqqELQQRYAELCAAAITCTAQCEKLEKIH 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 505 LREVESAKKQLEETQHDKDQLVLNIEALRAELDHMRLRGASLHhgRPHLGSVPDFRFPMadghTDSYSTSAVLRRPQKG- 583
Cdd:TIGR00618 461 LQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEP--CPLCGSCIHPNPAR----QDIDNPGPLTRRMQRGe 534
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 584 -RLAALRDEPSKV----QTLNEQDWERAQQASVLANVAQAFESDADVSdgEDDRDTLLSSVDLLSPSGQADA-------- 650
Cdd:TIGR00618 535 qTYAQLETSEEDVyhqlTSERKQRASLKEQMQEIQQSFSILTQCDNRS--KEDIPNLQNITVRLQDLTEKLSeaedmlac 612
|
490 500 510
....*....|....*....|....*....|....*
gi 578821804 651 --HTLAMMLQEQLDaiNKEIRLIQEEKENTEQRAE 683
Cdd:TIGR00618 613 eqHALLRKLQPEQD--LQDVRLHLQQCSQELALKL 645
|
|
| SAM_SARM1-like_repeat1 |
cd09501 |
SAM domain ot SARM1-like proteins, repeat 1; SAM (sterile alpha motif) domain repeat 1 of ... |
1074-1121 |
1.93e-03 |
|
SAM domain ot SARM1-like proteins, repeat 1; SAM (sterile alpha motif) domain repeat 1 of SARM1-like adaptor proteins is a protein-protein interaction domain. SARM1-like proteins contain two tandem SAM domains. SARM1-like proteins are involved in TLR (Toll-like receptor) signaling. They are responsible for targeted localization of the whole protein to post-synaptic regions of axons. In humans SARM1 expression is detected in kidney and liver.
Pssm-ID: 188900 [Multi-domain] Cd Length: 69 Bit Score: 38.05 E-value: 1.93e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 578821804 1074 EWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRGQLKMVDSFHRNSF 1121
Cdd:cd09501 11 TWLKQIGFEDYAEKFSESQVDGDLLLQLTEDELKQDLGMSSGLLRKRF 58
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
321-555 |
2.29e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 42.19 E-value: 2.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 321 RITTLEKRYLAAQREATSVHDL----NDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELA 396
Cdd:pfam07888 28 RAELLQNRLEECLQERAELLQAqeaaNRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 397 QRVAALSKSDLLSSGSSAAKEAKLLELtsklrkaeerhgniEERLRQMEAQLEEKNQELQRARQREKM------NEEHNK 470
Cdd:pfam07888 108 ASSEELSEEKDALLAQRAAHEARIREL--------------EEDIKTLTQRVLERETELERMKERAKKagaqrkEEEAER 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 471 RLSDTVDKLLSESNERLQLHLKERMAALEDKNSLLREVESAKKQLEETQHDKDQLVLNIEALRAELDHMRLRGASLHHGR 550
Cdd:pfam07888 174 KQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKV 253
|
....*
gi 578821804 551 PHLGS 555
Cdd:pfam07888 254 EGLGE 258
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
264-447 |
2.39e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 42.31 E-value: 2.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 264 REQSQMKERLASLSSHVTELEEDLDTARKDLIK----------SEEMNTKLQR------DVREAMAQKEDMEERITTLEK 327
Cdd:COG3206 168 LRREEARKALEFLEEQLPELRKELEEAEAALEEfrqknglvdlSEEAKLLLQQlselesQLAEARAELAEAEARLAALRA 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 328 R------YLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKN---RQLQERLELAEQKLQQTLRKAETLPEVEAE-LAQ 397
Cdd:COG3206 248 QlgsgpdALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHpdvIALRAQIAALRAQLQQEAQRILASLEAELEaLQA 327
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 578821804 398 RVAALSK--SDLLS-SGSSAAKEAKLLELTSKLRKAEERHGNIEERLRQMEAQ 447
