|
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 ... |
1284-1349 |
9.36e-45 |
|
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: 156.48 E-value: 9.36e-45
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2076569066 1284 MNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRGQLKMVDSFHRNSFQCGIMCLRRL 1349
Cdd:cd09565 1 MNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRTHLKMVDSFHRTSLQYGILCLKRL 66
|
|
| SAM_liprin-alpha1,2,3,4_repeat3 |
cd09568 |
SAM domain of liprin-alpha1,2,3,4 proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 ... |
1366-1436 |
1.03e-41 |
|
SAM domain of liprin-alpha1,2,3,4 proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 of liprin-alpha1,2,3,4 proteins is a protein-protein interaction domain. Liprin-alpha proteins contain three copies (repeats) of SAM domain. They may form heterodimers with liprin-beta proteins through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development and in axon guidance; in particular, liprin-alpha is involved in formation of the presynaptic active zone.
Pssm-ID: 188967 Cd Length: 72 Bit Score: 148.23 E-value: 1.03e-41
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2076569066 1366 VLVWSNDRVIRWVLSIGLREYAGNLAESGVHGALIALDETFDFSALALLLQIPTQNTQARAVLEREFNSLL 1436
Cdd:cd09568 2 VLVWSNERVIRWVQSIGLREYANNLLESGVHGALIALDETFDANSFALALQIPTQNTQARQILEREFNNLL 72
|
|
| SAM_liprin-alpha1,2,3,4_repeat1 |
cd09562 |
SAM domain of liprin-alpha1,2,3,4 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 ... |
1158-1228 |
3.30e-41 |
|
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: 146.56 E-value: 3.30e-41
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2076569066 1158 FAQWDGPTVVVWLELWVGMPAWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEVMSLT 1228
Cdd:cd09562 1 FALWNGPTVVAWLELWVGMPAWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEMVSLT 71
|
|
| SAM_liprin-kazrin_repeat2 |
cd09495 |
SAM domain of liprin/kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of ... |
1288-1347 |
1.41e-30 |
|
SAM domain of liprin/kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of liprin/kazrin proteins is a protein-protein interaction domain. The long form of liprin/kazrin proteins contains three copies (repeats) of SAM domain. Liprin-alpha may form heterodimers with liprin-beta through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development and in axon guidance. In particular, liprin-alpha is involved in formation of the presynaptic active zone; liprin-beta is involved in the maintenance of lymphatic vessel integrity. Kazrins are involved in interplay between desmosomes and in adheren junctions; additionally they play a role in regulation of intercellular differentiation, junction assembly, and cytoskeletal organization.
Pssm-ID: 188894 Cd Length: 60 Bit Score: 116.09 E-value: 1.41e-30
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 1288 WIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRGQLKMVDSFHRNSFQCGIMCLR 1347
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 ... |
1165-1223 |
5.55e-27 |
|
SAM domain of liprin/kazrin proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of liprin/kazrin proteins is a protein-protein interaction domain. The long form of liprin/kazrin proteins contains three copies (repeats) of the SAM domain. Liprin-alpha may form heterodimers with liprin-beta through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development and in axon guidance. In particular, liprin-alpha is involved in formation of the presynaptic active zone; liprin-beta is involved in the maintenance of lymphatic vessel integrity. Kazrins are involved in interplay between desmosomes and adherens junctions; additionally they play a role in regulation of intercellular differentiation, junction assembly, and cytoskeletal organization.
Pssm-ID: 188893 Cd Length: 58 Bit Score: 105.77 E-value: 5.55e-27
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 2076569066 1165 TVVVWLELWVGMPaWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQE 1223
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 ... |
1373-1433 |
1.28e-23 |
|
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: 96.07 E-value: 1.28e-23
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2076569066 1373 RVIRWVLSIGLREYAGNLAESGVHGALIALDETFDFSALALLLQIPTQNTQARAVLEREFN 1433
Cdd:cd09496 1 RVIHWIRSIDLREYANNLVESGVHGGLLVLEPNFDHNTMALVLQIPPQKTQARRHLETEFN 61
|
|
| SAM_kazrin_repeat3 |
cd09570 |
SAM domain of kazrin proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 of kazrin ... |
1365-1436 |
4.39e-20 |
|
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: 86.34 E-value: 4.39e-20
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2076569066 1365 NVLVWSNDRVIRWVLSIGLREYAGNLAESGVHGALIALDETFDFSALALLLQIPTQNTQARAVLEREFNSLL 1436
Cdd:cd09570 1 DPVVWTNQRVIKWARSIDLKEYADNLRDSGVHGALMVLEPSFNSDTMATALGIPSSKNIIRRHLTTEMEALV 72
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
295-564 |
4.83e-19 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 95.00 E-value: 4.83e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 295 EEDLAKVLELQEVVDRQ----------AREHCQMKERLATLSGHVAELEedLDTARKDLIKSEEVNSRLQRDVREAMAQK 364
Cdd:COG1196 185 EENLERLEDILGELERQleplerqaekAERYRELKEELKELEAELLLLK--LRELEAELEELEAELEELEAELEELEAEL 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 365 EDMEERITTLEKRYLAAQREATSVHDLNDKLESEIANKDAVHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAEL 444
Cdd:COG1196 263 AELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEEL 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 445 AQRV-----------AALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMSEEHSKRLSDTVDRLLsesgERLRL 513
Cdd:COG1196 343 EEELeeaeeeleeaeAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALL----ERLER 418
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 2076569066 514 HLKERTAALEDKNALLREVGDAKKQLEETQRDKDQLVLNVEALRAELDQVR 564
Cdd:COG1196 419 LEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELL 469
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
292-700 |
5.43e-19 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 95.00 E-value: 5.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 292 LSHEEDLAKVLELQEVVDRQAREHCQMKERLATLSGHVAELEEDLDTARKDLIKSEEVNSRLQRDVREAMAQKEDMEERI 371
Cdd:COG1196 225 LEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDI 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 372 TTLEKRYLAAQREATSVHDLNDKLESEIANKDAVHRQTEDKNRQLQERLELAEQKLQQT----LRKAETLPEVEAELAQR 447
Cdd:COG1196 305 ARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAeealLEAEAELAEAEEELEEL 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 448 VAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMSEEHSKRLSDTVDRLLSESGERLRLHLK---ERTAALED 524
Cdd:COG1196 385 AEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAEleeEEEALLEL 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 525 KNALLREVGDAKKQLEETQRDKDQLVLNVEALRAELDQ---------VRLGGPSLHHGRPHLGSVPDFRFPAADGPADPC 595
Cdd:COG1196 465 LAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADyegflegvkAALLLAGLRGLAGAVAVLIGVEAAYEAALEAAL 544
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 596 GSSAVRTLNEQDWERAQQASVLAS------------VAQAFESDRELSDGGEDQDALFGSAGLL---SPGGQADAQTLAV 660
Cdd:COG1196 545 AAALQNIVVEDDEVAAAAIEYLKAakagratflpldKIRARAALAAALARGAIGAAVDLVASDLreaDARYYVLGDTLLG 624
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 2076569066 661 MLQEQLDAINKEISRVTRGAARRRTLPWRTERHLAGEKAG 700
Cdd:COG1196 625 RTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTG 664
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
296-564 |
7.88e-19 |
|
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: 94.74 E-value: 7.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 296 EDLAKVLELQ-EVVDRQAR---EHCQMKERLATLSGHVA-----ELEEDLDTARKDLIKSEEVNSRLQRDVREAMAQKED 366
Cdd:TIGR02168 192 EDILNELERQlKSLERQAEkaeRYKELKAELRELELALLvlrleELREELEELQEELKEAEEELEELTAELQELEEKLEE 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 367 MEERITTLEKRYLAAQREATSVHDLNDKLESEIANKDAVHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQ 446
Cdd:TIGR02168 272 LRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKE 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 447 RVAALSKAEErhgNIEERLRQMEAQLEEKNQELQRAR----QREKMSEEHSKRLSDTVDRL--LSESGERLRLHLKERTA 520
Cdd:TIGR02168 352 ELESLEAELE---ELEAELEELESRLEELEEQLETLRskvaQLELQIASLNNEIERLEARLerLEDRRERLQQEIEELLK 428
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 2076569066 521 ALE--DKNALLREVGDAKKQLEETQRDKDQLVLNVEALRAELDQVR 564
Cdd:TIGR02168 429 KLEeaELKELQAELEELEEELEELQEELERLEEALEELREELEEAE 474
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
53-564 |
3.72e-18 |
|
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: 92.43 E-value: 3.72e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 53 DADSHFEQLMVSMLEERDRLMDT-LRETQETLALTQGKLHEVGHERDSLQRQLSTaLPQEFAALTKELsvcreqlLEREE 131
Cdd:TIGR02168 411 RLEDRRERLQQEIEELLKKLEEAeLKELQAELEELEEELEELQEELERLEEALEE-LREELEEAEQAL-------DAAER 482
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 132 EIAELKAERNNTRLLLEHLE--------CLVSRHERSLRMTVVKRQAQSPAGVSSEVEVlkALKSlfehhkALDEKVRER 203
Cdd:TIGR02168 483 ELAQLQARLDSLERLQENLEgfsegvkaLLKNQSGLSGILGVLSELISVDEGYEAAIEA--ALGG------RLQAVVVEN 554
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 204 LRVALERCSLLEEelgvthKEMGRWTFTVSKRLRrartARQVPPLLPHASASAEGAPGA----VSRQTPARR---PCRSG 276
Cdd:TIGR02168 555 LNAAKKAIAFLKQ------NELGRVTFLPLDSIK----GTEIQGNDREILKNIEGFLGVakdlVKFDPKLRKalsYLLGG 624
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 277 -----SPRAGLRLQR----------------SPDGSLSHEEDLA---------KVLELQEVVDRQAREHCQMKERLATLS 326
Cdd:TIGR02168 625 vlvvdDLDNALELAKklrpgyrivtldgdlvRPGGVITGGSAKTnssilerrrEIEELEEKIEELEEKIAELEKALAELR 704
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 327 GHVAELEEDLDTARKDLIKSEEVNSRLQRDVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKL-------ESEI 399
Cdd:TIGR02168 705 KELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAeeelaeaEAEI 784
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 400 ANKDAVHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKAEERhgnIEERLRQMEAQLEEKNQEL 479
Cdd:TIGR02168 785 EELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLED---LEEQIEELSEDIESLAAEI 861
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 480 QRAR-QREKMSEEHsKRLSDtvdrLLSESGERLRLHLKERTAALEDKNALLREVGDAKKQLEETQRDKDQLVLNVEALRA 558
Cdd:TIGR02168 862 EELEeLIEELESEL-EALLN----ERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEV 936
|
....*.
gi 2076569066 559 ELDQVR 564
Cdd:TIGR02168 937 RIDNLQ 942
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
295-491 |
7.45e-18 |
|
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: 85.36 E-value: 7.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 295 EEDLAKVLELQEVvDRQAREHcqmKERLATLSGHVAELEEDLDTARKDLIKSEEVNSRLQRDVREAMAQKEDMEERITTL 374
Cdd:COG1579 3 PEDLRALLDLQEL-DSELDRL---EHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 375 EKRylaaQREATSVHDLNDkLESEIANKDAVHRQTEDKNRQLQERLELAEQKLQqtlrkaetlpEVEAELAQRVAALSKA 454
Cdd:COG1579 79 EEQ----LGNVRNNKEYEA-LQKEIESLKRRISDLEDEILELMERIEELEEELA----------ELEAELAELEAELEEK 143
|
170 180 190
....*....|....*....|....*....|....*..
gi 2076569066 455 EERhgnIEERLRQMEAQLEEKNQElqRARQREKMSEE 491
Cdd:COG1579 144 KAE---LDEELAELEAELEELEAE--REELAAKIPPE 175
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
67-564 |
3.21e-17 |
|
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: 89.35 E-value: 3.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 67 EERDRLMDTLRETQETLALTQGKLHEVGHERDSLQRQLSTALPQEFAALTKELSvCREQLLEREEEIAELKAER---NNT 143
Cdd:TIGR02168 323 AQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEE-LEEQLETLRSKVAQLELQIaslNNE 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 144 RLLLE-HLECLVSRHER------SLRMTVVKRQAQSPAGVSSEVE-VLKALKSLFEHHKALDEKVRERLRVALERCSLLE 215
Cdd:TIGR02168 402 IERLEaRLERLEDRRERlqqeieELLKKLEEAELKELQAELEELEeELEELQEELERLEEALEELREELEEAEQALDAAE 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 216 EELgvtHKEMGRwtFTVSKRLRRA-----RTARQV-------PPLLPHASASAEGAPG----------------AVSRQT 267
Cdd:TIGR02168 482 REL---AQLQAR--LDSLERLQENlegfsEGVKALlknqsglSGILGVLSELISVDEGyeaaieaalggrlqavVVENLN 556
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 268 PAR------RPCRSG-----------------SPRAGLRLQRSPDGSL----SHEEDLAKVLE--LQE--VVD------R 310
Cdd:TIGR02168 557 AAKkaiaflKQNELGrvtflpldsikgteiqgNDREILKNIEGFLGVAkdlvKFDPKLRKALSylLGGvlVVDdldnalE 636
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 311 QAREHcQMKERLATLSGH--------------------------------VAELEEDLDTARKDLIKSEEVNSRLQRDVR 358
Cdd:TIGR02168 637 LAKKL-RPGYRIVTLDGDlvrpggvitggsaktnssilerrreieeleekIEELEEKIAELEKALAELRKELEELEEELE 715
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 359 EAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLESEIANKDAVHRQTEDKNRQLQERLELAEQKLQQtlrkaetlp 438
Cdd:TIGR02168 716 QLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEE--------- 786
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 439 eVEAELAQrvaalskAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMSEEHSKRLSDTVDRlLSESGERLRLHLKER 518
Cdd:TIGR02168 787 -LEAQIEQ-------LKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLED-LEEQIEELSEDIESL 857
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 2076569066 519 TAALEDKNALLREvgdAKKQLEETQRDKDQLVLNVEALRAELDQVR 564
Cdd:TIGR02168 858 AAEIEELEELIEE---LESELEALLNERASLEEALALLRSELEELS 900
|
|
| SAM_kazrin_repeat1 |
cd09564 |
SAM domain of kazrin proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of kazrin ... |
1159-1223 |
5.31e-17 |
|
SAM domain of kazrin proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of kazrin proteins is a protein-protein interaction domain. The long isoform of kazrin contains three copies (repeats) of SAM domain. Kazrin can interact with periplakin. It is involved into interplay between desmosomes and in adheren junctions. Additionally kazrins play a role in regulation of intercellular differentiation, junction assembly, and cytoskeletal organization.
Pssm-ID: 188963 Cd Length: 70 Bit Score: 77.49 E-value: 5.31e-17
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2076569066 1159 AQWDGPTVVVWLELWVGMPAwYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQE 1223
Cdd:cd09564 2 SRWKADMVLAWLEVVMHMPM-YSKACAENVKSGKVLLGLSDSELESGLGISNVLHRRKLRLAIEE 65
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
274-560 |
8.20e-17 |
|
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: 88.20 E-value: 8.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 274 RSGSPRAGLRLQRSpdGSLSHEEDLAKVLELQEVVDrqarehcQMKERLATLSGHVAELEEDLDTARKDLIKSEEVNSRL 353
Cdd:TIGR02169 651 KSGAMTGGSRAPRG--GILFSRSEPAELQRLRERLE-------GLKRELSSLQSELRRIENRLDELSQELSDASRKIGEI 721
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 354 QRDVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLESEIANKDAV----------------HRQTEDKNRQLQ 417
Cdd:TIGR02169 722 EKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDlhkleealndlearlsHSRIPEIQAELS 801
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 418 E----------RLELAEQKLQQTLRKAETLPEVEAELAQRVAALskaEERHGNIEERLRQMEAQLEEKNQELQRARQREK 487
Cdd:TIGR02169 802 KleeevsrieaRLREIEQKLNRLTLEKEYLEKEIQELQEQRIDL---KEQIKSIEKEIENLNGKKEELEEELEELEAALR 878
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 488 MSEEHSKRLSDTVDRL-------------LSESGERLRLHLKERTAALEDKNALLREVGDAKKQLEE---TQRDKDQLVL 551
Cdd:TIGR02169 879 DLESRLGDLKKERDELeaqlrelerkieeLEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEipeEELSLEDVQA 958
|
....*....
gi 2076569066 552 NVEALRAEL 560
Cdd:TIGR02169 959 ELQRVEEEI 967
|
|
| SAM_kazrin_repeat2 |
cd09567 |
SAM domain of kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of kazrin ... |
1283-1347 |
2.01e-16 |
|
SAM domain of kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of kazrin proteins is a protein-protein interaction domain. The long isoform of kazrins contains three copies (repeats) of SAM domain. Kazrin can interact with periplakin. It is involved in interplay between desmosomes and in adheren junctions. Additionally kazrins play a role in regulation of intercellular differentiation, junction assembly, and cytoskeletal organization.
Pssm-ID: 188966 Cd Length: 65 Bit Score: 75.91 E-value: 2.01e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2076569066 1283 DMNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRGQLKMVDSFHRNSFQCGIMCLR 1347
Cdd:cd09567 1 QLDHTWVAREWLRDLGLPQYSEAFREHLVDGRVLDTLSRKDLEKHLGVSKKFHQASLLRGIELLR 65
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
270-566 |
3.02e-16 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 83.41 E-value: 3.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 270 RRPCRSGSPRAGLRLQRSPDGSL--SHEEDLAKVLELQEVVDRQARehcQMKERLATLSGHVAELEEDLDTARKDLIKSE 347
Cdd:COG4372 3 RLGEKVGKARLSLFGLRPKTGILiaALSEQLRKALFELDKLQEELE---QLREELEQAREELEQLEEELEQARSELEQLE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 348 EVNSRLQRDVREAMAQKEDMEERITTLEKRYLAAQR-------EATSVHDLNDKLESEIANKDAVHRQTEDKNRQLQERL 420
Cdd:COG4372 80 EELEELNEQLQAAQAELAQAQEELESLQEEAEELQEeleelqkERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 421 ELAEQKLQQTLRKAETLPEVEAElaQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMSEEHSKRLSDTV 500
Cdd:COG4372 160 ESLQEELAALEQELQALSEAEAE--QALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSA 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2076569066 501 DRLLSESGERLRLHLKERTAALEDKNALLREVGDAKKQLEETQRDKDQLVLNVEALRAELDQVRLG 566
Cdd:COG4372 238 LLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLN 303
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
295-563 |
8.43e-16 |
|
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: 84.73 E-value: 8.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 295 EEDLAKVLELQEVVDRqaREHCQMKERLATLSGHVAELEE---DLDTARKDLIKSEEVNSRLQRDVREAMAQKEDMEERI 371
Cdd:TIGR02169 204 RREREKAERYQALLKE--KREYEGYELLKEKEALERQKEAierQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKI 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 372 TTL-EKRYLAAQREATSVHdlndkleSEIANKDAVHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAA 450
Cdd:TIGR02169 282 KDLgEEEQLRVKEKIGELE-------AEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDK 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 451 LskaEERHGNIEERLRQMEAQLEEKNQELQRARQ-----REKMSEEHSKR--LSDTVDRLLSE----SGERLRLH----- 514
Cdd:TIGR02169 355 L---TEEYAELKEELEDLRAELEEVDKEFAETRDelkdyREKLEKLKREIneLKRELDRLQEElqrlSEELADLNaaiag 431
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 2076569066 515 LKERTAALED-KNALLREVGDAKKQLEETQRDKDQLVLNVEALRAELDQV 563
Cdd:TIGR02169 432 IEAKINELEEeKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRV 481
|
|
| SAM_liprin-beta1,2_repeat2 |
cd09566 |
SAM domain of liprin-beta1,2 proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of ... |
1283-1347 |
1.16e-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: 73.50 E-value: 1.16e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2076569066 1283 DMNHEWIgNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRgQLKMVDSFHRNSFQCGIMCLR 1347
Cdd:cd09566 1 KLDTHWV-LRWLDDIGLPQYKDAFSEAKVDGRMLHYLTVDDLL-HLKVTSALHHASIRRGIQVLR 63
|
|
| SAM_liprin-beta1,2_repeat3 |
cd09569 |
SAM domain of liprin-beta proteins repeat 3; SAM (sterile alpha motif) domain repea t3 of ... |
1365-1436 |
2.85e-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: 72.87 E-value: 2.85e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2076569066 1365 NVLVWSNDRVIRWVLSIGLREYAGNLAESGVHGALIALDETFDFSALALLLQIPTQNTQARAVLEREFNSLL 1436
Cdd:cd09569 1 EVVLWTNHRVMEWLRSVDLAEYAPNLRGSGVHGALMVLEPRFTAETLAALLNIPPNKTLLRRHLATHFNQLL 72
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
317-565 |
3.97e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 82.29 E-value: 3.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 317 QMKERLATLSGHVAELEEDLD-------TARK-DLIKSEEVnsrlQRDVREAMAQKEDMEERITTLEKRYLAAQREATSV 388
Cdd:COG1196 183 ATEENLERLEDILGELERQLEplerqaeKAERyRELKEELK----ELEAELLLLKLRELEAELEELEAELEELEAELEEL 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 389 HDLNDKLESEIANKDAVHRQTEDKNRQLQERLELAEQKLQQTL----RKAETLPEVEAELAQRVAALSKAEERHGNIEER 464
Cdd:COG1196 259 EAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEqdiaRLEERRRELEERLEELEEELAELEEELEELEEE 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 465 LRQMEAQLEEKNQELQRARQREKMSEEHSKRLSDTVDRLLSESGERLRLHLKERTAALEDKN---ALLREVGDAKKQLEE 541
Cdd:COG1196 339 LEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAqleELEEAEEALLERLER 418
|
250 260
....*....|....*....|....
gi 2076569066 542 TQRDKDQLVLNVEALRAELDQVRL 565
Cdd:COG1196 419 LEEELEELEEALAELEEEEEEEEE 442
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
66-566 |
6.75e-15 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 80.97 E-value: 6.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 66 LEERDRLMDTLRETQETLALTQGKLHEVGHERDSLQRQLSTA-LPQEFAALTKELSVCREQLLEREEEIAELKAERNNTR 144
Cdd:COG4717 87 EEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLpLYQELEALEAELAELPERLEELEERLEELRELEEELE 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 145 LLLEHLEclvsRHERSLRMTVVKRQAQSPAGVSSEVEVLKALKSLFEHHKALDEKVRERLRVALERCSLLEEELGVTHKE 224
Cdd:COG4717 167 ELEAELA----ELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 225 mgrwtftvsKRLRRARTARQVPPLLPHASASAEGAPGAVSRQTPARRPCRSGSPRAGLRLQRSPdgsLSHEEDLAKVLEL 304
Cdd:COG4717 243 ---------ERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREK---ASLGKEAEELQAL 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 305 QEVVDRQAREHCQMKERL---ATLS-GHVAELEEDLDTARKDLIKSEEVNSRLQRDVREAmaqkedmeerittlEKRYLA 380
Cdd:COG4717 311 PALEELEEEELEELLAALglpPDLSpEELLELLDRIEELQELLREAEELEEELQLEELEQ--------------EIAALL 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 381 AQREATSVHDLNDKLEseiankdavhrQTEDKnRQLQERLELAEQKLQQ------TLRKAETLPEVEAELAQRVAALSKA 454
Cdd:COG4717 377 AEAGVEDEEELRAALE-----------QAEEY-QELKEELEELEEQLEEllgeleELLEALDEEELEEELEELEEELEEL 444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 455 EERHGNIEERLRQMEAQLE--EKNQELQRARQREKMSEEHSKRLSD--TVDRLLSESGERLRLHLKERTAA--LEDKNAL 528
Cdd:COG4717 445 EEELEELREELAELEAELEqlEEDGELAELLQELEELKAELRELAEewAALKLALELLEEAREEYREERLPpvLERASEY 524
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 2076569066 529 LREVGDAKKQLEETQ-------RDKDQLVLNVEAL-RAELDQ----VRLG 566
Cdd:COG4717 525 FSRLTDGRYRLIRIDedlslkvDTEDGRTRPVEELsRGTREQlylaLRLA 574
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
295-564 |
7.41e-15 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 81.64 E-value: 7.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 295 EEDLAKVLELQEVVDRQAREHCQMKERLATLSGHVAELEEDLDTARKDLIKSEEVNSRLQRDVREAMAQKEDMEERITTL 374
Cdd:TIGR02168 722 EELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKAL 801
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 375 EKRYLAAQREAT----SVHDLNDKLESEIANKDAVHRQTEDKNRQLqERLELAEQKLQQTLRKAET-LPEVEAELAQRVA 449
Cdd:TIGR02168 802 REALDELRAELTllneEAANLRERLESLERRIAATERRLEDLEEQI-EELSEDIESLAAEIEELEElIEELESELEALLN 880
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 450 ALSKAEERHGNIEERLRQMEAQL---EEKNQELQRARQ--REKMSEEHSK--RLSDTVDRLLSESGERLRLHLKErtaAL 522
Cdd:TIGR02168 881 ERASLEEALALLRSELEELSEELrelESKRSELRRELEelREKLAQLELRleGLEVRIDNLQERLSEEYSLTLEE---AE 957
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 2076569066 523 EDKNALLREVGDAKKQLEETQRDKDQL-VLNVEALrAELDQVR 564
Cdd:TIGR02168 958 ALENKIEDDEEEARRRLKRLENKIKELgPVNLAAI-EEYEELK 999
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
294-494 |
1.42e-14 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 80.87 E-value: 1.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 294 HEEDLAKVLELQEVVDRQAREHCQMKERLATLsghVAELEEDLDTARKDLIKSEEVNSRLQRDVREAMAQKEDMEERITT 373
Cdd:TIGR02168 307 LRERLANLERQLEELEAQLEELESKLDELAEE---LAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLET 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 374 LEKRYLAAQREATSvhdlndkLESEIANKDAVHRQTEDKNRQLQERLELAEQKLQQTLRKA--ETLPEVEAELAQRVAAL 451
Cdd:TIGR02168 384 LRSKVAQLELQIAS-------LNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKElqAELEELEEELEELQEEL 456
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2076569066 452 SKAEERHGNIEERLRQMEAQLEEKNQELQRARQR----EKMSEEHSK 494
Cdd:TIGR02168 457 ERLEEALEELREELEEAEQALDAAERELAQLQARldslERLQENLEG 503
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
295-564 |
2.02e-14 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 80.10 E-value: 2.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 295 EEDLAKVLELQEVVDRQAREHCQMKERLATLSGHVAELEEDLDTARKDLIKSEEVNSRLQRDVREAMAQKEDMEERITTL 374
Cdd:TIGR02168 778 AEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESL 857
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 375 EKRYLAAQREAtsvhdlnDKLESEIANKDAVHRQTEDKNRQLQERLELAEQKLQqtlrkaetlpEVEAELAQRVAALSKA 454
Cdd:TIGR02168 858 AAEIEELEELI-------EELESELEALLNERASLEEALALLRSELEELSEELR----------ELESKRSELRRELEEL 920
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 455 EERHGNIEERLRQMEAQLEEKnqeLQRARQREKMSEEHSKRLSDTVDRLLSESGERLRLH-------------------- 514
Cdd:TIGR02168 921 REKLAQLELRLEGLEVRIDNL---QERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLenkikelgpvnlaaieeyee 997
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 2076569066 515 LKERtaaLEDKNALLREVGDAKKQLEETQRDKDQLVLNVeaLRAELDQVR 564
Cdd:TIGR02168 998 LKER---YDFLTAQKEDLTEAKETLEEAIEEIDREARER--FKDTFDQVN 1042
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
334-564 |
2.70e-14 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 79.72 E-value: 2.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 334 EDLDTARKDLIK-SEEVNSRLQRdVREAMAQKEDMEERITTLEKRYLAAQREAtsvhdlnDKLESEIankdavhrqtedk 412
Cdd:PRK03918 158 DDYENAYKNLGEvIKEIKRRIER-LEKFIKRTENIEELIKEKEKELEEVLREI-------NEISSEL------------- 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 413 nRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKAEERHGNIEERLRQMEAQ---LEEKNQELQRARQREKMS 489
Cdd:PRK03918 217 -PELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEieeLEEKVKELKELKEKAEEY 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 490 EEHSKRLSDTVDRL--LSESGERLRLHLKERTAALEDKNALLREVGDAKKQLEETQRDKDQL---VLNVEALRAELDQVR 564
Cdd:PRK03918 296 IKLSEFYEEYLDELreIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELeerHELYEEAKAKKEELE 375
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
293-564 |
3.26e-14 |
|
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: 79.45 E-value: 3.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 293 SHEEDLAKVLELQEvvdrQAREHCQMKErlATLSGHVAELEEDLDTArkdliksEEVNSRLQRdvreamaQKEDMEERIT 372
Cdd:pfam01576 103 QHIQDLEEQLDEEE----AARQKLQLEK--VTTEAKIKKLEEDILLL-------EDQNSKLSK-------ERKLLEERIS 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 373 TLEKRYLAAQREATSVHDLNDKLESEIANKDaVHRQTEDKNRQLQERL---------ELAEQKLQQTLRKAE---TLPEV 440
Cdd:pfam01576 163 EFTSNLAEEEEKAKSLSKLKNKHEAMISDLE-ERLKKEEKGRQELEKAkrklegestDLQEQIAELQAQIAElraQLAKK 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 441 EAELAqrvAALSKAEE---RHGNIEERLRQMEAQLEEKNQELQRARQREKMSEEHSKRLSDTVDRLLSESGERLrlhlkE 517
Cdd:pfam01576 242 EEELQ---AALARLEEetaQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTL-----D 313
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 2076569066 518 RTAA-LEDKNALLREVGDAKKQLEETQRDKDQLVLN--------VEALRAELDQVR 564
Cdd:pfam01576 314 TTAAqQELRSKREQEVTELKKALEEETRSHEAQLQEmrqkhtqaLEELTEQLEQAK 369
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
96-503 |
5.20e-14 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 78.95 E-value: 5.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 96 ERDSLQRQLsTALPQEFAALTKELSVCREQLLEREEEIAELKAERNNTRLLLEHLECLVSRHERSLRmTVVKRQAQSPAG 175
Cdd:TIGR02168 678 EIEELEEKI-EELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVE-QLEERIAQLSKE 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 176 VSS----EVEVLKALKSLFEHHKALDEK---VRERLRVALERCSLLEEELGVTHKEMgrwtftvsKRLRRARTarqvppl 248
Cdd:TIGR02168 756 LTEleaeIEELEERLEEAEEELAEAEAEieeLEAQIEQLKEELKALREALDELRAEL--------TLLNEEAA------- 820
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 249 lphasasaegapgavsrqtparrpcrsgspRAGLRLQrspdgslSHEEDLAKVLELQEVVDRQARehcQMKERLATLSGH 328
Cdd:TIGR02168 821 ------------------------------NLRERLE-------SLERRIAATERRLEDLEEQIE---ELSEDIESLAAE 860
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 329 VAELEEDLDTARKDLIKSEEVNSRLQRDVREAMAQKEDMEERITTLEKRYLAAQREAtsvHDLNDKLESEIANKDavhrQ 408
Cdd:TIGR02168 861 IEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRREL---EELREKLAQLELRLE----G 933
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 409 TEDKNRQLQERL-ELAEQKLQQTLRKAETLPEVEAELAQRVAALSKAEERHGNI-----------EERLRQMEAQLEekn 476
Cdd:TIGR02168 934 LEVRIDNLQERLsEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVnlaaieeyeelKERYDFLTAQKE--- 1010
|
410 420 430
....*....|....*....|....*....|..
gi 2076569066 477 qELQRARQR-----EKMSEEHSKRLSDTVDRL 503
Cdd:TIGR02168 1011 -DLTEAKETleeaiEEIDREARERFKDTFDQV 1041
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
309-562 |
8.07e-14 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 78.16 E-value: 8.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 309 DRQAREhcQMKERLATLSGHVAELEEDLDTArKDLIKSEEVNSRLQRdvreamaQKEDMEERITTLEKRyLAAQRE-ATS 387
Cdd:PRK02224 473 DRERVE--ELEAELEDLEEEVEEVEERLERA-EDLVEAEDRIERLEE-------RREDLEELIAERRET-IEEKRErAEE 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 388 VHDLNDKLESEIANKDAVHRQTEDKNRQLQERLELAEQKLQ------QTLRKAETLPEVEAELAQRVAAL-----SKAE- 455
Cdd:PRK02224 542 LRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAelkeriESLERIRTLLAAIADAEDEIERLrekreALAEl 621
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 456 -----ERHGNIEERLRQMEAQ-----LEEKNQELQRARQREKMSEEHSKRLSDTVDRLLSESG------ERLRlHLKERT 519
Cdd:PRK02224 622 nderrERLAEKRERKRELEAEfdearIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGavenelEELE-ELRERR 700
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 2076569066 520 AALEDKNALLREVGDAKKQLEETQRDkdqlvlnveaLRAELDQ 562
Cdd:PRK02224 701 EALENRVEALEALYDEAEELESMYGD----------LRAELRQ 733
|
|
| SAM_1 |
pfam00536 |
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ... |
1283-1347 |
1.10e-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: 68.06 E-value: 1.10e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2076569066 1283 DMNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRgQLKMVDSFHRNSFQCGIMCLR 1347
Cdd:pfam00536 1 DGWSVEDVGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDDLL-KLGVTLLGHRKKILYAIQRLK 64
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
295-564 |
1.24e-13 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 77.41 E-value: 1.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 295 EEDLAKVLELQEVVDRQAREHCQMKERLATLSGHVAELEEDLDTARKDLIKSEEVNSRLQRDVREAMAQKEDMEE--RIT 372
Cdd:PRK03918 220 REELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEyiKLS 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 373 TLEKRYLAAQREatsVHDLNDKLESEIANKDAVHRQTEDKNRQLQE-------------RLELAEQKLQQTLRKAETLPE 439
Cdd:PRK03918 300 EFYEEYLDELRE---IEKRLSRLEEEINGIEERIKELEEKEERLEElkkklkelekrleELEERHELYEEAKAKKEELER 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 440 VEAELAQR-----VAALSKAEERHGNIEERLRQMEAQLEEKNQElqRARQREKMSE-EHSKRLSDTVDRLLSESgERLRL 513
Cdd:PRK03918 377 LKKRLTGLtpeklEKELEELEKAKEEIEEEISKITARIGELKKE--IKELKKAIEElKKAKGKCPVCGRELTEE-HRKEL 453
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 2076569066 514 hLKERTAALEDKNALLREVGDAKKQLEETQRDKDQLVLNVEALRAE---LDQVR 564
Cdd:PRK03918 454 -LEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLkelAEQLK 506
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
283-509 |
2.42e-13 |
|
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: 76.65 E-value: 2.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 283 RLQRSPDGSLSHEEDLA-KVLELQEVVDRQAREHCQMKERLATLSGHVAELEEDLDTARKDLIKS----EEVNSRLQRDV 357
Cdd:TIGR02169 305 SLERSIAEKERELEDAEeRLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLraelEEVDKEFAETR 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 358 REAMAQKEDMEEritTLEKRYlAAQREATSVHDLNDKLESEIANKDAVHRQTEDKNRQLQERLElaeqklqqtlRKAETL 437
Cdd:TIGR02169 385 DELKDYREKLEK---LKREIN-ELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKE----------DKALEI 450
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2076569066 438 PEVEAELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMSEEHSKRLSDTVDrLLSESGE 509
Cdd:TIGR02169 451 KKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEE-VLKASIQ 521
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
76-482 |
4.11e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 75.86 E-value: 4.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 76 LRETQETLALTQGKLHEVGHERDSLQRQLSTAlpQEFAALTKELSvcREQLLEREEEIAELKAERNNTRLLLEHLECLVS 155
Cdd:TIGR02168 181 LERTRENLDRLEDILNELERQLKSLERQAEKA--ERYKELKAELR--ELELALLVLRLEELREELEELQEELKEAEEELE 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 156 RHERSLRMTvvkrqaqspagvSSEVEVLKAlkslfEHHKaLDEKVRE---RLRVALERCSLLEEELGVThkemgrwtftv 232
Cdd:TIGR02168 257 ELTAELQEL------------EEKLEELRL-----EVSE-LEEEIEElqkELYALANEISRLEQQKQIL----------- 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 233 SKRLRRARTARQvppllphasasaegapgavsrqtparrpcrsgspRAGLRLQRSPDGSLSHEEDLA----KVLELQEVV 308
Cdd:TIGR02168 308 RERLANLERQLE----------------------------------ELEAQLEELESKLDELAEELAeleeKLEELKEEL 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 309 DRQAREHCQMKERLATLSGHVAELEEDLDTARKDLIKSEEVNSRLQRDVREAMAQKEDMEERITTLEKRYLAAQREATSv 388
Cdd:TIGR02168 354 ESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEE- 432
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 389 HDLnDKLESEIANKDAVHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKAEERHGNIEERLRQM 468
Cdd:TIGR02168 433 AEL-KELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKAL 511
|
410
....*....|....
