|
Name |
Accession |
Description |
Interval |
E-value |
| CCDC73 |
pfam15818 |
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil ... |
25-1092 |
0e+00 |
|
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil containing proteins. The function is not known. The alternative name is sarcoma antigen NY-SAR-79.
Pssm-ID: 464893 [Multi-domain] Cd Length: 1048 Bit Score: 1290.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020982037 25 RLLDFKTNLLEAIEELRIRRETETNYEDQINKIVIEKQELEWQKETLQHQTDTLQQQNKEAMAAFKKQLQARMFAMEEEK 104
Cdd:pfam15818 1 QLLDFKTSLLEALEELRMRREAETQYEEQIGKIIVETQELKWQKETLQNQKETLAKQHKEAMAVFKKQLQMKMCALEEEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020982037 105 GKYQLAAETKEKEIDGLKETLKALQISKYTLQKKLNEMDQKLQMHLTAKEEHHKKLNEVERCYATIASRFGVVKGVHGKL 184
Cdd:pfam15818 81 GKYQLATEIKEKEIEGLKETLKALQVSKYSLQKKVSEMEQKLQLHLLAKEDHHKQLNEIEKYYATITGQFGLVKENHGKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020982037 185 EHSVQEAIQHNKKLASVNKRQETEISNLKEELKKVTTDLIRSKVNSQYRVGEENINLAVKEKQFQELQQKIRMETAVSKK 264
Cdd:pfam15818 161 EQNVQEAIQLNKRLSALNKKQESEICSLKKELKKVTSDLIKSKVTCQYKMGEENINLTIKEQKFQELQERLNMELELNKK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020982037 265 VQEENTHIKEEKLEILSSLQCVQELLQRITQANVRMESELNALKEDYQALERDNELQREKAKENEEKFLNLQNEHEKALK 344
Cdd:pfam15818 241 INEEITHIQEEKQDIIISFQHMQQLLQQQTQANTEMEAELKALKENNQTLERDNELQREKVKENEEKFLNLQNEHEKALG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020982037 345 TWKNDEENMRREIQTIKNELNSLKELHRHLEDYHPPQGNQ----HSEHVENLqmqspaqPIPTNVSGQEHSKDSEILAIQ 420
Cdd:pfam15818 321 TWKKHVEELNGEINEIKNELSSLKETHIKLQEHYNKLCNQkkfeEDKKFQNV-------PEVNNENSEMSTEKSENLIIQ 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020982037 421 KENefmqsgiskcgncgNEEETEVKTTRDKSSSTEELKTEQNP------------QVLENSFKDEINVASPRELKQREAC 488
Cdd:pfam15818 394 KYN--------------SEQEIREENTKSFCSDTEYRETEKKKgppveeiiiedlQVLEKSFKNEIDTSVPQDKNQSEIS 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020982037 489 PRNTLCTDTDLTAQGHTseMHVTGGREAEDAGTAHRTLPDDSNANLDQKPLDSTEPLAAQHTQTRKDFLGSAERKsvGAD 568
Cdd:pfam15818 460 LSKTLCTDKDLISQGQT--LNVTDFRKSVTTEIKDKLCLEKDNGCSEFKSPNNLFLVADQSIETEKIHLESTEGL--GLH 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020982037 569 RKNGSQETDTSKEELCGTADESAcakagansDTRQHNRSVLTPEAPKPQSEAVLCTERSALHERSTDSHQAKQLSFGILH 648
Cdd:pfam15818 536 HADIHLETESNRSSFNGTLNEMA--------HNTNHNKDVSENEPFKQQFRLLLCTQENATEKRITNSDQTKAGLDSSLD 607
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020982037 649 STKENSQaeYQKCSLLNSDN-SVGSGLHKAEKtLNLSGLHRDKLPLEQTQVDAEGRNddnvrnvnntgvlaidavpETSA 727
Cdd:pfam15818 608 VKKNPVQ--CQKYSLQDSSNvSLDDKQCKIEQ-LLNKKSECSTLPLKQTSSFQQLCN-------------------DTSE 665
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020982037 728 QHPPTVCCD--------------NASADAAAAKECRENKSLSGTFNLCPPKTGRGINADDMHSKQPEQG-GAKPTGNAAN 792
Cdd:pfam15818 666 KPGLTIPCDtvvshpispaafsdNLKADLKNSDNNVNIMPMLVKPNSSPGKRTTRKNLDDMQSSQFKNClGGLENGVTIS 745
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020982037 793 RWASNAEAKSPVKADGLKIAQKPPPTDRACTDKliLCKNVNNGTQIHSIKTGHSLEID-TSTNNTLLK--EKKGSLSSAV 869
Cdd:pfam15818 746 HLQVNNENSHASQAKDLKTAVHPKTSTEIQFSS--KESQIDENQITEATKNDLFLLVNvNERQHTLLNntEKTESLNDIV 823
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020982037 870 PGMKLAEGHLKESSSLPMRTSGNLVNISLRSSFDLSTSDKKAEKSPLYLNFLALSSCSRVNQVRGQAAWTSASKEPSLLK 949
Cdd:pfam15818 824 SGKIYSEGQLEESHSFHIKPSGDLVNRSGRSAFDLSTSDKKTEKTPVYLNFLDPSPWSKVNQTEGQTVSTSTSSIPLLLK 903
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020982037 950 DKPA--LENTNIISKTQSQNLSENVDSEESGQGSSSLSRAANTLNASGIHREPQGEPSEEWNATAKAFYDSSFPTEHVtE 1027
Cdd:pfam15818 904 EKPIgpSENTKIISVTLCKNVGVDDVRKDIGPDTTSISRVADTLNNSSIHPDPKGEPSEERNATAKTFYDSSFPTEHV-K 982
|