Cdd:COG3206 328 REASLQAqlAQLEArLAELPELEAELRRLEREVEVARELYESLLQRLEEARLA 380
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
177-537 |
2.41e-03 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 42.15 E-value: 2.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 177 KVRERLRVALERCSLLEEELGATHKELMILKEQNNQKKTLTDGVLDINHEQENTPSTsgKRSSDGS--------LSH-EE 247
Cdd:pfam06160 83 KAKKALDEIEELLDDIEEDIKQILEELDELLESEEKNREEVEELKDKYRELRKTLLA--NRFSYGPaidelekqLAEiEE 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 248 DLAKVIEL---------QEIISKQSRE----QSQMK--------------ERLASLSSHVTELEED------------LD 288
Cdd:pfam06160 161 EFSQFEELtesgdyleaREVLEKLEEEtdalEELMEdipplyeelktelpDQLEELKEGYREMEEEgyalehlnvdkeIQ 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 289 TARKDLIKSEEMNTKLqrDVREAMAQKEDMEERITTL----EKRYLAAQreatSVHDLNDKLENEIankdsmhRQTEDKN 364
Cdd:pfam06160 241 QLEEQLEENLALLENL--ELDEAEEALEEIEERIDQLydllEKEVDAKK----YVEKNLPEIEDYL-------EHAEEQN 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 365 RQLQERLELaeqkLQQTLRKAETLPEVEAELAQRVAALSKSDLLSSGSSAAKEAKLLELTSKLRKaeerhgnIEERLRQM 444
Cdd:pfam06160 308 KELKEELER----VQQSYTLNENELERVRGLEKQLEELEKRYDEIVERLEEKEVAYSELQEELEE-------ILEQLEEI 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 445 EAQLEEKNQELQRARQREKmneEHNKRLsDTVDKLLSESNERLQlhlKERMAALEDknSLLREVESAKKQLEETQHDKDQ 524
Cdd:pfam06160 377 EEEQEEFKESLQSLRKDEL---EAREKL-DEFKLELREIKRLVE---KSNLPGLPE--SYLDYFFDVSDEIEDLADELNE 447
|
410
....*....|...
gi 578821804 525 LVLNIEALRAELD 537
Cdd:pfam06160 448 VPLNMDEVNRLLD 460
|
|
| SAM_1 |
pfam00536 |
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ... |
951-1013 |
2.45e-03 |
|
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily conserved protein binding domain that is involved in the regulation of numerous developmental processes in diverse eukaryotes. The SAM domain can potentially function as a protein interaction module through its ability to homo- and heterooligomerise with other SAM domains.
Pssm-ID: 425739 Cd Length: 64 Bit Score: 37.63 E-value: 2.45e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578821804 951 QWDGPTVVVWLElWVGMPAwYVAACRANVKSGAIMSALSDTEIqREIGISNPLHRLKLRLAIQ 1013
Cdd:pfam00536 2 GWSVEDVGEWLE-SIGLGQ-YIDSFRAGYIDGDALLQLTEDDL-LKLGVTLLGHRKKILYAIQ 61
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
194-450 |
2.57e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.21 E-value: 2.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 194 EELGATHKELMILKEQnnqKKTLTDGVLDINHEQENTPSTSGKRSSDGSLSHEEDLAKVIELQEIISKQSREQSQMKERL 273
Cdd:COG4913 235 DDLERAHEALEDAREQ---IELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAEL 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 274 ASLSSHVTELEEDLDTARKDLikseemntkLQRDVReamaQKEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIAnk 353
Cdd:COG4913 312 ERLEARLDALREELDELEAQI---------RGNGGD----RLEQLEREIERLERELEERERRRARLEALLAALGLPLP-- 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 354 dsmhrqtedknrqlQERLELAEQKlQQTLRKAETLPEVEAELAQRVAALsksdllsSGSSAAKEAKLLELTSKLRKAEER 433
Cdd:COG4913 377 --------------ASAEEFAALR-AEAAALLEALEEELEALEEALAEA-------EAALRDLRRELRELEAEIASLERR 434
|
250
....*....|....*..