gi 2076569066 469 EAQLEEKNQELQRA 482
Cdd:TIGR02168 512 LKNQSGLSGILGVL 525
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
67-541 |
6.62e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 74.97 E-value: 6.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 67 EERDRLMDTLRETQETLALTQGKLHEVGHERDSLQRQLSTALpQEFAALTKELSVCREQLLEREEEIAELKAERNNTRLL 146
Cdd:COG1196 323 EELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAE-EALLEAEAELAEAEEELEELAEELLEALRAAAELAAQ 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 147 LEHLEclvsRHERSLRmtvvKRQAQSPAGVSSEVEVLKALKSLFEHHKALDEKVRERLRVALERCSLLEEELGVTHKEMG 226
Cdd:COG1196 402 LEELE----EAEEALL----ERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAA 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 227 RWTFTVSKRLRRARTARQVPPLLPHASASAEGAPGAVSRQtpARRPCRSGSPRAGLRLQRSPDGSLSHEEDLAKVLELQE 306
Cdd:COG1196 474 LLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAA--LLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNI 551
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 307 VVDRQAREHCQMKERLATLSGHVAELEedLDTARKDLIKSEEVNSRLQRDVREAMAQKEDMEERITTLEKRYLAAQREAT 386
Cdd:COG1196 552 VVEDDEVAAAAIEYLKAAKAGRATFLP--LDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVA 629
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 387 SVHDLNDKLESEIANKDAVHRQTEDKNRQLQERLELAEQKLQQTLRKAETLpevEAELAQRVAALSKAEERHgniEERLR 466
Cdd:COG1196 630 ARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAE---LEELAERLAEEELELEEA---LLAEE 703
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2076569066 467 QMEAQLEEKNQELQRARQREKMSEEHSKRLSDTVDRLLSESGERLRLHLKERTAALEDKNALLREVGDAKKQLEE 541
Cdd:COG1196 704 EEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEA 778
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
296-562 |
7.37e-13 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 74.72 E-value: 7.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 296 EDLAKVLELQEVVDRQAREhcqMKERLATLSGHVAELEEDLDTARKDLiksEEVNSRLQRdvreamaqKEDMEERITTLE 375
Cdd:PRK03918 179 ERLEKFIKRTENIEELIKE---KEKELEEVLREINEISSELPELREEL---EKLEKEVKE--------LEELKEEIEELE 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 376 KRylaaqreatsvhdlNDKLESEIANKDAVHRQTEDKNRQLQERLELAEQK---LQQTLRKAETLPEVEAELAQRVAALS 452
Cdd:PRK03918 245 KE--------------LESLEGSKRKLEEKIRELEERIEELKKEIEELEEKvkeLKELKEKAEEYIKLSEFYEEYLDELR 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 453 KAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMSEEHSKRLS---------DTVDRLLSESgERLRLHLKERTaaLE 523
Cdd:PRK03918 311 EIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEeleerhelyEEAKAKKEEL-ERLKKRLTGLT--PE 387
|
250 260 270
....*....|....*....|....*....|....*....
gi 2076569066 524 DKNALLREVGDAKKQLEETqrdkdqlVLNVEALRAELDQ 562
Cdd:PRK03918 388 KLEKELEELEKAKEEIEEE-------ISKITARIGELKK 419
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
295-566 |
9.03e-13 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 74.72 E-value: 9.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 295 EEDLaKVLELQEVvDRQAREHCQMKERLATLSGHVAELEEDLDtarkdliKSEEVNSRLqrdvREAMAQKEDMEERITTL 374
Cdd:PRK03918 509 EEKL-KKYNLEEL-EKKAEEYEKLKEKLIKLKGEIKSLKKELE-------KLEELKKKL----AELEKKLDELEEELAEL 575
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 375 EKRYLaaQREATSVHDLNDKLES--EIANKDAVHRQTEDKNRQLQERLELAEQKLQQTLRK-AETLPEVEaELAQRVAAL 451
Cdd:PRK03918 576 LKELE--ELGFESVEELEERLKElePFYNEYLELKDAEKELEREEKELKKLEEELDKAFEElAETEKRLE-ELRKELEEL 652
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 452 SK--AEERHGNIEERLRQMEA----------QLEEKNQELQRA-----RQREKMSE--EHSKRLSDTVDRLlsesgERLR 512
Cdd:PRK03918 653 EKkySEEEYEELREEYLELSRelaglraeleELEKRREEIKKTleklkEELEEREKakKELEKLEKALERV-----EELR 727
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 2076569066 513 LHLKERTAALedKNALLREVGD-AKKQLEETQRDKDQLVlnveALRAELDQVRLG 566
Cdd:PRK03918 728 EKVKKYKALL--KERALSKVGEiASEIFEELTEGKYSGV----RVKAEENKVKLF 776
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
295-561 |
2.06e-12 |
|
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: 73.67 E-value: 2.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 295 EEDLAKVLELQEVVDRQAREHCQMKE---RLATLSGHVAELEEDLDTARKDLIKSEEVNSRLQRDVREAMAQKEDMEERI 371
Cdd:pfam01576 5 EEMQAKEEELQKVKERQQKAESELKElekKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHELESRL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 372 TTLEKRYLAAQRE----ATSVHDLNDKLESEIANKDAVHRQ---TEDKNRQLQER-LELAEQ--KLQQTlRKA--ETLPE 439
Cdd:pfam01576 85 EEEEERSQQLQNEkkkmQQHIQDLEEQLDEEEAARQKLQLEkvtTEAKIKKLEEDiLLLEDQnsKLSKE-RKLleERISE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 440 VEAELA---QRVAALSKAEERH----GNIEERLRQmeaqlEEKN-QELQRARQRekmSEEHSKRLSDTVDRLLSESGErL 511
Cdd:pfam01576 164 FTSNLAeeeEKAKSLSKLKNKHeamiSDLEERLKK-----EEKGrQELEKAKRK---LEGESTDLQEQIAELQAQIAE-L 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2076569066 512 RLHL----KERTAALE-------DKNALLREVGDAKKQLEETQRDKDQ--------------LVLNVEALRAELD 561
Cdd:pfam01576 235 RAQLakkeEELQAALArleeetaQKNNALKKIRELEAQISELQEDLESeraarnkaekqrrdLGEELEALKTELE 309
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
299-562 |
2.26e-12 |
|
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: 73.29 E-value: 2.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 299 AKVLELQEVVDRQAREH-CQMKERLATLSGHVAELEEDLDTARK---DLIKS----EEVNSRLQRDVREAMAQKEDMEER 370
Cdd:pfam01576 327 QEVTELKKALEEETRSHeAQLQEMRQKHTQALEELTEQLEQAKRnkaNLEKAkqalESENAELQAELRTLQQAKQDSEHK 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 371 -------ITTLEKRYLAAQREATSVHDLNDKLESEIANKDAVHRQTEDKN-----------RQLQERLELAEQKLQQTLR 432
Cdd:pfam01576 407 rkklegqLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNiklskdvssleSQLQDTQELLQEETRQKLN 486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 433 KAETLPEVEAELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMSEEHSKRLSDTVdrllsesgERLR 512
Cdd:pfam01576 487 LSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQREL--------EALT 558
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 2076569066 513 LHLKERTAALED----KNALLREVGDAKKQLEEtQRdkdQLVLNVEALRAELDQ 562
Cdd:pfam01576 559 QQLEEKAAAYDKlektKNRLQQELDDLLVDLDH-QR---QLVSNLEKKQKKFDQ 608
|
|
| SAM_liprin-beta1,2_repeat1 |
cd09563 |
SAM domain of liprin-beta1,2 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of ... |
1158-1222 |
4.95e-12 |
|
SAM domain of liprin-beta1,2 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of liprin-beta1,2 proteins is a protein-protein interaction domain. Liprin-beta protein contain three copies (repeats) of SAM domain. They may form heterodimers with liprins-alpha through their SAM domains. It was suggested based on bioinformatic approaches that the second SAM domain of liprin-beta is potentially able to form polymers. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development, in axon guidance, and in the maintenance of lymphatic vessel integrity.
Pssm-ID: 188962 Cd Length: 64 Bit Score: 63.40 E-value: 4.95e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2076569066 1158 FAQWDGPTVVVWL-ELWVGMpawYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQ 1222
Cdd:cd09563 1 FAEWSTEQVCDWLaELGLGQ---YVDECRRWVKSGQTLLKASPQELEKELGIKHPLHRKKLQLALQ 63
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
299-565 |
9.33e-12 |
|
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: 70.10 E-value: 9.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 299 AKVLELQEVVDRQAREHCQMKERLATLSGHVAELEEDLDTARKDLIKSEEVNSRLQRDVREAMAQKEDMEERITTLEKRY 378
Cdd:pfam19220 48 SRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVARLAKLEAALREAEAAKEELRIELRDKTAQAEALERQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 379 LAAQREATSVHDLNDKLESEIANKDAVHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKAEERH 458
Cdd:pfam19220 128 AAETEQNRALEEENKALREEAQAAEKALQRAEGELATARERLALLEQENRRLQALSEEQAAELAELTRRLAELETQLDAT 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 459 ----GNIEERLRQM-------EAQLEEKN--QELQRARQREKMSEEHSkRLSDTvDRLLSEsgerLRLHLKERTAALEDK 525
Cdd:pfam19220 208 rarlRALEGQLAAEqaereraEAQLEEAVeaHRAERASLRMKLEALTA-RAAAT-EQLLAE----ARNQLRDRDEAIRAA 281
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 2076569066 526 NALLREVGDAKKQLEETQRDKDQLVLNVEALRAELDQVRL 565
Cdd:pfam19220 282 ERRLKEASIERDTLERRLAGLEADLERRTQQFQEMQRARA 321
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
135-564 |
9.58e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 71.25 E-value: 9.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 135 ELKAERNNTRLLLEHLECLVSRHERSLRmtVVKRQAQSPAGVSSEV-EVLKALKSLFEHHKALDEKVR--ERLRVALERC 211
Cdd:PRK03918 297 KLSEFYEEYLDELREIEKRLSRLEEEIN--GIEERIKELEEKEERLeELKKKLKELEKRLEELEERHElyEEAKAKKEEL 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 212 SLLEEELGVTHKEmgrwtfTVSKRLRRARTARQVPPL----LPHASASAEGAPG----AVSRQTPARRPCrsgsPRAGLR 283
Cdd:PRK03918 375 ERLKKRLTGLTPE------KLEKELEELEKAKEEIEEeiskITARIGELKKEIKelkkAIEELKKAKGKC----PVCGRE 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 284 LqrspdgSLSHEEDLAKvlelqevvdrqarehcQMKERLATLSGHVAELEEDLDTARKDLIKSEEV---NSRLQRdVREA 360
Cdd:PRK03918 445 L------TEEHRKELLE----------------EYTAELKRIEKELKEIEEKERKLRKELRELEKVlkkESELIK-LKEL 501
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 361 MAQKEDMEERITTLEKRYL-AAQREATSVHDLNDKLESEIAN-KDAVHRQTEDKNR--QLQERLELAEQKLQQTLRKA-- 434
Cdd:PRK03918 502 AEQLKELEEKLKKYNLEELeKKAEEYEKLKEKLIKLKGEIKSlKKELEKLEELKKKlaELEKKLDELEEELAELLKELee 581
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 435 ---ETLPEVEAELAQ------RVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRArqrEKMSEEHSKRLSDTVDRLLS 505
Cdd:PRK03918 582 lgfESVEELEERLKElepfynEYLELKDAEKELEREEKELKKLEEELDKAFEELAET---EKRLEELRKELEELEKKYSE 658
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 2076569066 506 ESGERLRlhlkERTAALEdknallREVGDAKKQLEETQRDKDQLVLNVEALRAELDQVR 564
Cdd:PRK03918 659 EEYEELR----EEYLELS------RELAGLRAELEELEKRREEIKKTLEKLKEELEERE 707
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
293-563 |
2.87e-11 |
|
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: 69.82 E-value: 2.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 293 SHEEDLakvLELQEVVDRQAREHCQMKERLATLSGHVAELEEDLDTARKDLIKSEEVNS--------------------- 351
Cdd:pfam01576 135 KLEEDI---LLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISdleerlkkeekgrqelekakr 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 352 RLQRDVREAMAQKEDMEERITTL-------EKRYLAAQ-----------------REATS-VHDLNDKLESEIANKDavh 406
Cdd:pfam01576 212 KLEGESTDLQEQIAELQAQIAELraqlakkEEELQAALarleeetaqknnalkkiRELEAqISELQEDLESERAARN--- 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 407 rQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKAEERHGNIEE----RLRQMEAQ-LEEKNQELQR 481
Cdd:pfam01576 289 -KAEKQRRDLGEELEALKTELEDTLDTTAAQQELRSKREQEVTELKKALEEETRSHEaqlqEMRQKHTQaLEELTEQLEQ 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 482 ARqREKMSEEHSKRlsdtvdRLLSESGErLRLHLKERTAALED----KNALLREVGDAKKQLEETQRDKDQLVLNVEALR 557
Cdd:pfam01576 368 AK-RNKANLEKAKQ------ALESENAE-LQAELRTLQQAKQDsehkRKKLEGQLQELQARLSESERQRAELAEKLSKLQ 439
|
....*.
gi 2076569066 558 AELDQV 563
Cdd:pfam01576 440 SELESV 445
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
303-672 |
3.06e-11 |
|
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: 69.69 E-value: 3.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 303 ELQEVVDRQAREHCQMKERLATLSGHVAELEEDLDTARKDLIKSEEVNSRLQRDVREAMAQkEDMEERITTLEKRYLAAQ 382
Cdd:TIGR00606 574 QLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGS-QDEESDLERLKEEIEKSS 652
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 383 REATSvhdlndkLESEIANKDAVHRQTEDKN--------RQLQERLELAE--QKLQQTLRKAET-LPEVEAELA----QR 447
Cdd:TIGR00606 653 KQRAM-------LAGATAVYSQFITQLTDENqsccpvcqRVFQTEAELQEfiSDLQSKLRLAPDkLKSTESELKkkekRR 725
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 448 VAALSKAEERHGNIEERLRQMEaQLEEKNQELQRARQREKMSEEHSKRLSDTV-------DRLLSESG--ERLRLHLKE- 517
Cdd:TIGR00606 726 DEMLGLAPGRQSIIDLKEKEIP-ELRNKLQKVNRDIQRLKNDIEEQETLLGTImpeeesaKVCLTDVTimERFQMELKDv 804
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 518 -----RTAALEDKNALLREVGDAKKQLEETQRDKDQLVLNVEALRaELDQVRlggpslHHGRPHLGSvpdfrfpaadgpa 592
Cdd:TIGR00606 805 erkiaQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNR-KLIQDQ------QEQIQHLKS------------- 864
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 593 dpcgssavrTLNEQDWERAQQASVLASvAQAFESD------------RELSDGGEDqdalfgsaglLSPggqaDAQTLAV 660
Cdd:TIGR00606 865 ---------KTNELKSEKLQIGTNLQR-RQQFEEQlvelstevqsliREIKDAKEQ----------DSP----LETFLEK 920
|
410
....*....|..
gi 2076569066 661 MLQEQLDAINKE 672
Cdd:TIGR00606 921 DQQEKEELISSK 932
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
66-502 |
4.13e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 69.20 E-value: 4.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 66 LEERDRLMDTLRETQETLALTQGKLHEvghERDSLQRQLSTALPQEFAALTKELSvcreqlleREEEIAELKAERNNTRL 145
Cdd:COG1196 409 EEALLERLERLEEELEELEEALAELEE---EEEEEEEALEEAAEEEAELEEEEEA--------LLELLAELLEEAALLEA 477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 146 LLEHLecLVSRHERSLRMTVVKRQAQSPAGVSSEVEVLKALKSLfehhKALDEKVRERLRVALERCSLLEEELGVTHKEm 225
Cdd:COG1196 478 ALAEL--LEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGL----RGLAGAVAVLIGVEAAYEAALEAALAAALQN- 550
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 226 grwtfTVSKRLRRARTARQVppLLPHASASAEGAPGAVSRQTPARRpcRSGSPRAGLRLQRSPDGSLSHEEDLAKVLELQ 305
Cdd:COG1196 551 -----IVVEDDEVAAAAIEY--LKAAKAGRATFLPLDKIRARAALA--AALARGAIGAAVDLVASDLREADARYYVLGDT 621
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 306 EVVDRQAREHCQMKERLATLSGH----VAELEEDLDTARKDLIKSEEVNSRLQRDVREAMAQKEDMEERITTLEKRYLAA 381
Cdd:COG1196 622 LLGRTLVAARLEAALRRAVTLAGrlreVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLA 701
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 382 QREATSV-HDLNDKLESEIANKDAVHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKAEERHGN 460
Cdd:COG1196 702 EEEEERElAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEALGP 781
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 2076569066 461 I-----------EERLRQMEAQLEeknqELQRARQR-----EKMSEEHSKRLSDTVDR 502
Cdd:COG1196 782 VnllaieeyeelEERYDFLSEQRE----DLEEARETleeaiEEIDRETRERFLETFDA 835
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
370-565 |
4.30e-11 |
|
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: 65.79 E-value: 4.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 370 RITTLEKRYLAAQREATSVHDLNDKLESeIANKDAVhrqtEDKNRQLQERLELAEQKLQQ------TLRKAE-------- 435
Cdd:pfam12795 1 KLDELEKAKLDEAAKKKLLQDLQQALSL-LDKIDAS----KQRAAAYQKALDDAPAELRElrqelaALQAKAeaapkeil 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 436 ---TLPEVEAELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQRekmSEEHSKRLSDT--VDRLLSESger 510
Cdd:pfam12795 76 aslSLEELEQRLLQTSAQLQELQNQLAQLNSQLIELQTRPERAQQQLSEARQR---LQQIRNRLNGPapPGEPLSEA--- 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2076569066 511 LRLHLKERTAALEDKNALLREVGD--------AKKQLEETQRDKDQLVLNVEALRAELDQVRL 565
Cdd:pfam12795 150 QRWALQAELAALKAQIDMLEQELLsnnnrqdlLKARRDLLTLRIQRLEQQLQALQELLNEKRL 212
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
65-584 |
4.46e-11 |
|
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: 68.99 E-value: 4.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 65 MLEERDRLMDTLRETQETlalTQGKLHEVG--------------HERDSLQ----RQLSTALPQEFAALTKELSVCREQL 126
Cdd:pfam15921 164 MLEDSNTQIEQLRKMMLS---HEGVLQEIRsilvdfeeasgkkiYEHDSMStmhfRSLGSAISKILRELDTEISYLKGRI 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 127 LEREEEIAELKAE-RNNTRLLLEH----LECLVSRHERSLR-MTVVKRQAQSPA-GVSSEVEVLKalkslfehhkaldEK 199
Cdd:pfam15921 241 FPVEDQLEALKSEsQNKIELLLQQhqdrIEQLISEHEVEITgLTEKASSARSQAnSIQSQLEIIQ-------------EQ 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 200 VRERLRVALERCSLLEEelgvthkemgrwtfTVSKRLRRARTARqvppllphasasaegapgavsrqtparrpcrsgspr 279
Cdd:pfam15921 308 ARNQNSMYMRQLSDLES--------------TVSQLRSELREAK------------------------------------ 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 280 aglrlqRSPDGSLsheEDLAKVLELQEVVDRQAR-EHCQMKERLATLSGHVAELEEDLDTARKDLIKSEEVNSRL-QRDV 357
Cdd:pfam15921 338 ------RMYEDKI---EELEKQLVLANSELTEARtERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLwDRDT 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 358 REAMAQKEDMEErittLEKRYLAAQREATSVHDLNDKLESEIANKDAVhrqTEDKNRQLQERLELAEQkLQQTlrkAETL 437
Cdd:pfam15921 409 GNSITIDHLRRE----LDDRNMEVQRLEALLKAMKSECQGQMERQMAA---IQGKNESLEKVSSLTAQ-LEST---KEML 477
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 438 PEVEAELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQRE--KMSE-EHSKRLSDTVDRLLSESgERLRLH 514
Cdd:pfam15921 478 RKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVdlKLQElQHLKNEGDHLRNVQTEC-EALKLQ 556
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 515 LKERTAALE-------------------------DKNALLREVGDAKKQLEETQRDKDQLVLNVEALRA-----ELDQVR 564
Cdd:pfam15921 557 MAEKDKVIEilrqqienmtqlvgqhgrtagamqvEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEArvsdlELEKVK 636
|
570 580
....*....|....*....|
gi 2076569066 565 LggpsLHHGRPHLGSVPDFR 584
Cdd:pfam15921 637 L----VNAGSERLRAVKDIK 652
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
293-550 |
4.46e-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: 69.32 E-value: 4.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 293 SHEEDLAKVLELQEVVDRQAREHCQMKERLATLSGHVAELEEDLDTARKDLIKSEEVNSRLQRDVREAMAQKEDMEERIT 372
Cdd:TIGR02168 268 KLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLE 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 373 TLEKRYLAAQREATSVHDLNDKLESEIANKDAVHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALS 452
Cdd:TIGR02168 348 ELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELL 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 453 KAEERHgnieeRLRQMEAQLEEKNQELQRARQREKMSEEHSKRLSDTVDRLLSE--SGERLRLHLKERTAALEDKNALLR 530
Cdd:TIGR02168 428 KKLEEA-----ELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQAldAAERELAQLQARLDSLERLQENLE 502
|
250 260
....*....|....*....|
gi 2076569066 531 EVGDAKKQLEETQRDKDQLV 550
Cdd:TIGR02168 503 GFSEGVKALLKNQSGLSGIL 522
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
352-564 |
5.39e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 68.91 E-value: 5.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 352 RLQRDVREAMaqkEDMEERIttlekrylaAQREATSVHDLNDKLESEIANKDAVHRQTEDKNRQLQERLELAEQKLQQTL 431
Cdd:PRK02224 180 RVLSDQRGSL---DQLKAQI---------EEKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHE 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 432 RKAETLPEVEAELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMSEEHSKRLSDTVDRL---LSESG 508
Cdd:PRK02224 248 ERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELedrDEELR 327
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 509 ERLRLH-------------LKERTAALEDKNALLRE-VGDAKKQLEETQRDKDQLVLNVEALRAELDQVR 564
Cdd:PRK02224 328 DRLEECrvaaqahneeaesLREDADDLEERAEELREeAAELESELEEAREAVEDRREEIEELEEEIEELR 397
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
51-562 |
6.94e-11 |
|
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: 68.46 E-value: 6.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 51 QPDADSHFEQLMVSMLEERDRLMDT-LRETQETLALTQGKLH-----EVGHERDSLQRQLST----------ALPQEFAA 114
Cdd:TIGR00618 387 QKTTLTQKLQSLCKELDILQREQATiDTRTSAFRDLQGQLAHakkqqELQQRYAELCAAAITctaqceklekIHLQESAQ 466
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 115 LTKELSVCREQLLEREEEIAELKAERNNTRLLLEHLECLVsrhERSLRMTVVKRQAQSPAGVSSEvEVLKALKSLFEHHK 194
Cdd:TIGR00618 467 SLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPL---CGSCIHPNPARQDIDNPGPLTR-RMQRGEQTYAQLET 542
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 195 ALdEKVRERLRVALERCSLLEEELgvthkEMGRWTFTVSKRLRRArtarqvppllphASASAEGAPGAVSRQTPARRpcr 274
Cdd:TIGR00618 543 SE-EDVYHQLTSERKQRASLKEQM-----QEIQQSFSILTQCDNR------------SKEDIPNLQNITVRLQDLTE--- 601
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 275 sgsprAGLRLQRSPDGsLSHEEdlakVLELQEVVDRQ--AREHCQMKERLATLSGHVAELEEDLdtarkdlikseevnsr 352
Cdd:TIGR00618 602 -----KLSEAEDMLAC-EQHAL----LRKLQPEQDLQdvRLHLQQCSQELALKLTALHALQLTL---------------- 655
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 353 LQRDVREAMAQKEDMEERitTLEKRYLAAQREATSVHDLNDKLEsEIANKDAVHR---QTEDKNRQLQERLELAEQKLQQ 429
Cdd:TIGR00618 656 TQERVREHALSIRVLPKE--LLASRQLALQKMQSEKEQLTYWKE-MLAQCQTLLReleTHIEEYDREFNEIENASSSLGS 732
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 430 TLR-KAETLPEVEAEL-AQRVAALSKAEERHGN------IEERLRQMEAQLEEKNQELQRARQ------REKMSEEHSKR 495
Cdd:TIGR00618 733 DLAaREDALNQSLKELmHQARTVLKARTEAHFNnneevtAALQTGAELSHLAAEIQFFNRLREedthllKTLEAEIGQEI 812
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 496 LSDTVDRLLSE---SGERLRLHLKertaaLEDKNALLREVGDAKKQLEETQRDKDQLVLNVEALRAELDQ 562
Cdd:TIGR00618 813 PSDEDILNLQCetlVQEEEQFLSR-----LEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDK 877
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
331-564 |
8.36e-11 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 68.40 E-value: 8.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 331 ELEEDLDTARKDLiksEEVNsRLQRDVREAMAQKEDMEeRITTLEKRYLAAQREATSVHDLNDKLESEIAnkdavhrqtE 410
Cdd:COG4913 222 DTFEAADALVEHF---DDLE-RAHEALEDAREQIELLE-PIRELAERYAAARERLAELEYLRAALRLWFA---------Q 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 411 DKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKAEERHGNieERLRQMEAQLEEKNQELQRARQREKMSE 490
Cdd:COG4913 288 RRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGG--DRLEQLEREIERLERELEERERRRARLE 365
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2076569066 491 EHSKRLSDTVDrlLSESG-ERLRLHLKERTAALED-KNALLREVGDAKKQLEETQRDKDQLvlnvealRAELDQVR 564
Cdd:COG4913 366 ALLAALGLPLP--ASAEEfAALRAEAAALLEALEEeLEALEEALAEAEAALRDLRRELREL-------EAEIASLE 432
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
393-559 |
9.70e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 67.49 E-value: 9.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 393 DKLESEI---ANKDAVHRQTEDKNRQLQERLELAEQKLQQTLRKAETLpEVEAELAQRVAALSKAEERHGNIEERLRQME 469
Cdd:COG4717 74 KELEEELkeaEEKEEEYAELQEELEELEEELEELEAELEELREELEKL-EKLLQLLPLYQELEALEAELAELPERLEELE 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 470 AQLEEKNQELQRARQREKMSEEHSKRLSDTVDRLLSESGERLRLHLKERTAALEDKNALLREVGDAKKQLEETQRDKDQL 549
Cdd:COG4717 153 ERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQL 232
|
170
....*....|
gi 2076569066 550 VLNVEALRAE 559
Cdd:COG4717 233 ENELEAAALE 242
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
282-503 |
1.05e-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: 68.16 E-value: 1.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 282 LRLQRSPDGSLSHE--EDLAKVLELQEVVDRQAREHcqmKERLATLSGHVAELEEDLDTARKDLIKSEEVNSRLQRDVRE 359
Cdd:TIGR02168 272 LRLEVSELEEEIEElqKELYALANEISRLEQQKQIL---RERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEE 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 360 AMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLESEIA---NKDAVHRQTEDKNRQLQERLELAEQKLQQTLRKAET 436
Cdd:TIGR02168 349 LKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAqleLQIASLNNEIERLEARLERLEDRRERLQQEIEELLK 428
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2076569066 437 LPEvEAELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMSEEHSKRLSDTVDRL 503
Cdd:TIGR02168 429 KLE-EAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSL 494
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
295-496 |
1.08e-10 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 66.10 E-value: 1.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 295 EEDLAKVLELQEVVDRQAREHCQMKER------------LATLSgHVAELEEDLDTARKDLIKS-EEVNSRLQRDVREAM 361
Cdd:pfam13868 119 EEKLEKQRQLREEIDEFNEEQAEWKELekeeereederiLEYLK-EKAEREEEREAEREEIEEEkEREIARLRAQQEKAQ 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 362 AQKEDMEERittLEKRYLAAQrEATSVHDLNDKLESEIANKDAVHR----QTEDKNRQLQERLELAEQKLQQTLRKAETL 437
Cdd:pfam13868 198 DEKAERDEL---RAKLYQEEQ-ERKERQKEREEAEKKARQRQELQQareeQIELKERRLAEEAEREEEEFERMLRKQAED 273
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2076569066 438 PEVEAELAQRVAALSKA---------EERHgniEERLRQMEAQLEEKNQELQRARQREKMSEEHSKRL 496
Cdd:pfam13868 274 EEIEQEEAEKRRMKRLEhrrelekqiEERE---EQRAAEREEELEEGERLREEEAERRERIEEERQKK 338
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
330-569 |
1.11e-10 |
|
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: 66.33 E-value: 1.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 330 AELEEDLDTARKDLIKSEEVNSRLQRDVREAMAQKEDMEERITTLEKRYlaaqreatsvhdlnDKLESEIANKDAVHRQT 409
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRI--------------RALEQELAALEAELAEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 410 EDKNRQLQERLELAEQKLQQTLRKAETL---PEVEAELAQR-VAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQR 485
Cdd:COG4942 89 EKEIAELRAELEAQKEELAELLRALYRLgrqPPLALLLSPEdFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 486 EkmsEEHSKRLSDTVDRLLSESgERLRLHLKERTAALEDknaLLREVGDAKKQLEETQRDKDQLVLNVEALRAELDQVRL 565
Cdd:COG4942 169 L---EAERAELEALLAELEEER-AALEALKAERQKLLAR---LEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
....
gi 2076569066 566 GGPS 569
Cdd:COG4942 242 RTPA 245
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
178-541 |
1.54e-10 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 67.07 E-value: 1.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 178 SEVEVLKALKSLFEHHKALDEKVRERL--RVALERCSLLEEELGvthKEMGRwtftvSKRLRRARTARQVPpLLPHASAS 255
Cdd:pfam17380 266 TENEFLNQLLHIVQHQKAVSERQQQEKfeKMEQERLRQEKEEKA---REVER-----RRKLEEAEKARQAE-MDRQAAIY 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 256 AEGAPGAVSRQTPARRPCRSGSPRAGLRLQrspdgslshEEDLAKVLELQEVVDRQAREHCQMKERLatlsghvaelEED 335
Cdd:pfam17380 337 AEQERMAMERERELERIRQEERKRELERIR---------QEEIAMEISRMRELERLQMERQQKNERV----------RQE 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 336 LDTARKDLIKSEEVNSRLQRDVREAM--------AQKEDM----EERITTLEKRYLAAQREATSVHDLNDKLESEIANKD 403
Cdd:pfam17380 398 LEAARKVKILEEERQRKIQQQKVEMEqiraeqeeARQREVrrleEERAREMERVRLEEQERQQQVERLRQQEEERKRKKL 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 404 AVHRQTEDKNRQLQERLELAEQKLQQtlRKAETLPE------VEAELAQRVAALSKAEERHGNIEERLRQMEaqLEEKNQ 477
Cdd:pfam17380 478 ELEKEKRDRKRAEEQRRKILEKELEE--RKQAMIEEerkrklLEKEMEERQKAIYEEERRREAEEERRKQQE--MEERRR 553
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2076569066 478 ELQRARqreKMSEEHSkrlsdtvdrllsesgerlrlhlkeRTAALEDKNALLREVGDAKKQLEE 541
Cdd:pfam17380 554 IQEQMR---KATEERS------------------------RLEAMEREREMMRQIVESEKARAE 590
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
66-564 |
2.39e-10 |
|
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: 66.74 E-value: 2.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 66 LEERDRLMDTLRETQETLaltQGKLHEVGHERDSlQRQLSTALPQ---EF-AALTKELSVCREQLLEREEeiAELKAERN 141
Cdd:pfam01576 561 LEEKAAAYDKLEKTKNRL---QQELDDLLVDLDH-QRQLVSNLEKkqkKFdQMLAEEKAISARYAEERDR--AEAEAREK 634
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 142 NTRLL---------LEHLECLvSRHERSLRmtvvkrqAQSPAGVSSEVEVLKALKSLFEHHKALDEKVRErLRVALERcs 212
Cdd:pfam01576 635 ETRALslaraleeaLEAKEEL-ERTNKQLR-------AEMEDLVSSKDDVGKNVHELERSKRALEQQVEE-MKTQLEE-- 703
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 213 lLEEELGVThkEMGRWTFTVSKRLRRARTARQvppllphasasaegapgavsrqtparrpcrsgspraglrLQRSPDGSL 292
Cdd:pfam01576 704 -LEDELQAT--EDAKLRLEVNMQALKAQFERD---------------------------------------LQARDEQGE 741
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 293 SHEEDLAK-VLELQEVVDRQAREHCQMKERLATLSGHVAELEEDLDTAR-------KDLIKSEEVNSRLQRDVREAMAQK 364
Cdd:pfam01576 742 EKRRQLVKqVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANkgreeavKQLKKLQAQMKDLQRELEEARASR 821
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 365 EDM-------EERITTLEKRYLaaqreatsvhdlndKLESEIANKDAVHRQTEdknrqlQERLELAEQKLQQTLRKAETL 437
Cdd:pfam01576 822 DEIlaqskesEKKLKNLEAELL--------------QLQEDLAASERARRQAQ------QERDELADEIASGASGKSALQ 881
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 438 PE---VEAELAQRVAALskaEERHGNIE---ERLRQMEAQLEEKNQELQRAR---QREKMSEEHSKRLSDTVDRLLSESG 508
Cdd:pfam01576 882 DEkrrLEARIAQLEEEL---EEEQSNTEllnDRLRKSTLQVEQLTTELAAERstsQKSESARQQLERQNKELKAKLQEME 958
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2076569066 509 ERLRLHLKERTAALEDKNALL--------REVGDAKKQLEETQRDKDQLVLNVEALRAELDQVR 564
Cdd:pfam01576 959 GTVKSKFKSSIAALEAKIAQLeeqleqesRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYK 1022
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
295-548 |
3.47e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 66.32 E-value: 3.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 295 EEDLAKVLELQEVVD--RQAREHCQMKERLATLSGHVAELEEDLDTARK--------DLIKSEEVnsRLQRDVREAMAQK 364
Cdd:PTZ00121 1493 EEAKKKADEAKKAAEakKKADEAKKAEEAKKADEAKKAEEAKKADEAKKaeekkkadELKKAEEL--KKAEEKKKAEEAK 1570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 365 EDMEERITTLEKRYLAAQREATSVHDLNDKLESEIANKdavhrqTEDKNRQLQERLElAEQ--KLQQTLRKAETLPEVEA 442
Cdd:PTZ00121 1571 KAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMK------AEEAKKAEEAKIK-AEElkKAEEEKKKVEQLKKKEA 1643
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 443 ELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMSEEHSKRLSD---TVDRLLSESGERLRLHLKERT 519
Cdd:PTZ00121 1644 EEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEeakKAEELKKKEAEEKKKAEELKK 1723
|
250 260 270
....*....|....*....|....*....|..
gi 2076569066 520 AALEDK---NALLREVGDAKKQLEETQRDKDQ 548
Cdd:PTZ00121 1724 AEEENKikaEEAKKEAEEDKKKAEEAKKDEEE 1755
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
295-579 |
5.19e-10 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 64.15 E-value: 5.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 295 EEDLAKV-LELQEVVDRQArehcQMKERLATLSGHVAELEEDLDTARKDLIKSEEVNSRLQRDVREAMAQKEDMEERITT 373
Cdd:COG4372 65 EEELEQArSELEQLEEELE----ELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAE 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 374 LEKRYLAAQREATSVHDLNDKLESEIANKDAVHRQTEDK--NRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAAL 451
Cdd:COG4372 141 LQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAeaEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEEL 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 452 S--KAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMSEEHSKRLSDTVDRLLSESGERLRLHLKERTAALEDKN--A 527
Cdd:COG4372 221 LeaKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLlaL 300
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 2076569066 528 LLREVGDAKKQLEETQRDKDQLVLNVEALRAELDQVRLGGPSLHHGRPHLGS 579
Cdd:COG4372 301 LLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLD 352
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
63-564 |
6.19e-10 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 65.13 E-value: 6.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 63 VSMLEERDRLMD-TLRETQETLALTQGKLHEVgheRDSLQRQLST--ALPQEFAALTK-----------ELSVCREQLLE 128
Cdd:pfam05483 270 ANQLEEKTKLQDeNLKELIEKKDHLTKELEDI---KMSLQRSMSTqkALEEDLQIATKticqlteekeaQMEELNKAKAA 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 129 REEEIAELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSpagvsSEVEVLKALKS-----LFEHHKALDEKvrER 203
Cdd:pfam05483 347 HSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKS-----SELEEMTKFKNnkeveLEELKKILAED--EK 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 204 LRVALERCSLLEEELGVTHKEMgrwTFTVSKRlrrartARQVPPLLPHASAsaegapgavsrqtparrpcrsgspraglr 283
Cdd:pfam05483 420 LLDEKKQFEKIAEELKGKEQEL---IFLLQAR------EKEIHDLEIQLTA----------------------------- 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 284 LQRSPDGSLSHEEDLAKVLELQEVVDRQAREHCQMkerlatLSGHVAELEEDLDTARKDLIKSEEvnsrlqrDVREAMAQ 363
Cdd:pfam05483 462 IKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDK------LLLENKELTQEASDMTLELKKHQE-------DIINCKKQ 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 364 KEDMEERITTLEKRYLAAQREATSVHD----LNDKLESEIANKDAVHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPE 439
Cdd:pfam05483 529 EERMLKQIENLEEKEMNLRDELESVREefiqKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNK 608
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 440 VEAELAQRVAALSK---AEERHGNIEE-RLRQMEAQLEEKNQ---ELQRARQRE----KMSEEH-------SKRLSDTVD 501
Cdd:pfam05483 609 NIEELHQENKALKKkgsAENKQLNAYEiKVNKLELELASAKQkfeEIIDNYQKEiedkKISEEKlleevekAKAIADEAV 688
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2076569066 502 RLLSESGERLRLHLKERTAALE------DKNALLR--EVGDAKKQLEETQRDKDQLVLNVEALRAELDQVR 564
Cdd:pfam05483 689 KLQKEIDKRCQHKIAEMVALMEkhkhqyDKIIEERdsELGLYKNKEQEQSSAKAALEIELSNIKAELLSLK 759
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
295-525 |
6.66e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 65.47 E-value: 6.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 295 EEDLAKV-LELQEVVDRQAREHCQ--------MKERLATLSGHVAELEEDLD--TARKDLIKSEEVNsrLQRDVREAMAQ 363
Cdd:TIGR02169 771 EEDLHKLeEALNDLEARLSHSRIPeiqaelskLEEEVSRIEARLREIEQKLNrlTLEKEYLEKEIQE--LQEQRIDLKEQ 848
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 364 KEDMEERITTLEKRYLAAQREA----TSVHDLNDK---LESEIANKDAVHRQTEDKNRQLQERLELAEQKLQQTLRKAET 436
Cdd:TIGR02169 849 IKSIEKEIENLNGKKEELEEELeeleAALRDLESRlgdLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEA 928
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 437 LPEVEAELAQRVAA----------LSKAEERHGNIEERLRqmeaQLEEKNqelQRARQREKMSEEHSKRLSDTVDRLLSE 506
Cdd:TIGR02169 929 LEEELSEIEDPKGEdeeipeeelsLEDVQAELQRVEEEIR----ALEPVN---MLAIQEYEEVLKRLDELKEKRAKLEEE 1001
|
250
....*....|....*....
