|
Name |
Accession |
Description |
Interval |
E-value |
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
333-441 |
2.52e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.17 E-value: 2.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415018 333 EEQEHLQGTVKSLREELGALQEQLLEKDLEMKQLLQSKIDLEKELETAREGEKGRQEQEQALREEVEALTKKCQELEEAK 412
Cdd:COG1196 260 AELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEEL 339
|
90 100
....*....|....*....|....*....
gi 1720415018 413 REEKNSfVAVTHEKREAALDEAATVLQAA 441
Cdd:COG1196 340 EELEEE-LEEAEEELEEAEAELAEAEEAL 367
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
84-441 |
3.59e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 50.44 E-value: 3.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415018 84 EIIELKKSLHMQKSDVDLMRTKLRRLEEENSRKDRQIEQLLDpsrgpdfvrtlaeKKPDTGWVITGLKQRIFRLEQQCKE 163
Cdd:TIGR02168 678 EIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRK-------------ELEELSRQISALRKDLARLEAEVEQ 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415018 164 KDNTINKLQTDmkttnLEEMRIAMETYYEEIHRLQTLLASSEAtgkkpmvEKKLGVKRQKKMSSALLNLTRSVQELTEEN 243
Cdd:TIGR02168 745 LEERIAQLSKE-----LTELEAEIEELEERLEEAEEELAEAEA-------EIEELEAQIEQLKEELKALREALDELRAEL 812
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415018 244 QSLKEDLDRMLSNSPTISKIKGYGDWSKPRLLRRIAELEKKVSS--------SESPKQSTSELVnpnplvrSPSNISVQK 315
Cdd:TIGR02168 813 TLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESlaaeieelEELIEELESELE-------ALLNERASL 885
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415018 316 QPKGDQSPEDLPKVApcEEQEHLQGTVKSLREELGALQEQLLEKDLEMKQL------LQSKI--DLEKELETAREGEKGR 387
Cdd:TIGR02168 886 EEALALLRSELEELS--EELRELESKRSELRRELEELREKLAQLELRLEGLevridnLQERLseEYSLTLEEAEALENKI 963
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720415018 388 QEQEQALREEVEALTKKCQEL-------EEAKREEKNSFVAVTHEKREaaLDEAATVLQAA 441
Cdd:TIGR02168 964 EDDEEEARRRLKRLENKIKELgpvnlaaIEEYEELKERYDFLTAQKED--LTEAKETLEEA 1022
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
73-443 |
7.41e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 46.26 E-value: 7.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415018 73 SVYREKEDMY-DEIIELKKSLHMQKSDVDLMRTKLRRLEEENSRKDRQIEQLLDPSRGPDFVRTLAEKKPDTGW-VITGL 150
Cdd:pfam15921 331 SELREAKRMYeDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWdRDTGN 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415018 151 KQRIFRLEQQCKEKDNTINKLQTDMKTT------NLEEMRIAMETYYEEIHRLQTLLASSEATgkKPMVEKKLGVKRQKK 224
Cdd:pfam15921 411 SITIDHLRRELDDRNMEVQRLEALLKAMksecqgQMERQMAAIQGKNESLEKVSSLTAQLEST--KEMLRKVVEELTAKK 488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415018 225 MSsaLLNLTRSVQELTeenQSLKEDLDRMLSNSPTISKIKGygdwskpRLLRRIAELEKKVSSSESPKQSTSELvnpnpl 304
Cdd:pfam15921 489 MT--LESSERTVSDLT---ASLQEKERAIEATNAEITKLRS-------RVDLKLQELQHLKNEGDHLRNVQTEC------ 550
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415018 305 vrspSNISVQKQPKgDQSPEDLPKvaPCEEQEHLQG----TVKSLREELGALQEQLLEKDLEMKQLlqsKIDLEKELETA 380
Cdd:pfam15921 551 ----EALKLQMAEK-DKVIEILRQ--QIENMTQLVGqhgrTAGAMQVEKAQLEKEINDRRLELQEF---KILKDKKDAKI 620
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720415018 381 REGEKGRQEQEQALREEVEALTKKCQELEEAKREEKNSFVAVTHEKREA-ALDEAATVLQAAFR 443
Cdd:pfam15921 621 RELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELnSLSEDYEVLKRNFR 684
|
|
| IQCD |
cd23767 |
IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory ... |
425-455 |
2.72e-04 |
|
IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory complex protein 10 (DRC10), belongs to the IQ motif-containing protein family which contains a C-terminal conserved IQ motif domain and two coiled-coil domains. The IQ motif ([ILV]QxxxRxxxx[RK]), where x stands for any amino-acid residue, interacts with calmodulin (CaM) in a calcium-independent manner and is present in proteins with a wide diversity of biological functions. The IQCD protein was found to primarily accumulate in the acrosome area of round and elongating spermatids of the testis during late stage of spermiogenesis and was then localized to the acrosome and tail regions of mature spermatozoa. The expression of IQCD follows the trajectory of acrosome development during spermatogenesis. IQCD is associated with neuroblastoma and neurodegenerative diseases, and is reported to interact with the nuclear retinoid X receptor in the presence of 9-cis-retinoic acid, thereby activating the transcriptional activity of the receptor.
Pssm-ID: 467745 [Multi-domain] Cd Length: 37 Bit Score: 38.68 E-value: 2.72e-04
10 20 30
....*....|....*....|....*....|.