gi 578821804 434 HGNIEERLRQMEAQLEE 450
Cdd:COG4913 435 KSNIPARLLALRDALAE 451
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
258-525 |
2.74e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 41.93 E-value: 2.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 258 IISKQSREQSQMKERLASLSSHVTELEEDLDTARKDLIKSEEmntklqrdvreamaQKEDMEERITTLEKRylaaqreat 337
Cdd:TIGR04523 27 IANKQDTEEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEE--------------KINNSNNKIKILEQQ--------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 338 sVHDLNDKLENEIA-----NKDSMHRQTEDKN-RQLQERLELAEQKLQQTLRkaetlpEVEAELAQRVAALSKsdllssg 411
Cdd:TIGR04523 84 -IKDLNDKLKKNKDkinklNSDLSKINSEIKNdKEQKNKLEVELNKLEKQKK------ENKKNIDKFLTEIKK------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 412 ssaaKEAKLLELTSKLRKAEERHGNIEERLRQMEAQLEEKNQELQRARQR-----------EKMNEEHNKRLSDTVDklL 480
Cdd:TIGR04523 150 ----KEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKllklelllsnlKKKIQKNKSLESQISE--L 223
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 578821804 481 SESNERLQLHLKERMAALEDKNSLLREVESAKKQL-EETQHDKDQL 525
Cdd:TIGR04523 224 KKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLkDEQNKIKKQL 269
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
237-550 |
3.33e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.87 E-value: 3.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 237 RSSDGSLSHEEDLAKvielqeiiSKQSREQSQmkERLASLSSHVTELEEdldtARKDL-IKSEEMNTKLQRdVREAMAQK 315
Cdd:PRK04863 283 VHLEEALELRRELYT--------SRRQLAAEQ--YRLVEMARELAELNE----AESDLeQDYQAASDHLNL-VQTALRQQ 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 316 EDMEERITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQL---QERLELAE------QKLQQTLRKAE 386
Cdd:PRK04863 348 EKIERYQADLEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLadyQQALDVQQtraiqyQQAVQALERAK 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 387 TL---PEVEAELAqrvaalskSDLLSSGSSAAKEA--KLLELTSKLRKAEERHGNIE---ERLRQMEAQLEeKNQELQRA 458
Cdd:PRK04863 428 QLcglPDLTADNA--------EDWLEEFQAKEQEAteELLSLEQKLSVAQAAHSQFEqayQLVRKIAGEVS-RSEAWDVA 498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 459 RQREKMNEEHnkrlsdtvdKLLSESNERLQLHLKERMAALEDKNSLLREVESAKKQLEETQHDKDQLVLNIEALRAELDH 538
Cdd:PRK04863 499 RELLRRLREQ---------RHLAEQLQQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLES 569
|
330
....*....|..
gi 578821804 539 MRLRGASLHHGR 550
Cdd:PRK04863 570 LSESVSEARERR 581
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
175-511 |
3.58e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 41.81 E-value: 3.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 175 DEKVRERLRVALERCSLLEEELGATHKELMILKEQNNQKKTLTDgvlDINHEQENTPSTSGKRSSDGSLSHEEDLAKVIE 254
Cdd:PRK01156 464 EEKSNHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKE---YLESEEINKSINEYNKIESARADLEDIKIKINE 540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 255 LQEIISKQSreqsQMKERLASLSShvteleEDLDTARKDLIKSEEMNTKLqrDVREAMAQKEDMEERITTLEKRylaaqr 334
Cdd:PRK01156 541 LKDKHDKYE----EIKNRYKSLKL------EDLDSKRTSWLNALAVISLI--DIETNRSRSNEIKKQLNDLESR------ 602
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 335 eatsVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTlrkaETLPEVEAELAQRVAALSksdllssgssa 414
Cdd:PRK01156 603 ----LQEIEIGFPDDKSYIDKSIREIENEANNLNNKYNEIQENKILI----EKLRGKIDNYKKQIAEID----------- 663
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 415 AKEAKLLELTSKLRKaeerhgnIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVdkllSESNERLqlhlkER 494
Cdd:PRK01156 664 SIIPDLKEITSRIND-------IEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRI----NDINETL-----ES 727
|
330
....*....|....*..
gi 578821804 495 MAALEDKNSLLREVESA 511
Cdd:PRK01156 728 MKKIKKAIGDLKRLREA 744
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
251-397 |
3.66e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.54 E-value: 3.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 251 KVIELQEIISKQSREQSQMKERLASLSSHVTELEEDLDTARKDLIKSEEMNTKLQRD--VREAMAQKEDMEERITTLEKR 328
Cdd:COG3206 206 GLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSpvIQQLRAQLAELEAELAELSAR 285
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 329 YLAAQREATSVHDLNDKLENEIAN-KDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQ 397
Cdd:COG3206 286 YTPNHPDVIALRAQIAALRAQLQQeAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRR 355
|
|
| SAM_Neurabin-like |
cd09512 |
SAM domain of SAM_Neurabin-like subfamily; SAM (sterile alpha motif) domain of Neurabin-like ... |
1152-1216 |
3.87e-03 |
|
SAM domain of SAM_Neurabin-like subfamily; SAM (sterile alpha motif) domain of Neurabin-like (Neural actin-binding) subfamily is a putative protein-protein interaction domain. This group currently includes the SAM domains of neurobin-I, SAMD14 and neurobin-I/SAMD14-like proteins. Most are multidomain proteins and in addition to SAM domain they contain other protein-binding domains such as PDZ and actin-binding domains. Members of this subfamily participate in signal transduction. Neurabin-I is involved in the regulation of Ca signaling intensity in alpha-adrenergic receptors; it forms a functional pair of opposing regulators with neurabin-II. Neurabins are expressed almost exclusively in neuronal cells. They are known to interact with protein phosphatase 1 and inhibit its activity; they also can bind actin filaments; however, the exact role of the SAM domain is unclear, since SAM doesn't participate in these interactions.