gi 2076569066 507 SGErlrlhLKERTAALEDK 525
Cdd:TIGR02169 1002 RKA-----ILERIEEYEKK 1015
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
76-565 |
7.39e-10 |
|
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: 65.20 E-value: 7.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 76 LRETQETLALTQGKLHEVGHERDSLQRQLSTALPQeFAALTKELSvcreqllerEEEIAELKAERNNtRLLLEHLECLVS 155
Cdd:pfam01576 238 LAKKEEELQAALARLEEETAQKNNALKKIRELEAQ-ISELQEDLE---------SERAARNKAEKQR-RDLGEELEALKT 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 156 RHERSLRMTVVKRQAQSPAgvSSEVEVLKalKSLFE---------------HHKALDE-----KVRERLRVALERCSL-L 214
Cdd:pfam01576 307 ELEDTLDTTAAQQELRSKR--EQEVTELK--KALEEetrsheaqlqemrqkHTQALEElteqlEQAKRNKANLEKAKQaL 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 215 EEELGVTHKEMGrwTFTVSK---RLRRARTARQVPPLLPHASAS----AEGAPGAVSRQTPARRPCRSGSPRAGLRLQRS 287
Cdd:pfam01576 383 ESENAELQAELR--TLQQAKqdsEHKRKKLEGQLQELQARLSESerqrAELAEKLSKLQSELESVSSLLNEAEGKNIKLS 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 288 PDGSlSHEEDLAKVLELQEVVDRQarehcqmkeRLAtLSGHVAELEEDLDTARKDLIKSEEVNSRLQRDVREAMAQ---- 363
Cdd:pfam01576 461 KDVS-SLESQLQDTQELLQEETRQ---------KLN-LSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQlsdm 529
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 364 KEDMEERITTLEKRYLAAQREATSVHDLNDKLESEIANKDAVHRQTE-------------DKNRQLQERLELAEQKLQQT 430
Cdd:pfam01576 530 KKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNrlqqelddllvdlDHQRQLVSNLEKKQKKFDQM 609
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 431 L--------RKAETLPEVEAELAQ---RVAALSKA-EERHGNIEERLRQ------------------------------- 467
Cdd:pfam01576 610 LaeekaisaRYAEERDRAEAEAREketRALSLARAlEEALEAKEELERTnkqlraemedlvsskddvgknvhelerskra 689
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 468 -------MEAQLEEKNQELQRARQ----------------------REKMSEEHSKRLSDTVDRLLSE-SGERlrlhlKE 517
Cdd:pfam01576 690 leqqveeMKTQLEELEDELQATEDaklrlevnmqalkaqferdlqaRDEQGEEKRRQLVKQVRELEAElEDER-----KQ 764
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*
gi 2076569066 518 RTAALEDKNALLREVGDAKKQLEETQRDKDQLVLNVEALRA-------ELDQVRL 565
Cdd:pfam01576 765 RAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKKLQAqmkdlqrELEEARA 819
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
294-562 |
7.68e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 65.06 E-value: 7.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 294 HEEDLAKVL-ELQEVVdRQAREHCQMKERLA-TLSGHVAELEEDLDTARKdliKSEEVNSRLQ---RDVREAMAQKEDME 368
Cdd:PRK02224 315 RREELEDRDeELRDRL-EECRVAAQAHNEEAeSLREDADDLEERAEELRE---EAAELESELEearEAVEDRREEIEELE 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 369 ERITTLEKRY--LAAQREatsvhDLNDKLESEIANKDAVHRQ---TEDKNRQLQERLELAEQKLQ--------QTLRKA- 434
Cdd:PRK02224 391 EEIEELRERFgdAPVDLG-----NAEDFLEELREERDELREReaeLEATLRTARERVEEAEALLEagkcpecgQPVEGSp 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 435 ---------ETLPEVEAELAQ-------------RVAALSKAE-------ERHGNIEERLRQMEAQLEEKNQELQRARQR 485
Cdd:PRK02224 466 hvetieedrERVEELEAELEDleeeveeveerleRAEDLVEAEdrierleERREDLEELIAERRETIEEKRERAEELRER 545
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2076569066 486 --EKMSEEHSKRlsDTVDRLLSESGERLrlhlkERTAALEDKNALLREVGDAKKQLEETQRDKDQLVLNVEALRAELDQ 562
Cdd:PRK02224 546 aaELEAEAEEKR--EAAAEAEEEAEEAR-----EEVAELNSKLAELKERIESLERIRTLLAAIADAEDEIERLREKREA 617
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
296-534 |
7.84e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 65.16 E-value: 7.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 296 EDLAKVLELQEVVDRQAREHCQMKERLATLSGHVAELE-----EDLDTARKDLIKSEEVnsRLQRDVREAMAQ-KEDMEE 369
Cdd:PTZ00121 1567 EEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEkkmkaEEAKKAEEAKIKAEEL--KKAEEEKKKVEQlKKKEAE 1644
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 370 RITTLEKRYLAAQREATSVHDLNDKLESEIANKDAVHRQTEDKNRQLQERLELAEQKlqqtlRKAETLPEVEAELAQRVA 449
Cdd:PTZ00121 1645 EKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEA-----KKAEELKKKEAEEKKKAE 1719
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 450 ALSKAEE-RHGNIEERLRQME----------AQLEEKNQELQRARQREKMSEEHSKRLSDTVDRLLSESGERLRLHLKER 518
Cdd:PTZ00121 1720 ELKKAEEeNKIKAEEAKKEAEedkkkaeeakKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKK 1799
|
250
....*....|....*.
gi 2076569066 519 TAALEDKNALLREVGD 534
Cdd:PTZ00121 1800 IKDIFDNFANIIEGGK 1815
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
341-560 |
9.84e-10 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 61.38 E-value: 9.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 341 KDLIKSEeVNSRLQRdvreamaqkedMEERITTLEKRYlaaqREATSVHDlndKLESEIANKDAVHRQTEDKNRQLQERL 420
Cdd:COG1842 7 SDIIRAN-INALLDK-----------AEDPEKMLDQAI----RDMEEDLV---EARQALAQVIANQKRLERQLEELEAEA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 421 ELAEQKLQQTLRK---------AETLPEVEAELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMSeE 491
Cdd:COG1842 68 EKWEEKARLALEKgredlareaLERKAELEAQAEALEAQLAQLEEQVEKLKEALRQLESKLEELKAKKDTLKARAKAA-K 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2076569066 492 HSKRLSDTVDRLLSESGERLRLHLKERTAALEDKNALLREVGDAK---KQLEETQRDK---DQLvlnvEALRAEL 560
Cdd:COG1842 147 AQEKVNEALSGIDSDDATSALERMEEKIEEMEARAEAAAELAAGDsldDELAELEADSeveDEL----AALKAKM 217
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
346-562 |
1.18e-09 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 63.01 E-value: 1.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 346 SEEV---NSRLQR----DVREA-MAQKEDMEERITTLEKRyLAAQREATSVHDLNDKLESEIANKDAVHRQTEDKNRQLQ 417
Cdd:pfam13868 5 SDELrelNSKLLAakcnKERDAqIAEKKRIKAEEKEEERR-LDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 418 ERLELAEQKLQQTLRKAETLPE-VEAELAQRVAalsKAEERHgnieERLRQMEAQLEEKNQELQRARQREKMSEEhskrl 496
Cdd:pfam13868 84 EREQKRQEEYEEKLQEREQMDEiVERIQEEDQA---EAEEKL----EKQRQLREEIDEFNEEQAEWKELEKEEER----- 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2076569066 497 sdtvdrllsESGERLRLHLKERTAALEDKNALLREVGDAK--------KQLEETQRDKDQLvlnvEALRAELDQ 562
Cdd:pfam13868 152 ---------EEDERILEYLKEKAEREEEREAEREEIEEEKereiarlrAQQEKAQDEKAER----DELRAKLYQ 212
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
395-564 |
1.26e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 64.02 E-value: 1.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 395 LESEIANK-DAVHRQTEDKNRQLQERLELAEQKLQQtlrkaetLPEVEAELAQRVAALSKAEERHGNIEERLRQMEAQLE 473
Cdd:COG4717 47 LLERLEKEaDELFKPQGRKPELNLKELKELEEELKE-------AEEKEEEYAELQEELEELEEELEELEAELEELREELE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 474 EKNQELQRARQREKMsEEHSKRLSDTVDRLlsesgERLRLHLKERTAALEDKNALLREVGDAKKQLEETQRDKD------ 547
Cdd:COG4717 120 KLEKLLQLLPLYQEL-EALEAELAELPERL-----EELEERLEELRELEEELEELEAELAELQEELEELLEQLSlateee 193
|
170
....*....|....*....
gi 2076569066 548 --QLVLNVEALRAELDQVR 564
Cdd:COG4717 194 lqDLAEELEELQQRLAELE 212
|
|
| Macoilin |
pfam09726 |
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 ... |
288-579 |
1.37e-09 |
|
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 trasnmembrane helices, followed by a C-terminal coiled-coil region. Macoilin is a highly conserved protein present in eukaryotes. Macoilin appears to be found in the ER and be involved in the function of neurons.
Pssm-ID: 462859 [Multi-domain] Cd Length: 670 Bit Score: 64.10 E-value: 1.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 288 PDGSLSHEEDLAKV-LELQevvdrQAREHCQ-MKERLATLSGHVAELEEDLDTARKDlikseevNSRLQRDVREAMAQKE 365
Cdd:pfam09726 394 PDALVRLEQDIKKLkAELQ-----ASRQTEQeLRSQISSLTSLERSLKSELGQLRQE-------NDLLQTKLHNAVSAKQ 461
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 366 DMEERITTLEKRYLAAQREATSVhdlndklESEIANkdavhrqtEDKNRQLQERLELAEQKLQQTLRK--AETLPEVEAE 443
Cdd:pfam09726 462 KDKQTVQQLEKRLKAEQEARASA-------EKQLAE--------EKKRKKEEEATAARAVALAAASRGecTESLKQRKRE 526
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 444 LAQRVAALSKaeerhgniEERLRQMEA-QLEEKNQELQRARQREKMSEEHSKRLSDTVDRLL----SESGE-RLRLHLke 517
Cdd:pfam09726 527 LESEIKKLTH--------DIKLKEEQIrELEIKVQELRKYKESEKDTEVLMSALSAMQDKNQhlenSLSAEtRIKLDL-- 596
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2076569066 518 rTAALedknallrevGDAKKQLEETQ---RDKDQLVLNVEALRAELDQVRLGGPSLHHGRPHLGS 579
Cdd:pfam09726 597 -FSAL----------GDAKRQLEIAQgqiYQKDQEIKDLKQKIAEVMAVMPSTSRITPVTPHYSS 650
|
|
| ARGLU |
pfam15346 |
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ... |
395-560 |
1.74e-09 |
|
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is required for the oestrogen-dependent expression of ESR1 target genes. It functions in cooperation with MED1. The family of proteins is found in eukaryotes.
Pssm-ID: 405931 [Multi-domain] Cd Length: 151 Bit Score: 58.91 E-value: 1.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 395 LESEIANKDAVHRQTEDKNRQLQERLELAEQklqqtlrkaetlpEVEAELAQRVAalskaEERHgnieERLRQMEAQLE- 473
Cdd:pfam15346 3 AESKLLEEETARRVEEAVAKRVEEELEKRKD-------------EIEAEVERRVE-----EARK----IMEKQVLEELEr 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 474 EKNQELQRARQRekmsEEHSKRLSDTVDRLLSESGERL----RLHLKERTAALEDKNALLREVGDAKKQLEETQRDKDQL 549
Cdd:pfam15346 61 EREAELEEERRK----EEEERKKREELERILEENNRKIeeaqRKEAEERLAMLEEQRRMKEERQRREKEEEEREKREQQK 136
|
170
....*....|.
gi 2076569066 550 VLNVEALRAEL 560
Cdd:pfam15346 137 ILNKKNSRPKL 147
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
303-515 |
3.33e-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: 61.70 E-value: 3.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 303 ELQEVVDRQArehcQMKERLATLSGHVAELEEDLDTARKDLIKSEEVNSRLQRDVREAMAQKEDMEERITTLEKRyLAAQ 382
Cdd:COG4942 28 ELEQLQQEIA----ELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE-LEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 383 RE-------ATSVHDLNDKLESEIANKD------------AVHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAE 443
Cdd:COG4942 103 KEelaellrALYRLGRQPPLALLLSPEDfldavrrlqylkYLAPARREQAEELRADLAELAALRAELEAERAELEALLAE 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2076569066 444 LAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQR-EKMSEEHSKRLSDTVDRLLSESGERLRLHL 515
Cdd:COG4942 183 LEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEElEALIARLEAEAAAAAERTPAAGFAALKGKL 255
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
274-563 |
3.87e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 62.75 E-value: 3.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 274 RSGSPRAGL-RLQRSPDGSLS---------HEEDLAKVL--------ELQEVVDRQAREHCQMKERL----ATLSGH--- 328
Cdd:PRK02224 170 RASDARLGVeRVLSDQRGSLDqlkaqieekEEKDLHERLngleselaELDEEIERYEEQREQARETRdeadEVLEEHeer 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 329 ---VAELEEDLDTARKDLIKSEEVNSRLQRDVREAMAQKEDMEERITtlekrylaaqreatsvhDLNDKLESEIANKDAV 405
Cdd:PRK02224 250 reeLETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERD-----------------DLLAEAGLDDADAEAV 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 406 --HRQT-EDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAAL-SKAEERHGNIE---ERLRQMEAQLEEKNQE 478
Cdd:PRK02224 313 eaRREElEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELrEEAAELESELEearEAVEDRREEIEELEEE 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 479 LQRARQREKMSEEHSKRLSDTVDRLLSESgERLRLHLKERTAALED------KNALLREVG------------------- 533
Cdd:PRK02224 393 IEELRERFGDAPVDLGNAEDFLEELREER-DELREREAELEATLRTarerveEAEALLEAGkcpecgqpvegsphvetie 471
|
330 340 350
....*....|....*....|....*....|
gi 2076569066 534 DAKKQLEETQRDKDQLVLNVEALRAELDQV 563
Cdd:PRK02224 472 EDRERVEELEAELEDLEEEVEEVEERLERA 501
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
364-564 |
4.56e-09 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 62.62 E-value: 4.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 364 KEDMEERITTLEKRYLAAQREATSVHDLNDKLESeIANKDAVHRQTEdknrQLQERLELAEQKLQQTLRKAETLPEVEA- 442
Cdd:PRK11281 38 EADVQAQLDALNKQKLLEAEDKLVQQDLEQTLAL-LDKIDRQKEETE----QLKQQLAQAPAKLRQAQAELEALKDDNDe 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 443 ELAQRVAALSkaeerhgnieerLRQMEAQLEEKNQELQRARqrekmseehsKRLSDTVDRLLSESG--ERLRLHLKERTA 520
Cdd:PRK11281 113 ETRETLSTLS------------LRQLESRLAQTLDQLQNAQ----------NDLAEYNSQLVSLQTqpERAQAALYANSQ 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2076569066 521 ALEDKNALLREVGDAKKQLEETQRDKdqlvLNVE--ALRAELDQVR 564
Cdd:PRK11281 171 RLQQIRNLLKGGKVGGKALRPSQRVL----LQAEqaLLNAQNDLQR 212
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
294-491 |
4.77e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 62.09 E-value: 4.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 294 HEEDLAKVLELQEVVDRQAREHcqmkERLATLSGHVAELEEDLDTARKDLIKSEEVNSRLQR--DVREAMAQKEDMEERI 371
Cdd:COG4717 66 PELNLKELKELEEELKEAEEKE----EEYAELQEELEELEEELEELEAELEELREELEKLEKllQLLPLYQELEALEAEL 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 372 TTLEKRYLAAQREATSVHDLndklESEIANKDAVHRQTEDKNRQLQERLELA-EQKLQQTLRKAEtlpeveaELAQRVAA 450
Cdd:COG4717 142 AELPERLEELEERLEELREL----EEELEELEAELAELQEELEELLEQLSLAtEEELQDLAEELE-------ELQQRLAE 210
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2076569066 451 LSKAEERhgnIEERLRQMEAQLEEKNQELQRARQREKMSEE 491
Cdd:COG4717 211 LEEELEE---AQEELEELEEELEQLENELEAAALEERLKEA 248
|
|
| Tropomyosin_1 |
pfam12718 |
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ... |
352-474 |
5.34e-09 |
|
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and Tpm2, biochemical and sequence analyses indicate that Tpm2p spans four actin monomers along a filament, whereas Tpm1p spans five. Despite its shorter length, Tpm2p can compete with Tpm1p for binding to F-actin. Over-expression of Tpm2p in vivo alters the axial budding of haploids to a bipolar pattern, and this can be partially suppressed by co-over-expression of Tpm1p. This suggests distinct functions for the two tropomyosins, and indicates that the ratio between them is important for correct morphogenesis. The family also contains higher eukaryote Tpm3 members.
Pssm-ID: 403808 [Multi-domain] Cd Length: 142 Bit Score: 57.31 E-value: 5.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 352 RLQRDvrEAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLESEI-------------ANKDAVHRQTED----KNR 414
Cdd:pfam12718 6 KLEAE--NAQERAEELEEKVKELEQENLEKEQEIKSLTHKNQQLEEEVekleeqlkeakekAEESEKLKTNNEnltrKIQ 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2076569066 415 QLQERLELAE-------QKLQQTLRKAEtlpeveaELAQRVAALskaEERHGNIEERLRQMEAQLEE 474
Cdd:pfam12718 84 LLEEELEESDkrlkettEKLRETDVKAE-------HLERKVQAL---EQERDEWEKKYEELEEKYKE 140
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
353-716 |
5.94e-09 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 61.00 E-value: 5.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 353 LQRDVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLESEIankDAVHRQTEDKNRQLQERLELAEQKLQQTLR 432
Cdd:COG3883 21 KQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEI---DKLQAEIAEAEAEIEERREELGERARALYR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 433 KAETLPEVEA--------ELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQRekmseehskrlsdtvdrlL 504
Cdd:COG3883 98 SGGSVSYLDVllgsesfsDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAE------------------L 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 505 SESGERLRLHLKERTAALEDKNALLREVGDAKKQLEETQRDKDQLVLNVEALRAELDQVRLGGPSLHHGRPHLGSVPDFR 584
Cdd:COG3883 160 EALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 585 FPAADGPADPCGSSAVRtlneQDWERAQQASVLASVAQAFESDRELSDGGEDQDALFGSAGLLSPGGQADAQTLAVMLQE 664
Cdd:COG3883 240 AAAAASAAGAGAAGAAG----AAAGSAGAAGAAAGAAGAGAAAASAAGGGAGGAGGGGGGGGAASGGSGGGSGGAGGVGS 315
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 2076569066 665 QLDAINKEISRVTRGAARRRTLPWRTERHLAGEKAGPGVAPTARGSPAGPGS 716
Cdd:COG3883 316 GGGAGAVVGGASAGGGGGSGGGGGSSGGGSGGGGGGGGGGGGSSSGGGGGGV 367
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
293-478 |
7.26e-09 |
|
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: 58.38 E-value: 7.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 293 SHEEDLAKVLELQEVVDRQAREHCQ----MKERLATLSGHVAELEEDLDTARKDlikseevnsrlqrdvREAMAQkedME 368
Cdd:pfam13851 30 SLKEEIAELKKKEERNEKLMSEIQQenkrLTEPLQKAQEEVEELRKQLENYEKD---------------KQSLKN---LK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 369 ERITTLEKRYLAAQREATSVHDLNDKLESEianKDAVHRQTEDKNRQLQERLELAEQKLQQTLRK-AETLPEVEAELAQR 447
Cdd:pfam13851 92 ARLKVLEKELKDLKWEHEVLEQRFEKVERE---RDELYDKFEAAIQDVQQKTGLKNLLLEKKLQAlGETLEKKEAQLNEV 168
|
170 180 190
....*....|....*....|....*....|.
gi 2076569066 448 VAALSKAEERHGNIEERLRQMeaqLEEKNQE 478
Cdd:pfam13851 169 LAAANLDPDALQAVTEKLEDV---LESKNQL 196
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
295-567 |
7.75e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 61.32 E-value: 7.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 295 EEDLAKVLELQEVVDRQAREHC-QMKERLATLSGHVAELEEDLDTARKDLIKSEEVNSRLQRDVR--EAMAQKEDMEERI 371
Cdd:COG4717 166 EELEAELAELQEELEELLEQLSlATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEqlENELEAAALEERL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 372 TTLEKRYL--AAQREATSVHDLNDKLESEIA------------------NKDAVHRQTEDKNRQLQERLELAEQKLQQTL 431
Cdd:COG4717 246 KEARLLLLiaAALLALLGLGGSLLSLILTIAgvlflvlgllallflllaREKASLGKEAEELQALPALEELEEEELEELL 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 432 RKAETLPEVEA----ELAQRVAALSKAEERHGNIEERLRQMEAQlEEKNQELQRA-----RQREKMSEEHSKRLSDTvdR 502
Cdd:COG4717 326 AALGLPPDLSPeellELLDRIEELQELLREAEELEEELQLEELE-QEIAALLAEAgvedeEELRAALEQAEEYQELK--E 402
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2076569066 503 LLSESGERLRLHLKERTAALE--DKNALLREVGDAKKQLEETQRDKDQLVLNVEALRAELDQVRLGG 567
Cdd:COG4717 403 ELEELEEQLEELLGELEELLEalDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDG 469
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
72-546 |
8.68e-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: 61.52 E-value: 8.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 72 LMDTLRETQETLA-LTQgkLHEVGHERDSLQRQLSTALPQ------EFAALTK-----ELSVCREQLLEREEEIAEL--K 137
Cdd:TIGR00618 231 LREALQQTQQSHAyLTQ--KREAQEEQLKKQQLLKQLRARieelraQEAVLEEtqeriNRARKAAPLAAHIKAVTQIeqQ 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 138 AERNNTRLLLEHLECLVSRHERSlrmTVVKRQAQSPAGVSS-------------EVEVLKALKSLFEHHKALDEKVR--- 201
Cdd:TIGR00618 309 AQRIHTELQSKMRSRAKLLMKRA---AHVKQQSSIEEQRRLlqtlhsqeihirdAHEVATSIREISCQQHTLTQHIHtlq 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 202 ERLRVALERCSLLEEELGVTHKEMGrwtfTVSKRLRRARtARQVPPLLPHASASAEGAPGAVSRQTPARR-PCRSGSPRA 280
Cdd:TIGR00618 386 QQKTTLTQKLQSLCKELDILQREQA----TIDTRTSAFR-DLQGQLAHAKKQQELQQRYAELCAAAITCTaQCEKLEKIH 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 281 GLRLQRSPDGSLSHEEDLaKVLELQE---------VVDRQAREHCQMKERLATLSGH-VAELEEDLDTAR--------KD 342
Cdd:TIGR00618 461 LQESAQSLKEREQQLQTK-EQIHLQEtrkkavvlaRLLELQEEPCPLCGSCIHPNPArQDIDNPGPLTRRmqrgeqtyAQ 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 343 LIKSEE-VNSRLQRDVREAMAQKEDMEERITTLEKryLAAQREATS-----VHDLNDKLESEIANKDavhrQTEDKNRQL 416
Cdd:TIGR00618 540 LETSEEdVYHQLTSERKQRASLKEQMQEIQQSFSI--LTQCDNRSKedipnLQNITVRLQDLTEKLS----EAEDMLACE 613
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 417 QERLELAEQKLQQTLRKAETLPEVEAELAQRVAA-------LSKAEERHGNIeeRLRQMEAQLEEKNQELQRARQREKMS 489
Cdd:TIGR00618 614 QHALLRKLQPEQDLQDVRLHLQQCSQELALKLTAlhalqltLTQERVREHAL--SIRVLPKELLASRQLALQKMQSEKEQ 691
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2076569066 490 EEHSKRL---SDTVDRLLSESGERLRLHLKE-------RTAALEDKNALLREVgdaKKQLEETQRDK 546
Cdd:TIGR00618 692 LTYWKEMlaqCQTLLRELETHIEEYDREFNEienasssLGSDLAAREDALNQS---LKELMHQARTV 755
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
295-491 |
8.74e-09 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 60.61 E-value: 8.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 295 EEDLAKVLELQEVVDRQAREHCQMKERLATLSGHVAELEEDLDTARKDLIKseevnsrlqrdvreamaQKEDMEERITTL 374
Cdd:COG3883 33 EAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEE-----------------RREELGERARAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 375 EKR-----YLAAQREATSVHDLNDKLE--SEI--ANKDAVHRQTEDKNR--QLQERLELAEQKLQQTLRKAET-LPEVEA 442
Cdd:COG3883 96 YRSggsvsYLDVLLGSESFSDFLDRLSalSKIadADADLLEELKADKAEleAKKAELEAKLAELEALKAELEAaKAELEA 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2076569066 443 ELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMSEE 491
Cdd:COG3883 176 QQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAA 224
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
56-564 |
1.00e-08 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 61.52 E-value: 1.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 56 SHFEQLMVSMLEER------DRLMDTLRETQETLALTQGKLHEVGHERDSLQRQLsTALPQEFAALTKElsvcreqller 129
Cdd:TIGR00618 511 IHPNPARQDIDNPGpltrrmQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQM-QEIQQSFSILTQC----------- 578
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 130 eeeIAELKAERNNTRLLLEHLECLV---SRHERSLRmtvvkrqaqspagvssevEVLKALKSLFEHHKALdekvrERLRV 206
Cdd:TIGR00618 579 ---DNRSKEDIPNLQNITVRLQDLTeklSEAEDMLA------------------CEQHALLRKLQPEQDL-----QDVRL 632
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 207 ALERCSLlEEELGVTHKEMGRWTFTVSKRLRRARTARQVPPLLphasasaegapgavsrqtparrpcrsgspraGLRLQR 286
Cdd:TIGR00618 633 HLQQCSQ-ELALKLTALHALQLTLTQERVREHALSIRVLPKEL-------------------------------LASRQL 680
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 287 SPDGSLSHEEDLAKVLELQEVVDRQAREhcqMKERLATLSGHVAELEEDLDTARKDLikseevnsrLQRDVREAMAQKED 366
Cdd:TIGR00618 681 ALQKMQSEKEQLTYWKEMLAQCQTLLRE---LETHIEEYDREFNEIENASSSLGSDL---------AAREDALNQSLKEL 748
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 367 MEERITTLEKRYLAAQR---EATSVHDLNDKLESEIANkdavhrqTEDKNRQLQER---LELAEQKLQQTLRKAETLPEV 440
Cdd:TIGR00618 749 MHQARTVLKARTEAHFNnneEVTAALQTGAELSHLAAE-------IQFFNRLREEDthlLKTLEAEIGQEIPSDEDILNL 821
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 441 EAE-LAQRVAAL-SKAEERHGNIEErLRQMEAQLEEKNQELQRARQREKMSEEHSKRLSDTVDRLLSESGERLRLHLKER 518
Cdd:TIGR00618 822 QCEtLVQEEEQFlSRLEEKSATLGE-ITHQLLKYEECSKQLAQLTQEQAKIIQLSDKLNGINQIKIQFDGDALIKFLHEI 900
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 2076569066 519 TAaleDKNALL------REVGDAKKQLEETQRDKDQLVLNVEalrAELDQVR 564
Cdd:TIGR00618 901 TL---YANVRLanqsegRFHGRYADSHVNARKYQGLALLVAD---AYTGSVR 946
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
317-560 |
1.02e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 61.47 E-value: 1.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 317 QMKERLATLSGHVAEL---EEDLDTARKDLIKSEEVNsRLQRDVREAMAQKEDMEERITTLekRYLAAQREAtsvhdlnD 393
Cdd:COG4913 222 DTFEAADALVEHFDDLeraHEALEDAREQIELLEPIR-ELAERYAAARERLAELEYLRAAL--RLWFAQRRL-------E 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 394 KLESEIANKDAVHRQTEDKNRQLQERLELAEQKLQQTLRKAETLP-EVEAELAQRVAALskaeerhgniEERLRQMEAQL 472
Cdd:COG4913 292 LLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERL----------ERELEERERRR 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 473 EEKNQELQRARQREKMSEEHSKRLSDTVDRLLSESGERLRLHLKERTAALEDKNALLREVGDAKKQLEETQRDKDQLVLN 552
Cdd:COG4913 362 ARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPAR 441
|
....*...
gi 2076569066 553 VEALRAEL 560
Cdd:COG4913 442 LLALRDAL 449
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
229-539 |
1.24e-08 |
|
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: 59.44 E-value: 1.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 229 TFTVSKRLRRARTARQVPPLLPHASASAegapgavsrqTPARRPCRSgspragLRLQRSPDGSLSHEEDLaKVLELQ--- 305
Cdd:pfam15905 22 SFEKSQRFRKQKAAESQPNLNNSKDAST----------PATARKVKS------LELKKKSQKNLKESKDQ-KELEKEira 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 306 EVVDR--QAREHCQMKERL----ATLSGHVAE---LEEDLDTARKDLIKSEEVNSRLQRDVREAMAQKEdMeeRITTLEK 376
Cdd:pfam15905 85 LVQERgeQDKRLQALEEELekveAKLNAAVREktsLSASVASLEKQLLELTRVNELLKAKFSEDGTQKK-M--SSLSMEL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 377 RYLAAQREAT--SVHDLNDKLESEI--ANKDAVHRQteDKNRQLQERLELAEQKLQQTlrKAETLpeveaELAQRVAALS 452
Cdd:pfam15905 162 MKLRNKLEAKmkEVMAKQEGMEGKLqvTQKNLEHSK--GKVAQLEEKLVSTEKEKIEE--KSETE-----KLLEYITELS 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 453 KAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMSEEH-SKRLSDTVDR--LLSESGERLRLHLKERtaaledKNALL 529
Cdd:pfam15905 233 CVSEQVEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQElSKQIKDLNEKckLLESEKEELLREYEEK------EQTLN 306
|
330
....*....|
gi 2076569066 530 REVGDAKKQL 539
Cdd:pfam15905 307 AELEELKEKL 316
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
352-559 |
1.27e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 61.08 E-value: 1.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 352 RLQRDVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLESEIaNKDAVHRQTEDKNRQLqERLELAEQKLQqtl 431
Cdd:COG4913 614 ALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEI-DVASAEREIAELEAEL-ERLDASSDDLA--- 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 432 rkaetlpEVEAELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQRekmseehskrlsdtVDRLLSESGERL 511
Cdd:COG4913 689 -------ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDR--------------LEAAEDLARLEL 747
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2076569066 512 RLHLKERTAALEDKNALLREVGDAKKQLEETQRDKDQLVLNVEALRAE 559
Cdd:COG4913 748 RALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRA 795
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
282-562 |
1.28e-08 |
|
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: 60.47 E-value: 1.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 282 LRLQRSPDGSLSHEEDLAK-VLELQ---EVVDRQAREHCQMKERLATL---SGHVAELEEDLDTARKDLiksEEVNSrLQ 354
Cdd:pfam05622 76 FRLETARDDYRIKCEELEKeVLELQhrnEELTSLAEEAQALKDEMDILresSDKVKKLEATVETYKKKL---EDLGD-LR 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 355 RDVR-------EAMAQKEDMEERIttleKRY--LAAQREATS--VHDLNDKLESEiANKdAVHRQTEDKNrqLQERLElA 423
Cdd:pfam05622 152 RQVKlleernaEYMQRTLQLEEEL----KKAnaLRGQLETYKrqVQELHGKLSEE-SKK-ADKLEFEYKK--LEEKLE-A 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 424 EQKLQQTLRKA-----ETLPE------VEAELAQRVAALSK--------AEERH-----------------------GNI 461
Cdd:pfam05622 223 LQKEKERLIIErdtlrETNEElrcaqlQQAELSQADALLSPssdpgdnlAAEIMpaeireklirlqhenkmlrlgqeGSY 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 462 EERLRQMEAQLEEKNqelqraRQREKMSEEHskRLSDTVDRLLSESGERLRLHLKERTAALEDKNALLREVGDAKKQLEE 541
Cdd:pfam05622 303 RERLTELQQLLEDAN------RRKNELETQN--RLANQRILELQQQVEELQKALQEQGSKAEDSSLLKQKLEEHLEKLHE 374
|
330 340
....*....|....*....|.
gi 2076569066 542 TQRDKDQLVLNVEALRAELDQ 562
Cdd:pfam05622 375 AQSELQKKKEQIEELEPKQDS 395
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
324-571 |
1.52e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 60.82 E-value: 1.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 324 TLSGHVAELEEDLDTARKDLiksEEVNSRLQRDVREAmaqkEDMEERITTLEKRYLAAQREAtsvhdlnDKLESEIANKD 403
Cdd:PRK02224 311 AVEARREELEDRDEELRDRL---EECRVAAQAHNEEA----ESLREDADDLEERAEELREEA-------AELESELEEAR 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 404 AVHRQTEDKNRQLQERLELAEQKLQQTlrkAETLPEVEAELAQRVAALSKAEERHGNIEERLRQMEAQLEEkNQELQRAR 483
Cdd:PRK02224 377 EAVEDRREEIEELEEEIEELRERFGDA---PVDLGNAEDFLEELREERDELREREAELEATLRTARERVEE-AEALLEAG 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 484 Q-----REKMSEEHSKRLSDTVDRLlsESGERLRLHLKERTAALEDKNALLREVGDAKKQLEETQRDKDQLVLNVEALRA 558
Cdd:PRK02224 453 KcpecgQPVEGSPHVETIEEDRERV--EELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEERREDLEELIAERRE 530
|
250
....*....|...
gi 2076569066 559 ELDQVRLGGPSLH 571
Cdd:PRK02224 531 TIEEKRERAEELR 543
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
314-563 |
1.57e-08 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 60.23 E-value: 1.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 314 EHCQMKERLATLSGHVAELEEDLdtarkdlikseevnSRLqrDVREAMAQKEDMEERITTL----EKRYLAAQreatSVH 389
Cdd:PRK04778 250 DHLDIEKEIQDLKEQIDENLALL--------------EEL--DLDEAEEKNEEIQERIDQLydilEREVKARK----YVE 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 390 DLNDKLESEIANKDAVHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKAEERHGNIEERLRQME 469
Cdd:PRK04778 310 KNSDTLPDFLEHAKEQNKELKEEIDRVKQSYTLNESELESVRQLEKQLESLEKQYDEITERIAEQEIAYSELQEELEEIL 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 470 AQLE--EKNQE-----LQRARQ-----REKMsEEHSKRLSdTVDRLLsesgERLRL-HLKERtaALEDKNALLREVGDAK 536
Cdd:PRK04778 390 KQLEeiEKEQEklsemLQGLRKdeleaREKL-ERYRNKLH-EIKRYL----EKSNLpGLPED--YLEMFFEVSDEIEALA 461
|
250 260
....*....|....*....|....*..
gi 2076569066 537 KQLEetqrdkdQLVLNVEALRAELDQV 563
Cdd:PRK04778 462 EELE-------EKPINMEAVNRLLEEA 481
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
308-564 |
1.71e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 60.70 E-value: 1.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 308 VDRQAREHCQMKERLATLSGHVAELEEDLDTARKDLIKSEEVNSRLQRDVREAMAQKEDMEERITTLEKRYLAAQREATS 387
Cdd:COG4913 666 AEREIAELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARL 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 388 VH--DLNDKLESEIANK--DAVHRQTEDKNRQLQERLELAEQKLQQTLRK---------------AETLPEVEAELAQRV 448
Cdd:COG4913 746 ELraLLEERFAAALGDAveRELRENLEERIDALRARLNRAEEELERAMRAfnrewpaetadldadLESLPEYLALLDRLE 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 449 A-ALSKAEERhgnIEERL-RQMEAQLEEKNQELQRARqrekmsEEHSKRLsDTVDRLLSE----SGERLRLHLKERT-AA 521
Cdd:COG4913 826 EdGLPEYEER---FKELLnENSIEFVADLLSKLRRAI------REIKERI-DPLNDSLKRipfgPGRYLRLEARPRPdPE 895
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 2076569066 522 LEDKNALLREVGDAKKQLEETQRDKDQLVLN--VEALRAELDQVR 564
Cdd:COG4913 896 VREFRQELRAVTSGASLFDEELSEARFAALKrlIERLRSEEEESD 940
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
414-564 |
1.96e-08 |
|
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: 57.63 E-value: 1.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 414 RQLQERL-ELAE--QKLQQTLRKAETLPEVEAELAQRVAALskaEERHGNIEERLRQMEAQLEEKNQELQRARQREKMSE 490
Cdd:COG1579 3 PEDLRALlDLQEldSELDRLEHRLKELPAELAELEDELAAL---EARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 491 EHSKRLSDT--VDRLLSE--SGERLRLHLKERTAALEDK-NALLREVGDAKKQLEETQRD----KDQLVLNVEALRAELD 561
Cdd:COG1579 80 EQLGNVRNNkeYEALQKEieSLKRRISDLEDEILELMERiEELEEELAELEAELAELEAEleekKAELDEELAELEAELE 159
|
...
gi 2076569066 562 QVR 564
Cdd:COG1579 160 ELE 162
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
295-555 |
2.14e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 60.54 E-value: 2.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 295 EEDLAKVLELQEVVDRQAREHCQMKERLATLSGHVAELEEDLDTARK--------DLIKSEEVNS--RLQRDVREAmAQK 364
Cdd:PTZ00121 1239 AEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKaeekkkadEAKKAEEKKKadEAKKKAEEA-KKA 1317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 365 EDMEERITTLEKRYLAAQREATSVhdlndKLESEIANKDAvhRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAEL 444
Cdd:PTZ00121 1318 DEAKKKAEEAKKKADAAKKKAEEA-----KKAAEAAKAEA--EAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEK 1390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 445 AQRVAALSKAEERHGNIEERLRQMEA-----QLEEKNQELQRARQREKMSEEhsKRLSDTVDRLLSES--GERLRLHLKE 517
Cdd:PTZ00121 1391 KKADEAKKKAEEDKKKADELKKAAAAkkkadEAKKKAEEKKKADEAKKKAEE--AKKADEAKKKAEEAkkAEEAKKKAEE 1468
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 2076569066 518 RTAA--LEDKNALLREVGDAKKQLEETQRDKDQLVLNVEA 555
Cdd:PTZ00121 1469 AKKAdeAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEA 1508
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
296-485 |
2.15e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 60.31 E-value: 2.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 296 EDLAKVLELQEVVDRQAREHCQMKERLATLSGHVAELEEDLDTARKDLIKSEEVnsRLQRDVREAMAQKEDMEERITTLE 375
Cdd:COG4913 245 EDAREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELE--ELRAELARLEAELERLEARLDALR 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 376 KRYLAAQRE-ATSVHDLNDKLESEIankdavhrqtEDKNRQLQERLELAEQkLQQTLRKAE-TLPEVEAELAQRVAAL-- 451
Cdd:COG4913 323 EELDELEAQiRGNGGDRLEQLEREI----------ERLERELEERERRRAR-LEALLAALGlPLPASAEEFAALRAEAaa 391
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2076569066 452 ---------SKAEERHGNIEERLRQMEAQLEEKNQELQRARQR 485
Cdd:COG4913 392 llealeeelEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
|
|
| Lebercilin |
pfam15619 |
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ... |
283-433 |
2.53e-08 |
|
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: 56.45 E-value: 2.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 283 RLQRSPDGSLSHEEDLAKvlELQEVVDRQAREHCQMKERLATLSGHVAELEEDLDTARKDLIKSEEVNSRLQRDVREA-M 361
Cdd:pfam15619 39 RLQKRQEKALGKYEGTES--ELPQLIARHNEEVRVLRERLRRLQEKERDLERKLKEKEAELLRLRDQLKRLEKLSEDKnL 116
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2076569066 362 AQKEDMEERITTLEKRYLAAQREatsVHDLNDKLE-------SEIANKDAVHRQTEDKNRQLQERLELAEQKLQQTLRK 433
Cdd:pfam15619 117 AEREELQKKLEQLEAKLEDKDEK---IQDLERKLElenksfrRQLAAEKKKHKEAQEEVKILQEEIERLQQKLKEKERE 192
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
372-541 |
3.10e-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: 59.80 E-value: 3.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 372 TTLEKRYLAAQREATSVHDLNDKLESEIANKDAVHRQTEDKNRQLQERLElAEQKLqqtLRKAEtlpEVEAELAQRvaal 451
Cdd:pfam01576 1 TRQEEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQ-AETEL---CAEAE---EMRARLAAR---- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 452 sKAEerhgnIEERLRQMEAQLEE---KNQELQraRQREKMsEEHSKRLSDTVDrllSESGERLRLHLK------------ 516
Cdd:pfam01576 70 -KQE-----LEEILHELESRLEEeeeRSQQLQ--NEKKKM-QQHIQDLEEQLD---EEEAARQKLQLEkvtteakikkle 137
|
170 180
....*....|....*....|....*.
gi 2076569066 517 ERTAALEDKNA-LLREvgdaKKQLEE 541
Cdd:pfam01576 138 EDILLLEDQNSkLSKE----RKLLEE 159
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
286-563 |
3.89e-08 |
|
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
Pssm-ID: 310534 [Multi-domain] Cd Length: 258 Bit Score: 57.04 E-value: 3.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 286 RSPDGSLSHEEDLAKvlELQEVVDRQaREHcqmKERLATLSGHVAELEEDLDTarkdLIKSEEVNSRLQRDVREAMaqkE 365
Cdd:pfam06008 12 PAPYKINYNLENLTK--QLQEYLSPE-NAH---KIQIEILEKELSSLAQETEE----LQKKATQTLAKAQQVNAES---E 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 366 DMEERITTLekrYLAAQREATSVHDLNDKLESEIANKDAVhrqtedKNRQLQERLELAEQKLQQtLRKAET---LPEVEA 442
Cdd:pfam06008 79 RTLGHAKEL---AEAIKNLIDNIKEINEKVATLGENDFAL------PSSDLSRMLAEAQRMLGE-IRSRDFgtqLQNAEA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 443 ELAQRVAALSKAEERHGNIEERLRQMEAQLEEK----NQELQRARQREKMSEEHSKRlsdtVDRLLSESGERLRLHLKER 518
Cdd:pfam06008 149 ELKAAQDLLSRIQTWFQSPQEENKALANALRDSlaeyEAKLSDLRELLREAAAKTRD----ANRLNLANQANLREFQRKK 224
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 2076569066 519 taaledknallREVGDAKKQLEETQRDKDQLVLNVEALRAELDQV 563
Cdd:pfam06008 225 -----------EEVSEQKNQLEETLKTARDSLDAANLLLQEIDDA 258
|
|
| SAM |
smart00454 |
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ... |
1158-1222 |
4.08e-08 |
|
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related tyrosine kinases, appears to mediate cell-cell initiated signal transduction via the binding of SH2-containing proteins to a conserved tyrosine that is phosphorylated. In many cases mediates homodimerisation.