gi 1720415018 425 EKREAALDEAATVLQAAFRGHLARSKLVRSK 455
Cdd:cd23767 2 EEELQRMNRAATLIQALWRGYKVRKELKKKK 32
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
76-436 |
2.85e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.26 E-value: 2.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415018 76 REKEDMYDEIIELKKSLHMQKSDVDLMRTKLRRLEEENSRKDRQIEQLLDpsRGPDFVRTLAEKKPDTGWV---ITGLKQ 152
Cdd:PRK02224 272 REREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELED--RDEELRDRLEECRVAAQAHneeAESLRE 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415018 153 RIFRLEQQCKEKDNTINKLQTDmkttnLEEMRIAMETYYEEIHRLQTLLASSEAtgkkpmvekklgvkrqkkmssALLNL 232
Cdd:PRK02224 350 DADDLEERAEELREEAAELESE-----LEEAREAVEDRREEIEELEEEIEELRE---------------------RFGDA 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415018 233 TRSVQELTEENQSLKEDLDRmlsnsptiskikgygdwskprLLRRIAELEKKVSSSESPKQSTSELVNPNplvrspsnis 312
Cdd:PRK02224 404 PVDLGNAEDFLEELREERDE---------------------LREREAELEATLRTARERVEEAEALLEAG---------- 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415018 313 vqKQPKGDQSPEDLPKVAPCEEQEhlqGTVKSLREELGALQEQL--LEKDLE-----------MKQLLQSKIDLEKELET 379
Cdd:PRK02224 453 --KCPECGQPVEGSPHVETIEEDR---ERVEELEAELEDLEEEVeeVEERLEraedlveaedrIERLEERREDLEELIAE 527
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1720415018 380 AREGEKGRQEQEQALREEVEALTKKCQELEEAKREEknsfvavtHEKREAALDEAAT 436
Cdd:PRK02224 528 RRETIEEKRERAEELRERAAELEAEAEEKREAAAEA--------EEEAEEAREEVAE 576
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
333-441 |
1.43e-03 |
|
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: 41.97 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415018 333 EEQEHLQGTVKSLREELGALQEQLLEKDLEMKQL-------------LQSKI-DLEKELETAREGEKGRQEQEQALREEV 398
Cdd:TIGR02168 246 EELKEAEEELEELTAELQELEEKLEELRLEVSELeeeieelqkelyaLANEIsRLEQQKQILRERLANLERQLEELEAQL 325
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1720415018 399 EALTKKCQELEE--AKREEKNSFVAVTHEKREAALDEAATVLQAA 441
Cdd:TIGR02168 326 EELESKLDELAEelAELEEKLEELKEELESLEAELEELEAELEEL 370
|
|
| PLN03209 |
PLN03209 |
translocon at the inner envelope of chloroplast subunit 62; Provisional |
449-688 |
1.63e-03 |
|
translocon at the inner envelope of chloroplast subunit 62; Provisional
Pssm-ID: 178748 [Multi-domain] Cd Length: 576 Bit Score: 41.45 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415018 449 SKLVRSKVPDSRSPSLPGLLSPLNQSSPAPrvlspisPAEENPTQEEAVIviQSILRGYLAQarfiasccreiaassqre 528
Cdd:PLN03209 325 SQRVPPKESDAADGPKPVPTKPVTPEAPSP-------PIEEEPPQPKAVV--PRPLSPYTAY------------------ 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415018 529 tVSLTPSGSASPPSlraspewgPSGKNSEASSGEAAKDEDEAEEPPDLQPYSGVIRKELCASEELRETSASEPA------ 602
Cdd:PLN03209 378 -EDLKPPTSPIPTP--------PSSSPASSKSVDAVAKPAEPDVVPSPGSASNVPEVEPAQVEAKKTRPLSPYAryedlk 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415018 603 -PSVPySAQGGHGDCPSSSSLEAVPSMKDamceersSSPRSAGPSLAEPSPPELQPLSPPPVEDICSDDSDDIIFSPFLP 681
Cdd:PLN03209 449 pPTSP-SPTAPTGVSPSVSSTSSVPAVPD-------TAPATAATDAAAPPPANMRPLSPYAVYDDLKPPTSPSPAAPVGK 520
|
....*..
gi 1720415018 682 RKKSPSP 688
Cdd:PLN03209 521 VAPSSTN 527
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
214-440 |
2.09e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.54 E-value: 2.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415018 214 EKKLGVKRQKKMSSALLNLTRSVQELTEENQSLKEDLDRMLSNSPTISKIKGYGDwskprLLRRIAELEkkvsssespkq 293
Cdd:COG3206 213 EAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQ-----LRAQLAELE----------- 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415018 294 stselvnpnplvrspSNISVQKQPKGDQSPEdlpkvapceeqehlqgtVKSLREELGALQEQLLEkdlEMKQLLQSkidL 373
Cdd:COG3206 277 ---------------AELAELSARYTPNHPD-----------------VIALRAQIAALRAQLQQ---EAQRILAS---L 318
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415018 374 EKELETAREGEKGRQEQEQALREEVEALTKKCQELEEAKRE---EKNSFVAVTHEKREAALDEAATVLQA 440
Cdd:COG3206 319 EAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREvevARELYESLLQRLEEARLAEALTVGNV 388
|
|
| IQ |
smart00015 |
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ... |
431-451 |
2.53e-03 |
|
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln residues.
Pssm-ID: 197470 [Multi-domain] Cd Length: 23 Bit Score: 35.76 E-value: 2.53e-03
|
| IQ |
pfam00612 |
IQ calmodulin-binding motif; Calmodulin-binding motif. |
433-451 |
4.84e-03 |
|
IQ calmodulin-binding motif; Calmodulin-binding motif.
Pssm-ID: 459869 Cd Length: 21 Bit Score: 34.99 E-value: 4.84e-03
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
353-439 |
8.05e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 39.42 E-value: 8.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415018 353 QEQLLEKDLEMKQLLQSKIDLEKELET-AREGEKGRQEQEQaLREEVEaltKKCQELEEAKREEKNSFVAVTHEKREAAL 431
Cdd:PRK00409 508 KKLIGEDKEKLNELIASLEELERELEQkAEEAEALLKEAEK-LKEELE---EKKEKLQEEEDKLLEEAEKEAQQAIKEAK 583
|
....*...
gi 1720415018 432 DEAATVLQ 439
Cdd:PRK00409 584 KEADEIIK 591
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
333-441 |
2.52e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.17 E-value: 2.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415018 333 EEQEHLQGTVKSLREELGALQEQLLEKDLEMKQLLQSKIDLEKELETAREGEKGRQEQEQALREEVEALTKKCQELEEAK 412
Cdd:COG1196 260 AELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEEL 339
|
90 100
....*....|....*....|....*....
gi 1720415018 413 REEKNSfVAVTHEKREAALDEAATVLQAA 441
Cdd:COG1196 340 EELEEE-LEEAEEELEEAEAELAEAEEAL 367
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
333-441 |
1.86e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.48 E-value: 1.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415018 333 EEQEHLQGTVKSLREELGALQEQLLEKDLEMKQLLQSKIDLEKELETAREGEKGRQEQEQALREEVEALTKKCQELEEAK 412
Cdd:COG1196 295 AELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL 374
|
90 100
....*....|....*....|....*....
gi 1720415018 413 REEKNSFVAVTHEKREAALDEAATVLQAA 441
Cdd:COG1196 375 AEAEEELEELAEELLEALRAAAELAAQLE 403
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
333-443 |
3.10e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 50.71 E-value: 3.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415018 333 EEQEHLQGTVKSLREELGALQEQLLEKDLEMKQLLQSKIDLEKELETAREGEKGRQEQEQALREEVEALTKKCQELEEAK 412
Cdd:COG1196 281 LELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAEL 360
|
90 100 110
....*....|....*....|....*....|.