Pssm-ID: 188911 [Multi-domain] Cd Length: 70 Bit Score: 37.25 E-value: 3.87e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578821804 1152 VLVWSNDRVIRWILSIGLKEYANNLIESGVHG-ALLALDETfDFSALALllqiptQNTQARAVLER 1216
Cdd:cd09512 4 VSEWSVQQVCQWLMGLGLEQYIPEFTANNIDGqQLLQLDSS-KLKALGI------TSSSDRSLLKK 62
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
345-536 |
3.94e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 40.19 E-value: 3.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 345 KLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETlpeveaELAqRVAALSKSDLlssgssaakEAKLLELT 424
Cdd:COG1842 41 EARQALAQVIANQKRLERQLEELEAEAEKWEEKARLALEKGRE------DLA-REALERKAEL---------EAQAEALE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 425 SKLRKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNeEHNKRLSDTVDKLLSESNERLQLHLKERMAALEDKNSL 504
Cdd:COG1842 105 AQLAQLEEQVEKLKEALRQLESKLEELKAKKDTLKARAKAA-KAQEKVNEALSGIDSDDATSALERMEEKIEEMEARAEA 183
|
170 180 190
....*....|....*....|....*....|....*...
gi 578821804 505 LREVESAK---KQLEETQHDK---DQLvlniEALRAEL 536
Cdd:COG1842 184 AAELAAGDsldDELAELEADSeveDEL----AALKAKM 217
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
343-472 |
4.46e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 41.35 E-value: 4.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 343 NDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRvaalsksdllssgssAAKEAKlle 422
Cdd:PRK00409 515 KEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEE---------------AEKEAQ--- 576
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 578821804 423 ltSKLRKAEERHGNIEERLRQMEAQL--EEKNQELQRARQR-EKMNEEHNKRL 472
Cdd:PRK00409 577 --QAIKEAKKEADEIIKELRQLQKGGyaSVKAHELIEARKRlNKANEKKEKKK 627
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
193-541 |
4.50e-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: 461677 [Multi-domain] Cd Length: 660 Bit Score: 41.26 E-value: 4.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 193 EEELGATHKELMILKEQNNQKKTLTDGVLDINHEQENTPSTSgkrssdgsLSHEEdlaKVIELQEIISKQ---SREQSQM 269
Cdd:pfam05557 124 ELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSL--------AEAEQ---RIKELEFEIQSQeqdSEIVKNS 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 270 KERLASLSshvtELEedldtarKDLIKSEEMNTKLQRDVREAMAQKEDMEERITTLEkRYLAAQREATSVHDLNDKLENE 349
Cdd:pfam05557 193 KSELARIP----ELE-------KELERLREHNKHLNENIENKLLLKEEVEDLKRKLE-REEKYREEAATLELEKEKLEQE 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 350 iankdsmhrqtedknrqLQERLELAeQKLQQTLRKAETLPEVEAELAQRVAALSKSDLLSSGSSAAKEAKLLELTSK--- 426
Cdd:pfam05557 261 -----------------LQSWVKLA-QDTGLNLRSPEDLSRRIEQLQQREIVLKEENSSLTSSARQLEKARRELEQElaq 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 427 -------LRKAEERHGNIEERLRQ-----------MEAQLEEKNQELQRARQREKMNEEhNKRLSDTVDK---LLSESNE 485
Cdd:pfam05557 323 ylkkiedLNKKLKRHKALVRRLQRrvllltkerdgYRAILESYDKELTMSNYSPQLLER-IEEAEDMTQKmqaHNEEMEA 401
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 578821804 486 RLQLHLKERMAALEDKNSLLREVESAKKQleETQHDKDQLVLNIEALRAELDHMRL 541
Cdd:pfam05557 402 QLSVAEEELGGYKQQAQTLERELQALRQQ--ESLADPSYSKEEVDSLRRKLETLEL 455
|
|
| NIP100 |
COG5244 |
Dynactin complex subunit involved in mitotic spindle partitioning in anaphase B [Cell cycle ... |
382-542 |
4.84e-03 |
|
Dynactin complex subunit involved in mitotic spindle partitioning in anaphase B [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 227569 [Multi-domain] Cd Length: 669 Bit Score: 41.21 E-value: 4.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 382 LRKAETLPEVEaELAQRVaalskSDLLSSGSSAAKEAKLLELTsklrkaeerHGNIEERLRQMEAQLEEKN---QELQRA 458
Cdd:COG5244 442 IARIDKLIGKE-EISKQD-----NRLFLYPSCDITLSSILTIL---------FSDKLEVFFQGIESLLENItifPEQPSQ 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 459 RQREKMNEEHNKRLSDTvdklLSESNERL--QLHLKERMAALEDKNSLLREVESAKKQLEEtqhdkdqlvlNIEALRAEL 536
Cdd:COG5244 507 QTSDSENIKENSLLSDR----LNEENIRLkeVLVQKENMLTEETKIKIIIGRDLERKTLEE----------NIKTLKVEL 572
|
....*.