Pssm-ID: 197735 Cd Length: 68 Bit Score: 52.30 E-value: 4.08e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2076569066 1158 FAQWDGPTVVVWLELWvGMPAwYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQ 1222
Cdd:smart00454 1 VSQWSPESVADWLESI-GLEQ-YADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQ 63
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
300-549 |
4.18e-08 |
|
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: 58.75 E-value: 4.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 300 KVLELQEVVDRQAREHCQMKERLATLS----GHVA---ELEEDLDTARKDLIKSEEVNSRLQRDVREAMAQKEDMEERIT 372
Cdd:pfam07888 95 KHEELEEKYKELSASSEELSEEKDALLaqraAHEArirELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERK 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 373 TLEKRYLAAQREATSVHDLNDKLESEIANKDAVHRQTEDKNRQLQERLELAEQK---LQQTLRKAETLPEVEAELAQRVA 449
Cdd:pfam07888 175 QLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKeaeNEALLEELRSLQERLNASERKVE 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 450 AL-----SKAEERHGNIEE----RLR--QMEAQLEEKN-----------QELQRARQREKMSEEHSKRLSDTV----DRL 503
Cdd:pfam07888 255 GLgeelsSMAAQRDRTQAElhqaRLQaaQLTLQLADASlalregrarwaQERETLQQSAEADKDRIEKLSAELqrleERL 334
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 2076569066 504 LSESGERLRLHL---KERTAALEDKNALLREVGDAKKQLEETQRDKDQL 549
Cdd:pfam07888 335 QEERMEREKLEVelgREKDCNRVQLSESRRELQELKASLRVAQKEKEQL 383
|
|
| SAM |
smart00454 |
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ... |
1292-1347 |
4.41e-08 |
|
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related tyrosine kinases, appears to mediate cell-cell initiated signal transduction via the binding of SH2-containing proteins to a conserved tyrosine that is phosphorylated. In many cases mediates homodimerisation.
Pssm-ID: 197735 Cd Length: 68 Bit Score: 52.30 E-value: 4.41e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2076569066 1292 EWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRGQLKMVDSFHRNSFQCGIMCLR 1347
Cdd:smart00454 11 DWLESIGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKLK 66
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
185-519 |
4.70e-08 |
|
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: 59.07 E-value: 4.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 185 ALKSLFEhhkALDEKVR--ERLRVALER-CSLLEEELGVTHKEMGRWTFTVSKrLRRARTARQVP--PLLPHASASAega 259
Cdd:pfam10174 437 ALTTLEE---ALSEKERiiERLKEQREReDRERLEELESLKKENKDLKEKVSA-LQPELTEKESSliDLKEHASSLA--- 509
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 260 pgavsrQTPARRPCRSGSPRagLRLQRSPDGSLSHEEDLAKVLELQEvvdrQAREHCQMKERLATLSGHVAELEEDLDTA 339
Cdd:pfam10174 510 ------SSGLKKDSKLKSLE--IAVEQKKEECSKLENQLKKAHNAEE----AVRTNPEINDRIRLLEQEVARYKEESGKA 577
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 340 RKDLikseevnSRLQRDVREAMAQKEDMEERITTLEKRYLAAQRE-ATSVHDLNDKlESEIANKDA-----VHRQTEDKN 413
Cdd:pfam10174 578 QAEV-------ERLLGILREVENEKNDKDKKIAELESLTLRQMKEqNKKVANIKHG-QQEMKKKGAqlleeARRREDNLA 649
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 414 R-----QLQE---RLELAEQKLQQTLRKaetLPEVEAELAQRVAALSKAeeRHgnieERLRQMEAQLEEKNQELQRARQr 485
Cdd:pfam10174 650 DnsqqlQLEElmgALEKTRQELDATKAR---LSSTQQSLAEKDGHLTNL--RA----ERRKQLEEILEMKQEALLAAIS- 719
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 2076569066 486 EK--------MSEEHSKRLSDTVDRLLSESgERLRLHLKERT 519
Cdd:pfam10174 720 EKdanialleLSSSKKKKTQEEVMALKREK-DRLVHQLKQQT 760
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
317-534 |
5.32e-08 |
|
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.
Pssm-ID: 460211 [Multi-domain] Cd Length: 175 Bit Score: 55.35 E-value: 5.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 317 QMKERLATLSGHVAELEEDLDTARKDLIkseevnSRLQRDVREAMAQ-KEDMEerittlekrylaaqreatsvhDLNDKL 395
Cdd:pfam01442 1 LLEDSLDELSTYAEELQEQLGPVAQELV------DRLEKETEALRERlQKDLE---------------------EVRAKL 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 396 ESEIankDAVHRQTEDKNRQLQERLELAEQKLQQTLRKaetlpEVEaELAQRVAAlsKAEERHGNIEERLRQMEAQLEEK 475
Cdd:pfam01442 54 EPYL---EELQAKLGQNVEELRQRLEPYTEELRKRLNA-----DAE-ELQEKLAP--YGEELRERLEQNVDALRARLAPY 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2076569066 476 NQELqrarqREKMsEEHSKRLSDTVDRLLSESGERLRLHLKERTAALEDKNALLREVGD 534
Cdd:pfam01442 123 AEEL-----RQKL-AERLEELKESLAPYAEEVQAQLSQRLQELREKLEPQAEDLREKLD 175
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
210-565 |
5.34e-08 |
|
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: 58.68 E-value: 5.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 210 RCSLLEEELGVTHKEMGRWTFTVSKRLRRARTARQVPPLL--PHASASAEGAPGAVSRQTPARRPCRSGSPR----AGLR 283
Cdd:pfam10174 54 RISVLKEQYRVTQEENQHLQLTIQALQDELRAQRDLNQLLqqDFTTSPVDGEDKFSTPELTEENFRRLQSEHerqaKELF 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 284 LQR-----------SPDGSL-SHEEDLAKVLEL---QEVVDRQAREHCQMKERLATLSGHVAELEEDLDTARKDLIK-SE 347
Cdd:pfam10174 134 LLRktleemelrieTQKQTLgARDESIKKLLEMlqsKGLPKKSGEEDWERTRRIAEAEMQLGHLEVLLDQKEKENIHlRE 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 348 EVNSRLQ----RDVREAMAQKEDMEE-RITTLEKrylaaqreatSVHDLNDKLESEIANKDAVHRQTEDKNRQLQ----- 417
Cdd:pfam10174 214 ELHRRNQlqpdPAKTKALQTVIEMKDtKISSLER----------NIRDLEDEVQMLKTNGLLHTEDREEEIKQMEvyksh 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 418 -----ERLELAEQKLQ------QTLR-KAETLPEVEAELAQRVAALSK---AEERHGNIEE--------RLRQMEAQLEE 474
Cdd:pfam10174 284 skfmkNKIDQLKQELSkkeselLALQtKLETLTNQNSDCKQHIEVLKEsltAKEQRAAILQtevdalrlRLEEKESFLNK 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 475 KNQELQRarqrekMSEEHSK---RLSDTVDRLlsESGER--LRLH-----LKERtaaLEDKNALLREVGDAKKQL----- 539
Cdd:pfam10174 364 KTKQLQD------LTEEKSTlagEIRDLKDML--DVKERkiNVLQkkienLQEQ---LRDKDKQLAGLKERVKSLqtdss 432
|
410 420 430
....*....|....*....|....*....|....*
gi 2076569066 540 ---------EETQRDKDQLVLNVEALRAELDQVRL 565
Cdd:pfam10174 433 ntdtalttlEEALSEKERIIERLKEQREREDRERL 467
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
453-563 |
5.52e-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: 58.93 E-value: 5.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 453 KAEERHGNIEERLRQMEAQLEEKNQELQR-ARQREKmSEEHskrlsdtvDRLLSESGE-RLRLHLKERTAALEDKNALLR 530
Cdd:TIGR02169 174 KALEELEEVEENIERLDLIIDEKRQQLERlRREREK-AERY--------QALLKEKREyEGYELLKEKEALERQKEAIER 244
|
90 100 110
....*....|....*....|....*....|...
gi 2076569066 531 EVGDAKKQLEETQRDKDQLVLNVEALRAELDQV 563
Cdd:TIGR02169 245 QLASLEEELEKLTEEISELEKRLEEIEQLLEEL 277
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
359-562 |
5.70e-08 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 58.83 E-value: 5.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 359 EAMAQKEDMEERITTLEKRY----LAAQREATSVHDLNDKLESEIANKDAVHRQTEDKNRQLQERLELAEQKLQQtlrka 434
Cdd:TIGR00618 184 MEFAKKKSLHGKAELLTLRSqlltLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKK----- 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 435 etlpevEAELAQRVAAlskaeerhgniEERLRQMEAQLEEKNQELQRARQREKMSeEHSKRLSDtVDRLLSESGERLRLH 514
Cdd:TIGR00618 259 ------QQLLKQLRAR-----------IEELRAQEAVLEETQERINRARKAAPLA-AHIKAVTQ-IEQQAQRIHTELQSK 319
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2076569066 515 LKERTAALEDKNALLREvgdaKKQLEETQRDKDQLVLNVEALRAELDQ 562
Cdd:TIGR00618 320 MRSRAKLLMKRAAHVKQ----QSSIEEQRRLLQTLHSQEIHIRDAHEV 363
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
295-541 |
6.03e-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: 58.90 E-value: 6.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 295 EEDLAKVLELQEVVDRQAREHCQMKERLATLSGHVAELEEDLDTARKDLiksEEVNSRLQ--RDVREAMAQKEDMEERIT 372
Cdd:TIGR00606 726 DEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLL---GTIMPEEEsaKVCLTDVTIMERFQMELK 802
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 373 TLEKRY--LAAQREAT----SVHDLNDKLESEIANKDAVHRQTEDKNRQLQERLElAEQKLQQTLRkaetlpeveaELAQ 446
Cdd:TIGR00606 803 DVERKIaqQAAKLQGSdldrTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQE-QIQHLKSKTN----------ELKS 871
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 447 RVAALSKAEERHGnieerlrQMEAQLEEKNQELQRARQREKMSEEHSKRLSDTVDRLLSESGErlRLHLKErtaalEDKN 526
Cdd:TIGR00606 872 EKLQIGTNLQRRQ-------QFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEE--LISSKE-----TSNK 937
|
250
....*....|....*
gi 2076569066 527 ALLREVGDAKKQLEE 541
Cdd:TIGR00606 938 KAQDKVNDIKEKVKN 952
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
295-562 |
6.26e-08 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 58.49 E-value: 6.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 295 EEDLAKvlELQEVVDRQAREHCQMKERLATLSGHVAELEEDLDTARKDLIKSEEVNSRLQRDVREamaqKEDMEERIttl 374
Cdd:TIGR04523 305 EQDWNK--ELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEE----KQNEIEKL--- 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 375 ekrylaaQREATSVHDLNDKLESEIANKDAVHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEA-------ELAQR 447
Cdd:TIGR04523 376 -------KKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIknnseikDLTNQ 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 448 VAALSKAEERHGNIEERLRQ-----------MEAQLEEKNQELQRARQREKMSEEHSKRLSDTVDRLLSESGErlrlhLK 516
Cdd:TIGR04523 449 DSVKELIIKNLDNTRESLETqlkvlsrsinkIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISS-----LK 523
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 2076569066 517 ERTAALE-DKNALLREVGDAKKQLEetqrdKDQLVLNVEALRAELDQ 562
Cdd:TIGR04523 524 EKIEKLEsEKKEKESKISDLEDELN-----KDDFELKKENLEKEIDE 565
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
303-506 |
6.52e-08 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 58.16 E-value: 6.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 303 ELQEVVDRQArehcQMKERLATLSGHVAELE---------EDLDTARKDLIKSEEVNSRLQRdVREAMAQKED-MEERIT 372
Cdd:COG0497 173 ELEELRADEA----ERARELDLLRFQLEELEaaalqpgeeEELEEERRRLSNAEKLREALQE-ALEALSGGEGgALDLLG 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 373 TLEKRYLAAQREATSVHDLNDKLESEIANKDAVHRQTEDKNRQLQ---ERLELAEQKLQ---QTLRK----AETLPEVEA 442
Cdd:COG0497 248 QALRALERLAEYDPSLAELAERLESALIELEEAASELRRYLDSLEfdpERLEEVEERLAllrRLARKygvtVEELLAYAE 327
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2076569066 443 ELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQrekmseEHSKRLSDTVDRLLSE 506
Cdd:COG0497 328 ELRAELAELENSDERLEELEAELAEAEAELLEAAEKLSAARK------KAAKKLEKAVTAELAD 385
|
|
| SAM_superfamily |
cd09487 |
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ... |
1292-1343 |
9.48e-08 |
|
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: 50.70 E-value: 9.48e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 2076569066 1292 EWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRgQLKMVDSFHRNSFQCGI 1343
Cdd:cd09487 4 EWLESLGLEQYADLFRKNEIDGDALLLLTDEDLK-ELGITSPGHRKKILRAI 54
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
296-559 |
1.13e-07 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 57.81 E-value: 1.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 296 EDLAKVLElqevvdrQAREHC-QMKERLATLSGHVAELEEDLDTARKDLiksEEVNSRLQRDVREAMAQKEDMEERITTL 374
Cdd:pfam05483 257 KDLTFLLE-------ESRDKAnQLEEKTKLQDENLKELIEKKDHLTKEL---EDIKMSLQRSMSTQKALEEDLQIATKTI 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 375 ekrYLAAQREATSVHDLNDKLeseiANKDAVHRQTEDKNRQLQERLELAEQKLQqtlRKAETLPEVEAELAQRVAALSKA 454
Cdd:pfam05483 327 ---CQLTEEKEAQMEELNKAK----AAHSFVVTEFEATTCSLEELLRTEQQRLE---KNEDQLKIITMELQKKSSELEEM 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 455 EERHGNIEERLRQMEAQLEEKNQELQRARQREKMSEEHSKRLSDTVDRLLSESGERLRLHLkERTAALEDKNALLREVGD 534
Cdd:pfam05483 397 TKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEI-QLTAIKTSEEHYLKEVED 475
|
250 260
....*....|....*....|....*
gi 2076569066 535 AKKQLEETQRDKDQLVLNVEALRAE 559
Cdd:pfam05483 476 LKTELEKEKLKNIELTAHCDKLLLE 500
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
314-564 |
1.24e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 57.84 E-value: 1.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 314 EHCQMKERLATLSghVAELEEDLDTARK-DLIKSEEvnsrlQRDVREAMAQKED---MEERITTLEKRYLAAQREATSVH 389
Cdd:PTZ00121 1080 DFDAKEDNRADEA--TEEAFGKAEEAKKtETGKAEE-----ARKAEEAKKKAEDarkAEEARKAEDARKAEEARKAEDAK 1152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 390 DLNDKLESEIANKDAVHRQTEDKnRQLQERLELAEQKLQQTLRKAETLPEVEA----------ELAQRVAALSKAEERHG 459
Cdd:PTZ00121 1153 RVEIARKAEDARKAEEARKAEDA-KKAEAARKAEEVRKAEELRKAEDARKAEAarkaeeerkaEEARKAEDAKKAEAVKK 1231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 460 NIEERLRQMEAQLEEKNQELQRARQREKMSEEHSKRLSDTVDRLLSESGERLRLHLKERTAALEDKNALLREVGDAKKQL 539
Cdd:PTZ00121 1232 AEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKA 1311
|
250 260
....*....|....*....|....*
gi 2076569066 540 EEtQRDKDQLVLNVEALRAELDQVR 564
Cdd:PTZ00121 1312 EE-AKKADEAKKKAEEAKKKADAAK 1335
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
317-548 |
1.26e-07 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 55.42 E-value: 1.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 317 QMKERLATLSGHVAELEEDLDTARKDLIKSE-EVNSrLQRDVREAMAQKEDMEERITTlekrylaAQREATSVHDLNDkl 395
Cdd:pfam00261 5 QIKEELDEAEERLKEAMKKLEEAEKRAEKAEaEVAA-LNRRIQLLEEELERTEERLAE-------ALEKLEEAEKAAD-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 396 ESEIANKDAVHRQTEDKNR------QLQERLELAEQKLQQTLRKAETLPEVEAELA---QRV-AALSKA---EERHGNIE 462
Cdd:pfam00261 75 ESERGRKVLENRALKDEEKmeileaQLKEAKEIAEEADRKYEEVARKLVVVEGDLEraeERAeLAESKIvelEEELKVVG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 463 ERLRQMEAQlEEKnqelqrARQREKMSEEH----SKRLSDTVDRllSESGERLRLHLKERTAALEDknallrEVGDAKKQ 538
Cdd:pfam00261 155 NNLKSLEAS-EEK------ASEREDKYEEQirflTEKLKEAETR--AEFAERSVQKLEKEVDRLED------ELEAEKEK 219
|
250
....*....|
gi 2076569066 539 LEETQRDKDQ 548
Cdd:pfam00261 220 YKAISEELDQ 229
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
310-564 |
1.41e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 57.66 E-value: 1.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 310 RQAREHCQMKERLA---------TLSGHVAELEEDLDTARKD-------------------LIKSEEVN-SRLQRDVREA 360
Cdd:PRK04863 868 EQAKEGLSALNRLLprlnlladeTLADRVEEIREQLDEAEEAkrfvqqhgnalaqlepivsVLQSDPEQfEQLKQDYQQA 947
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 361 MAQKEDMEERITTLEkrYLAAQREATSVHDLNDKLEseiankdavhrQTEDKNRQLQERLELAEqklQQTLRKAETLPEV 440
Cdd:PRK04863 948 QQTQRDAKQQAFALT--EVVQRRAHFSYEDAAEMLA-----------KNSDLNEKLRQRLEQAE---QERTRAREQLRQA 1011
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 441 EAELAQRVAALSKAEERHgnieERLRQMEAQLEEKNQEL---------QRARQREkmsEEHSKRLSDTvdrllsesgerl 511
Cdd:PRK04863 1012 QAQLAQYNQVLASLKSSY----DAKRQMLQELKQELQDLgvpadsgaeERARARR---DELHARLSAN------------ 1072
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 2076569066 512 rlhlKERTAALEDKNALL-REVGDAKKQLEETQRDKDQLVLNVEALRAELDQVR 564
Cdd:PRK04863 1073 ----RSRRNQLEKQLTFCeAEMDNLTKKLRKLERDYHEMREQVVNAKAGWCAVL 1122
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
295-564 |
1.63e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 57.46 E-value: 1.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 295 EEDLAKVLELQEVVDRQAREHCQMKERLATLSGHVAELEEDLDTARKdliKSEEVNSRLQrDVREAMAQKEDMEERITTL 374
Cdd:PTZ00121 1352 AEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKK---KAEEDKKKAD-ELKKAAAAKKKADEAKKKA 1427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 375 EKRYLAAQ-----REATSVHDLNDKLEsEIANKDAVHRQTEDKnRQLQERLELAEQKlqqtlRKAETLPEVEAELAQRVA 449
Cdd:PTZ00121 1428 EEKKKADEakkkaEEAKKADEAKKKAE-EAKKAEEAKKKAEEA-KKADEAKKKAEEA-----KKADEAKKKAEEAKKKAD 1500
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 450 ALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMSEEHSKRLSDTVDRL--LSESGERLRLHLKERtaALEDKNA 527
Cdd:PTZ00121 1501 EAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAeeLKKAEEKKKAEEAKK--AEEDKNM 1578
|
250 260 270
....*....|....*....|....*....|....*..
gi 2076569066 528 LLREVGDAKKQleETQRDKDQLVLNVEALRAELDQVR 564
Cdd:PTZ00121 1579 ALRKAEEAKKA--EEARIEEVMKLYEEEKKMKAEEAK 1613
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
289-564 |
1.78e-07 |
|
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: 57.27 E-value: 1.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 289 DGSLSHEEDLAKVLELQevVDRQAReHCQMKERLATLSGHVAELEEDLDTARKDL------IKSEEVNSRLQRDVREAMA 362
Cdd:COG3096 285 ERALELRRELFGARRQL--AEEQYR-LVEMARELEELSARESDLEQDYQAASDHLnlvqtaLRQQEKIERYQEDLEELTE 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 363 QKEDMEERITTLEKRYLAAQREATSVHDLNDKLESEIANkdavHRQTEDknrqLQERLELAEQKLQQTLRKAETLPEvEA 442
Cdd:COG3096 362 RLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLAD----YQQALD----VQQTRAIQYQQAVQALEKARALCG-LP 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 443 ELAQRvaalskaeerhgNIEERLRQMEAQLEEKNQELQRARQREKMSEEHS----------KRLSDTVDRllSESGERLR 512
Cdd:COG3096 433 DLTPE------------NAEDYLAAFRAKEQQATEEVLELEQKLSVADAARrqfekayelvCKIAGEVER--SQAWQTAR 498
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2076569066 513 ---------LHLKERTAALEDKNA----LLREVGDAKKQLEE-TQRDKDQL--VLNVEALRAELDQVR 564
Cdd:COG3096 499 ellrryrsqQALAQRLQQLRAQLAeleqRLRQQQNAERLLEEfCQRIGQQLdaAEELEELLAELEAQL 566
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
291-483 |
2.01e-07 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 54.37 E-value: 2.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 291 SLSHEEDLAKVLELQEVVDRQAREhcqMKERLATLSgHVAELEEDLDTARKDliKSEEVNSRLQrDVREAMAQ-KEDMEE 369
Cdd:cd00176 25 STDYGDDLESVEALLKKHEALEAE---LAAHEERVE-ALNELGEQLIEEGHP--DAEEIQERLE-ELNQRWEElRELAEE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 370 RITTLEKRyLAAQREATSVHDLN---DKLESEIANKDAVHRQTE-----DKNRQLQERLELAEQKLQQTLRKAETLPEve 441
Cdd:cd00176 98 RRQRLEEA-LDLQQFFRDADDLEqwlEEKEAALASEDLGKDLESveellKKHKELEEELEAHEPRLKSLNELAEELLE-- 174
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2076569066 442 aelAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRAR 483
Cdd:cd00176 175 ---EGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
299-491 |
2.27e-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: 57.11 E-value: 2.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 299 AKVLELQEVVDRQAREHCQMKERLATLSGHVAELEEDLDTARKDLIKSEEVNSRLQRDVREAMAQKEDMEERITTLEKRY 378
Cdd:pfam01576 889 ARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMEGTVKSKFKSS 968
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 379 LAAqreatsvhdlndkLESEIANKDAVHRQtEDKNRQLQERL-ELAEQKLQqtlrkaETLPEVEAElaQRVAALSKAEER 457
Cdd:pfam01576 969 IAA-------------LEAKIAQLEEQLEQ-ESRERQAANKLvRRTEKKLK------EVLLQVEDE--RRHADQYKDQAE 1026
|
170 180 190
....*....|....*....|....*....|....*
gi 2076569066 458 HGNIeeRLRQMEAQLEEKNQELQRAR-QREKMSEE 491
Cdd:pfam01576 1027 KGNS--RMKQLKRQLEEAEEEASRANaARRKLQRE 1059
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
289-562 |
2.36e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 56.89 E-value: 2.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 289 DGSLSHEEDLAKVLELQEVVDRQAREhcqMKERLATLSGHVAELEEDLDTARkdlikseevnSRLQRdVREAMAQKEDME 368
Cdd:PRK04863 286 EEALELRRELYTSRRQLAAEQYRLVE---MARELAELNEAESDLEQDYQAAS----------DHLNL-VQTALRQQEKIE 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 369 ERITTLEKRYLAAQREATSVHDLNDKLESEIANKDAVHRQTEDKNRQL---QERLELAE------QKLQQTLRKAETL-- 437
Cdd:PRK04863 352 RYQADLEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLadyQQALDVQQtraiqyQQAVQALERAKQLcg 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 438 -PEVEAElaqrvaalskaeerhgNIEERLRQMEAQLEEKNQELQRARQREKMSEEHS----------KRLSDTVDR---- 502
Cdd:PRK04863 432 lPDLTAD----------------NAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHsqfeqayqlvRKIAGEVSRseaw 495
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2076569066 503 --------------LLSESGERLRLHLKERTAALEDKNALLREVGDAKKQLEETQRDKDQLvlnvEALRAELDQ 562
Cdd:PRK04863 496 dvarellrrlreqrHLAEQLQQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDEDEL----EQLQEELEA 565
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
301-562 |
2.42e-07 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 56.90 E-value: 2.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 301 VLELQEVVDRQArehcQMK--ERLATLSGhVAELEEDLD--TARKDLIKSEEVNSRLQRDVREAMAQKED-MEERITTLE 375
Cdd:pfam02463 137 FLVQGGKIEIIA----MMKpeRRLEIEEE-AAGSRLKRKkkEALKKLIEETENLAELIIDLEELKLQELKlKEQAKKALE 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 376 KRYLAAQREATsvhdlndkLESEIANKDAVHRQTEDKNRQLQERLElaeqklQQTLRKAETLPEVEAELAQRVAALSKAE 455
Cdd:pfam02463 212 YYQLKEKLELE--------EEYLLYLDYLKLNEERIDLLQELLRDE------QEEIESSKQEIEKEEEKLAQVLKENKEE 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 456 ER-HGNIEERLRQMEAQLEEKNQELQRARQRE-------KMSEEHSKRLSDTVDRLLSESGER------------LRLHL 515
Cdd:pfam02463 278 EKeKKLQEEELKLLAKEEEELKSELLKLERRKvddeeklKESEKEKKKAEKELKKEKEEIEELekelkeleikreAEEEE 357
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 2076569066 516 KERTAALEDKNALLREVGDAKKQLEETQRDKDQLVLNVEALRAELDQ 562
Cdd:pfam02463 358 EEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEE 404
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
417-562 |
3.34e-07 |
|
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.
Pssm-ID: 466641 [Multi-domain] Cd Length: 120 Bit Score: 51.46 E-value: 3.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 417 QERLELaEQKLQQtlrkaetlpeVEAELAQRVAALSKAEERHGNIEERLRQMEAQ---LEEKNQELQRARQREKMSeehs 493
Cdd:pfam20492 6 REKQEL-EERLKQ----------YEEETKKAQEELEESEETAEELEEERRQAEEEaerLEQKRQEAEEEKERLEES---- 70
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2076569066 494 krlsdtvdrllSESGERLRLHLKERTAALEDKNALLREvgDAKKQLEETQRdkdqlvLNVEALRAELDQ 562
Cdd:pfam20492 71 -----------AEMEAEEKEQLEAELAEAQEEIARLEE--EVERKEEEARR------LQEELEEAREEE 120
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
407-544 |
3.42e-07 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 53.88 E-value: 3.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 407 RQTEDKNRQLQERLELAEQKLQQTLRKAEtlpEVEAElaqrVAALSKaeerhgnieeRLRQMEAQLEEKNQELQRARQRE 486
Cdd:pfam00261 4 QQIKEELDEAEERLKEAMKKLEEAEKRAE---KAEAE----VAALNR----------RIQLLEEELERTEERLAEALEKL 66
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2076569066 487 KMSEEHSKrlsdtvdrllsESgERLRLHLKERTAALEDKNALLRE--------VGDAKKQLEETQR 544
Cdd:pfam00261 67 EEAEKAAD-----------ES-ERGRKVLENRALKDEEKMEILEAqlkeakeiAEEADRKYEEVAR 120
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
449-564 |
3.61e-07 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 53.68 E-value: 3.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 449 AALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMSEEHSKRLSDTVDRLlsesGERLRLHLK---ERTA--ALE 523
Cdd:COG1842 16 ALLDKAEDPEKMLDQAIRDMEEDLVEARQALAQVIANQKRLERQLEELEAEAEKW----EEKARLALEkgrEDLAreALE 91
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 2076569066 524 DKNALLREVGDAKKQLEETQRDKDQLVLNVEALRAELDQVR 564
Cdd:COG1842 92 RKAELEAQAEALEAQLAQLEEQVEKLKEALRQLESKLEELK 132
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
295-559 |
4.02e-07 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 54.92 E-value: 4.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 295 EEDLAKVLELQEVVDRQAREhcQMKERLATLSGHVAELEEdldtaRKDLIKSEEVNSRLQRDVREAMAQKEDMEERITTL 374
Cdd:pfam13868 50 EEERERALEEEEEKEEERKE--ERKRYRQELEEQIEEREQ-----KRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 375 EKR---------YLAAQREATSVHDLNDKLEsEIANKDAVHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELA 445
Cdd:pfam13868 123 EKQrqlreeideFNEEQAEWKELEKEEEREE-DERILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKA 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 446 QRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMSEEHSKRLSDTVDRllsesGERLRLHLKERTAALEDK 525
Cdd:pfam13868 202 ERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAER-----EEEEFERMLRKQAEDEEI 276
|
250 260 270
....*....|....*....|....*....|....
gi 2076569066 526 NALLREvgDAKKQLEETQRDKDQLVLNVEALRAE 559
Cdd:pfam13868 277 EQEEAE--KRRMKRLEHRRELEKQIEEREEQRAA 308
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
295-566 |
4.63e-07 |
|
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: 56.11 E-value: 4.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 295 EEDLAKVLELQEVVdrqaREHCQmkerlatlsgHVAELEEDLDTARKDLIKSEEvnsrLQRDVREAMAQKEDMEERITTL 374
Cdd:COG3096 899 REELDAAQEAQAFI----QQHGK----------ALAQLEPLVAVLQSDPEQFEQ----LQADYLQAKEQQRRLKQQIFAL 960
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 375 EkrYLAAQREATSVHD----------LNDKLESEIANKDAVHRQTEDKNRQLQERLELAEQKLQQtLR-----KAETLPE 439
Cdd:COG3096 961 S--EVVQRRPHFSYEDavgllgensdLNEKLRARLEQAEEARREAREQLRQAQAQYSQYNQVLAS-LKssrdaKQQTLQE 1037
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 440 VEAELAQ-RVAALSKAEER-HGNIEERLRQMEAQLEEKNQ-ELQRARQREKMseehskrlsDTVDRLLSESGERLRLHLK 516
Cdd:COG3096 1038 LEQELEElGVQADAEAEERaRIRRDELHEELSQNRSRRSQlEKQLTRCEAEM---------DSLQKRLRKAERDYKQERE 1108
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 2076569066 517 ERTAALEDKNALLREVGDakKQLEETQRDKDQLVLNVEALRAELDQvRLG 566
Cdd:COG3096 1109 QVVQAKAGWCAVLRLARD--NDVERRLHRRELAYLSADELRSMSDK-ALG 1155
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
295-565 |
4.84e-07 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 55.60 E-value: 4.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 295 EEDLA---KVLE-LQEVVDRQAREhcqmkerlatlsghvaeLEEDLDTARKDLIKSEEVNSRLQRDVREAMAQKEDMEER 370
Cdd:pfam10174 442 EEALSekeRIIErLKEQREREDRE-----------------RLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEH 504
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 371 ITTLekrylaaqreATSVHDLNDKLES-EIankdAVHRQTEDKNrqlqeRLELAEQKLQQTLRKAETLPEV-------EA 442
Cdd:pfam10174 505 ASSL----------ASSGLKKDSKLKSlEI----AVEQKKEECS-----KLENQLKKAHNAEEAVRTNPEIndrirllEQ 565
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 443 ELAQRVAALSKAEERHGNIEERLRQMEaqlEEKNQELQRARQREKMSEEHSKRLSDTVDRLLSESGERLRLHLKERTAAL 522
Cdd:pfam10174 566 EVARYKEESGKAQAEVERLLGILREVE---NEKNDKDKKIAELESLTLRQMKEQNKKVANIKHGQQEMKKKGAQLLEEAR 642
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 2076569066 523 EDKNALLREVgdAKKQLEEtqrdkdqLVLNVEALRAELDQVRL 565
Cdd:pfam10174 643 RREDNLADNS--QQLQLEE-------LMGALEKTRQELDATKA 676
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
292-564 |
5.21e-07 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 55.35 E-value: 5.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 292 LSHEEDLAKvlELQEVVDRQAREHCQMKERlatlsghVAELEEDLDTAR-----KDLIKSEEVNSRLQRDVREA----MA 362
Cdd:COG5185 270 LGENAESSK--RLNENANNLIKQFENTKEK-------IAEYTKSIDIKKateslEEQLAAAEAEQELEESKRETetgiQN 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 363 QKEDMEERITTLEKRYLAAQREATSVHDLNDKleseiankdavhRQTEDKNRQLQERLELAEQKLQQTLRKAE-TLPEVE 441
Cdd:COG5185 341 LTAEIEQGQESLTENLEAIKEEIENIVGEVEL------------SKSSEELDSFKDTIESTKESLDEIPQNQRgYAQEIL 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 442 AELAQRVAALSKAEERH-GNIEERLRQMEAQLEEKNQ-ELQRARQREKMSEEHSKRLSDTVDRLLSESGERLR------L 513
Cdd:COG5185 409 ATLEDTLKAADRQIEELqRQIEQATSSNEEVSKLLNElISELNKVMREADEESQSRLEEAYDEINRSVRSKKEdlneelT 488
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 2076569066 514 HLKERTAALEDKNALLREVGDAKKQLEETQRDKDQLVLNVEALRAELDQVR 564
Cdd:COG5185 489 QIESRVSTLKATLEKLRAKLERQLEGVRSKLDQVAESLKDFMRARGYAHIL 539
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
307-565 |
5.97e-07 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 54.54 E-value: 5.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 307 VVDRQAREHCQMKErlatlsghvAELEEDldtARKDLIKSEEVNSRLQRDVREAMAQKED-----------MEERITTLE 375
Cdd:pfam13868 23 ERDAQIAEKKRIKA---------EEKEEE---RRLDEMMEEERERALEEEEEKEEERKEErkryrqeleeqIEEREQKRQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 376 KRYLAAQREATSVHDLNDKLESEIANKdavHRQTEDKNRQLQErlELAEQKLQQTLRKAETLPEVEAELAQRVAALSKAE 455
Cdd:pfam13868 91 EEYEEKLQEREQMDEIVERIQEEDQAE---AEEKLEKQRQLRE--EIDEFNEEQAEWKELEKEEEREEDERILEYLKEKA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 456 ERhgnIEERLRQMEAQLEEKNQELQRARQREKMSEEHSKRLSDTVDRLLSESGERlRLHLKERTAAlEDKNALLREVgda 535
Cdd:pfam13868 166 ER---EEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQER-KERQKEREEA-EKKARQRQEL--- 237
|
250 260 270
....*....|....*....|....*....|
gi 2076569066 536 KKQLEETQRDKdQLVLNVEALRAELDQVRL 565
Cdd:pfam13868 238 QQAREEQIELK-ERRLAEEAEREEEEFERM 266
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
345-564 |
6.98e-07 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 53.76 E-value: 6.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 345 KSEEVNSRLqrdvREAMAQKEDMEERITTLEKrylaaQREAtsvhdLNDKLESEIANKDAVHRQTEDKNRQLQERLELAE 424
Cdd:COG1340 2 KTDELSSSL----EELEEKIEELREEIEELKE-----KRDE-----LNEELKELAEKRDELNAQVKELREEAQELREKRD 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 425 QKLQQTLRKAETLPEVEAELAQRVAALSKAEERHGNIEERLRQMEaQLEEKNQELQRARQREKMSEEHSKRLSDTVDRLL 504
Cdd:COG1340 68 ELNEKVKELKEERDELNEKLNELREELDELRKELAELNKAGGSID-KLRKEIERLEWRQQTEVLSPEEEKELVEKIKELE 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2076569066 505 SESGERLRLH-----LKERTAALEDKNALLREVGDAKKQL-EETQRDKDQLVlnveALRAELDQVR 564
Cdd:COG1340 147 KELEKAKKALeknekLKELRAELKELRKEAEEIHKKIKELaEEAQELHEEMI----ELYKEADELR 208
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
311-544 |
7.41e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 54.38 E-value: 7.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 311 QAREHCQMKERLATLSGHVAELEEDLDTARKDLIKSEEVNSRLQRDVREAMAQKEDMEERITTLEKRYLAAQREATSVHD 390
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 391 LNDKLESEIANkdaVHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKAEERHGNIEERLRQMEA 470
Cdd:COG4942 98 ELEAQKEELAE---LLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2076569066 471 QLEEKNQELQraRQREKMSEEHSKRlsdtvDRLLSESGERLRLHLKERTAALEDKNALLREVGDAKKQLEETQR 544
Cdd:COG4942 175 ELEALLAELE--EERAALEALKAER-----QKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
296-564 |
7.41e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 55.53 E-value: 7.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 296 EDLAKVLELQEVVDRQAREHCQMKE--RLATLSgHVAELEEDLDTARK--DLIKSEEVnsRLQRDVREAMAQKEDMEERI 371
Cdd:PTZ00121 1137 EDARKAEEARKAEDAKRVEIARKAEdaRKAEEA-RKAEDAKKAEAARKaeEVRKAEEL--RKAEDARKAEAARKAEEERK 1213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 372 TTLEKRYLAAQReATSVHdlndklESEIANKDAVHRQTEDKNRQLQERLELAEQKLQQTLRKAETlpeVEAELAQRVAAL 451
Cdd:PTZ00121 1214 AEEARKAEDAKK-AEAVK------KAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAA---IKAEEARKADEL 1283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 452 SKAEERHGNIE----ERLRQMEaQLEEKNQELQRARQREKMSEEHSKRlSDTVDRLLSESGERLRLHLKERTAALEDKNA 527
Cdd:PTZ00121 1284 KKAEEKKKADEakkaEEKKKAD-EAKKKAEEAKKADEAKKKAEEAKKK-ADAAKKKAEEAKKAAEAAKAEAEAAADEAEA 1361
|
250 260 270
....*....|....*....|....*....|....*..