gi 1720415018 413 REEKNSFVAVThEKREAALDEAATVLQAAFR 443
Cdd:COG1196 361 AEAEEALLEAE-AELAEAEEELEELAEELLE 390
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
84-441 |
3.59e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 50.44 E-value: 3.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415018 84 EIIELKKSLHMQKSDVDLMRTKLRRLEEENSRKDRQIEQLLDpsrgpdfvrtlaeKKPDTGWVITGLKQRIFRLEQQCKE 163
Cdd:TIGR02168 678 EIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRK-------------ELEELSRQISALRKDLARLEAEVEQ 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415018 164 KDNTINKLQTDmkttnLEEMRIAMETYYEEIHRLQTLLASSEAtgkkpmvEKKLGVKRQKKMSSALLNLTRSVQELTEEN 243
Cdd:TIGR02168 745 LEERIAQLSKE-----LTELEAEIEELEERLEEAEEELAEAEA-------EIEELEAQIEQLKEELKALREALDELRAEL 812
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415018 244 QSLKEDLDRMLSNSPTISKIKGYGDWSKPRLLRRIAELEKKVSS--------SESPKQSTSELVnpnplvrSPSNISVQK 315
Cdd:TIGR02168 813 TLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESlaaeieelEELIEELESELE-------ALLNERASL 885
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415018 316 QPKGDQSPEDLPKVApcEEQEHLQGTVKSLREELGALQEQLLEKDLEMKQL------LQSKI--DLEKELETAREGEKGR 387
Cdd:TIGR02168 886 EEALALLRSELEELS--EELRELESKRSELRRELEELREKLAQLELRLEGLevridnLQERLseEYSLTLEEAEALENKI 963
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720415018 388 QEQEQALREEVEALTKKCQEL-------EEAKREEKNSFVAVTHEKREaaLDEAATVLQAA 441
Cdd:TIGR02168 964 EDDEEEARRRLKRLENKIKELgpvnlaaIEEYEELKERYDFLTAQKED--LTEAKETLEEA 1022
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
129-411 |
9.24e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 49.28 E-value: 9.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415018 129 GPDFVRTLAEKKPDTGwvITGLKQRIFRLEQQCKEKDNTINKLQTdmkttNLEEMRIAMETYYEEIHRLQTLLASSEatg 208
Cdd:TIGR02168 656 RPGGVITGGSAKTNSS--ILERRREIEELEEKIEELEEKIAELEK-----ALAELRKELEELEEELEQLRKELEELS--- 725
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415018 209 KKPMVEKKLGVKRQKKMSSALLNLTRSVQELTEENQSLKEDLDRMLSNSPTISkikgygdwskpRLLRRIAELEKKVS-S 287
Cdd:TIGR02168 726 RQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELA-----------EAEAEIEELEAQIEqL 794
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415018 288 SESPKQSTSELVNPNPLVRSpSNISVQKQPKGDQSPEDlpKVAPCEEQ--------EHLQGTVKSLREELGALQEQLLEK 359
Cdd:TIGR02168 795 KEELKALREALDELRAELTL-LNEEAANLRERLESLER--RIAATERRledleeqiEELSEDIESLAAEIEELEELIEEL 871
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1720415018 360 DLEMKQLLQSKIDLEKELETAREGEKGRQEQEQALREEVEALTKKCQELEEA 411
Cdd:TIGR02168 872 ESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREK 923
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
150-438 |
1.01e-05 |
|
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: 48.90 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415018 150 LKQRIFRLEQQC------KEKDNTINKLQTDMKTTNLEEMRIAMETYYEEIHRLQTLLAssEATGKKPMVEKKLGVKRqk 223
Cdd:TIGR02168 198 LERQLKSLERQAekaeryKELKAELRELELALLVLRLEELREELEELQEELKEAEEELE--ELTAELQELEEKLEELR-- 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415018 224 kmsSALLNLTRSVQELTEENQSLKEDLDRmlsnsptiskikgygdwskprLLRRIAELEKKVSSsespkqstselvnpnp 303
Cdd:TIGR02168 274 ---LEVSELEEEIEELQKELYALANEISR---------------------LEQQKQILRERLAN---------------- 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415018 304 LVRSPSNISVQKQPKGDQSPEDLPKVAPCEEQehlqgtVKSLREELGALQEQLLEKDLEMKQLLQSKIDLEKELETAREG 383
Cdd:TIGR02168 314 LERQLEELEAQLEELESKLDELAEELAELEEK------LEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSK 387
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1720415018 384 EKGRQEQEQALREEVEALTKKCQELEEAKREEKNSFVAVTHEKREAALDEAATVL 438
Cdd:TIGR02168 388 VAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAEL 442
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
333-458 |
1.24e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 47.23 E-value: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415018 333 EEQEHLQGTVKSLREELGALQEQLLEKDLEMKQL------LQSKID-----------------LEKELETAREGEKGRQE 389
Cdd:COG1579 31 AELAELEDELAALEARLEAAKTELEDLEKEIKRLeleieeVEARIKkyeeqlgnvrnnkeyeaLQKEIESLKRRISDLED 110
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720415018 390 QEQALREEVEALTKKCQELEEAKREEKNSFvavthEKREAALDEAATVLQAAFRGHLARSKLVRSKVPD 458
Cdd:COG1579 111 EILELMERIEELEEELAELEAELAELEAEL-----EEKKAELDEELAELEAELEELEAEREELAAKIPP 174
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
333-441 |
1.26e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.78 E-value: 1.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415018 333 EEQEHLQGTVKSLREELGALQEQLLEKDLEMKQLLQSKIDLEKELETAREGEKGRQEQEQALREEVEALTKKCQELEEAK 412
Cdd:COG1196 351 EELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEAL 430
|
90 100
....*....|....*....|....*....
gi 1720415018 413 REEKNSFVAVTHEKREAALDEAATVLQAA 441
Cdd:COG1196 431 AELEEEEEEEEEALEEAAEEEAELEEEEE 459
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
333-441 |
1.51e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.39 E-value: 1.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415018 333 EEQEHLQGTVKSLREELGALQEQLLEKDLEMKQLLQSKIDLEKELETAREGEKGRQEQEQALREEVEALTKkcQELEEAK 412
Cdd:COG1196 323 EELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR--AAAELAA 400
|
90 100
....*....|....*....|....*....
gi 1720415018 413 REEKNSFVAVTHEKREAALDEAATVLQAA 441
Cdd:COG1196 401 QLEELEEAEEALLERLERLEEELEELEEA 429
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
316-414 |
1.53e-05 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 48.32 E-value: 1.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415018 316 QPKGDQSPEDLPKVAPCEEQEH------LQGTVKSLREELGALQEQLLEKDLEMKqllqskiDLEKELETAR--EGEKGR 387
Cdd:COG2433 390 LPEEEPEAEREKEHEERELTEEeeeirrLEEQVERLEAEVEELEAELEEKDERIE-------RLERELSEARseERREIR 462
|
90 100
....*....|....*....|....*...
gi 1720415018 388 QEQE-QALREEVEALTKKCQELEEAKRE 414
Cdd:COG2433 463 KDREiSRLDREIERLERELEEERERIEE 490
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
333-441 |
3.03e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 47.62 E-value: 3.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415018 333 EEQEHLQGTVKSLREELGALQEQLLEKDLEMKQLLQSKIDLEKELETAREGEKGRQEQEQALREEVEALTKKCQELEEAK 412
Cdd:COG1196 302 QDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEEL 381
|
90 100
....*....|....*....|....*....