gi 578821804 537 DHMRLR 542
Cdd:COG5244 573 NNKNNK 578
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
250-538 |
5.11e-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: 461677 [Multi-domain] Cd Length: 660 Bit Score: 41.26 E-value: 5.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 250 AKVIELQEIISKQSREQSQM----KERLASLSSHVTELEEDLDTARKdliKSEEMNTKLQ----RDVREAMAQKEDMEEr 321
Cdd:pfam05557 2 AELIESKARLSQLQNEKKQMelehKRARIELEKKASALKRQLDRESD---RNQELQKRIRllekREAEAEEALREQAEL- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 322 iTTLEKRYLAAQREA--------TSVHDLNDKLENEIA-------NKDSMHRQTEDKNRQLQERLEL-------AEQKLQ 379
Cdd:pfam05557 78 -NRLKKKYLEALNKKlnekesqlADAREVISCLKNELSelrrqiqRAELELQSTNSELEELQERLDLlkakaseAEQLRQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 380 QTLRKAETLPEVEA---ELAQRVAAL---------SKSDLLSSGSSAAKEAKLLELTSKLRKAEERHGNIEERLRQMEAQ 447
Cdd:pfam05557 157 NLEKQQSSLAEAEQrikELEFEIQSQeqdseivknSKSELARIPELEKELERLREHNKHLNENIENKLLLKEEVEDLKRK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 448 LE--EKNQ------ELQRARQREKMNE----EHNKRLSDTVDKLLSESNERLQlhlKERMAALEDKNSLLREVESAKKQL 515
Cdd:pfam05557 237 LEreEKYReeaatlELEKEKLEQELQSwvklAQDTGLNLRSPEDLSRRIEQLQ---QREIVLKEENSSLTSSARQLEKAR 313
|
330 340
....*....|....*....|...
gi 578821804 516 EETQHDKDQLVLNIEALRAELDH 538
Cdd:pfam05557 314 RELEQELAQYLKKIEDLNKKLKR 336
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
256-537 |
5.25e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 41.31 E-value: 5.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 256 QEIISKQSREQSQMKERLASLSSHVTELE--------------EDLDTARKDLIKSEEMNTKLQRDVREAMAQKEDMEER 321
Cdd:pfam01576 4 EEEMQAKEEELQKVKERQQKAESELKELEkkhqqlceeknalqEQLQAETELCAEAEEMRARLAARKQELEEILHELESR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 322 ITTLEKRYLAAQRE----ATSVHDLNDKLENEIANKDSMHRQ---TEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAE 394
Cdd:pfam01576 84 LEEEEERSQQLQNEkkkmQQHIQDLEEQLDEEEAARQKLQLEkvtTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 395 LAQRVAALSKSDLLSSGSSAAKEAKLLELTSKLRKAEERHGNIEERLRQMEAQLEEKNQELQRARQR----EKMNEEHNK 470
Cdd:pfam01576 164 FTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQiaelRAQLAKKEE 243
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578821804 471 RLSDTVDKLLSESNERLQLHLKERmaALEDKNSLLRE-VESAKKQLEETQHDKDQLVLNIEALRAELD 537
Cdd:pfam01576 244 ELQAALARLEEETAQKNNALKKIR--ELEAQISELQEdLESERAARNKAEKQRRDLGEELEALKTELE 309
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
276-457 |
5.27e-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: 461130 [Multi-domain] Cd Length: 215 Bit Score: 40.05 E-value: 5.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 276 LSSHVTELEEDLDTARKDLIKSEEMNTKLQRDVREAMAQKEDMEERIT-TLEKRYLAAQREATSVhdlNDKLENEIANKD 354
Cdd:pfam04012 27 LEQAIRDMQSELVKARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQaALTKGNEELAREALAE---KKSLEKQAEALE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 355 SMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLpEVEAELAQRVAALSKSDLLSSGSSAAK-----EAKLLELTSKLRK 429
Cdd:pfam04012 104 TQLAQQRSAVEQLRKQLAALETKIQQLKAKKNLL-KARLKAAKAQEAVQTSLGSLSTSSATDsferiEEKIEEREARADA 182
|
170 180 190
....*....|....*....|....*....|
gi 578821804 430 AEERHG--NIEERLRQMEAQLEEKNQELQR 457