gi 2076569066 528 LLREVGDAKKQLEETQRdkdqlvlNVEALRAELDQVR 564
Cdd:PTZ00121 1362 AEEKAEAAEKKKEEAKK-------KADAAKKKAEEKK 1391
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
296-559 |
7.53e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 55.53 E-value: 7.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 296 EDLAKVLELQEVVDrQAREHCQMKERLATLSGHVAELEEDLDTARK---------DLIKSEEvnSRLQRDVREAmAQKED 366
Cdd:PTZ00121 1460 EEAKKKAEEAKKAD-EAKKKAEEAKKADEAKKKAEEAKKKADEAKKaaeakkkadEAKKAEE--AKKADEAKKA-EEAKK 1535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 367 MEERITTLEKRYLAAQREATSVHDLNDKLESEIANkdavhRQTEDKN---RQLQERLELAEQKLQQTLRKAETLPEVEAE 443
Cdd:PTZ00121 1536 ADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAK-----KAEEDKNmalRKAEEAKKAEEARIEEVMKLYEEEKKMKAE 1610
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 444 LAQRVA-ALSKAEERHGNIEER-----LRQMEAQLEEKNQELQRARQREKMSEEHSKRLSDTVDRllseSGERLRLHLKE 517
Cdd:PTZ00121 1611 EAKKAEeAKIKAEELKKAEEEKkkveqLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKK----KAEEAKKAEED 1686
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 2076569066 518 RTAALEdknALLREVGDAKKqLEETQRDKDQLVLNVEALRAE 559
Cdd:PTZ00121 1687 EKKAAE---ALKKEAEEAKK-AEELKKKEAEEKKKAEELKKA 1724
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
292-474 |
8.30e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 55.31 E-value: 8.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 292 LSHEEDLAKVLELQEVVDRQAREHCQMKERLATLSGHVAELEEDLDTARkdlikseevNSRLQRDVReamaQKEDMEERI 371
Cdd:COG4913 281 LRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELE---------AQIRGNGGD----RLEQLEREI 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 372 TTLEKRYLAAQREATSVHDLNDKLESEI--------ANKDAVHRQTEDknrqLQERLELAEQKLQQTLRKAETLPEVEAE 443
Cdd:COG4913 348 ERLERELEERERRRARLEALLAALGLPLpasaeefaALRAEAAALLEA----LEEELEALEEALAEAEAALRDLRRELRE 423
|
170 180 190
....*....|....*....|....*....|.
gi 2076569066 444 LAQRVAALskaEERHGNIEERLRQMEAQLEE 474
Cdd:COG4913 424 LEAEIASL---ERRKSNIPARLLALRDALAE 451
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
300-564 |
8.39e-07 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 55.11 E-value: 8.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 300 KVLELQevvdRQAREHCQMKERLATLsghvaELEEDLDTaRKDLIKSEEVNSRLQRDVREAMAqkedmeeRITTLEKRYL 379
Cdd:pfam05483 113 KIIEAQ----RKAIQELQFENEKVSL-----KLEEEIQE-NKDLIKENNATRHLCNLLKETCA-------RSAEKTKKYE 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 380 AAQREATSVH-DLNDKLESEIANKDAVHRQTEDKNRQLQERLELAEQKLQQTlrKAETLPEVEAELAQRVAALSKAEERh 458
Cdd:pfam05483 176 YEREETRQVYmDLNNNIEKMILAFEELRVQAENARLEMHFKLKEDHEKIQHL--EEEYKKEINDKEKQVSLLLIQITEK- 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 459 gniEERLRQMEAQLEEKNQELQRARQREKMSEEHSKRLSDTVDRLLSEsgerlrlhlkertaaLEDKNALLREVGDAKKQ 538
Cdd:pfam05483 253 ---ENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKE---------------LEDIKMSLQRSMSTQKA 314
|
250 260 270
....*....|....*....|....*....|
gi 2076569066 539 LEE----TQRDKDQLVLNVEALRAELDQVR 564
Cdd:pfam05483 315 LEEdlqiATKTICQLTEEKEAQMEELNKAK 344
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
351-560 |
9.69e-07 |
|
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: 52.37 E-value: 9.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 351 SRLQRDVREAMAQKED-MEERITTLEKrylaAQREATSVHDlndKLESEIANKDAVHRQTEDKNRQLQERLELAEQKLQQ 429
Cdd:pfam04012 3 KRLGRLVRANIHEGLDkAEDPEKMLEQ----AIRDMQSELV---KARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 430 TLRKAE----------------TLPEVEAELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMSEE-H 492
Cdd:pfam04012 76 ALTKGNeelarealaekkslekQAEALETQLAQQRSAVEQLRKQLAALETKIQQLKAKKNLLKARLKAAKAQEAVQTSlG 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2076569066 493 SKRLSDTVDRLlsesgERLRLHLKERtAALEDKNALLREVGDAKKQLEETQRDKDqlvlNVEALRAEL 560
Cdd:pfam04012 156 SLSTSSATDSF-----ERIEEKIEER-EARADAAAELASAVDLDAKLEQAGIQME----VSEDVLARL 213
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
330-564 |
9.86e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 55.15 E-value: 9.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 330 AELEEDLDTARKdliKSEEVNSRLQRDVREAMAQKE-----DMEERITTLEKRYLAAQREATSVHDLNDKLESEIANKDA 404
Cdd:PTZ00121 1479 AEEAKKADEAKK---KAEEAKKKADEAKKAAEAKKKadeakKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAE 1555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 405 VHRQTEDKNRQLQERLElaEQKLQQTLRKAETLPEVEAELAQRVAALSKaEERHGNIEERLRQMEAQLeeKNQELQRARQ 484
Cdd:PTZ00121 1556 ELKKAEEKKKAEEAKKA--EEDKNMALRKAEEAKKAEEARIEEVMKLYE-EEKKMKAEEAKKAEEAKI--KAEELKKAEE 1630
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 485 REKMSEEHSKRLSDTVDRllsesGERLRlhlKERTAALEDKNALLREVGDAKKQLEETQRDKDQLVLNVEALRAELDQVR 564
Cdd:PTZ00121 1631 EKKKVEQLKKKEAEEKKK-----AEELK---KAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAK 1702
|
|
| SAM |
smart00454 |
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ... |
1366-1436 |
1.15e-06 |
|
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related tyrosine kinases, appears to mediate cell-cell initiated signal transduction via the binding of SH2-containing proteins to a conserved tyrosine that is phosphorylated. In many cases mediates homodimerisation.
Pssm-ID: 197735 Cd Length: 68 Bit Score: 48.06 E-value: 1.15e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2076569066 1366 VLVWSNDRVIRWVLSIGLREYAGNLAESGVHGALIALDETFDfsalaLLLQIPTQNTQARAVLEREFNSLL 1436
Cdd:smart00454 1 VSQWSPESVADWLESIGLEQYADNFRKNGIDGALLLLLTSEE-----DLKELGITKLGHRKKILKAIQKLK 66
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
78-563 |
1.74e-06 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 54.07 E-value: 1.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 78 ETQETLALTQGKLHE--VGHERDSLQRQ-----LSTALPQEFAALTKELSvcreqlLEREEEIAELKAERNNTRLLLEHL 150
Cdd:pfam12128 251 NTLESAELRLSHLHFgyKSDETLIASRQeerqeTSAELNQLLRTLDDQWK------EKRDELNGELSAADAAVAKDRSEL 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 151 ECLVSRHERSLRMTVVKR---QAQSPAgVSSEVEVL-KALKSLFEHHKALDEKVRERLRVALERCSlleEELGVTHKEMG 226
Cdd:pfam12128 325 EALEDQHGAFLDADIETAaadQEQLPS-WQSELENLeERLKALTGKHQDVTAKYNRRRSKIKEQNN---RDIAGIKDKLA 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 227 RWTFTVSKRLRRARTARQvppllPHASASAEGAPGAVSRQTPARRPCRSGSPRAGLRLqrspDGSLSHEEDLAKVLELQE 306
Cdd:pfam12128 401 KIREARDRQLAVAEDDLQ-----ALESELREQLEAGKLEFNEEEYRLKSRLGELKLRL----NQATATPELLLQLENFDE 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 307 VVDRqarehcqMKERLATLSGHVAELEEDLDTARKdliKSEEVNSRLQRDVREAMAQKEDMEERITTLEKR------YLA 380
Cdd:pfam12128 472 RIER-------AREEQEAANAEVERLQSELRQARK---RRDQASEALRQASRRLEERQSALDELELQLFPQagtllhFLR 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 381 AQreatsVHDLNDKLeSEIANKDAVHR----------QTEDKNRQLQERLELAEQKLQQTLRKAETLpevEAELAQRVAA 450
Cdd:pfam12128 542 KE-----APDWEQSI-GKVISPELLHRtdldpevwdgSVGGELNLYGVKLDLKRIDVPEWAASEEEL---RERLDKAEEA 612
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 451 LSKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMSEEHSKRLSDTV----DRLLSESGERLRLHLKERTAALEDKN 526
Cdd:pfam12128 613 LQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKqsekDKKNKALAERKDSANERLNSLEAQLK 692
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 2076569066 527 ALLREVGDAKKQLEE------TQRDKDQLVLnVEALRAELDQV 563
Cdd:pfam12128 693 QLDKKHQAWLEEQKEqkrearTEKQAYWQVV-EGALDAQLALL 734
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
310-562 |
1.90e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 54.19 E-value: 1.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 310 RQAREhcqmkERLATLSGHVAELEEDLDTARKDLIKSEEVNSRLQRDVRE--AMAQKEDMEERIttlekRYLAAQREats 387
Cdd:PRK04863 781 RAARE-----KRIEQLRAEREELAERYATLSFDVQKLQRLHQAFSRFIGShlAVAFEADPEAEL-----RQLNRRRV--- 847
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 388 vhdlndKLESEIANKDAVHRQTEDKNRQLQERLELAEQKLQQ-TLRKAETLPEVEAELAQRVAALSKAE---ERHGNIEE 463
Cdd:PRK04863 848 ------ELERALADHESQEQQQRSQLEQAKEGLSALNRLLPRlNLLADETLADRVEEIREQLDEAEEAKrfvQQHGNALA 921
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 464 RLRQMEAQLEEKNQELQRARQREKMSEEHSKRLSDTVdRLLSESGERlRLHLK-ERTAALEDKNALLREvgDAKKQLEET 542
Cdd:PRK04863 922 QLEPIVSVLQSDPEQFEQLKQDYQQAQQTQRDAKQQA-FALTEVVQR-RAHFSyEDAAEMLAKNSDLNE--KLRQRLEQA 997
|
250 260
....*....|....*....|
gi 2076569066 543 QRDKDQLvlnVEALRAELDQ 562
Cdd:PRK04863 998 EQERTRA---REQLRQAQAQ 1014
|
|
| RNase_Y_N |
pfam12072 |
RNase Y N-terminal region; |
414-532 |
1.95e-06 |
|
RNase Y N-terminal region;
Pssm-ID: 463456 [Multi-domain] Cd Length: 201 Bit Score: 51.04 E-value: 1.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 414 RQLQERLELAEQKLQQTLRKAETLP----------------EVEAELAQRVAALSKAEERHGNIEERL-RQMEAqLEEKN 476
Cdd:pfam12072 27 AKIGSAEELAKRIIEEAKKEAETKKkealleakeeihklraEAERELKERRNELQRQERRLLQKEETLdRKDES-LEKKE 105
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 2076569066 477 QELQRARQREKMSEEHSKRLSDTVDRLLSESGERLrlhlkERTAAL---EDKNALLREV 532
Cdd:pfam12072 106 ESLEKKEKELEAQQQQLEEKEEELEELIEEQRQEL-----ERISGLtseEAKEILLDEV 159
|
|
| Lebercilin |
pfam15619 |
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ... |
415-560 |
1.97e-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: 51.06 E-value: 1.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 415 QLQERLELAEQKLQQTLRKAETLPEV--------------EAELAQRVAALSkaEERHgNIEERLRQMEAQ-------LE 473
Cdd:pfam15619 15 ELQNELAELQSKLEELRKENRLLKRLqkrqekalgkyegtESELPQLIARHN--EEVR-VLRERLRRLQEKerdlerkLK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 474 EKNQELQRAR---QR-EKMS--------EEHSKRLSDTVDRLLSESGERLRLhlkERTAALEDKNaLLREVGDAKKQLEE 541
Cdd:pfam15619 92 EKEAELLRLRdqlKRlEKLSedknlaerEELQKKLEQLEAKLEDKDEKIQDL---ERKLELENKS-FRRQLAAEKKKHKE 167
|
170
....*....|....*....
gi 2076569066 542 TQRDKDQLVLNVEALRAEL 560
Cdd:pfam15619 168 AQEEVKILQEEIERLQQKL 186
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
393-541 |
2.05e-06 |
|
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.
Pssm-ID: 462316 [Multi-domain] Cd Length: 129 Bit Score: 49.56 E-value: 2.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 393 DKLESEIANKDAVHRQTEDKNRQLQERLELAEQKLQQTLRKAETlpEV--EAELAQrvaALSKAEERHGNIEERLRQMEA 470
Cdd:pfam07926 4 SSLQSEIKRLKEEAADAEAQLQKLQEDLEKQAEIAREAQQNYER--ELvlHAEDIK---ALQALREELNELKAEIAELKA 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2076569066 471 QLEEKNQELQRAR-----QREKMSEEhskrlsdtvdrlLSEsgerlrlhLKERTAALEDKNALLREvgdakkQLEE 541
Cdd:pfam07926 79 EAESAKAELEESEesweeQKKELEKE------------LSE--------LEKRIEDLNEQNKLLHD------QLES 128
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
299-559 |
2.06e-06 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 52.62 E-value: 2.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 299 AKVLELQEVVDRQAR---EHCQ-----MKERLATLSGHVAELEEDLDTARKDL----IKSE-EVNSR---------LQRD 356
Cdd:pfam00038 32 TKISELRQKKGAEPSrlySLYEkeiedLRRQLDTLTVERARLQLELDNLRLAAedfrQKYEdELNLRtsaendlvgLRKD 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 357 VREAMAQKEDMEERITTLEKRyLAAQReatSVHdlndklESEIANKDAVHRQTE-----DKNRQLQERLELAEQKLQQTL 431
Cdd:pfam00038 112 LDEATLARVDLEAKIESLKEE-LAFLK---KNH------EEEVRELQAQVSDTQvnvemDAARKLDLTSALAEIRAQYEE 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 432 RKAETLPEVEAELAQRVAALSKAEERHGnieERLRQMEAQLEEKNQELQRARqrekmSE-EHSKRLSDTVDRLLSESGER 510
Cdd:pfam00038 182 IAAKNREEAEEWYQSKLEELQQAAARNG---DALRSAKEEITELRRTIQSLE-----IElQSLKKQKASLERQLAETEER 253
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 2076569066 511 LRLHLKERTAALEDKNALLREV-GDAKKQLEETQrdkdQLvLNVE-ALRAE 559
Cdd:pfam00038 254 YELQLADYQELISELEAELQETrQEMARQLREYQ----EL-LNVKlALDIE 299
|
|
| TACC_C |
pfam05010 |
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a ... |
295-480 |
2.51e-06 |
|
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a C-terminal domain found in the the proteins TACC 1, 2 and 3 (TACC1-3). TACC1 is found concentrated in the centrosomes of eukaryotes which may play a conserved role in organizing centrosomal microtubules. The human TACC proteins have been linked to cancer and TACC2 has been identified as a possible tumour suppressor (AZU-1). TACC 3 from Xenopus laevis, also known as maskin, associates XMAP215 and promotes efficient microtubule elongation during mitosis. Maskin is also found to bind CPEB and elF-4E. Interestingly, the functional homolog (Alp7) in Schizosaccharomyces pombe (not included in this entry) has been shown to be required for organization of bipolar spindles.
Pssm-ID: 461517 [Multi-domain] Cd Length: 201 Bit Score: 50.83 E-value: 2.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 295 EEDLAKVLELQEVVDRQAREHCQMKERLATLSGHVAELEEDLDtARKDLIKSEEvnSRLQRDVREAMAQKEDMEERITTL 374
Cdd:pfam05010 18 EEKELEINELKAKYEELRRENLEMRKIVAEFEKTIAQMIEEKQ-KQKELEHAEI--QKVLEEKDQALADLNSVEKSFSDL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 375 EKRYLAaQREATSVHDLNDklesEIANKDAvhrqtedknRQLQERLELAEQKLQ-------QTLRKA-ETLPEVEAELAQ 446
Cdd:pfam05010 95 FKRYEK-QKEVISGYKKNE----ESLKKCA---------QDYLARIKKEEQRYQalkahaeEKLDQAnEEIAQVRSKAKA 160
|
170 180 190
....*....|....*....|....*....|....
gi 2076569066 447 RVAALsKAEERHGNIeeRLRQMEAQLEEKNQELQ 480
Cdd:pfam05010 161 ETAAL-QASLRKEQM--KVQSLERQLEQKTKENE 191
|
|
| DUF1978 |
pfam09321 |
Domain of unknown function (DUF1978); Members of this family are found in various hypothetical ... |
313-535 |
2.53e-06 |
|
Domain of unknown function (DUF1978); Members of this family are found in various hypothetical proteins produced by the bacterium Chlamydia pneumoniae. Their exact function has not, as yet, been identified.
Pssm-ID: 312723 [Multi-domain] Cd Length: 244 Bit Score: 51.46 E-value: 2.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 313 REHCQMKERLATLSGHVAELEEDLDTARKDLIKSEEVNSRLQRDVREAMAQKEDMEE--RITTLEKRYLAAQREATSVHD 390
Cdd:pfam09321 11 KEFREMLERLSDYRKVVFWLSENGVIDLPNDPGKWGLSGIPCRDALSEISRHELWEKkaHLKHLESLYTQARDRFEKQSS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 391 LNDKLESEIANKDAVhRQTEDKNRQLQERLELAEQKLQQtlRKAETL-PEVEAELAQRVAALSKAEERHGNIEERLRQ-M 468
Cdd:pfam09321 91 KKNQKELEEAEQEYL-SSWEDVKDQEIERVQERLQALQA--LYPEVSvSEEETEGQETVTPTVDLETALGRIEESYREcV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 469 EAQ----LEEKNQELQRARQ-REKMSEEHSKRLSD---TVDRLLSESGERLRL-------HLKERTAALEDKnallrEVG 533
Cdd:pfam09321 168 RDQedywKEEESKEVEMSAEfREEGGKKKSEEFQEqlgSLERFLKEHSEELEVlekhilkHESEATAENEKK-----ELS 242
|
..
gi 2076569066 534 DA 535
Cdd:pfam09321 243 DA 244
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
396-775 |
2.55e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 52.52 E-value: 2.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 396 ESEIANKDAVHRQTEDKNRQLQERLELAEQKLQQTLRKAET----LPEVEAELAQRVAALSKAEERhgnIEERlrqmEAQ 471
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNElqaeLEALQAEIDKLQAEIAEAEAE---IEER----REE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 472 LEEKNQELQRARQREKMSEE--HSKRLSDTVDRLLSesgerlrlhlkeRTAALEDKNALLREVGDAKKQLEETQRDKDQL 549
Cdd:COG3883 88 LGERARALYRSGGSVSYLDVllGSESFSDFLDRLSA------------LSKIADADADLLEELKADKAELEAKKAELEAK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 550 VLNVEALRAELDQVRlggpslhhgrphlgsvpdfrfpaadgpadpcgSSAVRTLNEQDWERAQQASVLASVAQAFESDRE 629
Cdd:COG3883 156 LAELEALKAELEAAK--------------------------------AELEAQQAEQEALLAQLSAEEAAAEAQLAELEA 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 630 LSDGGEDQDALFGSAGLLSPGGQADAQTLAVMLQEQLDAINKEISRVTRGAARRRTLPWRTERHLAGEKAGPGVAPTArG 709
Cdd:COG3883 204 ELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAAASA-A 282
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2076569066 710 SPAGPGSRGPRPVMGGFAQSRSASPECAGSGVLGGGLQALLPSGRDGSLGRARSPGSPAPSRPRAP 775
Cdd:COG3883 283 GGGAGGAGGGGGGGGAASGGSGGGSGGAGGVGSGGGAGAVVGGASAGGGGGSGGGGGSSGGGSGGG 348
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
400-554 |
2.99e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 52.86 E-value: 2.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 400 ANKDAVhRQTEDKNRQLQERLELAEQKLQQTLRKAETlpEVEAELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQEL 479
Cdd:PRK12704 36 AEEEAK-RILEEAKKEAEAIKKEALLEAKEEIHKLRN--EFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEEL 112
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2076569066 480 QRARQREKMSEEHSKRLSDTVDRLLSESGERLrlhlkERTAAL---EDKNALLREVgdakkqLEETQRDKDQLVLNVE 554
Cdd:PRK12704 113 EKKEKELEQKQQELEKKEEELEELIEEQLQEL-----ERISGLtaeEAKEILLEKV------EEEARHEAAVLIKEIE 179
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
328-481 |
3.01e-06 |
|
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: 50.83 E-value: 3.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 328 HVAELEEDLDTARKDLIKSEEVNSRLQRDVREAMAQKEDMEE-------------------RITTLEKRYLAAQREATSV 388
Cdd:pfam04012 30 AIRDMQSELVKARQALAQTIARQKQLERRLEQQTEQAKKLEEkaqaaltkgneelarealaEKKSLEKQAEALETQLAQQ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 389 HDLNDKLESEIANKDAVHRQTEDKNRQLQERLEL--AEQKLQQTLRKAET------LPEVEAELAQRVAALSKAEERHG- 459
Cdd:pfam04012 110 RSAVEQLRKQLAALETKIQQLKAKKNLLKARLKAakAQEAVQTSLGSLSTssatdsFERIEEKIEEREARADAAAELASa 189
|
170 180
....*....|....*....|...
gi 2076569066 460 -NIEERLRQMEAQLEEKNQELQR 481
Cdd:pfam04012 190 vDLDAKLEQAGIQMEVSEDVLAR 212
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
287-543 |
3.26e-06 |
|
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: 53.13 E-value: 3.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 287 SPDGSLSHEEDLAKVLELQEVVDRQAREhcqmKERLATLSGHVAELEEDLDTARKDLiKSEEVNsrlqrdVREAMAQKED 366
Cdd:TIGR00606 817 GSDLDRTVQQVNQEKQEKQHELDTVVSK----IELNRKLIQDQQEQIQHLKSKTNEL-KSEKLQ------IGTNLQRRQQ 885
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 367 MEERITTLEKRYLAAQRE-----------ATSVHDLNDKLESEIANKDAVHRQTEDKNRQLQERLELA-------EQKLQ 428
Cdd:TIGR00606 886 FEEQLVELSTEVQSLIREikdakeqdsplETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIhgymkdiENKIQ 965
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 429 QTlrKAETLPEVEAELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQE-------LQRARQREKMSE------EHSKR 495
Cdd:TIGR00606 966 DG--KDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQerwlqdnLTLRKRENELKEveeelkQHLKE 1043
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 2076569066 496 LSDtvDRLLSESGERLRLHLKERTAALEDKNALLR------EVGDAKKQLEETQ 543
Cdd:TIGR00606 1044 MGQ--MQVLQMKQEHQKLEENIDLIKRNHVLALGRqkgyekEIKHFKKELREPQ 1095
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
356-566 |
3.53e-06 |
|
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: 52.77 E-value: 3.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 356 DVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLESEIANKDA--------------VHRQTEdknrQLQE--- 418
Cdd:pfam05622 1 DLSEAQEEKDELAQRCHELDQQVSLLQEEKNSLQQENKKLQERLDQLESgddsgtpggkkyllLQKQLE----QLQEenf 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 419 RLELAEQKLQQtlrKAETLPEVEAELAQRVAALSK-AEE-----------RHGNieERLRQMEAQ--------------- 471
Cdd:pfam05622 77 RLETARDDYRI---KCEELEKEVLELQHRNEELTSlAEEaqalkdemdilRESS--DKVKKLEATvetykkkledlgdlr 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 472 -----LEEKNQE-LQRARQREKMS----------EEHSKRLSDTVDRLLSESGerlrlhlKERTAALEDKNalLREvgda 535
Cdd:pfam05622 152 rqvklLEERNAEyMQRTLQLEEELkkanalrgqlETYKRQVQELHGKLSEESK-------KADKLEFEYKK--LEE---- 218
|
250 260 270
....*....|....*....|....*....|.
gi 2076569066 536 kkQLEETQRDKDQLVLNVEALRAELDQVRLG 566
Cdd:pfam05622 219 --KLEALQKEKERLIIERDTLRETNEELRCA 247
|
|
| FAM184 |
pfam15665 |
Family with sequence similarity 184, A and B; The function of FAM184 is not known. |
392-564 |
3.79e-06 |
|
Family with sequence similarity 184, A and B; The function of FAM184 is not known.
Pssm-ID: 464788 [Multi-domain] Cd Length: 211 Bit Score: 50.43 E-value: 3.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 392 NDKLESEI-----ANKDAVHR---QTEDKNRQLQERLElAEQKLQqtlRKAETLPEVEAE-LAQRVAALSKAEERHGNIE 462
Cdd:pfam15665 9 NDEHEAEIqalkeAHEEEIQQilaETREKILQYKSKIG-EELDLK---RRIQTLEESLEQhERMKRQALTEFEQYKRRVE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 463 ERLRQMEAQLEEKNQELqrARQREKMSEEHSKRLsdtvdrllsESGERLRLHL-KERTAALED-KNALLREVgdakKQLE 540
Cdd:pfam15665 85 ERELKAEAEHRQRVVEL--SREVEEAKRAFEEKL---------ESFEQLQAQFeQEKRKALEElRAKHRQEI----QELL 149
|
170 180 190
....*....|....*....|....*....|
gi 2076569066 541 ETQRDK------DQLVLNvEALRAELDQVR 564
Cdd:pfam15665 150 TTQRAQsasslaEQEKLE-ELHKAELESLR 178
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
293-541 |
4.34e-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: 53.03 E-value: 4.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 293 SHEEDLAKVLE---LQEVVDRQAREHCQMKERLATLSGHVAELEEDLDTARKDLIKSEEVNSRL-------QR--DV--- 357
Cdd:COG3096 331 AASDHLNLVQTalrQQEKIERYQEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLksqladyQQalDVqqt 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 358 -----REAMAQKEDMEER-------ITTLEKRYLAAQREATSVHDLNDKLESEIANKDAVHRQTEdKNRQLQERL----- 420
Cdd:COG3096 411 raiqyQQAVQALEKARALcglpdltPENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFE-KAYELVCKIageve 489
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 421 -ELAEQKLQQTLRKAetlPEVEAeLAQRVAALskaEERHGNIEERLRQM---EAQLEEKNQELQRARQREKMSEEHSKRL 496
Cdd:COG3096 490 rSQAWQTARELLRRY---RSQQA-LAQRLQQL---RAQLAELEQRLRQQqnaERLLEEFCQRIGQQLDAAEELEELLAEL 562
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 2076569066 497 SDTVDRL---LSESGERL------RLHLKERTAALEDKNALLREVGDAKKQLEE 541
Cdd:COG3096 563 EAQLEELeeqAAEAVEQRselrqqLEQLRARIKELAARAPAWLAAQDALERLRE 616
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
384-564 |
5.13e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 52.61 E-value: 5.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 384 EATSVHDLNDKLESEIANKDAVHRQTEDKNRQLqERLELAEQKLQQTLRKAETLPEVEAELAQrvAALSKAEERHGNIEE 463
Cdd:COG4913 219 EEPDTFEAADALVEHFDDLERAHEALEDAREQI-ELLEPIRELAERYAAARERLAELEYLRAA--LRLWFAQRRLELLEA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 464 RLRQMEAQLEEKNQELQRARQREkmsEEHSKRLSDTVDRLLSESGERLrlhlkertaaledkNALLREVGDAKKQLEETQ 543
Cdd:COG4913 296 ELEELRAELARLEAELERLEARL---DALREELDELEAQIRGNGGDRL--------------EQLEREIERLERELEERE 358
|
170 180
....*....|....*....|.
gi 2076569066 544 RDKDQLVLNVEALRAELDQVR 564
Cdd:COG4913 359 RRRARLEALLAALGLPLPASA 379
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
317-471 |
5.93e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 51.94 E-value: 5.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 317 QMKERLATLSGHVAELEEDLDTARKDLIKSEEVNSRLQRD--VREAMAQKEDMEERITTLEKRYL-------AAQREats 387
Cdd:COG3206 223 ELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSpvIQQLRAQLAELEAELAELSARYTpnhpdviALRAQ--- 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 388 VHDLNDKLESEIAnkdAVHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKAEERHGNIEERLRQ 467
Cdd:COG3206 300 IAALRAQLQQEAQ---RILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEE 376
|
....
gi 2076569066 468 MEAQ 471
Cdd:COG3206 377 ARLA 380
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
2709-3112 |
7.41e-06 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 52.18 E-value: 7.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 2709 HLPEAQWEGRPAACRRTTEGWWPLSSGRVCVRTAEAMSRLSLRGPAGVTREQPCPAAREGPGRRQHPSARPHRLSTRCPL 2788
Cdd:COG3321 862 PLPTYPFQREDAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAALLALVALAAAAAA 941
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 2789 RRAGQSCQAWPVRACAGRWTRGCGAHACLLWRGLAAPVPSAEPGSARALQGARQPAGRARLPRSRSQAGPRRTPSGDTEP 2868
Cdd:COG3321 942 LLALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAAALLLAAAAAAAAL 1021
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 2869 GALLLDAPTPAGRERLRRDHRLAAPGATRPGAQQPAQSAPSLPPARPRRLAGKFSGPGAGATARDSACGFGLPSPGAPAA 2948
Cdd:COG3321 1022 LALAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAALALAAALAAAALALALAA 1101
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 2949 AGPEVGSAAVRVGQRGHTPGRGGGAQRPEGSGTDRGEGVLRLGDGTPAPSSPSLTGQCRRVGHRLGCLRPRAPAHVAVRA 3028
Cdd:COG3321 1102 LAAALLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAALLAAAALLLALALAL 1181
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 3029 DVQPPRVGLRAGPGEGAGGATRRGGAWGRGLRGPDAPRPAAEPEVGPGRSGGRSAAGGGGRTERAAVSARRGGPGLWAGA 3108
Cdd:COG3321 1182 AAALAAALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALALLALAAAAAAVAALAAAAAALLAALAA 1261
|
....
gi 2076569066 3109 PAAR 3112
Cdd:COG3321 1262 LALL 1265
|
|
| Nuf2_DHR10-like |
pfam18595 |
Nuf2, DHR10-like domain; This domain is found at the C-terminal region of Nuf2 proteins. This ... |
417-531 |
8.45e-06 |
|
Nuf2, DHR10-like domain; This domain is found at the C-terminal region of Nuf2 proteins. This domain was identified as MazG related domain also designated as Designed helical repeat protein 10 (DHR10) that actually adopts a coiled-coil structure. Nuf2 is part of the Ndc80 complex, which binds to the spindle and is required for chromosome segregation and spindle checkpoint activity.
Pssm-ID: 465814 [Multi-domain] Cd Length: 117 Bit Score: 47.19 E-value: 8.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 417 QERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKAE---ERHGNIEERLRQMEAQLEEKNQELQRARQREKMSEehs 493
Cdd:pfam18595 8 KEELAELERKARELQAKIDALQVVEKDLRSCIKLLEEIEaelAKLEEAKKKLKELRDALEEKEIELRELERREERLQ--- 84
|
90 100 110
....*....|....*....|....*....|....*...
gi 2076569066 494 KRLSDTVDRLlsesgERLRLHLKERTAALEDKNALLRE 531
Cdd:pfam18595 85 RQLENAQEKL-----ERLREQAEEKREAAQARLEELRE 117
|
|
| F-BAR_GAS7 |
cd07649 |
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Growth Arrest Specific protein ... |
344-526 |
9.43e-06 |
|
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Growth Arrest Specific protein 7; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Growth Arrest Specific protein 7 (GAS7) is mainly expressed in the brain and is required for neurite outgrowth. It may also play a role in the protection and migration of embryonic stem cells. Treatment-related acute myeloid leukemia (AML) has been reported resulting from mixed-lineage leukemia (MLL)-GAS7 translocations as a complication of primary cancer treatment. GAS7 contains an N-terminal SH3 domain, followed by a WW domain, and a central F-BAR domain. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.