gi 1720415018 413 REEKNSFVAVTHEKREAALDEAATVLQAA 441
Cdd:COG1196 382 EELAEELLEALRAAAELAAQLEELEEAEE 410
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
73-443 |
7.41e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 46.26 E-value: 7.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415018 73 SVYREKEDMY-DEIIELKKSLHMQKSDVDLMRTKLRRLEEENSRKDRQIEQLLDPSRGPDFVRTLAEKKPDTGW-VITGL 150
Cdd:pfam15921 331 SELREAKRMYeDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWdRDTGN 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415018 151 KQRIFRLEQQCKEKDNTINKLQTDMKTT------NLEEMRIAMETYYEEIHRLQTLLASSEATgkKPMVEKKLGVKRQKK 224
Cdd:pfam15921 411 SITIDHLRRELDDRNMEVQRLEALLKAMksecqgQMERQMAAIQGKNESLEKVSSLTAQLEST--KEMLRKVVEELTAKK 488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415018 225 MSsaLLNLTRSVQELTeenQSLKEDLDRMLSNSPTISKIKGygdwskpRLLRRIAELEKKVSSSESPKQSTSELvnpnpl 304
Cdd:pfam15921 489 MT--LESSERTVSDLT---ASLQEKERAIEATNAEITKLRS-------RVDLKLQELQHLKNEGDHLRNVQTEC------ 550
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415018 305 vrspSNISVQKQPKgDQSPEDLPKvaPCEEQEHLQG----TVKSLREELGALQEQLLEKDLEMKQLlqsKIDLEKELETA 380
Cdd:pfam15921 551 ----EALKLQMAEK-DKVIEILRQ--QIENMTQLVGqhgrTAGAMQVEKAQLEKEINDRRLELQEF---KILKDKKDAKI 620
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720415018 381 REGEKGRQEQEQALREEVEALTKKCQELEEAKREEKNSFVAVTHEKREA-ALDEAATVLQAAFR 443
Cdd:pfam15921 621 RELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELnSLSEDYEVLKRNFR 684
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
342-450 |
1.37e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.29 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415018 342 VKSLREELGALQEQL--LEK-DLEMKQLLQSKIDLEKELETAREGEKGRQEQEQALREEVEALTKKCQELEEAKREEKNS 418
Cdd:COG4913 663 VASAEREIAELEAELerLDAsSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDL 742
|
90 100 110
....*....|....*....|....*....|....*..
gi 1720415018 419 FVAVTHEK-----REAALDEAATVLQAAFRGHLARSK 450
Cdd:COG4913 743 ARLELRALleerfAAALGDAVERELRENLEERIDALR 779
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
333-441 |
1.60e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.93 E-value: 1.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415018 333 EEQEHLQGTVKSLREELGALQEQLLEKDLEMKQLLQSKIDLEKELETAREGEKGRQEQEQALREEVEALTKKCQELEEAK 412
Cdd:COG1196 274 LELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEEL 353
|
90 100
....*....|....*....|....*....
gi 1720415018 413 REEKNSFVAVTHEKREAALDEAATVLQAA 441
Cdd:COG1196 354 EEAEAELAEAEEALLEAEAELAEAEEELE 382
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
333-429 |
2.00e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.12 E-value: 2.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415018 333 EEQEHLQGTVKSLREELGALQEQLLEKDLEMKQLLQSKIDLEKELETAREGEKGRQEQEQALREEVEALTKKCQELEEAK 412
Cdd:COG4372 59 EELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQI 138
|
90
....*....|....*..
gi 1720415018 413 REEKNSFVAVTHEKREA 429
Cdd:COG4372 139 AELQSEIAEREEELKEL 155
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
76-401 |
2.12e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 44.43 E-value: 2.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415018 76 REKEDMYDEIIELKKSLHMQKSDVDlmrTKLRRLEEENSRKDRQIEQLLDPSRGPDfvRTLAEKKPDTGWVITGLKQRIF 155
Cdd:pfam10174 411 RDKDKQLAGLKERVKSLQTDSSNTD---TALTTLEEALSEKERIIERLKEQRERED--RERLEELESLKKENKDLKEKVS 485
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415018 156 RLEQQCKEKDNTINKLQTDM---------KTTNLEEMRIAMETYYEEIHRLQTLLASSEatgkkpmvEKKLGVKRQKKMS 226
Cdd:pfam10174 486 ALQPELTEKESSLIDLKEHAsslassglkKDSKLKSLEIAVEQKKEECSKLENQLKKAH--------NAEEAVRTNPEIN 557
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415018 227 SALLNLTRSVQELTEENQSLKEDLDRMLSNSPTISKIKGYGDwskprllRRIAELEKKVSSSESPKQSTSELVNPNPLVR 306
Cdd:pfam10174 558 DRIRLLEQEVARYKEESGKAQAEVERLLGILREVENEKNDKD-------KKIAELESLTLRQMKEQNKKVANIKHGQQEM 630
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415018 307 SPSNISVQKQPKgdqSPEDLPKVAPCEEQ-EHLQGTVKSLREELGAL-------QEQLLEKD-----------------L 361
Cdd:pfam10174 631 KKKGAQLLEEAR---RREDNLADNSQQLQlEELMGALEKTRQELDATkarlsstQQSLAEKDghltnlraerrkqleeiL 707
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1720415018 362 EMKQ-LLQSKIDlEKE-----LETAREGEKGRQEQEQALREEVEAL 401
Cdd:pfam10174 708 EMKQeALLAAIS-EKDanialLELSSSKKKKTQEEVMALKREKDRL 752
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
82-417 |
2.45e-04 |
|
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: 44.66 E-value: 2.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415018 82 YDEIIELKKSLHMQKSDVDLMRTKLRRLEEENSRKDRQIEQLLDpsrgpdFVRTLAEKKPDTGWVITGLKQRIFRLEQQC 161
Cdd:TIGR02168 231 VLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRL------EVSELEEEIEELQKELYALANEISRLEQQK 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415018 162 KEKDNTINKLQTDMKTTNLEemriaMETYYEEIHRLQTLLASSEATGKKPMVEKKLGVKRQKKMSSALLNLTRSVQELTE 241
Cdd:TIGR02168 305 QILRERLANLERQLEELEAQ-----LEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEE 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415018 242 ENQSLKEDLDRMLSNSPTISKikgygdwskprllrRIAELEKKVSSSESpkqstselvnpnplvrspsnisvqKQPKGDQ 321
Cdd:TIGR02168 380 QLETLRSKVAQLELQIASLNN--------------EIERLEARLERLED------------------------RRERLQQ 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415018 322 SPEDLPKVAPCEEQEHLQGTVKSLREELGALQEQLlekdlemKQLLQSKIDLEKELETAREGEKGRQEQEQALREEVEAL 401
Cdd:TIGR02168 422 EIEELLKKLEEAELKELQAELEELEEELEELQEEL-------ERLEEALEELREELEEAEQALDAAERELAQLQARLDSL 494
|
330
....*....|....*.