Cdd:pfam04012 183 AAELASavDLDAKLEQAGIQMEVSEDVLAR 212
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
389-527 |
5.42e-03 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 40.42 E-value: 5.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 389 PEVEAELAQRVAALsksdllssgssAAKEAKLLELTSKLRKAEERHGnIEERLRQMEAQLEEKNQELQRARQ-------- 460
Cdd:COG1566 79 TDLQAALAQAEAQL-----------AAAEAQLARLEAELGAEAEIAA-AEAQLAAAQAQLDLAQRELERYQAlykkgavs 146
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578821804 461 REKMNEEHNKRlsDTVDKLLSESNERLQLhLKERMAALEDKNSLLREVESAKKQLEETQHDKDQLVL 527
Cdd:COG1566 147 QQELDEARAAL--DAAQAQLEAAQAQLAQ-AQAGLREEEELAAAQAQVAQAEAALAQAELNLARTTI 210
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
161-450 |
5.45e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.20 E-value: 5.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 161 LKALKSLFEHHKALDEKVR----ERLRVALERCSLLEEELGATHKELMILKEQNNQKKTLTDGVLDINHEQENTpstsgk 236
Cdd:PRK03918 495 LIKLKELAEQLKELEEKLKkynlEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDEL------ 568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 237 rssdgslshEEDLAKVieLQEIISKQSREQSQMKERLASLSSHVTELEEdLDTARKDLIKSEEMNTKLQRDVREAMAQKE 316
Cdd:PRK03918 569 ---------EEELAEL--LKELEELGFESVEELEERLKELEPFYNEYLE-LKDAEKELEREEKELKKLEEELDKAFEELA 636
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 317 DMEERITTLEKRYLAAQREATsvhdlndklENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTlrkAETLPEVEAELA 396
Cdd:PRK03918 637 ETEKRLEELRKELEELEKKYS---------EEEYEELREEYLELSRELAGLRAELEELEKRREEI---KKTLEKLKEELE 704
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 578821804 397 QRvaalsksdllssgSSAAKEAKLLEltsklrKAEERHGNIEERLRQMEAQLEE 450
Cdd:PRK03918 705 ER-------------EKAKKELEKLE------KALERVEELREKVKKYKALLKE 739
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
45-277 |
5.67e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.52 E-value: 5.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 45 EERDRLLDTLRETQETLALTQGKLHEVGHERDSLQRQLNtALPQEFAALTKELNVCREQLLEREEEIAELKAERNNTRLL 124
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLA-ALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 125 LEHLECLVSRHERSLRMTVVKRQAQ---SPAGVSSEVEVLKALKSLFEHHKALdekvRERLRVALERCSLLEEELGATHK 201
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRQPPLAlllSPEDFLDAVRRLQYLKYLAPARREQ----AEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578821804 202 ELM-ILKEQNNQKKTLTDGVldinHEQENTPSTSGKRSSDGSLSHEEDLAKVIELQEIISKQSREQSQMKERLASLS 277
Cdd:COG4942 175 ELEaLLAELEEERAALEALK----AERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
244-402 |
7.04e-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: 464001 [Multi-domain] Cd Length: 200 Bit Score: 39.12 E-value: 7.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 244 SHEEDLAKVIELQEIISKQ----SREQSQMKERLASLSSHVTELEEDLDTARKD---LIKSEEMNTKLQRDVREAMAQKE 316
Cdd:pfam13851 30 SLKEEIAELKKKEERNEKLmseiQQENKRLTEPLQKAQEEVEELRKQLENYEKDkqsLKNLKARLKVLEKELKDLKWEHE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 317 DMEERITTLEKRYLAA-QREATSVHDLNDK-------LENEIANkdsMHRQTEDKNRQLQERLELAEQKLQQTLRKAETL 388
Cdd:pfam13851 110 VLEQRFEKVERERDELyDKFEAAIQDVQQKtglknllLEKKLQA---LGETLEKKEAQLNEVLAAANLDPDALQAVTEKL 186
|
170
....*....|....