Pssm-ID: 153333 [Multi-domain] Cd Length: 233 Bit Score: 49.63 E-value: 9.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 344 IKSEEVNSRLQRDVREAMAQKEDMEERITTLEKRYLAAQREATsVHDLNDKLESEIANKDAVHRQTEDKNR-QLQERLEL 422
Cdd:cd07649 15 LKGKQMQKEMAEFIRERIKIEEEYAKNLSKLSQSSLAAQEEGT-LGEAWAQVKKSLADEAEVHLKFSSKLQsEVEKPLLN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 423 AEQKLQQTLRKAET-LPEVEAELAQRVAALSKAE----ERHGNIEERLRQMEAQLEEKNQE-LQRARQRekmSEEHSKRL 496
Cdd:cd07649 94 FRENFKKDMKKLDHhIADLRKQLASRYAAVEKARkallERQKDLEGKTQQLEIKLSNKTEEdIKKARRK---STQAGDDL 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2076569066 497 SDTVD---------------------RLLSESGERLRLHLKERTAALEDKN 526
Cdd:cd07649 171 MRCVDlynqaqskwfeemvttsleleRLEVERIEMIRQHLCQYTQLRHETD 221
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
352-564 |
1.15e-05 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 48.98 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 352 RLQRDVREAMAQKEDMEERITTLEKRylaaqREATSVHDLNDKLEseiankdavhrqtedknrQLQERLELAEQKLQQTL 431
Cdd:cd00176 4 QFLRDADELEAWLSEKEELLSSTDYG-----DDLESVEALLKKHE------------------ALEAELAAHEERVEALN 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 432 RKAETLPEVEAELAQRVaalskaEERHGNIEERLRQMEAQLEEKNQELQRARQREKMSEEHS---KRLSDTVDRLLSESG 508
Cdd:cd00176 61 ELGEQLIEEGHPDAEEI------QERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADdleQWLEEKEAALASEDL 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2076569066 509 ERLRLHLKErtaALEDKNALLREVGDAKKQLEETQRDKDQLVLNV-----EALRAELDQVR 564
Cdd:cd00176 135 GKDLESVEE---LLKKHKELEEELEAHEPRLKSLNELAEELLEEGhpdadEEIEEKLEELN 192
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
59-562 |
1.17e-05 |
|
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: 51.51 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 59 EQLMVSMLEERDRLM---DTLRETQETLALTQGKLHE--VGHERDSLQRQLSTALPQE-FAALTKELSVCREQLLEREEE 132
Cdd:pfam02463 278 EKEKKLQEEELKLLAkeeEELKSELLKLERRKVDDEEklKESEKEKKKAEKELKKEKEeIEELEKELKELEIKREAEEEE 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 133 IAELKAERNNTRLLLEHLECLVSRH-ERSLRMTVVKRQAQSPAGV-SSEVEVLKALKSLFEHHK--------ALDEKVRE 202
Cdd:pfam02463 358 EEELEKLQEKLEQLEEELLAKKKLEsERLSSAAKLKEEELELKSEeEKEAQLLLELARQLEDLLkeekkeelEILEEEEE 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 203 RLRVALERCSLLEEELGVTHKEMGRWTFTVSKRLRRARTARQVPPLLPHASASAEGAPG-AVSRQTPARRPC-----RSG 276
Cdd:pfam02463 438 SIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEeRSQKESKARSGLkvllaLIK 517
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 277 SPRAGLRLQRSPDGSLSHEEDLAK---------VLELQEVVDRQAREHCQMKERLATLSGHVAELEEDLDTARKDLIKSE 347
Cdd:pfam02463 518 DGVGGRIISAHGRLGDLGVAVENYkvaistaviVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVL 597
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 348 EVNSRLQR-------------DVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKL--ESEIANKDAVHRQTEDK 412
Cdd:pfam02463 598 EIDPILNLaqldkatleadedDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLaeKSEVKASLSELTKELLE 677
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 413 NRQLQERLELAEQKLQQTLR---------KAETLPEVEAELAQRVAALSKAEERHgNIEERLRQMEAQLEEKNQELQRAR 483
Cdd:pfam02463 678 IQELQEKAESELAKEEILRRqleikkkeqREKEELKKLKLEAEELLADRVQEAQD-KINEELKLLKQKIDEEEEEEEKSR 756
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 484 QrEKMSEEHSKRLSDTVDRLLSESGERLRLHLKERT------AALEDKNALLREVGDAKKQLEETQRDKDQLVLNVEALR 557
Cdd:pfam02463 757 L-KKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEkeeklkAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEEL 835
|
....*
gi 2076569066 558 AELDQ 562
Cdd:pfam02463 836 EELAL 840
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
64-489 |
1.32e-05 |
|
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: 50.45 E-value: 1.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 64 SMLEERDRLMDTLRETQETLALTQGKLHEVGHERDSLQRQLSTALpQEFAALTKELSVCREQLLEREEEIAELKAERNNT 143
Cdd:pfam19220 38 AILRELPQAKSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAE-GELEELVARLAKLEAALREAEAAKEELRIELRDK 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 144 RLLLEHLEclvsrherslrmtvvkRQAQSPAGVSSEVEvlKALKSLFEHHKALDEKVRE---RLRVALERCSLLEEElgv 220
Cdd:pfam19220 117 TAQAEALE----------------RQLAAETEQNRALE--EENKALREEAQAAEKALQRaegELATARERLALLEQE--- 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 221 thkemgrwtftvsKRLRRARTARQVPPLLPHASASAEgapgavsrqtparrpcRSGSPRAGLRLQRSPDGSLSHEEDLAK 300
Cdd:pfam19220 176 -------------NRRLQALSEEQAAELAELTRRLAE----------------LETQLDATRARLRALEGQLAAEQAERE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 301 VLE--LQEVVDRQAREHCQMKERLATLSGHVAELEEDLDTARKDLIkseevnsrlqrdvreamaqkeDMEERITTLEKRY 378
Cdd:pfam19220 227 RAEaqLEEAVEAHRAERASLRMKLEALTARAAATEQLLAEARNQLR---------------------DRDEAIRAAERRL 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 379 LAAQREATSVHDLNDKLESEIAnkdavhRQTEDKNRQLQERLELAEQklQQTLRKAetlpeveaeLAQRVAALSKAEERH 458
Cdd:pfam19220 286 KEASIERDTLERRLAGLEADLE------RRTQQFQEMQRARAELEER--AEMLTKA---------LAAKDAALERAEERI 348
|
410 420 430
....*....|....*....|....*....|....*...
gi 2076569066 459 GNIEERLRQME-------AQLEEKNQELQRARQREKMS 489
Cdd:pfam19220 349 ASLSDRIAELTkrfeverAALEQANRRLKEELQRERAE 386
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
305-510 |
1.35e-05 |
|
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: 50.42 E-value: 1.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 305 QEVVDRQAREHCQMKERLATLSghvAELEEDLDTARKDLIKSEE------------VNSRLQRDVREAMAQKEDMEERIT 372
Cdd:pfam15558 54 LLLQQSQEQWQAEKEQRKARLG---REERRRADRREKQVIEKESrwreqaedqenqRQEKLERARQEAEQRKQCQEQRLK 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 373 TLEkRYLAAQREatSVHDLNDKLESEIANKDAVHRQTEDKNRQLqerLELAEQKLQQTLRKAETLPEVEAELAQRVA--- 449
Cdd:pfam15558 131 EKE-EELQALRE--QNSLQLQERLEEACHKRQLKEREEQKKVQE---NNLSELLNHQARKVLVDCQAKAEELLRRLSleq 204
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2076569066 450 ALSKAEERH-GNIEERLRQMEAQLEEKNQELQRARQR-EKMSEEHSKRLsdtvdRLLSESGER 510
Cdd:pfam15558 205 SLQRSQENYeQLVEERHRELREKAQKEEEQFQRAKWRaEEKEEERQEHK-----EALAELADR 262
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
293-615 |
1.36e-05 |
|
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: 51.20 E-value: 1.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 293 SHEEDLAKVLELQEVVDRQAREHCQMKERLATLSGHV---AELEEDLDTARKDLIKSEEVNSRL---QRD---------- 356
Cdd:TIGR00606 316 EKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLqlqADRHQEHIRARDSLIQSLATRLELdgfERGpfserqiknf 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 357 ---VREAMAQKEDM-EERITTLEKRYLAAQREATSVHDLNDKLESEIANKdavhrqtEDKNRQLQERLELAEQKLQQTLR 432
Cdd:TIGR00606 396 htlVIERQEDEAKTaAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELK-------KEILEKKQEELKFVIKELQQLEG 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 433 KAETLPEVEAELAQRVAALSKAEErHGNIEERLRQmEAQLEEKNQELQRARQREKMSEEHSKRLSDTVDRLLSESGERLR 512
Cdd:TIGR00606 469 SSDRILELDQELRKAERELSKAEK-NSLTETLKKE-VKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMD 546
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 513 LHLKERTAALEDKNALLREVGD--AKKQLEET----QRDKDQLV-----LNVEALRAELDQvrlggpslHHGRPHLGSVP 581
Cdd:TIGR00606 547 KDEQIRKIKSRHSDELTSLLGYfpNKKQLEDWlhskSKEINQTRdrlakLNKELASLEQNK--------NHINNELESKE 618
|
330 340 350
....*....|....*....|....*....|....
gi 2076569066 582 DFRFPAADGPADPCGSSAVRTLNEQDWERAQQAS 615
Cdd:TIGR00606 619 EQLSSYEDKLFDVCGSQDEESDLERLKEEIEKSS 652
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
299-489 |
1.40e-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: 50.15 E-value: 1.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 299 AKVLELQEVVDRQAREHCQMKERLATLSGHVAELEEDLDTARKDLIKSEEVNSRLQRDVREAM-AQKEDMEE--RITTLE 375
Cdd:COG4942 62 RRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALlLSPEDFLDavRRLQYL 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 376 KRYLAAQREATS--VHDLND--KLESEIANKDAVHRQTEDKNRQLQERLELAEQKLQQTLRKaetLPEVEAELAQRVAAL 451
Cdd:COG4942 142 KYLAPARREQAEelRADLAElaALRAELEAERAELEALLAELEEERAALEALKAERQKLLAR---LEKELAELAAELAEL 218
|
170 180 190
....*....|....*....|....*....|....*...
gi 2076569066 452 SKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMS 489
Cdd:COG4942 219 QQEAEELEALIARLEAEAAAAAERTPAAGFAALKGKLP 256
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
309-495 |
2.12e-05 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 49.87 E-value: 2.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 309 DRQAREHCQMKERLATLSGHV-----AELEEDLDTARKDLIKSEEVNSRLQRDVR---EAMAQKEDMEERITTLEKRYLA 380
Cdd:pfam02029 149 VRQAEEEGEEEEDKSEEAEEVptenfAKEEVKDEKIKKEKKVKYESKVFLDQKRGhpeVKSQNGEEEVTKLKVTTKRRQG 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 381 --AQREATSVhDLNDKLESEiankdavhRQTEDKNRQLQERLELAEQKLQQTLRKAEtlpeVEAELAQRvaalsKAEERH 458
Cdd:pfam02029 229 glSQSQEREE-EAEVFLEAE--------QKLEELRRRRQEKESEEFEKLRQKQQEAE----LELEELKK-----KREERR 290
|
170 180 190
....*....|....*....|....*....|....*..
gi 2076569066 459 GNIEERLRQMEAqlEEKNQELQRARQREKMSEEHSKR 495
Cdd:pfam02029 291 KLLEEEEQRRKQ--EEAERKLREEEEKRRMKEEIERR 325
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
423-562 |
2.20e-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: 48.38 E-value: 2.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 423 AEQKLQQTLRKaetLPEVEAELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRA----RQREKMSEEHSKRLSD 498
Cdd:COG1579 1 AMPEDLRALLD---LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLekeiKRLELEIEEVEARIKK 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2076569066 499 TVDRLLSESGER----LRL---HLKERTAALEDK-NALLREVGDAKKQLEETQRDKDQLVLNVEALRAELDQ 562
Cdd:COG1579 78 YEEQLGNVRNNKeyeaLQKeieSLKRRISDLEDEiLELMERIEELEEELAELEAELAELEAELEEKKAELDE 149
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
310-562 |
2.26e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 50.34 E-value: 2.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 310 RQAREhcqmkERLATLSGHVAELEEDLDTARKDLIKSEevnsRLQRDVREAMAQ------KEDMEERITTLEKRylaaQR 383
Cdd:COG3096 780 RAARE-----KRLEELRAERDELAEQYAKASFDVQKLQ----RLHQAFSQFVGGhlavafAPDPEAELAALRQR----RS 846
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 384 EatsvhdlndkLESEIANKDAVHRQTEDKNRQLQERLELAEQKLQQT-LRKAETLPEVEAELAQRVAALSKAE---ERHG 459
Cdd:COG3096 847 E----------LERELAQHRAQEQQLRQQLDQLKEQLQLLNKLLPQAnLLADETLADRLEELREELDAAQEAQafiQQHG 916
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 460 NIEER-------LRQMEAQLEEKNQELQRARQREKMSEEHSKRLSDTVDRLL----SESGERLrlhlkERTAALEDKnal 528
Cdd:COG3096 917 KALAQleplvavLQSDPEQFEQLQADYLQAKEQQRRLKQQIFALSEVVQRRPhfsyEDAVGLL-----GENSDLNEK--- 988
|
250 260 270
....*....|....*....|....*....|....
gi 2076569066 529 LREvgdakkQLEETQRDKDQLVLNVEALRAELDQ 562
Cdd:COG3096 989 LRA------RLEQAEEARREAREQLRQAQAQYSQ 1016
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
304-484 |
2.41e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 50.02 E-value: 2.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 304 LQEVVDRQAREhcqMKERLATLSGHVAELEEDLDTARKDLIK----------SEEVN------SRLQRDVREAMAQKEDM 367
Cdd:COG3206 162 LEQNLELRREE---ARKALEFLEEQLPELRKELEEAEAALEEfrqknglvdlSEEAKlllqqlSELESQLAEARAELAEA 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 368 EERITTLEKR------YLAAQREATSVHDLNDKLESEIANKDAVHRQTEDKN---RQLQERLELAEQKLQQTLRKAETLP 438
Cdd:COG3206 239 EARLAALRAQlgsgpdALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHpdvIALRAQIAALRAQLQQEAQRILASL 318
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2076569066 439 EVEAE-LAQRVAALSKAEERhgnIEERLRQM---EAQLEEKNQELQRARQ 484
Cdd:COG3206 319 EAELEaLQAREASLQAQLAQ---LEARLAELpelEAELRRLEREVEVARE 365
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
380-491 |
2.72e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 49.78 E-value: 2.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 380 AAQREATSVhdlndKLESEIANKDAVHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKAEERHG 459
Cdd:PRK12704 46 EAKKEAEAI-----KKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELE 120
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 2076569066 460 NIEERLRQMEAQLEEK----NQELQR--------ARQR--EKMSEE 491
Cdd:PRK12704 121 QKQQELEKKEEELEELieeqLQELERisgltaeeAKEIllEKVEEE 166
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
317-487 |
3.16e-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: 3.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 317 QMKERLATLSGHVAELEEDLDTARKDLIKSE-EVNS-RLQRDVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDK 394
Cdd:COG3206 165 NLELRREEARKALEFLEEQLPELRKELEEAEaALEEfRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAA 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 395 LESEIA-NKDAVHRQTEDKN-RQLQERLELAEQKLQQTLRK-AETLPEVEAELAQRVAALSKAEERHGNIEERLRQMEAQ 471
Cdd:COG3206 245 LRAQLGsGPDALPELLQSPViQQLRAQLAELEAELAELSARyTPNHPDVIALRAQIAALRAQLQQEAQRILASLEAELEA 324
|
170
....*....|....*.
gi 2076569066 472 LEEKNQELQRARQREK 487
Cdd:COG3206 325 LQAREASLQAQLAQLE 340
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
410-541 |
3.24e-05 |
|
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.
Pssm-ID: 461709 [Multi-domain] Cd Length: 153 Bit Score: 46.57 E-value: 3.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 410 EDKNRQLQERLELAEQKLQqtlRKAETLPEVEAELAQRVAALSKAEErhgnieERLRQMEAQLEEKNQELQRARQREKMS 489
Cdd:pfam05672 25 EQREREEQERLEKEEEERL---RKEELRRRAEEERARREEEARRLEE------ERRREEEERQRKAEEEAEEREQREQEE 95
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 2076569066 490 EEHSKRLSDTVDRLLSESGERLRLHlKERTAALEDKNALLRevgdaKKQLEE 541
Cdd:pfam05672 96 QERLQKQKEEAEAKAREEAERQRQE-REKIMQQEEQERLER-----KKRIEE 141
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
295-408 |
3.75e-05 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 47.51 E-value: 3.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 295 EEDLAKVL-----ELQEVVDRQAREHCQMKERLATLSGHVAELEEDLDTAR--KDLIKSEEVNSRLQRDVREAMAQK--- 364
Cdd:COG1842 82 REDLAREAlerkaELEAQAEALEAQLAQLEEQVEKLKEALRQLESKLEELKakKDTLKARAKAAKAQEKVNEALSGIdsd 161
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 2076569066 365 ------EDMEERITTLEKRyLAAQREATSVHDLNDKLEsEIANKDAVHRQ 408
Cdd:COG1842 162 datsalERMEEKIEEMEAR-AEAAAELAAGDSLDDELA-ELEADSEVEDE 209
|
|
| SAM_2 |
pfam07647 |
SAM domain (Sterile alpha motif); |
1292-1347 |
3.87e-05 |
|
SAM domain (Sterile alpha motif);
Pssm-ID: 429573 Cd Length: 66 Bit Score: 43.80 E-value: 3.87e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 2076569066 1292 EWLPSLGLPQYRSYFMECLVD-ARMLDHLTKKDLrGQLKMVDSFHRNSFQCGIMCLR 1347
Cdd:pfam07647 11 DWLRSIGLEQYTDNFRDQGITgAELLLRLTLEDL-KRLGITSVGHRRKILKKIQELK 66
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
334-564 |
3.93e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 49.51 E-value: 3.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 334 EDLDTARKDLIKSEEVNSRLqrDVREAMAQKEDMEERITTLEKRylaAQREATSVHDLNDKLESEIankdavhRQTEDKN 413
Cdd:PRK01156 561 EDLDSKRTSWLNALAVISLI--DIETNRSRSNEIKKQLNDLESR---LQEIEIGFPDDKSYIDKSI-------REIENEA 628
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 414 RQLQERLELAEQK--LQQTLR-KAETLPEVEAELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMSE 490
Cdd:PRK01156 629 NNLNNKYNEIQENkiLIEKLRgKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILR 708
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2076569066 491 EHSKRLSDTVDrllsesgerlrlhlkERTAALEDKNALLREVGDAKKQLEETQRDKDQLVLNVEALRAELDQVR 564
Cdd:PRK01156 709 TRINELSDRIN---------------DINETLESMKKIKKAIGDLKRLREAFDKSGVPAMIRKSASQAMTSLTR 767
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
310-477 |
3.96e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 49.57 E-value: 3.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 310 RQAREHCQMKERLATLSGHVAELEEDLDTARKDLIKSEEVNSRLQRDVREAmaqkEDMEERITTLEkrylaAQREatsvh 389
Cdd:COG3096 502 RRYRSQQALAQRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAA----EELEELLAELE-----AQLE----- 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 390 DLNDKLESEIANKDAVHRQTEDKNRQ-------------LQERLE-LAEQkLQQTLrkaETLPEVEAELAQRVAALSKAE 455
Cdd:COG3096 568 ELEEQAAEAVEQRSELRQQLEQLRARikelaarapawlaAQDALErLREQ-SGEAL---ADSQEVTAAMQQLLEREREAT 643
|
170 180
....*....|....*....|..
gi 2076569066 456 ERHGNIEERLRQMEAQLEEKNQ 477
Cdd:COG3096 644 VERDELAARKQALESQIERLSQ 665
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
313-427 |
4.22e-05 |
|
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.
Pssm-ID: 466641 [Multi-domain] Cd Length: 120 Bit Score: 45.29 E-value: 4.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 313 REHCQMKERLAtlsghvaELEEDLDTARKDLIKSEEVNSRLQRDVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLN 392
Cdd:pfam20492 6 REKQELEERLK-------QYEEETKKAQEELEESEETAEELEEERRQAEEEAERLEQKRQEAEEEKERLEESAEMEAEEK 78
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 2076569066 393 DKLESEIANKDA-VHRQTEDKNR------QLQERLELAEQKL 427
Cdd:pfam20492 79 EQLEAELAEAQEeIARLEEEVERkeeearRLQEELEEAREEE 120
|
|
| Nuf2_DHR10-like |
pfam18595 |
Nuf2, DHR10-like domain; This domain is found at the C-terminal region of Nuf2 proteins. This ... |
392-496 |
4.74e-05 |
|
Nuf2, DHR10-like domain; This domain is found at the C-terminal region of Nuf2 proteins. This domain was identified as MazG related domain also designated as Designed helical repeat protein 10 (DHR10) that actually adopts a coiled-coil structure. Nuf2 is part of the Ndc80 complex, which binds to the spindle and is required for chromosome segregation and spindle checkpoint activity.
Pssm-ID: 465814 [Multi-domain] Cd Length: 117 Bit Score: 45.27 E-value: 4.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 392 NDKLESEianKDAVhRQTEDKNRQLQERLE---LAEQKLQQTLRKAEtlpEVEAELAQRVAALSKAEERHGNIEE----- 463
Cdd:pfam18595 1 SSTLAEE---KEEL-AELERKARELQAKIDalqVVEKDLRSCIKLLE---EIEAELAKLEEAKKKLKELRDALEEkeiel 73
|
90 100 110
....*....|....*....|....*....|....*....
gi 2076569066 464 -----RLRQMEAQLEEKNQELQRAR-QREKMSEEHSKRL 496
Cdd:pfam18595 74 relerREERLQRQLENAQEKLERLReQAEEKREAAQARL 112
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
319-561 |
4.98e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 49.25 E-value: 4.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 319 KERLATLSGHVAELEEDLDTARKDLIKSEEVNSRLQRDVREAMAQKEDMEERITTLEK-------RYLAAQREATSVHDL 391
Cdd:TIGR04523 95 KDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKeleklnnKYNDLKKQKEELENE 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 392 NDKLESEIANK----DAVHRQ-------------TEDKNRQLQ-ERLELAEQklQQTLRKaeTLPEVEAELAQRVAALSK 453
Cdd:TIGR04523 175 LNLLEKEKLNIqkniDKIKNKllklelllsnlkkKIQKNKSLEsQISELKKQ--NNQLKD--NIEKKQQEINEKTTEISN 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 454 AEERHGNIEERLRQMEAQLEEKNQELQRARQREKMSEEHSKRLSDTVDRLLSESGERLRLHLKERtaaLEDKNALLREVg 533
Cdd:TIGR04523 251 TQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELKSE---LKNQEKKLEEI- 326
|
250 260
....*....|....*....|....*...
gi 2076569066 534 daKKQLEETQRDKDQLVLNVEALRAELD 561
Cdd:TIGR04523 327 --QNQISQNNKIISQLNEQISQLKKELT 352
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
302-514 |
6.06e-05 |
|
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: 48.11 E-value: 6.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 302 LELQEVVDRQARE--HCQMKERL--ATLSGHVAELEEDLDtaRKDLIKSEEVNSRLqRDVREAMAQKEDMEERITTLEKR 377
Cdd:pfam15558 129 LKEKEEELQALREqnSLQLQERLeeACHKRQLKEREEQKK--VQENNLSELLNHQA-RKVLVDCQAKAEELLRRLSLEQS 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 378 YLAAQ-REATSVHDLNDKLESEIANKDA----VHRQTEDKNRQLQERLE----LAEQKLQQ--------TLRKAETLPE- 439
Cdd:pfam15558 206 LQRSQeNYEQLVEERHRELREKAQKEEEqfqrAKWRAEEKEEERQEHKEalaeLADRKIQQarqvahktVQDKAQRAREl 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 440 -VEAELAQRVAAL-------SKAEERHGNIEERLRQMEAQLEEKNQELQRARQ--------REKMSEEHSKRlsdTVDRL 503
Cdd:pfam15558 286 nLEREKNHHILKLkvekeekCHREGIKEAIKKKEQRSEQISREKEATLEEARKtarasfhmREKVREETNNR---TFDKM 362
|
250
....*....|.
gi 2076569066 504 LSESGERLRLH 514
Cdd:pfam15558 363 ALEAQLHASLQ 373
|
|
| BAR_SNX |
cd07596 |
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid ... |
329-542 |
6.54e-05 |
|
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.
Pssm-ID: 153280 [Multi-domain] Cd Length: 218 Bit Score: 46.97 E-value: 6.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 329 VAELEEDLDTARKdlikseevnsRLQRDVREAMAQKEDMEERITTLEKryLAAQrEATSVHDLNDKLESEIANKDAVHRQ 408
Cdd:cd07596 13 ILKLEEQLKKLSK----------QAQRLVKRRRELGSALGEFGKALIK--LAKC-EEEVGGELGEALSKLGKAAEELSSL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 409 TEDKNRQLQERL-----------ELAEQKLQQTLRKAETLPEVEAELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQ 477
Cdd:cd07596 80 SEAQANQELVKLleplkeylrycQAVKETLDDRADALLTLQSLKKDLASKKAQLEKLKAAPGIKPAKVEELEEELEEAES 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2076569066 478 ELQRARQR-EKMSEEHSKrlsdtvdrllsesgERLRLHlKERTAALedkNALLREVGDAKKQLEET 542
Cdd:cd07596 160 ALEEARKRyEEISERLKE--------------ELKRFH-EERARDL---KAALKEFARLQVQYAEK 207
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
417-564 |
7.42e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.76 E-value: 7.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 417 QERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKAEERHGNIEE------RLRQMEAQLEEKNQELQRARQRekmse 490
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEyswdeiDVASAEREIAELEAELERLDAS----- 683
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 491 ehskrlSDTVDRLlsesGERLRLHLKERTAALEDKNALLREVGDAKKQLEETQRDKDQLVLNVEA--------LRAELDQ 562
Cdd:COG4913 684 ------SDDLAAL----EEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAaedlarleLRALLEE 753
|
..
gi 2076569066 563 VR 564
Cdd:COG4913 754 RF 755
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
321-555 |
8.15e-05 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 48.31 E-value: 8.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 321 RLATLSGHVAELEEDLDT-----ARKDLiksEEVNSRLQ------RDVREAMAQKEDMEER----ITTLEKRY------L 379
Cdd:pfam06160 61 SLPDIEELLFEAEELNDKyrfkkAKKAL---DEIEELLDdieediKQILEELDELLESEEKnreeVEELKDKYrelrktL 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 380 AAQREA--TSVHDLNDKL---ESEIA-----NKDAVHRQTEDKNRQLQERLELAEQKLQQT---LRKAET-LPEVEAELA 445
Cdd:pfam06160 138 LANRFSygPAIDELEKQLaeiEEEFSqfeelTESGDYLEAREVLEKLEEETDALEELMEDIpplYEELKTeLPDQLEELK 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 446 QRVAALsKAEE---RHGNIEERLRQMEAQLEE-----KNQELQRARQREKMSEEHSKRLSDT----------VDRLLSES 507
Cdd:pfam06160 218 EGYREM-EEEGyalEHLNVDKEIQQLEEQLEEnlallENLELDEAEEALEEIEERIDQLYDLlekevdakkyVEKNLPEI 296
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 2076569066 508 GERLR------LHLKERTAALeDKNALL--REVGDAK---KQLEETQRDKDQLVLNVEA 555
Cdd:pfam06160 297 EDYLEhaeeqnKELKEELERV-QQSYTLneNELERVRgleKQLEELEKRYDEIVERLEE 354
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
325-488 |
9.28e-05 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 48.21 E-value: 9.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 325 LSGHVAELEEDLDTARKDLIkseEVNSRLQRDVREAMAQKEDMEERITTLEKRYLAAQREAtSVHDLNDKLESEIAnkdA 404
Cdd:pfam09731 285 LNSLIAHAHREIDQLSKKLA---ELKKREEKHIERALEKQKEELDKLAEELSARLEEVRAA-DEAQLRLEFERERE---E 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 405 VHRQTEDKNR-QLQERLELAEQKLQQTLRKAETLPEVEAE-------LAQRVAALSKAEERHGNieerLRQMEAQLEEKN 476
Cdd:pfam09731 358 IRESYEEKLRtELERQAEAHEEHLKDVLVEQEIELQREFLqdikekvEEERAGRLLKLNELLAN----LKGLEKATSSHS 433
|
170
....*....|..
gi 2076569066 477 QELQRARQREKM 488
Cdd:pfam09731 434 EVEDENRKAQQL 445
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
291-517 |
9.57e-05 |
|
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: 48.43 E-value: 9.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 291 SLSHEEDLAKVLELQEVVDRQAREHCQMKERLATLSGHVAELEEDLDTARKDLIKSEEVNSRLQRDVREAM-AQKEDMEE 369
Cdd:pfam02463 833 EELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEeESQKLNLL 912
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 370 RITTLEKRYLAAQREATSVHDLNDKLESEIANKDAVHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVA 449
Cdd:pfam02463 913 EEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNK 992
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2076569066 450 ALSKAEErhgNIEERLRQMEAQLEEKNQELQRARqreKMSEEHSKRLSDTVDRLLSESGERLRLHLKE 517
Cdd:pfam02463 993 DELEKER---LEEEKKKLIRAIIEETCQRLKEFL---ELFVSINKGWNKVFFYLELGGSAELRLEDPD 1054
|
|
| SAM_2 |
pfam07647 |
SAM domain (Sterile alpha motif); |
1366-1436 |
1.07e-04 |
|
SAM domain (Sterile alpha motif);
Pssm-ID: 429573 Cd Length: 66 Bit Score: 42.64 E-value: 1.07e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2076569066 1366 VLVWSNDRVIRWVLSIGLREYAGNLAESGVHGALIALDETFDFsalalLLQIPTQNTQARAVLEREFNSLL 1436
Cdd:pfam07647 1 VESWSLESVADWLRSIGLEQYTDNFRDQGITGAELLLRLTLED-----LKRLGITSVGHRRKILKKIQELK 66
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
329-506 |
1.18e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 47.85 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 329 VAELEEDLDTARKDLIKseEVNSRLQRDVREAMAQKEDMEERITTLEKRYLaaQREATsvhdLNDKLESeiankdavhrq 408
Cdd:PRK12704 44 LEEAKKEAEAIKKEALL--EAKEEIHKLRNEFEKELRERRNELQKLEKRLL--QKEEN----LDRKLEL----------- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 409 TEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQ---RVAALSKAEERhgniEERLRQMEAQLEEKNQELqrARQR 485
Cdd:PRK12704 105 LEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQeleRISGLTAEEAK----EILLEKVEEEARHEAAVL--IKEI 178
|
170 180
....*....|....*....|....*.
gi 2076569066 486 EKMSEEHSKR-----LSDTVDRLLSE 506
Cdd:PRK12704 179 EEEAKEEADKkakeiLAQAIQRCAAD 204
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
298-564 |
1.55e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 47.59 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 298 LAKVLElqevVDRQAREHCQMKERLATLSGHVAeleeDLDTARKDLikseevnSRLQRDVREAMAQKEDMEERITTLEKR 377
Cdd:PRK01156 155 LDEILE----INSLERNYDKLKDVIDMLRAEIS----NIDYLEEKL-------KSSNLELENIKKQIADDEKSHSITLKE 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 378 YLAAQREATSVHDLNDKLESEIANKDAvhrQTEDKNRqLQERLELAEQKLQQTLRKAETLPEVEAELAQRV--AALSKAE 455
Cdd:PRK01156 220 IERLSIEYNNAMDDYNNLKSALNELSS---LEDMKNR-YESEIKTAESDLSMELEKNNYYKELEERHMKIIndPVYKNRN 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 456 ERHG---------NIEERLRQMEAQLEEKNQELQRARQREKMSEEH--SKRLSDTVDRLLSEsgerlrlhLKERTaalED 524
Cdd:PRK01156 296 YINDyfkykndieNKKQILSNIDAEINKYHAIIKKLSVLQKDYNDYikKKSRYDDLNNQILE--------LEGYE---MD 364
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 2076569066 525 KNALLREVGDAKKQLEETQRDKDQL-----------VLNVEALRAELDQVR 564
Cdd:PRK01156 365 YNSYLKSIESLKKKIEEYSKNIERMsafiseilkiqEIDPDAIKKELNEIN 415
|
|
| CAGE1 |
pfam15066 |
Cancer-associated gene protein 1 family; CAGE-1 is a family of proteins overexpressed in ... |
287-549 |
1.55e-04 |
|
Cancer-associated gene protein 1 family; CAGE-1 is a family of proteins overexpressed in tumour tissues compared with surrounding tissues. CAGE-1 gene showed testis-specific expression among normal tissues and displayed wide expression in a variety of cancer cell lines and cancer tissues. CAGE-1 is predominantly expressed during post-meiotic stages. It localizes to the acrosomal matrix and acrosomal granule showing it to be a component of the acrosome of mammalian spermatids and spermatozoa.
Pssm-ID: 464481 Cd Length: 528 Bit Score: 47.14 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 287 SPDGSLSH-EEDLAKVLELQEVV-----------DRQAREHCQMKERLATLSGhVAELEEDLDTarkdliksEEVNSRLQ 354
Cdd:pfam15066 254 IPEMSVSHqKEVTEEGVESPEIAstwspagiswsSGASQENCKTPDTEQSFES-LQPLEEDMAL--------NEVLQKLK 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 355 RDVREAMAQKEDMEERITTLEKRYLAAQREATSVH---DLNDKL----ESEIANKDAVHRQTEDKNRQLQ---ERLELAE 424
Cdd:pfam15066 325 HTNRKQQMQIQDLQCSNLYLEKKVKELQMKITKQQvfvDIINKLkenvEELIEDKYNVILEKNDINKTLQnlqEILANTQ 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 425 QKLQQTLRKAETLpevEAELAQRVAALSKAEERHGN-IEERLR------QMEAQLEEKNQELQRARQrekMSEEHSKRLS 497
Cdd:pfam15066 405 KHLQESRKEKETL---QLELKKIKVNYVHLQERYITeMQQKNKsvsqclEMDKTLSKKEEEVERLQQ---LKGELEKATT 478
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 2076569066 498 DTVDRLLSESGERLR--LHLKERTAALEDKNallrevgdakkqLEETQRDKDQL 549
Cdd:pfam15066 479 SALDLLKREKETREQefLSLQEEFQKHEKEN------------LEERQKLKSRL 520
|
|
| Nuf2_DHR10-like |
pfam18595 |
Nuf2, DHR10-like domain; This domain is found at the C-terminal region of Nuf2 proteins. This ... |
328-451 |
1.72e-04 |
|
Nuf2, DHR10-like domain; This domain is found at the C-terminal region of Nuf2 proteins. This domain was identified as MazG related domain also designated as Designed helical repeat protein 10 (DHR10) that actually adopts a coiled-coil structure. Nuf2 is part of the Ndc80 complex, which binds to the spindle and is required for chromosome segregation and spindle checkpoint activity.
Pssm-ID: 465814 [Multi-domain] Cd Length: 117 Bit Score: 43.73 E-value: 1.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 328 HVAELEEdldTARkDLIKSEEVNSRLQRDVREAMAQKEDMEERITTLEKrylaAQREATSVHDLNDKLESEiankdavHR 407
Cdd:pfam18595 10 ELAELER---KAR-ELQAKIDALQVVEKDLRSCIKLLEEIEAELAKLEE----AKKKLKELRDALEEKEIE-------LR 74
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 2076569066 408 QTEDKNRQLQERLELAEQKLQQTLRKAEtlpEVEAELAQRVAAL 451
Cdd:pfam18595 75 ELERREERLQRQLENAQEKLERLREQAE---EKREAAQARLEEL 115
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
66-564 |
1.89e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 47.37 E-value: 1.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 66 LEERDRLMDTLRETQETLALTQGKLHEvgHERDSLQRQLSTaLPQEFAALTKELSvcreqllereeeiaELKAERNNTRL 145
Cdd:TIGR02169 210 AERYQALLKEKREYEGYELLKEKEALE--RQKEAIERQLAS-LEEELEKLTEEIS--------------ELEKRLEEIEQ 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 146 LLEHLECLVSRhERSLRMTVVKRQAQSpagVSSEVEVLK-ALKSLFEHHKALDEKVR---ERLRVALERCSLLEEELGVT 221
Cdd:TIGR02169 273 LLEELNKKIKD-LGEEEQLRVKEKIGE---LEAEIASLErSIAEKERELEDAEERLAkleAEIDKLLAEIEELEREIEEE 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 222 HKEMGRWTFTVSKRLRRARTARQvppllphaSASAEGAPGAVSRQtparrpcRSGSPRAGLRLQRSPDGSLSHEEDlakv 301
Cdd:TIGR02169 349 RKRRDKLTEEYAELKEELEDLRA--------ELEEVDKEFAETRD-------ELKDYREKLEKLKREINELKRELD---- 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 302 lELQEVVDRQAREHCQMKERLATLSGHVAELEEDLDTARKDLIKSEEVNSRLQRDVREAMAQKEDMEERITTLEKRYLAA 381
Cdd:TIGR02169 410 -RLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKL 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 382 QREATSVHDLNDKLESEIANKDAVHRQTEDKN-------RQL------------------------------QERLELAE 424
Cdd:TIGR02169 489 QRELAEAEAQARASEERVRGGRAVEEVLKASIqgvhgtvAQLgsvgeryataievaagnrlnnvvveddavaKEAIELLK 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 425 Q------------KLQQTLRKAETL----------------PEVEA---------------ELAQRVA------------ 449
Cdd:TIGR02169 569 RrkagratflplnKMRDERRDLSILsedgvigfavdlvefdPKYEPafkyvfgdtlvvediEAARRLMgkyrmvtlegel 648
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 450 ------------ALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMSEEHSKRLSDtvdrLLSESGERLRLHLKE 517
Cdd:TIGR02169 649 feksgamtggsrAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQ----ELSDASRKIGEIEKE 724
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 2076569066 518 RTAALEDKNALLREVGDAKKQLEETQRDKdqlvlnvEALRAELDQVR 564
Cdd:TIGR02169 725 IEQLEQEEEKLKERLEELEEDLSSLEQEI-------ENVKSELKELE 764
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
1541-2099 |
1.91e-04 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 47.56 E-value: 1.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 1541 WAAGRAPGLTWVCagglaLGLLLPALPSLSPSCPAPAPAIARARSEEALSPTGRGPSQVLGRGSQRPAGRCGAAARPALG 1620
Cdd:COG3321 841 WVAGVPVDWSALY-----PGRGRRRVPLPTYPFQREDAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAA 915
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 1621 SRCWMAPAALEKGPLPGSRPGGVSRQTLTPRALGSLGTLVTLRAAPARPcscRAGQRGASVGPVGAGGAFPEGVQVVLPG 1700
Cdd:COG3321 916 AAALALAAAALAALLALVALAAAAAALLALAAAAAAAAAALAAAEAGAL---LLLAAAAAAAAAAAAAAAAAAAAAAAAA 992
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 1701 RSANLTFSSAEVRLGVSASCSVPACERRGRGEAVRSRARRPGQGRRWEGAAPGPPSALLGLEDARSAPPAGRGRALAGCT 1780
Cdd:COG3321 993 AAALAAAAALALLAAAALLLAAAAAAAALLALAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLA 1072
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 1781 LPRAGLSIPTPAHVHARPGHAPGSLPSAGRSPRAPEGPPPPSWQGPRPGLPRLVAPEIARRRGVDAAPRPPQPLGRAPGP 1860
Cdd:COG3321 1073 ALAELALAAAALALAAALAAAALALALAALAAALLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALAL 1152
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 1861 GGRGQecvsdnAACRARRGWILRRSGLTPAEAPGRQGRLARAQLGLVTLWPPARTRRCPVSRLLGEcscscfFREPEQPL 1940
Cdd:COG3321 1153 AAAAA------ALAAALAAALLAAAALLLALALALAAALAAALAGLAALLLAALLAALLAALLALA------LAALAAAA 1220
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 1941 VRRLLVSVPGPAAGGRTWPSSALAGCPLLPLGAWGTRWARRQAGPRTAPPGQAANWFSGSCGRGLPRGPAGCPCLTPGWD 2020
Cdd:COG3321 1221 AALLAAAAAAAALALLALAAAAAAVAALAAAAAALLAALAALALLAAAAGLAALAAAAAAAAAALALAAAAAAAAAALAA 1300
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2076569066 2021 GSEALFARGCGRRGAACAHVRRASRAASSWPVRASAEHAGGRGSRGHRASGQGWPETDRAAPLAAYPHYFYRAALGAQR 2099
Cdd:COG3321 1301 LLAAAAAAAAAAAAAAAAAALAAALLAAALAALAAAVAAALALAAAAAAAAAAAAAAAAAAALAAAAGAAAAAAALALA 1379
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
194-543 |
2.23e-04 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 46.95 E-value: 2.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 194 KALDEKVRERLRVALERCSLLEEELGVTHKEmgrWTFTVSKRLRRARTARQVppllphASASAEgAPGAVSRQT------ 267
Cdd:pfam05701 123 KAQLEVAKARHAAAVAELKSVKEELESLRKE---YASLVSERDIAIKRAEEA------VSASKE-IEKTVEELTieliat 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 268 -----PARRPCRSGSP-RAGLRLQRSPDgSLSHEEDLAKVLELQEVVDRQAREHCQMKERLATLSGHVAELEEDL----D 337
Cdd:pfam05701 193 kesleSAHAAHLEAEEhRIGAALAREQD-KLNWEKELKQAEEELQRLNQQLLSAKDLKSKLETASALLLDLKAELaaymE 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 338 TARKDLIKSEEVNSRLQRDVREAMAQ-KEDMEERITTLEKrylaAQREATSVHDLNDKLESEIANkdavhrqtedknrql 416
Cdd:pfam05701 272 SKLKEEADGEGNEKKTSTSIQAALASaKKELEEVKANIEK----AKDEVNCLRVAAASLRSELEK--------------- 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 417 qERLELAEqkLQQTLRKAE-TLPEVEAELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMSEEH--- 492
Cdd:pfam05701 333 -EKAELAS--LRQREGMASiAVSSLEAELNRTKSEIALVQAKEKEAREKMVELPKQLQQAAQEAEEAKSLAQAAREElrk 409
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 2076569066 493 SKRLSDTVDRLLSESGERLRLHLKERTAALEDKNALLrevgDAKKQLEETQ 543
Cdd:pfam05701 410 AKEEAEQAKAAASTVESRLEAVLKEIEAAKASEKLAL----AAIKALQESE 456
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
294-565 |
2.32e-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: 47.27 E-value: 2.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 294 HEEDLAK----VLELQEVVDRQAREHCQMKERLATLSGHVAELEEDLDTARKDLIKSEEVNSRLQRDVREAMAQKEDMEE 369
Cdd:pfam02463 319 SEKEKKKaekeLKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELE 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 370 RITTLEKRYLAAQREATSVHDLNDKLESEIANKDAV--HRQTEDKNRQLQERLELaeqklqQTLRKAETLPEVEAELAQR 447
Cdd:pfam02463 399 LKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEeeESIELKQGKLTEEKEEL------EKQELKLLKDELELKKSED 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 448 VAALSKAEERHGNIEERLRqmEAQLEEKNQELQRARQREKMSEEHSKRLsdTVDRLLSESGERLRLHLKERTAALEDKNA 527
Cdd:pfam02463 473 LLKETQLVKLQEQLELLLS--RQKLEERSQKESKARSGLKVLLALIKDG--VGGRIISAHGRLGDLGVAVENYKVAISTA 548
|
250 260 270
....*....|....*....|....*....|....*...