gi 1720415018 402 TKKCQELEEAKREEKN 417
Cdd:TIGR02168 495 ERLQENLEGFSEGVKA 510
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
69-428 |
2.67e-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: 44.29 E-value: 2.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415018 69 VSGTSVY-REKEDMYDEIIELKKSLHMQKSDVDLMRTKLRRLEEENSRKDRQIEqLLDPSRGPDFVRTLAEKK------- 140
Cdd:TIGR02169 162 IAGVAEFdRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQA-LLKEKREYEGYELLKEKEalerqke 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415018 141 ------PDTGWVITGLKQRIFRLEQQCKEKDNTINKLQTDMKTTNLEEMRiameTYYEEIHRLQTLLASSEATGKKPMVE 214
Cdd:TIGR02169 241 aierqlASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQL----RVKEKIGELEAEIASLERSIAEKERE 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415018 215 KKLGVKRQKKMSSALLNLTRSVQELTEENQSLKEDLDRMLSNspTISKIKGYGDwskprLLRRIAELEKK----VSSSES 290
Cdd:TIGR02169 317 LEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEE--YAELKEELED-----LRAELEEVDKEfaetRDELKD 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415018 291 PKQSTSELVNP-NPLVRSPSNISVQKQPKGdqspedlpkvapcEEQEHLQGTVKSLREELGALQEQLLEKDLEMKQLLQS 369
Cdd:TIGR02169 390 YREKLEKLKREiNELKRELDRLQEELQRLS-------------EELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWK 456
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720415018 370 KIDLEKELETAREGEKGRQEQEQALREEVEALTKKCQELE---EAKREEKNSFVAVTHEKRE 428
Cdd:TIGR02169 457 LEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEaqaRASEERVRGGRAVEEVLKA 518
|
|
| IQCD |
cd23767 |
IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory ... |
425-455 |
2.72e-04 |
|
IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory complex protein 10 (DRC10), belongs to the IQ motif-containing protein family which contains a C-terminal conserved IQ motif domain and two coiled-coil domains. The IQ motif ([ILV]QxxxRxxxx[RK]), where x stands for any amino-acid residue, interacts with calmodulin (CaM) in a calcium-independent manner and is present in proteins with a wide diversity of biological functions. The IQCD protein was found to primarily accumulate in the acrosome area of round and elongating spermatids of the testis during late stage of spermiogenesis and was then localized to the acrosome and tail regions of mature spermatozoa. The expression of IQCD follows the trajectory of acrosome development during spermatogenesis. IQCD is associated with neuroblastoma and neurodegenerative diseases, and is reported to interact with the nuclear retinoid X receptor in the presence of 9-cis-retinoic acid, thereby activating the transcriptional activity of the receptor.
Pssm-ID: 467745 [Multi-domain] Cd Length: 37 Bit Score: 38.68 E-value: 2.72e-04
10 20 30
....*....|....*....|....*....|.
gi 1720415018 425 EKREAALDEAATVLQAAFRGHLARSKLVRSK 455
Cdd:cd23767 2 EEELQRMNRAATLIQALWRGYKVRKELKKKK 32
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
76-436 |
2.85e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.26 E-value: 2.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415018 76 REKEDMYDEIIELKKSLHMQKSDVDLMRTKLRRLEEENSRKDRQIEQLLDpsRGPDFVRTLAEKKPDTGWV---ITGLKQ 152
Cdd:PRK02224 272 REREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELED--RDEELRDRLEECRVAAQAHneeAESLRE 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415018 153 RIFRLEQQCKEKDNTINKLQTDmkttnLEEMRIAMETYYEEIHRLQTLLASSEAtgkkpmvekklgvkrqkkmssALLNL 232
Cdd:PRK02224 350 DADDLEERAEELREEAAELESE-----LEEAREAVEDRREEIEELEEEIEELRE---------------------RFGDA 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415018 233 TRSVQELTEENQSLKEDLDRmlsnsptiskikgygdwskprLLRRIAELEKKVSSSESPKQSTSELVNPNplvrspsnis 312
Cdd:PRK02224 404 PVDLGNAEDFLEELREERDE---------------------LREREAELEATLRTARERVEEAEALLEAG---------- 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415018 313 vqKQPKGDQSPEDLPKVAPCEEQEhlqGTVKSLREELGALQEQL--LEKDLE-----------MKQLLQSKIDLEKELET 379
Cdd:PRK02224 453 --KCPECGQPVEGSPHVETIEEDR---ERVEELEAELEDLEEEVeeVEERLEraedlveaedrIERLEERREDLEELIAE 527
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1720415018 380 AREGEKGRQEQEQALREEVEALTKKCQELEEAKREEknsfvavtHEKREAALDEAAT 436
Cdd:PRK02224 528 RRETIEEKRERAEELRERAAELEAEAEEKREAAAEA--------EEEAEEAREEVAE 576
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
273-422 |
3.06e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.99 E-value: 3.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415018 273 RLLRRIAELEKKVSSSESPKQSTSELVNPNPLVRSPSNISVQKQPKGDQSPEDLPKVAP----CEEQEHLQGTVKSLREE 348
Cdd:COG4717 99 ELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEElrelEEELEELEAELAELQEE 178
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720415018 349 LGALQEQL-LEKDLEMKQLLQSKIDLEKELETAREGEKGRQEQEQALREEVEALTKKCQELEEAKREEKNSFVAV 422
Cdd:COG4717 179 LEELLEQLsLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLL 253
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
147-418 |
3.55e-04 |
|
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: 43.86 E-value: 3.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415018 147 ITGLKQRIFRLEQQCKEKDNTINKLQTDMKTTNLEEmriamETYYEEIHRLQTLLASSEATGKKPMVEKKLGVKRQKKMS 226
Cdd:TIGR04523 77 IKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEI-----KNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKE 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415018 227 SALLNLTRSVQELTEENQSLKEDLDRMLSNsptISKIKGYGDWSKPRLLRriaeLEKKVSSSESPKQSTSELVNP-NPLV 305
Cdd:TIGR04523 152 KELEKLNNKYNDLKKQKEELENELNLLEKE---KLNIQKNIDKIKNKLLK----LELLLSNLKKKIQKNKSLESQiSELK 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415018 306 RSPSNISVQKQPKGDQSPEDLPKVAPCEEQehlqgtVKSLREELGALQEQLLEKDLEMKQLLQSKIDLEKELETAR-EGE 384
Cdd:TIGR04523 225 KQNNQLKDNIEKKQQEINEKTTEISNTQTQ------LNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKsEIS 298
|
250 260 270
....*....|....*....|....*....|....*
gi 1720415018 385 KGRQEQEQALREEV-EALTKKCQELEEAKREEKNS 418
Cdd:TIGR04523 299 DLNNQKEQDWNKELkSELKNQEKKLEEIQNQISQN 333
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
343-441 |
3.75e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.77 E-value: 3.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415018 343 KSLREELGALQEQLLEKDLEMKQLLQSKIDLEKELETAREGEKGRQEQEQALREEVEALTKKCQELEEAKR--EEKNSFV 420
Cdd:COG1196 235 RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIArlEERRREL 314
|
90 100
....*....|....*....|.