gi 578821804 389 PEVEAELAQRVAAL 402
Cdd:pfam13851 187 EDVLESKNQLIKDL 200
|
|
| Stathmin |
pfam00836 |
Stathmin family; The Stathmin family of proteins play an important role in the regulation of ... |
416-524 |
7.41e-03 |
|
Stathmin family; The Stathmin family of proteins play an important role in the regulation of the microtubule cytoskeleton. They regulate microtubule dynamics by promoting depolymerization of microtubules and/or preventing polymerization of tubulin heterodimers.
Pssm-ID: 459956 [Multi-domain] Cd Length: 136 Bit Score: 38.10 E-value: 7.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 416 KEAKLLELTSKLRKAEERHGNIEErlrQMEAQLEEKNQELQRARQreKMNEEHNKRLSDTVDKLlsesNERLQLHLKERM 495
Cdd:pfam00836 40 KDSSLEEIQKKLEAAEERRKSLEA---QKLKQLAEKREKEEEALQ--KADEENNNFSKMAEEKL----KQKMEAYKENRE 110
|
90 100
....*....|....*....|....*....
gi 578821804 496 AALEDKNSLLREVEsakKQLEETQHDKDQ 524
Cdd:pfam00836 111 AQIAALKEKLKEKE---KHVEEVRKNKEQ 136
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
155-503 |
7.56e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.89 E-value: 7.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 155 SSEVEVLKALKSLFEHHKALD-EKVRERLRVALERCSLLEEELGATHKELMILKEQNNQKKTltdgvldinheQENTPST 233
Cdd:PTZ00121 1548 ADELKKAEELKKAEEKKKAEEaKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKA-----------EEAKKAE 1616
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 234 SGKRSSDGSLSHEEDLAKVIELQEIISKQSREQSQMKErlaslsshvtELEEDLDTARKDLIKSEEMNTKLQRdvreamA 313
Cdd:PTZ00121 1617 EAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKK----------AEEENKIKAAEEAKKAEEDKKKAEE------A 1680
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 314 QKEDMEERitTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQErlelAEQKLQQTLRKAETLpEVEA 393
Cdd:PTZ00121 1681 KKAEEDEK--KAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEE----AKKEAEEDKKKAEEA-KKDE 1753
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 394 ELAQRVAALSKSDLLSSGSSAAKEAKLLELTSKlRKAEERHGNIEERLRQM----EAQLEEKNQELQRARQREKMNEEHN 469
Cdd:PTZ00121 1754 EEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELD-EEDEKRRMEVDKKIKDIfdnfANIIEGGKEGNLVINDSKEMEDSAI 1832
|
330 340 350
....*....|....*....|....*....|....