gi 2076569066 528 LLREVGDAKKQLEETQRdkdqLVLNVEALRAELDQVRL 565
Cdd:pfam02463 549 VIVEVSATADEVEERQK----LVRALTELPLGARKLRL 582
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
370-564 |
2.71e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 46.43 E-value: 2.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 370 RITTLEKRYLAAQREATSVHDL----NDKLESEIANKDAVHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPE------ 439
Cdd:pfam07888 28 RAELLQNRLEECLQERAELLQAqeaaNRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEkykels 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 440 -VEAELAQRVAALSKAEERHgniEERLRQME-------AQLEEKNQELQRARQREKMS-----EEHSKRLSDTVDRLLSE 506
Cdd:pfam07888 108 aSSEELSEEKDALLAQRAAH---EARIRELEediktltQRVLERETELERMKERAKKAgaqrkEEEAERKQLQAKLQQTE 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2076569066 507 SGER-LRLHLKERTAALEDKNALLREVGDAKKQLEETQRDKDQLVLNVEALRAELDQVR 564
Cdd:pfam07888 185 EELRsLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQ 243
|
|
| SAM_STIM-1,2-like |
cd09504 |
SAM domain of STIM-1,2-like proteins; SAM (sterile alpha motif) domain of STIM-1,2-like ... |
1161-1219 |
2.83e-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: 41.55 E-value: 2.83e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2076569066 1161 WDGPTVVVWLELWVGMPAwYVAACRANVKSGAIMSALSDTE---IQREIGISNPLHRLKLRL 1219
Cdd:cd09504 5 WTVEDTVEWLVNSVELPQ-YVEAFKENGVDGSALPRLAVNNpsfLTSVLGIKDPIHRQKLSL 65
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
392-496 |
2.87e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 46.74 E-value: 2.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 392 NDKLESEIANKDAVHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRV-----AALSKAEERHGNIEERLR 466
Cdd:PRK00409 515 KEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAekeaqQAIKEAKKEADEIIKELR 594
|
90 100 110
....*....|....*....|....*....|...
gi 2076569066 467 QMEAQL--EEKNQELQRARQR-EKMSEEHSKRL 496
Cdd:PRK00409 595 QLQKGGyaSVKAHELIEARKRlNKANEKKEKKK 627
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
235-513 |
2.95e-04 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 46.40 E-value: 2.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 235 RLRRARTA--RQVPPLLPHASASAEGAPGAvSRQTPARRPCRSGSPRAGLRLQRSPDGSLSHEEDLAKvlELQEVVDRQA 312
Cdd:pfam02029 11 RRRRAREErrRQKEEEEPSGQVTESVEPNE-HNSYEEDSELKPSGQGGLDEEEAFLDRTAKREERRQK--RLQEALERQK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 313 REH---CQMKERLATLSGHVaELEEDLDTARKDLIKSE--------------EVNSRLQRDVREAMAQKEDMEERITTLE 375
Cdd:pfam02029 88 EFDptiADEKESVAERKENN-EEEENSSWEKEEKRDSRlgrykeeeteirekEYQENKWSTEVRQAEEEGEEEEDKSEEA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 376 KRYLAAQREATSVHDLNDKLESEIANKDAVHRQ-----TEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAA 450
Cdd:pfam02029 167 EEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDqkrghPEVKSQNGEEEVTKLKVTTKRRQGGLSQSQEREEEAEVFLEA 246
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2076569066 451 LSKAEE---RHGNIEE------RLRQMEAQLEEKNQELQRARQREKMSEEHSKRLSDTVDRLLSESGERLRL 513
Cdd:pfam02029 247 EQKLEElrrRRQEKESeefeklRQKQQEAELELEELKKKREERRKLLEEEEQRRKQEEAERKLREEEEKRRM 318
|
|
| SHE3 |
pfam17078 |
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an ... |
374-561 |
3.29e-04 |
|
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an RNA-binding protein that binds specific mRNAs, including the mRNA of Ash1, which is invalid in cell-fate determination. She3 acts as an adapter protein that docks the myosin motor Myo4p onto an Ash1-She2p ribonucleoprotein complex. She3 seems to bind to Myo4p and Shep2p via different domains.
Pssm-ID: 293683 [Multi-domain] Cd Length: 228 Bit Score: 44.73 E-value: 3.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 374 LEKRYLAAQREATSVHDL------NDKLESEIANKDAVHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELaqr 447
Cdd:pfam17078 30 LSKLEIAQQKESKFLENLaslkheNDNLSSMLNRKERRLKDLEDQLSELKNSYEELTESNKQLKKRLENSSASETTL--- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 448 vaalskaeerhgniEERLRQMEAQ----LEEKNqelqraRQREKMSEEHSKrLSDTVDRLLSESGERLRLHLKERTAALE 523
Cdd:pfam17078 107 --------------EAELERLQIQydalVDSQN------EYKDHYQQEINT-LQESLEDLKLENEKQLENYQQRISSNDK 165
|
170 180 190
....*....|....*....|....*....|....*....
gi 2076569066 524 DKNALLREVGDAKKQLEETQRDKDQLVLN-VEALRAELD 561
Cdd:pfam17078 166 DIDTKLDSYNNKFKNLDNIYVNKNNKLLTkLDSLAQLLD 204
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
77-565 |
3.81e-04 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 46.28 E-value: 3.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 77 RETQETLALTQGKLHEV--GHER---------DSLQRQLSTaLPQEFAALTKELSVCREQLLEREEEIAELKAERNNTRL 145
Cdd:pfam07111 140 RELEEIQRLHQEQLSSLtqAHEEalssltskaEGLEKSLNS-LETKRAGEAKQLAEAQKEAELLRKQLSKTQEELEAQVT 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 146 LLEHLECLVSRH------------ERSLRMTVVKRQAQSPAGVSSEVEVLKALKSLFEHHKALDEkvrERLRVALERCSL 213
Cdd:pfam07111 219 LVESLRKYVGEQvppevhsqtwelERQELLDTMQHLQEDRADLQATVELLQVRVQSLTHMLALQE---EELTRKIQPSDS 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 214 LEEELGVTHKEM-GRW-----TFTVSKRLRRARTARQVPPLLPHASASAEGAPGAVSRQTPARRPCRSGSprAGLRLQRS 287
Cdd:pfam07111 296 LEPEFPKKCRSLlNRWrekvfALMVQLKAQDLEHRDSVKQLRGQVAELQEQVTSQSQEQAILQRALQDKA--AEVEVERM 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 288 PDGSLSHEEDLAkvlelQEVVDRQAREHCQMKERLATLSGHVAELEEDLDTARKDLIKS----EEVNSRLQRDVREAMAQ 363
Cdd:pfam07111 374 SAKGLQMELSRA-----QEARRRQQQQTASAEEQLKFVVNAMSSTQIWLETTMTRVEQAvariPSLSNRLSYAVRKVHTI 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 364 KEDMEERITTLEKRY-------------------LAAQREATSVHDLNDKLESEIANKDA--VHRQTEDKNRQLQERLEL 422
Cdd:pfam07111 449 KGLMARKVALAQLRQescpppppappvdadlsleLEQLREERNRLDAELQLSAHLIQQEVgrAREQGEAERQQLSEVAQQ 528
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 423 AEQKLQQTlrkAETLPEVEAELAQRVAALSKAEERHGNIEERLRQME----AQLEEKNQELQrARQREKMSEehSKRLSD 498
Cdd:pfam07111 529 LEQELQRA---QESLASVGQQLEVARQGQQESTEEAASLRQELTQQQeiygQALQEKVAEVE-TRLREQLSD--TKRRLN 602
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2076569066 499 TVDRLLSESGERLRlHLKERTAALEDKNALLREVGD-AKKQ--------LEETQRDKDQLV--LNVEALRAELDQVRL 565
Cdd:pfam07111 603 EARREQAKAVVSLR-QIQHRATQEKERNQELRRLQDeARKEegqrlarrVQELERDKNLMLatLQQEGLLSRYKQQRL 679
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
331-530 |
3.90e-04 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 45.26 E-value: 3.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 331 ELEEDLDTARKDLIK-----SEEVNSRLQRDVREAMAQK----------------EDMEErittLEKRYLAAQR---EAT 386
Cdd:cd16269 94 KLMEQLEEKKEEFCKqneeaSSKRCQALLQELSAPLEEKisqgsysvpggyqlylEDREK----LVEKYRQVPRkgvKAE 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 387 SVhdLNDKLESeianKDAVHR---QTeDKNRQLQERlELAEQKLQQTLRKAET--LPEVEAELAQRVaalsKAEERhgNI 461
Cdd:cd16269 170 EV--LQEFLQS----KEAEAEailQA-DQALTEKEK-EIEAERAKAEAAEQERklLEEQQRELEQKL----EDQER--SY 235
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2076569066 462 EERLRQMEAQLEEKnqelqrarqREKMSEEHSKRLsdtvDRLLSESGERLRLHLKERTAALEDKNALLR 530
Cdd:cd16269 236 EEHLRQLKEKMEEE---------RENLLKEQERAL----ESKLKEQEALLEEGFKEQAELLQEEIRSLK 291
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
2271-2473 |
4.74e-04 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 46.02 E-value: 4.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 2271 PVKALGMAVIVLESDAAVPSACAQVSGRSRASSRERSRVPAALRAHRR---PRGPAEAAVAGGQPRRGRQCPPTSRALPA 2347
Cdd:PRK12323 374 PATAAAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAapaRRSPAPEALAAARQASARGPGGAPAPAPA 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 2348 SLPGPelradslagKRARRRRTAGPRNRLRAHWRPLASPSRRGHPCPGPEVPCPGPEAP--CAAPARASQGTARTAWGPR 2425
Cdd:PRK12323 454 PAAAP---------AAAARPAAAGPRPVAAAAAAAPARAAPAAAPAPADDDPPPWEELPpeFASPAPAQPDAAPAGWVAE 524
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2076569066 2426 LGPSVPPTPPSAFCLARASGAGTSGPRSAASACLLRQACGPACLNKAG 2473
Cdd:PRK12323 525 SIPDPATADPDDAFETLAPAPAAAPAPRAAAATEPVVAPRPPRASASG 572
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
331-524 |
4.99e-04 |
|
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.
Pssm-ID: 460721 [Multi-domain] Cd Length: 297 Bit Score: 44.97 E-value: 4.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 331 ELEEDLDTARKDLIKSEEVNSRLQRdvrEAMAQK--EDMEERIttlekrylaaQREATSV---HDLNDKLESEIANKdav 405
Cdd:pfam02841 100 ELVELLEAKKDDFLKQNEEASSKYC---SALLQDlsEPLEEKI----------SQGTFSKpggYKLFLEERDKLEAK--- 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 406 HRQTEDKNRQ----LQERLE----LAEQKLQ--QTLRKAETLPEVEAElaqRVAALSKAEERhgnIEERLRQMEAQLE-- 473
Cdd:pfam02841 164 YNQVPRKGVKaeevLQEFLQskeaVEEAILQtdQALTAKEKAIEAERA---KAEAAEAEQEL---LREKQKEEEQMMEaq 237
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2076569066 474 EKNQELQRARQREKMSEEHSKRLSD---TVDRLLSESGERLRLHLKERTAALED 524
Cdd:pfam02841 238 ERSYQEHVKQLIEKMEAEREQLLAEqerMLEHKLQEQEELLKEGFKTEAESLQK 291
|
|
| BAR_SNX |
cd07596 |
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid ... |
403-564 |
5.02e-04 |
|
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.
Pssm-ID: 153280 [Multi-domain] Cd Length: 218 Bit Score: 44.27 E-value: 5.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 403 DAVHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKAEErhgNIEERLRQMEAQLEEKNQELqrA 482
Cdd:cd07596 3 DQEFEEAKDYILKLEEQLKKLSKQAQRLVKRRRELGSALGEFGKALIKLAKCEE---EVGGELGEALSKLGKAAEEL--S 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 483 RQREKMSEEHSKRLSDTVDRLLSESGErLRLHLKERTAALEDKNALLREVGDAKKQLEETQRDKDQLVLNVEALRAELDQ 562
Cdd:cd07596 78 SLSEAQANQELVKLLEPLKEYLRYCQA-VKETLDDRADALLTLQSLKKDLASKKAQLEKLKAAPGIKPAKVEELEEELEE 156
|
..
gi 2076569066 563 VR 564
Cdd:cd07596 157 AE 158
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
413-565 |
5.31e-04 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 45.04 E-value: 5.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 413 NRQLQERLELAEQKLQQtlrkaetlpeVEAELAqRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQrekmseeh 492
Cdd:COG1566 78 PTDLQAALAQAEAQLAA----------AEAQLA-RLEAELGAEAEIAAAEAQLAAAQAQLDLAQRELERYQA-------- 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 493 skrlsdtvdrlLSESG-------ERLRLHLKERTAALEdknALLREVGDAKKQLEEtQRDKDQLVLNVEALRAELDQVRL 565
Cdd:COG1566 139 -----------LYKKGavsqqelDEARAALDAAQAQLE---AAQAQLAQAQAGLRE-EEELAAAQAQVAQAEAALAQAEL 203
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
294-550 |
5.68e-04 |
|
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: 45.81 E-value: 5.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 294 HEED----LAKVLELQEVVDR--QAREHCQMKERL----ATLSGHVAELEEDLDTARKDLIKSEEVNSRL-QRDVREAMA 362
Cdd:TIGR00606 157 HQEDsnwpLSEGKALKQKFDEifSATRYIKALETLrqvrQTQGQKVQEHQMELKYLKQYKEKACEIRDQItSKEAQLESS 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 363 QK--EDMEERITTLEKRYLAAQREATSVHdlndKLESEIANKDAVHRQTEDKNRQLQERLELAEQKLQQTLRKAEtlpev 440
Cdd:TIGR00606 237 REivKSYENELDPLKNRLKEIEHNLSKIM----KLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLY----- 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 441 eaELAQRvaalskaEERhgNIEERLRQMEAQLEEKNQELQRARQREKMSEEHSKRLSDTVDR----LLSESGERLRLHLK 516
Cdd:TIGR00606 308 --HNHQR-------TVR--EKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRhqehIRARDSLIQSLATR 376
|
250 260 270
....*....|....*....|....*....|....
gi 2076569066 517 ERTAALEDKNALLREVGDAKKQLEETQRDKDQLV 550
Cdd:TIGR00606 377 LELDGFERGPFSERQIKNFHTLVIERQEDEAKTA 410
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
304-483 |
5.99e-04 |
|
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant proteins that are filament-like. It interacts with the nuclear envelope-associated protein, MAF1, the WPP family pfam13943.
Pssm-ID: 461778 [Multi-domain] Cd Length: 859 Bit Score: 45.82 E-value: 5.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 304 LQEVVDRQAREhcQMKERlatlsghvAELEEDLDTARKDLIKSEEVNSRLQRDVREamaqKEDM-----EER------IT 372
Cdd:pfam05911 72 IHDVVLKKTKE--WEKIK--------AELEAKLVETEQELLRAAAENDALSRSLQE----RENLlmklsEEKsqaeaeIE 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 373 TLEKRYLAAQREATS----VHDLNDKLEseIAN--KDAVHRQTEDKNRQLQE------RLElAE-QKLQQTLRKaeTLP- 438
Cdd:pfam05911 138 ALKSRLESCEKEINSlkyeLHVLSKELE--IRNeeKNMSRRSADAAHKQHLEsvkkiaKLE-AEcQRLRGLVRK--KLPg 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 439 ---------EVE------AELAQR---------------VAALSKAEERHGNIE---ERLRQMEAQ-------LEEKNQE 478
Cdd:pfam05911 213 paalaqmklEVEmlgrdsGETRLRrspvknssphlspdpDFSEDSLQTPHKENEfltERLLAMEEEtkmlkeaLAKRNSE 292
|
....*
gi 2076569066 479 LQRAR 483
Cdd:pfam05911 293 LQASR 297
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
314-561 |
5.99e-04 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 45.56 E-value: 5.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 314 EHCQMKERLATLSGHVAELEEDLDTARKdliKSEEVNSRLQ-------RDVREAMAQKEDMEERITTLeKRYLAAqreat 386
Cdd:PRK10246 284 SLAQPARQLRPHWERIQEQSAALAHTRQ---QIEEVNTRLQstmalraRIRHHAAKQSAELQAQQQSL-NTWLAE----- 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 387 svHDLNDKLESEIANKDAV-HRQTEDKN--RQLQERLELAEQKL------------------------QQTLRKA----- 434
Cdd:PRK10246 355 --HDRFRQWNNELAGWRAQfSQQTSDREqlRQWQQQLTHAEQKLnalpaitltltadevaaalaqhaeQRPLRQRlvalh 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 435 ETLPEVEAELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKmSEEHSKRLSDTVDRLlsESGERLRLH 514
Cdd:PRK10246 433 GQIVPQQKRLAQLQVAIQNVTQEQTQRNAALNEMRQRYKEKTQQLADVKTICE-QEARIKDLEAQRAQL--QAGQPCPLC 509
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 2076569066 515 LKERTAALEDKNALlrEVGDAKKQLEETQRDKDQLVLNVEALRAELD 561
Cdd:PRK10246 510 GSTSHPAVEAYQAL--EPGVNQSRLDALEKEVKKLGEEGAALRGQLD 554
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
375-569 |
6.79e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 45.72 E-value: 6.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 375 EKRYLAAQREAtsvhdlndkLESEIANKDAVHRQTEDKNRQLQErlelAEQKLQQTLRKAETLPEVEAELAQRVAALSKA 454
Cdd:PRK04863 507 EQRHLAEQLQQ---------LRMRLSELEQRLRQQQRAERLLAE----FCKRLGKNLDDEDELEQLQEELEARLESLSES 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 455 EERHGNIEERLRQMEAQLEEKNQELQRARQrekmsEEHSkrLSDTVDRLLSESGErlrlhlkertaALEDKNALLREVGD 534
Cdd:PRK04863 574 VSEARERRMALRQQLEQLQARIQRLAARAP-----AWLA--AQDALARLREQSGE-----------EFEDSQDVTEYMQQ 635
|
170 180 190
....*....|....*....|....*....|....*
gi 2076569066 535 AKKQLEETQRDKDQLVLNVEALRAELDqvRLGGPS 569
Cdd:PRK04863 636 LLERERELTVERDELAARKQALDEEIE--RLSQPG 668
|
|
| SAM_1 |
pfam00536 |
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ... |
1160-1222 |
7.05e-04 |
|
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily conserved protein binding domain that is involved in the regulation of numerous developmental processes in diverse eukaryotes. The SAM domain can potentially function as a protein interaction module through its ability to homo- and heterooligomerise with other SAM domains.
Pssm-ID: 425739 Cd Length: 64 Bit Score: 40.33 E-value: 7.05e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2076569066 1160 QWDGPTVVVWLElWVGMPAwYVAACRANVKSGAIMSALSDTEIqREIGISNPLHRLKLRLAIQ 1222
Cdd:pfam00536 2 GWSVEDVGEWLE-SIGLGQ-YIDSFRAGYIDGDALLQLTEDDL-LKLGVTLLGHRKKILYAIQ 61
|
|
| SAM_SARM1-like_repeat1 |
cd09501 |
SAM domain ot SARM1-like proteins, repeat 1; SAM (sterile alpha motif) domain repeat 1 of ... |
1292-1339 |
7.12e-04 |
|
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: 40.36 E-value: 7.12e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 2076569066 1292 EWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRGQLKMVDSFHRNSF 1339
Cdd:cd09501 11 TWLKQIGFEDYAEKFSESQVDGDLLLQLTEDELKQDLGMSSGLLRKRF 58
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
2314-2721 |
7.13e-04 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 45.36 E-value: 7.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 2314 RAHRRPRGPAEAAVAGGQPRRGRQCPPtsralPASLPGPELRADSLAGKRARRRRTAGPRnrlrahwrPLASPSRRGHPC 2393
Cdd:PRK07764 380 RLERRLGVAGGAGAPAAAAPSAAAAAP-----AAAPAPAAAAPAAAAAPAPAAAPQPAPA--------PAPAPAPPSPAG 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 2394 PGPEVPCPGPEAPCAAPAR-ASQGTARTAWGPRLGPSVPPTPPSAFCLARASGAGTSGPRSAASAclLRQACgPACLNKA 2472
Cdd:PRK07764 447 NAPAGGAPSPPPAAAPSAQpAPAPAAAPEPTAAPAPAPPAAPAPAAAPAAPAAPAAPAGADDAAT--LRERW-PEILAAV 523
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 2473 G----VGFRLLLRCVSVL---RGVAWVDFPSTGRACR----------PRILRVVAGRCCADLWTVA----ATSPASSPRA 2531
Cdd:PRK07764 524 PkrsrKTWAILLPEATVLgvrGDTLVLGFSTGGLARRfaspgnaevlVTALAEELGGDWQVEAVVGpapgAAGGEGPPAP 603
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 2532 LSSVSCSYHVDIVEQTRLPQDAQDGGAGRPlSQGSRLSAASAEEGAWSPGQSQMGVLAKAARGARPAVAAVTQPQGAAWA 2611
Cdd:PRK07764 604 ASSGPPEEAARPAAPAAPAAPAAPAPAGAA-AAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPP 682
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 2612 GGCQGWGWAERAVRRliPPALFPRPSRVGPSGRWTPAQPLERADGAANeptwtSQPHAHEEKTKCRPSPPGPGPGPPGPR 2691
Cdd:PRK07764 683 PAPAPAAPAAPAGAA--PAQPAPAPAATPPAGQADDPAAQPPQAAQGA-----SAPSPAADDPVPLPPEPDDPPDPAGAP 755
|
410 420 430
....*....|....*....|....*....|
gi 2076569066 2692 APAPLERHPLRPADTGEHLPEAQWEGRPAA 2721
Cdd:PRK07764 756 AQPPPPPAPAPAAAPAAAPPPSPPSEEEEM 785
|
|
| MLKL_NTD |
cd21037 |
N-terminal domain of mixed lineage kinase domain-like protein (MLKL) and similar proteins; ... |
301-428 |
7.86e-04 |
|
N-terminal domain of mixed lineage kinase domain-like protein (MLKL) and similar proteins; MLKL is a pseudokinase that does not have protein kinase activity and plays a key role in tumor necrosis factor (TNF)-induced necroptosis, a programmed cell death process. The model corresponds to the MLKL N-terminal region that reveals a four-helix bundle with an additional helix at the top which is likely key for MLKL function. The N-terminal domain binds directly to phospholipids and induces membrane permeabilization.
Pssm-ID: 411030 [Multi-domain] Cd Length: 138 Bit Score: 42.35 E-value: 7.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 301 VLELQEVVDrQAREHcqmKERLATLSGHVAELEEDLDTARKDliKSEEVNSRLQRDVREAMAQKEDMEERITTLE----- 375
Cdd:cd21037 7 ALEILEAVE-TVKSN---KEACRRLAERVAELLLALEELLEG--KEEDLSPELREALEELERTLEEIKEFVEKISkrsrl 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 2076569066 376 KRYLAAQREATSVHDLNDKLES-----EIANKDAVHRQTEDKNRQLQERLELAEQKLQ 428
Cdd:cd21037 81 KRFLKAKSIAEKLEELNERLDDalqlfQLALQIEIRAWLLEDLEEIREDLEELLERLE 138
|
|
| KASH_CCD |
pfam14662 |
Coiled-coil region of CCDC155 or KASH; This coiled-coil region is found in the central part of ... |
284-479 |
7.95e-04 |
|
Coiled-coil region of CCDC155 or KASH; This coiled-coil region is found in the central part of KASH or Klarsicht/ANC-1/Syne/homology proteins. KASH are a meiosis-specific proteins that localize at telomeres and interact with SUN1, thus being implicated in meiotic chromosome dynamics and homolog pairing.
Pssm-ID: 405365 [Multi-domain] Cd Length: 191 Bit Score: 43.24 E-value: 7.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 284 LQRSPDGSlshEEDLAKVLELQEVVDRQARE--HCQMKERLatlsghvaeLEEDLDTARKDLIKSEEVNSRLQRDVREAM 361
Cdd:pfam14662 27 LKATVETR---EETNAKLLEENLNLRKQAKSqqQAVQKEKL---------LEEELEDLKLIVNSLEEARRSLLAQNKQLE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 362 AQKEDMEERITTLEKRYLAAQREatsvhdlNDKLESEianKDAVHRQTEDKNRQLQERLELA---EQKLQQTLRKAEtlp 438
Cdd:pfam14662 95 KENQSLLQEIESLQEENKKNQAE-------RDKLQKK---KKELLKSKACLKEQLHSCEDLAcnrETILIEKTTQIE--- 161
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2076569066 439 eveaELAQRVaalskaeERHGNIEERLRQMEAQLEEKNQEL 479
Cdd:pfam14662 162 ----ELKSTV-------EEYSSIEEELRAEKSRLESQLPDM 191
|
|
| Sipho_Gp157 |
pfam05565 |
Siphovirus Gp157; This family contains both viral and bacterial proteins which are related to ... |
410-574 |
7.95e-04 |
|
Siphovirus Gp157; This family contains both viral and bacterial proteins which are related to the Gp157 protein of the Streptococcus thermophilus SFi bacteriophages. It is thought that bacteria possessing the gene coding for this protein have an increased resistance to the bacteriophage.
Pssm-ID: 398934 Cd Length: 162 Bit Score: 42.63 E-value: 7.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 410 EDKNRQLQERLELAEQKLQQTLrkAETLPEVEAELAqrvaalSKAEerhgNIEERLRQMEAQLEEKNQELQRARQREKMS 489
Cdd:pfam05565 6 TDQYLQLLELLEELDVDLPEEI--ADTLESLEGEFE------EKAE----NIAKVIKNLEADAEAIKAEEKRLAERKKAA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 490 EEHSKRLSDTVDRLLSESG------ERLRLHLKertaaledKNALLREVGDAKKQLEETQRDKDQLVLNVEALRAEL-DQ 562
Cdd:pfam05565 74 ENRAKRLKEYLLRNMEATGkkkiktPLFTLSIR--------KNPPSVVIDDEEKIPAEYMTPQVPKKPDKKAIKKALkAG 145
|
170
....*....|..
gi 2076569066 563 VRLGGPSLHHGR 574
Cdd:pfam05565 146 EEVPGAELEQGE 157
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
331-486 |
9.26e-04 |
|
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.
Pssm-ID: 460721 [Multi-domain] Cd Length: 297 Bit Score: 44.20 E-value: 9.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 331 ELEEDLDTARKDLIKSEEVnsrLQRDVREamaqKEDMEERITTLEK--------------RYLAAQREATSvhdLNDKLE 396
Cdd:pfam02841 159 KLEAKYNQVPRKGVKAEEV---LQEFLQS----KEAVEEAILQTDQaltakekaieaeraKAEAAEAEQEL---LREKQK 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 397 SEIANKDAVHRQTEDKNRQLQERLELAEQKLQQTLRKAetlpeveaelaqrvaalskaeerhgnIEERLRQMEAQLEEKN 476
Cdd:pfam02841 229 EEEQMMEAQERSYQEHVKQLIEKMEAEREQLLAEQERM--------------------------LEHKLQEQEELLKEGF 282
|
170
....*....|
gi 2076569066 477 QELQRARQRE 486
Cdd:pfam02841 283 KTEAESLQKE 292
|
|
| PHA02682 |
PHA02682 |
ORF080 virion core protein; Provisional |
2337-2453 |
1.00e-03 |
|
ORF080 virion core protein; Provisional
Pssm-ID: 177464 [Multi-domain] Cd Length: 280 Bit Score: 44.08 E-value: 1.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 2337 QCPPTSRALPASLPGPELRADSLAgKRARRRRTAGPRNRLRAHWRPLASPSRRGHPCPGPEVPCPGPEAPCAAPARASQG 2416
Cdd:PHA02682 28 KCPQATIPAPAAPCPPDADVDPLD-KYSVKEAGRYYQSRLKANSACMQRPSGQSPLAPSPACAAPAPACPACAPAAPAPA 106
|
90 100 110
....*....|....*....|....*....|....*...
gi 2076569066 2417 TARTAWGPRLGPSVPPT-PPSAFCLARASGAGTSGPRS 2453
Cdd:PHA02682 107 VTCPAPAPACPPATAPTcPPPAVCPAPARPAPACPPST 144
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
208-564 |
1.09e-03 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 44.63 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 208 LERCSLLEEELGVTHKEMGRWtftvSKRLRRARTAR-QVPPLLPHASASAEGAPGAVSRQTPARRPCRSGSPRAGLRLQR 286
Cdd:pfam05701 34 VERRKLVELELEKVQEEIPEY----KKQSEAAEAAKaQVLEELESTKRLIEELKLNLERAQTEEAQAKQDSELAKLRVEE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 287 SPDGsLSHEEDLAKVLELQEVVDRQAREHCQM---KERLATLSGHVAELEEDLDTARKdliKSEEVNSRLQ---RDVREA 360
Cdd:pfam05701 110 MEQG-IADEASVAAKAQLEVAKARHAAAVAELksvKEELESLRKEYASLVSERDIAIK---RAEEAVSASKeieKTVEEL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 361 ----MAQKE----------DMEER----ITTLEKRYLAAQREATSVHD----LNDKLeseIANKDAVHRQTEDKNRQLQE 418
Cdd:pfam05701 186 tielIATKEslesahaahlEAEEHrigaALAREQDKLNWEKELKQAEEelqrLNQQL---LSAKDLKSKLETASALLLDL 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 419 RLELA---EQKLQQTLRKAETLPEVEAELAQRVAALSKA-EERHGNIE------ERLR----QMEAQLEEKNQELQRARQ 484
Cdd:pfam05701 263 KAELAaymESKLKEEADGEGNEKKTSTSIQAALASAKKElEEVKANIEkakdevNCLRvaaaSLRSELEKEKAELASLRQ 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 485 REKMSEEHSKRLSDTVDRLLSESGErlrLHLKERTAAledknallREVGDAKKQLEETQRDKDQLVLNVEALRAELDQVR 564
Cdd:pfam05701 343 REGMASIAVSSLEAELNRTKSEIAL---VQAKEKEAR--------EKMVELPKQLQQAAQEAEEAKSLAQAAREELRKAK 411
|
|
| Nuf2_DHR10-like |
pfam18595 |
Nuf2, DHR10-like domain; This domain is found at the C-terminal region of Nuf2 proteins. This ... |
295-425 |
1.26e-03 |
|
Nuf2, DHR10-like domain; This domain is found at the C-terminal region of Nuf2 proteins. This domain was identified as MazG related domain also designated as Designed helical repeat protein 10 (DHR10) that actually adopts a coiled-coil structure. Nuf2 is part of the Ndc80 complex, which binds to the spindle and is required for chromosome segregation and spindle checkpoint activity.
Pssm-ID: 465814 [Multi-domain] Cd Length: 117 Bit Score: 41.03 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 295 EEDLAKVLELQEVVDRQAREHcQMK-ERLATLSGHVAELEEDLDTARKDLIKSEEVNSRLQrDVREAMAQKE----DMEE 369
Cdd:pfam18595 1 SSTLAEEKEELAELERKAREL-QAKiDALQVVEKDLRSCIKLLEEIEAELAKLEEAKKKLK-ELRDALEEKEielrELER 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 2076569066 370 RITTLEKRYLAAQreatsvhdlnDKLESeiankdaVHRQTEDKNRQLQERLELAEQ 425
Cdd:pfam18595 79 REERLQRQLENAQ----------EKLER-------LREQAEEKREAAQARLEELRE 117
|
|
| CAF-1_p150 |
pfam11600 |
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ... |
406-519 |
1.27e-03 |
|
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide subunit of CAF-1, which functions in depositing newly synthesized and acetylated histones H3/H4 into chromatin during DNA replication and repair. CAF-1_p150 includes the HP1 interaction site, the PEST, KER and ED interacting sites. CAF-1_p150 interacts directly with newly synthesized and acetylated histones through the acidic KER and ED domains. The PEST domain is associated with proteins that undergo rapid proteolysis.
Pssm-ID: 402959 [Multi-domain] Cd Length: 164 Bit Score: 42.37 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 406 HRQTEDKNRQLQERLELAEQ---KLQQTLRKAETLPE---VEAELAQRVAALSKAEERHGNIEER--------------L 465
Cdd:pfam11600 7 VQSQEEKEKQRLEKDKERLRrqlKLEAEKEEKERLKEeakAEKERAKEEARRKKEEEKELKEKERrekkekdekekaekL 86
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 2076569066 466 RQMEAQLEEKnQELQRARQREKMSEEHSKRLSDTVDRLLSESGERLRLHLKERT 519
Cdd:pfam11600 87 RLKEEKRKEK-QEALEAKLEEKRKKEEEKRLKEEEKRIKAEKAEITRFLQKPKT 139
|
|
| CENP-F_leu_zip |
pfam10473 |
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, ... |
380-532 |
1.42e-03 |
|
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, microtubule-binding protein consisting of two 1,600-amino acid-long coils, is essential for the full functioning of the mitotic checkpoint pathway. There are several leucine-rich repeats along the sequence of LEK1 that are considered to be zippers, though they do not appear to be binding DNA directly in this instance.
Pssm-ID: 463102 [Multi-domain] Cd Length: 140 Bit Score: 41.51 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 380 AAQREATSVHDLNDKLESEiankdavhrqtedknrqlqerLELAEQKLQQTLRKAETlpeveaelaQRvAALSKAEERHG 459
Cdd:pfam10473 14 ESERKADSLKDKVENLERE---------------------LEMSEENQELAILEAEN---------SK-AEVETLKAEIE 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 460 NIEERLRQMEAQL----EEK---NQELQraRQREKMSEEHSkRLSDTvDRLLSESgERLRLHLKERT-AALEDKNALLRE 531
Cdd:pfam10473 63 EMAQNLRDLELDLvtlrSEKenlTKELQ--KKQERVSELES-LNSSL-ENLLEEK-EQEKVQMKEESkTAVEMLQTQLKE 137
|
.
gi 2076569066 532 V 532
Cdd:pfam10473 138 L 138
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
293-474 |
1.42e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 44.06 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 293 SHEEDL----AKVLELQEVVDRQAREHCQMKERLATLSGHVAELE-------EDLDTARKDLIKSEEVNSRLQRDVREAm 361
Cdd:PRK04778 352 QLEKQLesleKQYDEITERIAEQEIAYSELQEELEEILKQLEEIEkeqeklsEMLQGLRKDELEAREKLERYRNKLHEI- 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 362 aqKEDMEER-ITTLEKRYLAAQREAT-SVHDLNDKLESEIANKDAVHRQ----TEDKNRqLQERLE-------LAEQKLQ 428
Cdd:PRK04778 431 --KRYLEKSnLPGLPEDYLEMFFEVSdEIEALAEELEEKPINMEAVNRLleeaTEDVET-LEEETEelvenatLTEQLIQ 507
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2076569066 429 QTLRKAETLPEVEaelaqrvAALSKAEE--RHGNIEERLRQMEAQLEE 474
Cdd:PRK04778 508 YANRYRSDNEEVA-------EALNEAERlfREYDYKAALEIIATALEK 548
|
|
| LRRFIP |
pfam09738 |
LRRFIP family; LRRFIP1 is a transcriptional repressor which preferentially binds to the ... |
355-573 |
1.45e-03 |
|
LRRFIP family; LRRFIP1 is a transcriptional repressor which preferentially binds to the GC-rich consensus sequence (5'- AGCCCCCGGCG-3') and may regulate expression of TNF, EGFR and PDGFA. LRRFIP2 may function as activator of the canonical Wnt signalling pathway, in association with DVL3, upstream of CTNNB1/beta-catenin.