gi 1720415018 421 AVTHEKREAALDEAATVLQAA 441
Cdd:COG1196 315 EERLEELEEELAELEEELEEL 335
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
76-416 |
4.63e-04 |
|
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: 43.47 E-value: 4.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415018 76 REKEDMYDEIIELKKSLHMQKSDVDLMRTKLRRLEEENSRKDRQIEQLLDPsrgpdfVRTLAEKKPDTGWVITGLKQRIF 155
Cdd:TIGR04523 321 KKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNE------IEKLKKENQSYKQEIKNLESQIN 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415018 156 RLEQQCKEKDNTINKLQTDMKTTNLEEmriamETYYEEIHRLQTLLASSEATGK---KPMVEKKLGVKRqkkmssalLNL 232
Cdd:TIGR04523 395 DLESKIQNQEKLNQQKDEQIKKLQQEK-----ELLEKEIERLKETIIKNNSEIKdltNQDSVKELIIKN--------LDN 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415018 233 TRSVQElteenQSLKEdldrmLSNSptISKIKGYGDWSKprllrriAELEKKVSSSESPKQSTSELVNPNPLVRSPSNIS 312
Cdd:TIGR04523 462 TRESLE-----TQLKV-----LSRS--INKIKQNLEQKQ-------KELKSKEKELKKLNEEKKELEEKVKDLTKKISSL 522
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415018 313 VQKQpkgdqspEDLPKVAPCEEQE--HLQGTVKSLREEL--GALQEQLLEKDLEMKQLLQSKIDLEKELETAREGEKGRQ 388
Cdd:TIGR04523 523 KEKI-------EKLESEKKEKESKisDLEDELNKDDFELkkENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKE 595
|
330 340 350
....*....|....*....|....*....|..
gi 1720415018 389 EQEQALREEVEALTKKC----QELEEAKREEK 416
Cdd:TIGR04523 596 KEKKDLIKEIEEKEKKIssleKELEKAKKENE 627
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
333-443 |
5.51e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.39 E-value: 5.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415018 333 EEQEHLQGTVKSLREELGALQEQLLEKDLEMKQLLQSKIDLEKELETAREGEKGRQEQEQALREEVEALTKKCQELEE-- 410
Cdd:COG1196 239 AELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEErl 318
|
90 100 110
....*....|....*....|....*....|....*.
gi 1720415018 411 ---AKREEKNSFVAVTHEKREAALDEAATVLQAAFR 443
Cdd:COG1196 319 eelEEELAELEEELEELEEELEELEEELEEAEEELE 354
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
362-456 |
6.28e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 43.15 E-value: 6.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415018 362 EMKQLLQSKIDLEKELETA-REGEKGRQEQEQALREEVEALTKKCQELEEAKREEKNSFVAVTH-----EKREAALDEAA 435
Cdd:COG0542 412 ELDELERRLEQLEIEKEALkKEQDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQElkeelEQRYGKIPELE 491
|
90 100
....*....|....*....|.
gi 1720415018 436 TVLQAAFRGHLARSKLVRSKV 456
Cdd:COG0542 492 KELAELEEELAELAPLLREEV 512
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
333-441 |
1.43e-03 |
|
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: 41.97 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415018 333 EEQEHLQGTVKSLREELGALQEQLLEKDLEMKQL-------------LQSKI-DLEKELETAREGEKGRQEQEQALREEV 398
Cdd:TIGR02168 246 EELKEAEEELEELTAELQELEEKLEELRLEVSELeeeieelqkelyaLANEIsRLEQQKQILRERLANLERQLEELEAQL 325
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1720415018 399 EALTKKCQELEE--AKREEKNSFVAVTHEKREAALDEAATVLQAA 441
Cdd:TIGR02168 326 EELESKLDELAEelAELEEKLEELKEELESLEAELEELEAELEEL 370
|
|
| PLN03209 |
PLN03209 |
translocon at the inner envelope of chloroplast subunit 62; Provisional |
449-688 |
1.63e-03 |
|
translocon at the inner envelope of chloroplast subunit 62; Provisional
Pssm-ID: 178748 [Multi-domain] Cd Length: 576 Bit Score: 41.45 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415018 449 SKLVRSKVPDSRSPSLPGLLSPLNQSSPAPrvlspisPAEENPTQEEAVIviQSILRGYLAQarfiasccreiaassqre 528
Cdd:PLN03209 325 SQRVPPKESDAADGPKPVPTKPVTPEAPSP-------PIEEEPPQPKAVV--PRPLSPYTAY------------------ 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415018 529 tVSLTPSGSASPPSlraspewgPSGKNSEASSGEAAKDEDEAEEPPDLQPYSGVIRKELCASEELRETSASEPA------ 602
Cdd:PLN03209 378 -EDLKPPTSPIPTP--------PSSSPASSKSVDAVAKPAEPDVVPSPGSASNVPEVEPAQVEAKKTRPLSPYAryedlk 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415018 603 -PSVPySAQGGHGDCPSSSSLEAVPSMKDamceersSSPRSAGPSLAEPSPPELQPLSPPPVEDICSDDSDDIIFSPFLP 681
Cdd:PLN03209 449 pPTSP-SPTAPTGVSPSVSSTSSVPAVPD-------TAPATAATDAAAPPPANMRPLSPYAVYDDLKPPTSPSPAAPVGK 520
|
....*..
gi 1720415018 682 RKKSPSP 688
Cdd:PLN03209 521 VAPSSTN 527
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
214-440 |
2.09e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.54 E-value: 2.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415018 214 EKKLGVKRQKKMSSALLNLTRSVQELTEENQSLKEDLDRMLSNSPTISKIKGYGDwskprLLRRIAELEkkvsssespkq 293
Cdd:COG3206 213 EAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQ-----LRAQLAELE----------- 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415018 294 stselvnpnplvrspSNISVQKQPKGDQSPEdlpkvapceeqehlqgtVKSLREELGALQEQLLEkdlEMKQLLQSkidL 373
Cdd:COG3206 277 ---------------AELAELSARYTPNHPD-----------------VIALRAQIAALRAQLQQ---EAQRILAS---L 318
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415018 374 EKELETAREGEKGRQEQEQALREEVEALTKKCQELEEAKRE---EKNSFVAVTHEKREAALDEAATVLQA 440
Cdd:COG3206 319 EAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREvevARELYESLLQRLEEARLAEALTVGNV 388
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
76-419 |
2.12e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 41.54 E-value: 2.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415018 76 REKEDMYDEIielkKSLHMQKSDvdlMRTKLRRLEEENSRKDRQIEQLLDPSRgpdfvrtLAEKKpdtgwvITGLKQRIF 155
Cdd:TIGR04523 377 KENQSYKQEI----KNLESQIND---LESKIQNQEKLNQQKDEQIKKLQQEKE-------LLEKE------IERLKETII 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415018 156 RLEQQCKEKDNTINKLQTDMKttNLEEMRIAMETYYEEIHRLQTLLASSEATGKKPMVEKKlgvkrqkkmsSALLNLTRS 235
Cdd:TIGR04523 437 KNNSEIKDLTNQDSVKELIIK--NLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKE----------KELKKLNEE 504
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415018 236 VQELTEENQSLKEDldrmlsNSPTISKIKgygdwskpRLLRRIAELEKKVSSSESPKQSTSELVNPNPLVRSPSNISvQK 315
Cdd:TIGR04523 505 KKELEEKVKDLTKK------ISSLKEKIE--------KLESEKKEKESKISDLEDELNKDDFELKKENLEKEIDEKN-KE 569
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415018 316 QPKGDQSPEDLPKvapceEQEHLQGTVKSLREELGALQEQLLEKDlemkqllQSKIDLEKELETAREGEKGRQEQEQALR 395
Cdd:TIGR04523 570 IEELKQTQKSLKK-----KQEEKQELIDQKEKEKKDLIKEIEEKE-------KKISSLEKELEKAKKENEKLSSIIKNIK 637
|
330 340
....*....|....*....|....
gi 1720415018 396 EEVEALTKKCQELEEAKREEKNSF 419
Cdd:TIGR04523 638 SKKNKLKQEVKQIKETIKEIRNKW 661
|
|
| IQ |
smart00015 |
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ... |
431-451 |
2.53e-03 |
|
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln residues.