gi 578821804 470 KRLSDTVDKLLSESNERLQLHLKERMAALEDKNS 503
Cdd:PTZ00121 1833 KEVADSKNMQLEEADAFEKHKFNKNNENGEDGNK 1866
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
46-544 |
8.27e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 40.66 E-value: 8.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 46 ERDRLLDTLRETQETLALTQGKLHEVGHERDSLQRQLNtalpqEFAALTKELNVCREQLLEREEEIAELKAERNNTRLLL 125
Cdd:PRK01156 160 EINSLERNYDKLKDVIDMLRAEISNIDYLEEKLKSSNL-----ELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDY 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 126 EHLEC----LVSRHERSLRMTVVKRQAQSPagVSSEVEVLKALKSLFEHHKALDE----KVRERLRVAL----------E 187
Cdd:PRK01156 235 NNLKSalneLSSLEDMKNRYESEIKTAESD--LSMELEKNNYYKELEERHMKIINdpvyKNRNYINDYFkykndienkkQ 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 188 RCSLLEEELG---ATHKELMILKEQNNQKKTLTDGVLDINHEQENTPSTSGKRSSdgSLSHEEDLAKVIELQEIisKQSR 264
Cdd:PRK01156 313 ILSNIDAEINkyhAIIKKLSVLQKDYNDYIKKKSRYDDLNNQILELEGYEMDYNS--YLKSIESLKKKIEEYSK--NIER 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 265 EQSQMKERLASLSSHVTELEEDLDTARKDLIKSEEMNTKLQRDVREAMAQKEDMEERITTLEKRYLAAqreaTSVHDLND 344
Cdd:PRK01156 389 MSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSVCP----VCGTTLGE 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 345 KLENEIANKDSmhrqtEDKNRqlqerlelAEQKLQQTLRKAETLPEVEAELAQRVAALSKSDLLSSGSSAAK-EAKLLEL 423
Cdd:PRK01156 465 EKSNHIINHYN-----EKKSR--------LEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKiESARADL 531
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 424 T------SKLRKAEERHGNIEERLRQMEAQ-LEEKNQELQRA-RQREKMNEEHNKRLSDTVDKLLSESNERLQlhlkERM 495
Cdd:PRK01156 532 EdikikiNELKDKHDKYEEIKNRYKSLKLEdLDSKRTSWLNAlAVISLIDIETNRSRSNEIKKQLNDLESRLQ----EIE 607
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 578821804 496 AALEDKNS----LLREVESAKKQLEETQHDKDQLVLNIEALRAELDHMRLRGA 544
Cdd:PRK01156 608 IGFPDDKSyidkSIREIENEANNLNNKYNEIQENKILIEKLRGKIDNYKKQIA 660
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
296-535 |
9.14e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 40.55 E-value: 9.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 296 KSEEMNTKLQ------RDVREAMAQKEDMEERITTLEKRYLAAqreatsvHDLNDKLENEIAN-KDSMHRQTEDKN--RQ 366
Cdd:PRK10246 312 QIEEVNTRLQstmalrARIRHHAAKQSAELQAQQQSLNTWLAE-------HDRFRQWNNELAGwRAQFSQQTSDREqlRQ 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 367 LQERLELAEQKLQQTLRKAETLP--EVEAELAQRVAALSKSDLLSS--GSSAAKEAKLLELTSKLRKAEERHGNIEERLR 442
Cdd:PRK10246 385 WQQQLTHAEQKLNALPAITLTLTadEVAAALAQHAEQRPLRQRLVAlhGQIVPQQKRLAQLQVAIQNVTQEQTQRNAALN 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 443 QMEAQLEEKNQELQRAR------QREKMNEEHNKRLS----------------DTVDKLLSESNERLQLHLKERMAALED 500
Cdd:PRK10246 465 EMRQRYKEKTQQLADVKticeqeARIKDLEAQRAQLQagqpcplcgstshpavEAYQALEPGVNQSRLDALEKEVKKLGE 544
|
250 260 270
....*....|....*....|....*....|....*.
gi 578821804 501 KNSLLR-EVESAKKQLEETQHDKDQLVLNIEALRAE 535
Cdd:PRK10246 545 EGAALRgQLDALTKQLQRDESEAQSLRQEEQALTQQ 580
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
299-537 |
9.26e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 40.38 E-value: 9.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 299 EMNTKLQRDVREAMAQKEDMEERITTLEKRyLAAQREatSVHDLNDKLENEIANKDSMHrqtedknrqlQERLELAEQKL 378
Cdd:PHA02562 167 EMDKLNKDKIRELNQQIQTLDMKIDHIQQQ-IKTYNK--NIEEQRKKNGENIARKQNKY----------DELVEEAKTIK 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 379 QQTLRKAETLPEVEAELAQRVAALSK-----SDLLSSGSSAAKEAKLLE-------LTSKLRKAEERHGNIEERLRQMEA 446
Cdd:PHA02562 234 AEIEELTDELLNLVMDIEDPSAALNKlntaaAKIKSKIEQFQKVIKMYEkggvcptCTQQISEGPDRITKIKDKLKELQH 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578821804 447 QLEEKNQELQRARQREKMNEEHNKRLSDTVDKLlseSNERLQLhlkermAALEDKNsllREVESAKKQLEETQHDKDQlv 526
Cdd:PHA02562 314 SLEKLDTAIDELEEIMDEFNEQSKKLLELKNKI---STNKQSL------ITLVDKA---KKVKAAIEELQAEFVDNAE-- 379
|
250
....*....|.
gi 578821804 527 lNIEALRAELD 537
Cdd:PHA02562 380 -ELAKLQDELD 389
|
|
| |