Pssm-ID: 462869 [Multi-domain] Cd Length: 303 Bit Score: 43.53 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 355 RDVREAMAqkeDMEER-----ITTL----EKRYLAAQreatsVHDLNDKLEsEIANKDA-VHRQTEDKNRQLqERLELAE 424
Cdd:pfam09738 89 RDIKHELK---EVEEKyrkamISNAqldnEKSNLMYQ-----VDLLKDKLE-EMEESLAeLQRELREKNKEL-ERLKRNL 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 425 QKLQqtlrkaETLPEVEAELAQRVAALSKaeerHGNIeerLRQMEAQLEEKNQELQRARqREKMSEEHSKRLSDTVDRLL 504
Cdd:pfam09738 159 RRLQ------FQLAELKEQLKQRDELIEK----HGLV---IVPDENTNGEEENSPADAK-RALVSVEAAEVLESAGEGSL 224
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2076569066 505 sesGERLRLHLKErtaaledKNALLREVGDAKKQLEETQRDKdqlvlnvealRAELDQVRLGGPSLHHG 573
Cdd:pfam09738 225 ---DVRLKKLADE-------KEELLDEVRKLKLQLEEEKSKR----------NSTRSSQSPDGFGLENG 273
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
2788-2979 |
1.46e-03 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 44.48 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 2788 LRRAGQSCQAWPVRACAGRWTRGCGAhacllwrglAAPVPSAEPGSARALQGARQPAGRARLPRSRSQAGPRRTPSGDTE 2867
Cdd:PRK12323 363 FRPGQSGGGAGPATAAAAPVAQPAPA---------AAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEAL 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 2868 PGALLLDAPTPAGRERLrrdhrLAAPGATrPGAQQPAQSAPSLPPARPRRLAGKFSGPGAGATARDSACGFGLPSPGAPA 2947
Cdd:PRK12323 434 AAARQASARGPGGAPAP-----APAPAAA-PAAAARPAAAGPRPVAAAAAAAPARAAPAAAPAPADDDPPPWEELPPEFA 507
|
170 180 190
....*....|....*....|....*....|..
gi 2076569066 2948 AAGPEVGSAAVRVGQRGHTPGRGGGAQRPEGS 2979
Cdd:PRK12323 508 SPAPAQPDAAPAGWVAESIPDPATADPDDAFE 539
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
349-565 |
1.55e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.24 E-value: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 349 VNSRLQRDVREAMAQKEDMEERITTLEKRYLAAQ------REATSVHDLNDK----------LESEIANKDAVHRQTEDK 412
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQLPELRKELEEAEaaleefRQKNGLVDLSEEaklllqqlseLESQLAEARAELAEAEAR 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 413 NRQLQERLELAEQKLQQTLRkAETLPEVEAELAQRVAALSKAEER----HGNIEERLRQMEAQLEEKNQELQRARQRekm 488
Cdd:COG3206 242 LAALRAQLGSGPDALPELLQ-SPVIQQLRAQLAELEAELAELSARytpnHPDVIALRAQIAALRAQLQQEAQRILAS--- 317
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2076569066 489 seehskrlsdtvdrlLSESGERLRLHLKERTAALEDKNALLREVGDAKKQLEETQRDKDQLVLNVEALRAELDQVRL 565
Cdd:COG3206 318 ---------------LEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEARL 379
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
414-564 |
1.58e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.00 E-value: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 414 RQLQERLELAEQKLQQTLRKAETlpevEAElAQRVAALSKAEERhgnIEERLRQMEAQLEEKNQELQRARQREKMSEEHs 493
Cdd:PRK12704 27 KIAEAKIKEAEEEAKRILEEAKK----EAE-AIKKEALLEAKEE---IHKLRNEFEKELRERRNELQKLEKRLLQKEEN- 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2076569066 494 krlsdtvdrllsesgerlrlhLKERTAALEDKnallrevgdaKKQLEETQRDKDQLVLNVEALRAELDQVR 564
Cdd:PRK12704 98 ---------------------LDRKLELLEKR----------EEELEKKEKELEQKQQELEKKEEELEELI 137
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
305-521 |
1.81e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 44.05 E-value: 1.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 305 QEVVDRQAREHCQMKERLATLSGHV--------------------------AELEEDLDTARKDLIK-SEEVNSRLQRDV 357
Cdd:NF041483 123 TEAVQRRQQLDQELAERRQTVESHVnenvawaeqlrartesqarrlldesrAEAEQALAAARAEAERlAEEARQRLGSEA 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 358 REAMAQKEDMEERITTLEKRYL-AAQREATSVHDLNDKLESEIANK-DAVHRQTEDKNRQLQERLELAEQKLQQTLRKAE 435
Cdd:NF041483 203 ESARAEAEAILRRARKDAERLLnAASTQAQEATDHAEQLRSSTAAEsDQARRQAAELSRAAEQRMQEAEEALREARAEAE 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 436 -TLPEVEAELAQRVAALSKAEerhgniEERLRQMEAQLEEKNQElqRARQREKMSEEHSKRLSD---TVDRLLSESGERL 511
Cdd:NF041483 283 kVVAEAKEAAAKQLASAESAN------EQRTRTAKEEIARLVGE--ATKEAEALKAEAEQALADaraEAEKLVAEAAEKA 354
|
250
....*....|
gi 2076569066 512 RLHLKERTAA 521
Cdd:NF041483 355 RTVAAEDTAA 364
|
|
| ADIP |
pfam11559 |
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ... |
365-498 |
1.91e-03 |
|
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at cell-cell adherens junctions, and in Sch. pombe and other fungi where it anchors spindle-pole bodies to spindle microtubules. It is a coiled-coil structure, and in pombe, it is required for anchoring the minus end of spindle microtubules to the centrosome equivalent, the spindle-pole body. The name ADIP derives from the family being composed of Afadin- and alpha -Actinin-Binding Proteins localized at Cell-Cell Adherens Junctions.
Pssm-ID: 463295 [Multi-domain] Cd Length: 151 Bit Score: 41.53 E-value: 1.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 365 EDMEERITTLEKRYLAAQREA---TSVHDLNDKLESEIANKDAVHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVE 441
Cdd:pfam11559 31 ENIARIINVIYELLQQRDRDLefrESLNETIRTLEAEIERLQSKIERLKTQLEDLERELALLQAKERQLEKKLKTLEQKL 110
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 2076569066 442 AELAQRVAalskaeerhgnieeRLRQMEAQLeeKNQELQRARQREKMSEEHSKRLSD 498
Cdd:pfam11559 111 KNEKEELQ--------------RLKNALQQI--KTQFAHEVKKRDREIEKLKERLAQ 151
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
365-544 |
1.92e-03 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 43.79 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 365 EDMEERITTLEKRYLAAQREATSvhDLNDKLESEIANKDAVH-----RQTEDKNRQLQERLELAEQ-----KLQQTLRKA 434
Cdd:pfam15709 310 ESEEERSEEDPSKALLEKREQEK--ASRDRLRAERAEMRRLEverkrREQEEQRRLQQEQLERAEKmreelELEQQRRFE 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 435 ETL---PEVEAELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQRE-----------------KMSEEHsK 494
Cdd:pfam15709 388 EIRlrkQRLEEERQRQEEEERKQRLQLQAAQERARQQQEEFRRKLQELQRKKQQEeaeraeaekqrqkelemQLAEEQ-K 466
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2076569066 495 RLSDTVD-------RLLSESGERLRLHLKERTAALEDKNALLREvgDAKKQLEETQR 544
Cdd:pfam15709 467 RLMEMAEeerleyqRQKQEAEEKARLEAEERRQKEEEAARLALE--EAMKQAQEQAR 521
|
|
| SAM_superfamily |
cd09487 |
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ... |
1166-1223 |
2.08e-03 |
|
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of approximately 70 amino acids. This domain is found in the Fungi/Metazoa group and in a restricted number of bacteria. Proteins with SAM domains are represented by a wide variety of domain architectures and have different intracellular localization, including nucleus, cytoplasm and membranes. SAM domains have diverse functions. They can interact with proteins, RNAs and membrane lipids, contain site of phosphorylation and/or kinase docking site, and play a role in protein homo and hetero dimerization/oligomerization in processes ranging from signal transduction to regulation of transcription. Mutations in SAM domains have been linked to several diseases.
Pssm-ID: 188886 [Multi-domain] Cd Length: 56 Bit Score: 38.76 E-value: 2.08e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 2076569066 1166 VVVWLElWVGMPaWYVAACRANVKSGAIMSALSDTEIQrEIGISNPLHRLKLRLAIQE 1223
Cdd:cd09487 2 VAEWLE-SLGLE-QYADLFRKNEIDGDALLLLTDEDLK-ELGITSPGHRKKILRAIQR 56
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
313-564 |
2.36e-03 |
|
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in eukaryotes. CCCAP is also known as SDCCAG8, serologically defined colon cancer antigen 8. It is associated with the centrosome.
Pssm-ID: 435040 [Multi-domain] Cd Length: 703 Bit Score: 43.74 E-value: 2.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 313 REHCQMKERLATLSGHVAELEEDLDTARKDLIkseEVNSRLQRDVREAMAQKEDMEEriTTLEKRYLAAQReatsvhdln 392
Cdd:pfam15964 396 KEREELGATMLALSQNVAQLEAQVEKVTREKN---SLVSQLEEAQKQLASQEMDVTK--VCGEMRYQLNQT--------- 461
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 393 dKLESEIANKDavHRQTEDK-NRQL----QE----RLELAE--QKLQQTLRKA-----------ETLPEVEAEL------ 444
Cdd:pfam15964 462 -KMKKDEAEKE--HREYRTKtGRQLeikdQEieklGLELSEskQRLEQAQQDAarareeclkltELLGESEHQLhltrle 538
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 445 --------AQRVAALS-KAEERHGNIEERLRQMEAQLEEKNQEL------QRARQReKMSEE---HSKRLSDTVDRLLSE 506
Cdd:pfam15964 539 kesiqqsfSNEAKAQAlQAQQREQELTQKMQQMEAQHDKTVNEQyslltsQNTFIA-KLKEEcctLAKKLEEITQKSRSE 617
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 507 ----SGERLRLH-----LKERTAALEDK---------------NALLREVGDAKKQLEETQRDKDQLVLNVEALRAELDQ 562
Cdd:pfam15964 618 veqlSQEKEYLQdrlekLQKRNEELEEQcvqhgrmhermkqrlRQLDKHCQATAQQLVQLLSKQNQLFKERQNLTEEVQS 697
|
..
gi 2076569066 563 VR 564
Cdd:pfam15964 698 LR 699
|
|
| BBP1_C |
pfam15272 |
Spindle pole body component BBP1, C-terminal; This C-terminal domain of BBP1, a spindle pole ... |
328-491 |
2.43e-03 |
|
Spindle pole body component BBP1, C-terminal; This C-terminal domain of BBP1, a spindle pole body component, carries coiled-coils that are necessary for the localization of BBP1 to the spindle pole body (SPB). Although not a membrane protein itself, BBP1 binds to Mps2 as well as to Spc29 and the half-bridge protein Kar1, thus providing a model for how the SPB core is tethered within the nuclear envelope and to the half-bridge
Pssm-ID: 405864 [Multi-domain] Cd Length: 183 Bit Score: 41.61 E-value: 2.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 328 HVAELEEDLDtarkDLIKSEEVNSRLQRDVREamaQKEDMEERITTLEKRYLAAQREatsvhdLNDKLESEiankdavhR 407
Cdd:pfam15272 2 YTSEYLELLD----KLDKNNRALHLLNKDVRE---RDEHYQLQETSYKKKYLQTRNE------LINELKQS--------K 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 408 QTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAalSKAEERHgNIEERLRQMEAQleekNQELQRARQREK 487
Cdd:pfam15272 61 KLYDNYYKLYSKYQQLKKISNESLDLQSTITNLESQLVDQAI--DKDREIH-NLNEKILSLELR----NQELETKREIDK 133
|
....
gi 2076569066 488 MSEE 491
Cdd:pfam15272 134 MKYE 137
|
|
| BAR_SNX7 |
cd07666 |
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexin 7; BAR domains are dimerization, lipid ... |
359-505 |
2.49e-03 |
|
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexin 7; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. The specific function of SNX7 is still unknown. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.
Pssm-ID: 153350 Cd Length: 243 Bit Score: 42.58 E-value: 2.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 359 EAMAQK----EDMEERITTLEKRYLAAQREATSVHDLNDKLESEIANK--------DAVHRQTEDKNRQLQERLE----- 421
Cdd:cd07666 64 EAFSQKinvlDKISQRIYKEQREYFEELKEYGPIYTLWSASEEELADSlkgmasciDRCCKATDKRMKGLSEQLLpvihe 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 422 --LAEQKLQQTLRKAEtlpEVEAELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQR--ARQREKMSEEHSKRLS 497
Cdd:cd07666 144 yvLYSETLMGVIKRRD---QIQAELDSKVEALANKKADRDLLKEEIEKLEDKVECANNALKAdwERWKQNMQTDLRSAFT 220
|
....*...
gi 2076569066 498 DTVDRLLS 505
Cdd:cd07666 221 DMAENNIS 228
|
|
| BBC |
smart00502 |
B-Box C-terminal domain; Coiled coil region C-terminal to (some) B-Box domains |
363-482 |
2.51e-03 |
|
B-Box C-terminal domain; Coiled coil region C-terminal to (some) B-Box domains
Pssm-ID: 128778 Cd Length: 127 Bit Score: 40.33 E-value: 2.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 363 QKEDMEERITTLEKRylaaqreatsvhdlNDKLESEIANKDAVHRQTEDKNRQLQERLELAEQKLQQTLRKAetlpevEA 442
Cdd:smart00502 1 QREALEELLTKLRKK--------------AAELEDALKQLISIIQEVEENAADVEAQIKAAFDELRNALNKR------KK 60
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 2076569066 443 ELAQRVaalskaEERHGNIEERLRQMEAQLEEKNQELQRA 482
Cdd:smart00502 61 QLLEDL------EEQKENKLKVLEQQLESLTQKQEKLSHA 94
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
305-453 |
2.54e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 43.03 E-value: 2.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 305 QEVVDRQAREHCQMKERLATLSGHVAELEEDLDTARKDLIKSEEVNSRLQRDVREAMAQKEDMEERITTLEKRyLAAQ-- 382
Cdd:PRK09039 52 DSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELAQE-LDSEkq 130
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2076569066 383 ---REATSVHDLNDKLEseiankdAVHRQTEDknrqLQERLELAEQKLQQTLRKAETL-PEVEAELAQRVAALSK 453
Cdd:PRK09039 131 vsaRALAQVELLNQQIA-------ALRRQLAA----LEAALDASEKRDRESQAKIADLgRRLNVALAQRVQELNR 194
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
2823-3112 |
2.63e-03 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 43.62 E-value: 2.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 2823 AAPVPSAEPGSARALQGARQPAGRARLPRSRSQAGPRRTPSGDTEPGALLLDAPTPAGRErlrrdHRLAAPGATRPGAQQ 2902
Cdd:PHA03307 124 ASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQAALPLSSPEETA-----RAPSSPPAEPPPSTP 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 2903 PAQSAPslPPARPRRLAGKFSGPGAGATARDSACGFGLPSPGAPAAAGPEVGSaavrvGQRGHTPGRGGGAQRPEGSGTD 2982
Cdd:PHA03307 199 PAAASP--RPPRRSSPISASASSPAPAPGRSAADDAGASSSDSSSSESSGCGW-----GPENECPLPRPAPITLPTRIWE 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 2983 RGEGVLRLGDGTPAPSSPSLTGQCRRVGHRLGCLRPRAPAHVAVRADVQPPRVGL------RAGPGEGAGGATRRGGAWG 3056
Cdd:PHA03307 272 ASGWNGPSSRPGPASSSSSPRERSPSPSPSSPGSGPAPSSPRASSSSSSSRESSSsstsssSESSRGAAVSPGPSPSRSP 351
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 2076569066 3057 RGLRGPDAPRPAAEPEVGPGRSGGRSAAGGGGRTERAAVSARRGGPGLWAGAPAAR 3112
Cdd:PHA03307 352 SPSRPPPPADPSSPRKRPRPSRAPSSPAASAGRPTRRRARAAVAGRARRRDATGRF 407
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
2310-2661 |
2.69e-03 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 43.44 E-value: 2.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 2310 PAALRAHRRPRGPAEAAVAGGQPRRGRQCPPTSRALPASLPGPElradslAGKRARRRRTAGPRNRLRAHwRPLASPSRR 2389
Cdd:PRK07764 393 APAAAAPSAAAAAPAAAPAPAAAAPAAAAAPAPAAAPQPAPAPA------PAPAPPSPAGNAPAGGAPSP-PPAAAPSAQ 465
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 2390 GHPCPGPEVPCPGPEAPCAAPARASQGTARTawgprlgPSVPPTPPSAfclarasgAGTSGPRSAASAclLRQACGpacl 2469
Cdd:PRK07764 466 PAPAPAAAPEPTAAPAPAPPAAPAPAAAPAA-------PAAPAAPAGA--------DDAATLRERWPE--ILAAVP---- 524
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 2470 NKAGVGFRLLLRCVSVL---RGVAWVDFPSTGRACR----------PRILRVVAGRCCADLWTVA----ATSPASSPRAL 2532
Cdd:PRK07764 525 KRSRKTWAILLPEATVLgvrGDTLVLGFSTGGLARRfaspgnaevlVTALAEELGGDWQVEAVVGpapgAAGGEGPPAPA 604
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 2533 SSVSCSYHVDIVEQTRLPQDAQDGGAGRPlSQGSRLSAASAEEGAWSPGQSQMGVLAKAARGARPAVAAVTQPQGAAWAG 2612
Cdd:PRK07764 605 SSGPPEEAARPAAPAAPAAPAAPAPAGAA-AAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPP 683
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 2076569066 2613 GCQGWGWAERAVRRliPPALFPRPSRVGPSGRWTPAQPLERADGAANEP 2661
Cdd:PRK07764 684 APAPAAPAAPAGAA--PAQPAPAPAATPPAGQADDPAAQPPQAAQGASA 730
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
359-496 |
2.69e-03 |
|
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.
Pssm-ID: 466641 [Multi-domain] Cd Length: 120 Bit Score: 40.29 E-value: 2.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 359 EAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLeseiankdavhrqtEDKNRQLQERLELAEQKLQqtlrkaetlp 438
Cdd:pfam20492 3 EAEREKQELEERLKQYEEETKKAQEELEESEETAEEL--------------EEERRQAEEEAERLEQKRQ---------- 58
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 2076569066 439 evEAELAQRVAALSKAEErhgnIEERlRQMEAQLEEKNQELQRARQREKMSEEHSKRL 496
Cdd:pfam20492 59 --EAEEEKERLEESAEME----AEEK-EQLEAELAEAQEEIARLEEEVERKEEEARRL 109
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
407-567 |
2.75e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 43.79 E-value: 2.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 407 RQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALskaEERHGNIEERLRQMEAQLEEKNQELQRARQRE 486
Cdd:COG3096 525 EQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEEL---EEQAAEAVEQRSELRQQLEQLRARIKELAARA 601
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 487 KMSEEhskrLSDTVDRLLSESGErlrlhlkertaALEDKNALLREVGDAKKQLEETQRDKDQLVLNVEALRAELDQVRLG 566
Cdd:COG3096 602 PAWLA----AQDALERLREQSGE-----------ALADSQEVTAAMQQLLEREREATVERDELAARKQALESQIERLSQP 666
|
.
gi 2076569066 567 G 567
Cdd:COG3096 667 G 667
|
|
| RRP36 |
pfam06102 |
rRNA biogenesis protein RRP36; RRP36 is involved in the early processing steps of the pre-rRNA. |
391-487 |
2.86e-03 |
|
rRNA biogenesis protein RRP36; RRP36 is involved in the early processing steps of the pre-rRNA.
Pssm-ID: 461829 [Multi-domain] Cd Length: 158 Bit Score: 41.00 E-value: 2.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 391 LNDKLESEIANKDAVHRQTEDKNRqlQERLELAEQKLQQTL-------RKAETLPEVEAELAQRVAA------LSKAEER 457
Cdd:pfam06102 54 LDEYRKKEIEELKKQLKKTKDPEE--KEELKRTLQSMESRLkakkrkdREREVLKEHKKEEKEKVKQgkkpfyLKKSEKK 131
|
90 100 110
....*....|....*....|....*....|
gi 2076569066 458 hgnieerlrqmEAQLEEKNQELQRARQREK 487
Cdd:pfam06102 132 -----------KLLLKEKFEELKKSGKLDK 150
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
414-561 |
2.95e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 43.16 E-value: 2.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 414 RQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKAEERHGNIEERlrqmeaqlEEKNQELQRARQREKMSEEHS 493
Cdd:PRK12705 26 KKRQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARRER--------EELQREEERLVQKEEQLDARA 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2076569066 494 KRLSDTVDRLLSESGerlrlHLKERTAALEDKNALLREvgdakkQLEE----TQRDKDQLVLNveALRAELD 561
Cdd:PRK12705 98 EKLDNLENQLEEREK-----ALSARELELEELEKQLDN------ELYRvaglTPEQARKLLLK--LLDAELE 156
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
327-564 |
3.00e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.08 E-value: 3.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 327 GHVAELEEDLDTaRKDLIKSeevnsrlqRDVREAMAQKEDMEERITTLEKRYLAAqreatsVHDLNDKLE-SEIANKDAV 405
Cdd:COG3206 74 SSLSASDSPLET-QIEILKS--------RPVLERVVDKLNLDEDPLGEEASREAA------IERLRKNLTvEPVKGSNVI 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 406 HRQTEDKNRQLQERL--ELAEQKLQQTLRkaetlpeveaelaQRVAALSKAEERhgnIEERLRQMEAQLEEKNQELQRAR 483
Cdd:COG3206 139 EISYTSPDPELAAAVanALAEAYLEQNLE-------------LRREEARKALEF---LEEQLPELRKELEEAEAALEEFR 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 484 QREKM--SEEHSKRLSDTVDRLLSESgERLRLHLKERTAALEDKNALLREVGDA-------------KKQLEETQRDKDQ 548
Cdd:COG3206 203 QKNGLvdLSEEAKLLLQQLSELESQL-AEARAELAEAEARLAALRAQLGSGPDAlpellqspviqqlRAQLAELEAELAE 281
|
250 260
....*....|....*....|...
gi 2076569066 549 LVLN-------VEALRAELDQVR 564
Cdd:COG3206 282 LSARytpnhpdVIALRAQIAALR 304
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
2823-3001 |
3.41e-03 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 43.05 E-value: 3.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 2823 AAPVPSAEPGSARALQGARQPAGRARLPRsRSQAGPRRTPSGDTEPGALLLDAPTPAGRerlrRDHRLAAPGATRPGAQQ 2902
Cdd:PRK07764 616 AAPAAPAAPAAPAPAGAAAAPAEASAAPA-PGVAAPEHHPKHVAVPDASDGGDGWPAKA----GGAAPAAPPPAPAPAAP 690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 2903 PAQSAPSLPPARPRRLAGKFSGPGAGATARDsacgfglPSPGAPAAAGPEVGSAAVRVGQRGHTPGRGGGAQRPEgsgtd 2982
Cdd:PRK07764 691 AAPAGAAPAQPAPAPAATPPAGQADDPAAQP-------PQAAQGASAPSPAADDPVPLPPEPDDPPDPAGAPAQP----- 758
|
170
....*....|....*....
gi 2076569066 2983 RGEGVLRLGDGTPAPSSPS 3001
Cdd:PRK07764 759 PPPPAPAPAAAPAAAPPPS 777
|
|
| SAM_Neurabin-like |
cd09512 |
SAM domain of SAM_Neurabin-like subfamily; SAM (sterile alpha motif) domain of Neurabin-like ... |
1366-1430 |
3.82e-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: 38.40 E-value: 3.82e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2076569066 1366 VLVWSNDRVIRWVLSIGLREYAGNLAESGVHG-ALIALDETfDFSALALllqiptQNTQARAVLER 1430
Cdd:cd09512 4 VSEWSVQQVCQWLMGLGLEQYIPEFTANNIDGqQLLQLDSS-KLKALGI------TSSSDRSLLKK 62
|
|
| I-BAR_IMD |
cd07605 |
Inverse (I)-BAR, also known as the IRSp53/MIM homology Domain (IMD), a dimerization module ... |
350-531 |
4.09e-03 |
|
Inverse (I)-BAR, also known as the IRSp53/MIM homology Domain (IMD), a dimerization module that binds and bends membranes; Inverse (I)-BAR (or IMD) is a member of the Bin/Amphiphysin/Rvs (BAR) domain family. It is a dimerization and lipid-binding module that bends membranes and induces membrane protrusions in the opposite direction compared to classical BAR and F-BAR domains, which produce membrane invaginations. IMD domains are found in Insulin Receptor tyrosine kinase Substrate p53 (IRSp53), Missing in Metastasis (MIM), and Brain-specific Angiogenesis Inhibitor 1-Associated Protein 2-like (BAIAP2L) proteins. These are multi-domain proteins that act as scaffolding proteins and transducers of a variety of signaling pathways that link membrane dynamics and the underlying actin cytoskeleton. Most members contain an N-terminal IMD, an SH3 domain, and a WASP homology 2 (WH2) actin-binding motif at the C-terminus, exccept for MIM which does not carry an SH3 domain. Some members contain additional domains and motifs. The IMD domain binds and bundles actin filaments, binds membranes and produces membrane protrusions, and interacts with the small GTPase Rac.
Pssm-ID: 153289 [Multi-domain] Cd Length: 223 Bit Score: 41.58 E-value: 4.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 350 NSRLQRDVREAMAQkedMEERITTLEkrylaAQREATS-------VHDLNDKLESEIANKDAVHRQTEDKNRQLQERLEl 422
Cdd:cd07605 59 QSRGSQELGEALKQ---IVDTHKSIE-----ASLEQVAkafhgelILPLEKKLELDQKVINKFEKDYKKEYKQKREDLD- 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 423 aeqKLQQTLRKAEtlpeveaelaqrvaalSKAEERH-GNIEERLRQMEAQLEEKNQELQR---ARQREKMSEEHsKRLSD 498
Cdd:cd07605 130 ---KARSELKKLQ----------------KKSQKSGtGKYQEKLDQALEELNDKQKELEAfvsQGLRDALLEER-RRYCF 189
|
170 180 190
....*....|....*....|....*....|...
gi 2076569066 499 TVDRLLSESGERLRLHLKERTaALEDKNALLRE 531
Cdd:cd07605 190 LVDKHCSVAKHEIAYHAKAMT-LLSTRLPLWQE 221
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
417-563 |
4.10e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.02 E-value: 4.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 417 QERLELAEQKLQQTLRKAETLPEVEAELAQRVAALS------KAEERHGNIEER----LRQMEAQLEEKNQELQRARQRE 486
Cdd:PRK04863 299 RRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASdhlnlvQTALRQQEKIERyqadLEELEERLEEQNEVVEEADEQQ 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 487 KMSEEHSKRLSDTVDRL---LSESGERLRLhlkERTAALEDKNA--LLREvgdAKKQLEETQRDKDQLVLNVEALRAELD 561
Cdd:PRK04863 379 EENEARAEAAEEEVDELksqLADYQQALDV---QQTRAIQYQQAvqALER---AKQLCGLPDLTADNAEDWLEEFQAKEQ 452
|
..
gi 2076569066 562 QV 563
Cdd:PRK04863 453 EA 454
|
|
| DUF4355 |
pfam14265 |
Domain of unknown function (DUF4355); This family of proteins is found in bacteria and viruses. ... |
410-498 |
4.20e-03 |
|
Domain of unknown function (DUF4355); This family of proteins is found in bacteria and viruses. Proteins in this family are typically between 180 and 214 amino acids in length.
Pssm-ID: 405026 [Multi-domain] Cd Length: 119 Bit Score: 39.60 E-value: 4.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 410 EDKNRQLQERLELAEQKLQQTLrkaetlpEVEAELAQRVAALSKAEERhgniEERLRQMEAQLEEKNQELqrarQREKMS 489
Cdd:pfam14265 2 SEVDKIVAKALATKKNNLEKEI-------EDEIKEAKKLAKMNAEEKA----KYELEKLQKELEEEKAEL----ARKELK 66
|
....*....
gi 2076569066 490 EEHSKRLSD 498
Cdd:pfam14265 67 AEARKMLSE 75
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
2319-2457 |
4.83e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 43.00 E-value: 4.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 2319 PRGPAEAAVAGGQPRRGRQCPPTSRALPASLPGPELRA--------DSLAGKRARRRRTAGPRNRLRAHWRPLASPSRRG 2390
Cdd:PHA03247 2608 PRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTvppperprDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRA 2687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 2391 ------------HPCPGPEVPCPGPEAPCAA-PARASQGTARTAWGPRLGPSVPPTPPSAFCL-----ARASGAGTSGPR 2452
Cdd:PHA03247 2688 arptvgsltslaDPPPPPPTPEPAPHALVSAtPLPPGPAAARQASPALPAAPAPPAVPAGPATpggpaRPARPPTTAGPP 2767
|
....*
gi 2076569066 2453 SAASA 2457
Cdd:PHA03247 2768 APAPP 2772
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
2548-3002 |
4.90e-03 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 42.67 E-value: 4.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 2548 RLPQDAQDGGAGRPLSQGSRLSAASAEEGAWSPGQSQMGVLAKAARGARPAVAAVTQPQGAAwaggcqgwgwaeravrrl 2627
Cdd:PRK07764 380 RLERRLGVAGGAGAPAAAAPSAAAAAPAAAPAPAAAAPAAAAAPAPAAAPQPAPAPAPAPAP------------------ 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 2628 iPPALFPRPSRVGPSGRWTPAQPLERADGAANEPTWTSQPhaheektkcrpsPPGPGPGPPGPRAPAPLERHPLRPADTG 2707
Cdd:PRK07764 442 -PSPAGNAPAGGAPSPPPAAAPSAQPAPAPAAAPEPTAAP------------APAPPAAPAPAAAPAAPAAPAAPAGADD 508
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 2708 EHLPEAQWEGRPAACRRTTEGWWPLSSGRVCV------------RTAEAMSRLSLRGPAGVTREqpcpAAREGPGRrqhp 2775
Cdd:PRK07764 509 AATLRERWPEILAAVPKRSRKTWAILLPEATVlgvrgdtlvlgfSTGGLARRFASPGNAEVLVT----ALAEELGG---- 580
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 2776 sarphRLSTRCPLRRAGQSCQAWPVRACAGRWTRGCGAHAcllwrglAAPVPSAEPGSARALQGARQPAGRARLPRSRSQ 2855
Cdd:PRK07764 581 -----DWQVEAVVGPAPGAAGGEGPPAPASSGPPEEAARP-------AAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVA 648
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 2856 AGPRR-------TPSGDTEPGALLLDAPTPAGRERlRRDHRLAAPGATRPGAQQPAQSAPSLPPARPRRLAGKFSGPGAG 2928
Cdd:PRK07764 649 APEHHpkhvavpDASDGGDGWPAKAGGAAPAAPPP-APAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQG 727
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2076569066 2929 ATARDSACGFGLPSPGAPaAAGPEVGSAAVRVGQRGHTPGRGGGAQRPEGSgtDRGEGVLRLGDGTPAPSSPSL 3002
Cdd:PRK07764 728 ASAPSPAADDPVPLPPEP-DDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPS--PPSEEEEMAEDDAPSMDDEDR 798
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
393-518 |
5.21e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 42.38 E-value: 5.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 393 DKLESEIAN----KDAVHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAAL-SKAEERHGNIEErlrq 467
Cdd:COG0542 414 DELERRLEQleieKEALKKEQDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELkEELEQRYGKIPE---- 489
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2076569066 468 MEAQLEEKNQELQRARQ--REKMSEEH-----SKRlsdT---VDRLLSESGERLrLHLKER 518
Cdd:COG0542 490 LEKELAELEEELAELAPllREEVTEEDiaevvSRW---TgipVGKLLEGEREKL-LNLEEE 546
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
2285-2467 |
5.21e-03 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 42.56 E-value: 5.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 2285 DAAVPSAC-AQVSGRSRASSRERSRVPAALRAHRRPRGPAEAAVAGGQPRRGrqcppTSRALPASLPGPELRADSLAGKR 2363
Cdd:PRK12323 371 GAGPATAAaAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAA-----PARRSPAPEALAAARQASARGPG 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 2364 ARRRRTAGPRNRLRAHWRPLASPSRrghPCPGPEVPCPGPEAPCAAPARASQGTARTAWGPRLGPSVPPTPPSAFCLARA 2443
Cdd:PRK12323 446 GAPAPAPAPAAAPAAAARPAAAGPR---PVAAAAAAAPARAAPAAAPAPADDDPPPWEELPPEFASPAPAQPDAAPAGWV 522
|
170 180
....*....|....*....|....
gi 2076569066 2444 SGAGTSGPRSAASACLLRQACGPA 2467
Cdd:PRK12323 523 AESIPDPATADPDDAFETLAPAPA 546
|
|
| Mod_r |
pfam07200 |
Modifier of rudimentary (Mod(r)) protein; This family represents a conserved region ... |
387-507 |
5.88e-03 |
|
Modifier of rudimentary (Mod(r)) protein; This family represents a conserved region approximately 150 residues long within a number of eukaryotic proteins that show homology with Drosophila melanogaster Modifier of rudimentary (Mod(r)) proteins. The N-terminal half of Mod(r) proteins is acidic, whereas the C-terminal half is basic, and both of these regions are represented in this family. Members of this family include the Vps37 subunit of the endosomal sorting complex ESCRT-I, a complex involved in recruiting transport machinery for protein sorting at the multivesicular body (MVB). The yeast ESCRT-I complex consists of three proteins (Vps23, Vps28 and Vps37). The mammalian homolog of Vps37 interacts with Tsg101 (Pfam: PF05743) through its mod(r) domain and its function is essential for lysosomal sorting of EGF receptors.
Pssm-ID: 462117 [Multi-domain] Cd Length: 146 Bit Score: 39.91 E-value: 5.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 387 SVHDLN------DKLESEIANKDAVHRQTEDKNRQLQERLELAEQKLQQtlrkaetLPEVEaELAQRVAALSkaeerhgn 460
Cdd:pfam07200 4 STEELQellndeDKLDAFVHSLPQVKALQAEKEELLAENESLAEENLSL-------EPELE-ELRSQLQELL-------- 67
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 2076569066 461 ieERLRQMEAQLEEKNQELQRARQreKMSEEHSK-RLSDTVDRLLSES 507
Cdd:pfam07200 68 --EELKALKSEYEEKEQELDELLS--KFSPDALLaRLQAAAAEAEEES 111
|
|
| PRK07003 |
PRK07003 |
DNA polymerase III subunit gamma/tau; |
2739-2943 |
6.47e-03 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 235906 [Multi-domain] Cd Length: 830 Bit Score: 42.14 E-value: 6.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 2739 VRTAEAMSRLSLRGPAGVTREQPCPAAREGPGRRQHPSARPHRLSTRCPLRRAGQSCQAWPVRACAGRWTRGCGAHACLL 2818
Cdd:PRK07003 410 LAPKAAAAAAATRAEAPPAAPAPPATADRGDDAADGDAPVPAKANARASADSRCDERDAQPPADSGSASAPASDAPPDAA 489
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 2819 WrglaAPVPSAEPGSARALQGARQPAGRA-------------RLPRSRSQAGPRRTPSGDTEPGALLLDAPTPAG----R 2881
Cdd:PRK07003 490 F----EPAPRAAAPSAATPAAVPDARAPAaasredapaaaapPAPEARPPTPAAAAPAARAGGAAAALDVLRNAGmrvsS 565
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2076569066 2882 ERLRRDHRLAAPGATRPGAQQPAQSAPSLPPARPRRLAGKFSGPGAGAT-ARDSACGFGLPSP 2943
Cdd:PRK07003 566 DRGARAAAAAKPAAAPAAAPKPAAPRVAVQVPTPRARAATGDAPPNGAArAEQAAESRGAPPP 628
|
|
| DUF4201 |
pfam13870 |
Domain of unknown function (DUF4201); This is a family of coiled-coil proteins from eukaryotes. ... |
451-565 |
7.36e-03 |
|
Domain of unknown function (DUF4201); This is a family of coiled-coil proteins from eukaryotes. The function is not known.
Pssm-ID: 464008 [Multi-domain] Cd Length: 177 Bit Score: 40.28 E-value: 7.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 451 LSKAEERHGNIEERLRQMEA----------------------QLEEKNQELQRARqreKMSEEHSKRLSdtvdrllsesg 508
Cdd:pfam13870 15 LITLKHTLAKIQEKLEQKEElgegltmidflqlqienqalneKIEERNKELKRLK---LKVTNTVHALT----------- 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 2076569066 509 erlrlHLKERTAALEDKNALLrevgdaKKQLEETQRDKDQlvlnveaLRAELDQVRL 565
Cdd:pfam13870 81 -----HLKEKLHFLSAELSRL------KKELRERQELLAK-------LRKELYRVKL 119
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
305-781 |
8.96e-03 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 41.56 E-value: 8.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 305 QEVVDRQAREHcQMKERLATLSGHVAELEEDLDTARKDLIKSEEVNSRLQRDVRE-AMAQKEDMEERittLEKRYLAAQR 383
Cdd:COG3064 2 QEALEEKAAEA-AAQERLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEeAREAKAEAEQR---AAELAAEAAK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 384 EATSVHDLNDKLESEIANKDAVHRQTEDKNRQLQERLELAE-QKLQQTLRKAETLPEVEAELAQRVAAlskAEERHGNIE 462
Cdd:COG3064 78 KLAEAEKAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEkEKAEEAKRKAEEEAKRKAEEERKAAE---AEAAAKAEA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 463 ERLRQMEAQLEEKNQELQRARQREKMSEEHSKRLSDTVDrLLSESGERLRLHLKERTAALEDKNALLREVGDAKKQLEET 542
Cdd:COG3064 155 EAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAA-DTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 543 QRDKDQLVLNVEALRAELDQVRLGGPSLHHGRPHLGSVPDFRFPAADGPADPCGSSAVRTLNEQDWERAQQASVLASVAQ 622
Cdd:COG3064 234 LAAVEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 623 AFESDRELSDGGEDQDALFGSAGLLSPGGQADAQTLAVMLQEQLDAINKEISRVTRGAARRRTLPWR--TERHLAGEKAG 700
Cdd:COG3064 314 EEAVLAAAAAAGALVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLadVEEAAGAGILA 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076569066 701 PGVAPTARGSPAGPGSRGPRPVMGGFAQSRSASPECAGSGVLGGGLQALLPSGRDGSLGRARSPGSPAPSRPRAPSRSRL 780
Cdd:COG3064 394 AAGGGGLLGLRLDLGAALLEAASAVELRVLLALAGAAGAVVALLVKLVADLAGGLVGIGKALTGDADALLGILKAVALDG 473
|
.
gi 2076569066 781 I 781
Cdd:COG3064 474 G 474
|
|
| |