Pssm-ID: 197470 [Multi-domain] Cd Length: 23 Bit Score: 35.76 E-value: 2.53e-03
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
338-448 |
3.02e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.91 E-value: 3.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415018 338 LQGTVKSLREELGALQEQL--LEKDLEMKQLLQSKIDLEKELETAREGEKGRQEQEQALREEVEALTKKCQELEEAKREe 415
Cdd:COG4717 93 LQEELEELEEELEELEAELeeLREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAE- 171
|
90 100 110
....*....|....*....|....*....|...
gi 1720415018 416 knsfvavtHEKREAALDEAATVLQAAFRGHLAR 448
Cdd:COG4717 172 --------LAELQEELEELLEQLSLATEEELQD 196
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
103-450 |
3.06e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 41.11 E-value: 3.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415018 103 RTKLRRLEEENSRKDRQIEQLLDPSRGpdfvRTLAEKKPDTGWVITGLKQ-------RIFRLEQ-QCKE--KDNTINKLQ 172
Cdd:TIGR00618 92 RTLRCTRSHRKTEQPEQLYLEQKKGRG----RILAAKKSETEEVIHDLLKldyktftRVVLLPQgEFAQflKAKSKEKKE 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415018 173 TDMKTTNLEEMR-IAMETYyeEIHRlqTLLASSEATGKKPMVEKKLGVKRQKKMSSALLNLTRSVQELTEENQSLKEdld 251
Cdd:TIGR00618 168 LLMNLFPLDQYTqLALMEF--AKKK--SLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQ--- 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415018 252 rmlsnsptiskikgygdwSKPRLLRRIAELEKKVSSSESPKQSTSELVNPNPLVRSPSNisvqKQPKGDQSPEDLPKVap 331
Cdd:TIGR00618 241 ------------------SHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEE----TQERINRARKAAPLA-- 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415018 332 cEEQEHLQGTVKSLREELGALQEQ--LLEKDL--------------EMKQLLQSKIDLEKELETAREGEKGRQEQEQALR 395
Cdd:TIGR00618 297 -AHIKAVTQIEQQAQRIHTELQSKmrSRAKLLmkraahvkqqssieEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQH 375
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1720415018 396 EEVEALTKKCQELEEAKREEKNSFVAVTHEKREAALDEAATVLQAAFRGHLARSK 450
Cdd:TIGR00618 376 TLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAK 430
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
460-688 |
3.25e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 41.08 E-value: 3.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415018 460 RSPSLPGLLSPLNQSS----------PAPRVLSPISPAEENPTQEEaviviQSILRGYLAQARFIASCCREIAASSQRET 529
Cdd:PHA03247 2684 RRRAARPTVGSLTSLAdpppppptpePAPHALVSATPLPPGPAAAR-----QASPALPAAPAPPAVPAGPATPGGPARPA 2758
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415018 530 VSLTPSGSASPPSLRAsPEWGPSGKNSEASSGEAAKDEDEAEEPPDLQPYSGVIRKELCASEELRETSASEPAPSVPYSA 609
Cdd:PHA03247 2759 RPPTTAGPPAPAPPAA-PAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPT 2837
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720415018 610 QGGHGDCPSSSSLEAVPSMKDAMCEERSSSPRSAGPSLAEPSPPELQPLSPPPVEDICSDDSDDIIFSPFLPRKKSPSP 688
Cdd:PHA03247 2838 APPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPP 2916
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
78-414 |
3.42e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.82 E-value: 3.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415018 78 KEDMYDEIIELKKSLHMQKSDVDLMRTKLRRLEEENSRKDRQIEQL-----------LDPSRGPDFVRTLAEKKPDTGWV 146
Cdd:PRK03918 188 TENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELeelkeeieeleKELESLEGSKRKLEEKIRELEER 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415018 147 ITGLKQRIFRLEQQCKEkdntINKLQTDMKTtnLEEMRIAMETYYEEIHRLQTLLA--SSEATG-KKPMVEKKLGVKRQK 223
Cdd:PRK03918 268 IEELKKEIEELEEKVKE----LKELKEKAEE--YIKLSEFYEEYLDELREIEKRLSrlEEEINGiEERIKELEEKEERLE 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415018 224 KMSSALLNLTRSVQELtEENQSLKEDLDRMLSNSPTISKIKgyGDWSKPRLLRRIAELEK-KVSSSESPKQSTSELVNPN 302
Cdd:PRK03918 342 ELKKKLKELEKRLEEL-EERHELYEEAKAKKEELERLKKRL--TGLTPEKLEKELEELEKaKEEIEEEISKITARIGELK 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415018 303 PLVRS-PSNISVQKQPKGdqspedlpKVAPCE---EQEHLQGTVKSLREELGALQEQLLEKDLEMKQLLQSKIDLEKELE 378
Cdd:PRK03918 419 KEIKElKKAIEELKKAKG--------KCPVCGrelTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLK 490
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1720415018 379 TAREGEKGRQ--EQEQALREE-----VEALTKKCQELEEAKRE 414
Cdd:PRK03918 491 KESELIKLKElaEQLKELEEKlkkynLEELEKKAEEYEKLKEK 533
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
75-464 |
3.81e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.52 E-value: 3.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415018 75 YREKEDMYDEIIELKKSLHMQKSDVDLMRTKLRRLEEENSRKDRQIEQLLD--PSRGPDFVRTLAEKkpdtgwvITGLKQ 152
Cdd:COG4717 134 LEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEqlSLATEEELQDLAEE-------LEELQQ 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415018 153 RIFRLEQQCKEKDNTINKLQTDMKTTNLEEMRIAMETYYEEIHRLQTLLA-----SSEATGKKPMVEKKLGV-------- 219
Cdd:COG4717 207 RLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAallalLGLGGSLLSLILTIAGVlflvlgll 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415018 220 -------KRQKKMSSALLNLTRSVQELTE-ENQSLKEDLDR-MLSNSPTISKIKGYGDW--SKPRLLRRIAELEKKVSSS 288
Cdd:COG4717 287 allflllAREKASLGKEAEELQALPALEElEEEELEELLAAlGLPPDLSPEELLELLDRieELQELLREAEELEEELQLE 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415018 289 ESPKQSTSELvnpnplvrspsnisvqkQPKGDQSPEDLPKVApcEEQEHLQgtvkSLREELGALQEQLLEKDLEMKQLLQ 368
Cdd:COG4717 367 ELEQEIAALL-----------------AEAGVEDEEELRAAL--EQAEEYQ----ELKEELEELEEQLEELLGELEELLE 423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415018 369 --SKIDLEKELETAregekgrQEQEQALREEVEALTKKCQELEEAKRE-EKNSFVAVTHEKREAALDEAATVLQAAFRGH 445
Cdd:COG4717 424 alDEEELEEELEEL-------EEELEELEEELEELREELAELEAELEQlEEDGELAELLQELEELKAELRELAEEWAALK 496
|
410 420
....*....|....*....|.
gi 1720415018 446 LARSKL--VRSKVPDSRSPSL 464
Cdd:COG4717 497 LALELLeeAREEYREERLPPV 517
|
|
| IQ |
pfam00612 |
IQ calmodulin-binding motif; Calmodulin-binding motif. |
433-451 |
4.84e-03 |
|
IQ calmodulin-binding motif; Calmodulin-binding motif.
Pssm-ID: 459869 Cd Length: 21 Bit Score: 34.99 E-value: 4.84e-03
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
155-363 |
5.08e-03 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 39.84 E-value: 5.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415018 155 FRLEQQCKEKDNTINKLQTDMKTTNLEEMRIAMETYYEEIHRLQTLL-ASSEAtgkKPMVEKKLGvkrqkkmssallNLT 233
Cdd:pfam06160 233 LNVDKEIQQLEEQLEENLALLENLELDEAEEALEEIEERIDQLYDLLeKEVDA---KKYVEKNLP------------EIE 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415018 234 RSVQELTEENQSLKEDLDRM-----LSNSpTISKIKGYGDWSKpRLLRRIAELEKKVsssESPKQSTSELvnpnplvrsp 308
Cdd:pfam06160 298 DYLEHAEEQNKELKEELERVqqsytLNEN-ELERVRGLEKQLE-ELEKRYDEIVERL---EEKEVAYSEL---------- 362
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1720415018 309 snISVQKQPKgdqspEDLPKVApcEEQEHLQGTVKSLREELGALQEQLLEKDLEM 363
Cdd:pfam06160 363 --QEELEEIL-----EQLEEIE--EEQEEFKESLQSLRKDELEAREKLDEFKLEL 408
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
336-441 |
5.83e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.90 E-value: 5.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415018 336 EHLQGTVKSLREELGALQEQLLEKDLEMKQlLQSKIDLEKELETAREGE---KGRQEQEQALREEVEALTKKCQELEEAK 412
Cdd:COG4913 613 AALEAELAELEEELAEAEERLEALEAELDA-LQERREALQRLAEYSWDEidvASAEREIAELEAELERLDASSDDLAALE 691
|
90 100
....*....|....*....|....*....
gi 1720415018 413 REEknsfvavthEKREAALDEAATVLQAA 441
Cdd:COG4913 692 EQL---------EELEAELEELEEELDEL 711
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
453-662 |
5.93e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 40.31 E-value: 5.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415018 453 RSKVPDSRSPSLPGLLSPLNQSSPAPR--VLSPISPAEENPTQEEAVIVIQSILRGYLAQARfiASCCREIAASSQRETV 530
Cdd:PHA03247 2599 RAPVDDRGDPRGPAPPSPLPPDTHAPDppPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGR--VSRPRRARRLGRAAQA 2676
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415018 531 SLTPSG---------------SASPPSLRASPEWGPSGKNSEASSGEAAKDEDEAEEPPDLQPY-----SGVIRKELCAS 590
Cdd:PHA03247 2677 SSPPQRprrraarptvgsltsLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAppavpAGPATPGGPAR 2756
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415018 591 EELRETSASEPAPSVPYSAQGG-------HGDCPSSSSLEAVPSMKD------AMCEERSSSPRSAGPSLAEPSPPELQP 657
Cdd:PHA03247 2757 PARPPTTAGPPAPAPPAAPAAGpprrltrPAVASLSESRESLPSPWDpadppaAVLAPAAALPPAASPAGPLPPPTSAQP 2836
|
....*
gi 1720415018 658 LSPPP 662
Cdd:PHA03247 2837 TAPPP 2841
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
353-439 |
8.05e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 39.42 E-value: 8.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415018 353 QEQLLEKDLEMKQLLQSKIDLEKELET-AREGEKGRQEQEQaLREEVEaltKKCQELEEAKREEKNSFVAVTHEKREAAL 431
Cdd:PRK00409 508 KKLIGEDKEKLNELIASLEELERELEQkAEEAEALLKEAEK-LKEELE---EKKEKLQEEEDKLLEEAEKEAQQAIKEAK 583
|
....*...
gi 1720415018 432 DEAATVLQ 439
Cdd:PRK00409 584 KEADEIIK 591
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
271-416 |
8.50e-03 |
|
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: 39.34 E-value: 8.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415018 271 KPRLLRRIAELEKKvssSESPKQSTSELVNPNPLVRSPSNISVQKQPKGDQSPEDL--PKVAPCEEQEHLQGTVKSLREE 348
Cdd:pfam17380 346 RERELERIRQEERK---RELERIRQEEIAMEISRMRELERLQMERQQKNERVRQELeaARKVKILEEERQRKIQQQKVEM 422
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720415018 349 LGALQEQLLEKDLEMKQLLQSKidlEKELETAREGEKGRQEQEQALREEVEALTKKCQELEEAKREEK 416
Cdd:pfam17380 423 EQIRAEQEEARQREVRRLEEER---AREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRK 487
|
|
| PRK07003 |
PRK07003 |
DNA polymerase III subunit gamma/tau; |
476-653 |
8.64e-03 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 235906 [Multi-domain] Cd Length: 830 Bit Score: 39.45 E-value: 8.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415018 476 PAPRVLSPISPAEENPTQEEAVIVIqsilrgylaqarfIASCCREIAASSQRETVSLTPSGSASPPSLRASPEWGPSGKN 555
Cdd:PRK07003 381 PAPGARAAAAVGASAVPAVTAVTGA-------------AGAALAPKAAAAAAATRAEAPPAAPAPPATADRGDDAADGDA 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415018 556 SEASSGEAAKDEDEAEEPPDLQPYSGViRKELCASEELRETSASEPAPSVPYSAQGGHGDCPSSSSLeAVPSMKDAMCEE 635
Cdd:PRK07003 448 PVPAKANARASADSRCDERDAQPPADS-GSASAPASDAPPDAAFEPAPRAAAPSAATPAAVPDARAP-AAASREDAPAAA 525
|
170
....*....|....*...
gi 1720415018 636 RSSSPRSAGPSLAEPSPP 653
Cdd:PRK07003 526 APPAPEARPPTPAAAAPA 543
|
|
| |