1050 1060 1070 1080 1090 1100
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1020982037 1028 GLAAFQNKQKSPHMTVSPARSEKALKDEDSCSLQNSIIQNQTGGIEKLLNLERLHSARKRKYEEG 1092
Cdd:pfam15818 983 TEPLKSTVLQSHFQTVKIKDSPDLLKSSPGEDDWQSLITNQITEIEKLLSLENDNQPKKRKAEEM 1047
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
33-371 |
2.49e-11 |
|
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: 68.17 E-value: 2.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020982037 33 LLEAIEELRIRRETETNYEDqinkIVIEKQELEWqketlqhqtdTLQQQNKEAMAAFKKQLQARMFAMEEEKGKYQLAAE 112
Cdd:TIGR02169 196 KRQQLERLRREREKAERYQA----LLKEKREYEG----------YELLKEKEALERQKEAIERQLASLEEELEKLTEEIS 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020982037 113 TKEKEIDGLKETLKalqiskyTLQKKLNEMDQKLQmhLTAKEEHHKKLNEVERCYATIASrfgvvkgvhgkLEHSVQEAI 192
Cdd:TIGR02169 262 ELEKRLEEIEQLLE-------ELNKKIKDLGEEEQ--LRVKEKIGELEAEIASLERSIAE-----------KERELEDAE 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020982037 193 QHNKKLASVNKRQETEISNLKEELKKVTTDliRSKVNSQYRVGEENinLAVKEKQFQELQQKIRMETAVSKKVQEENTHI 272
Cdd:TIGR02169 322 ERLAKLEAEIDKLLAEIEELEREIEEERKR--RDKLTEEYAELKEE--LEDLRAELEEVDKEFAETRDELKDYREKLEKL 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020982037 273 KEEKLEILSSLQCVQELLQRITQANVRMESELNALKEDYQALERDNELQREKAKENEEKflnlqnehekaLKTWKNDEEN 352
Cdd:TIGR02169 398 KREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWK-----------LEQLAADLSK 466
|
330 340
....*....|....*....|
gi 1020982037 353 MRREIQTIKNELNSL-KELH 371
Cdd:TIGR02169 467 YEQELYDLKEEYDRVeKELS 486
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
43-378 |
1.13e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 62.77 E-value: 1.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020982037 43 RRETETNYED-QINKIVIEK--QELEWQKETLQhqtdtLQQQNKEAMAAFKKQLQarmfamEEEKGKYQLAAETKEKEID 119
Cdd:TIGR02168 174 RKETERKLERtRENLDRLEDilNELERQLKSLE-----RQAEKAERYKELKAELR------ELELALLVLRLEELREELE 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020982037 120 GLKETLKALQISKYTLQKKLNEMDQKLqmhltakEEHHKKLNEVERCYATIASRFGVVKGVHGKLEHSVQEAIQHNKKLA 199
Cdd:TIGR02168 243 ELQEELKEAEEELEELTAELQELEEKL-------EELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLE 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020982037 200 SVNKRQETEISNLKEELKKVTTDLIRSKVnsqyrvgeeniNLAVKEKQFQELQQKIrmeTAVSKKVQEENTHIKEEKLEI 279
Cdd:TIGR02168 316 RQLEELEAQLEELESKLDELAEELAELEE-----------KLEELKEELESLEAEL---EELEAELEELESRLEELEEQL 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020982037 280 LSSLQCVQELLQRITQAN---VRMESELNALKEDYQALERDNELQREKAKENEEKFLNLQ-NEHEKALKTWKNDEENMRR 355
Cdd:TIGR02168 382 ETLRSKVAQLELQIASLNneiERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAElEELEEELEELQEELERLEE 461
|
330 340
....*....|....*....|...
gi 1020982037 356 EIQTIKNELNSLKELHRHLEDYH 378
Cdd:TIGR02168 462 ALEELREELEEAEQALDAAEREL 484
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
35-376 |
2.24e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.41 E-value: 2.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020982037 35 EAIEELRirrETETNyEDQINKIViekQELEWQKETLQHQTDTLQ--QQNKEAMAAFKKQLQA-RMFAMEEEKGKYQLAA 111
Cdd:COG1196 176 EAERKLE---ATEEN-LERLEDIL---GELERQLEPLERQAEKAEryRELKEELKELEAELLLlKLRELEAELEELEAEL 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020982037 112 ETKEKEIDGLKETLKALQISKYTLQKKLNEMDQKLQMHLTAKEEHHKKLNEVERcyatiasrfgvvkgvhgKLEHSVQEA 191
Cdd:COG1196 249 EELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQ-----------------DIARLEERR 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020982037 192 IQHNKKLAsvnkRQETEISNLKEELKKVTTDLIRSKVNSQyrvgEENINLAVKEKQFQELQQKIRMETAVSKKVQEENTH 271
Cdd:COG1196 312 RELEERLE----ELEEELAELEEELEELEEELEELEEELE----EAEEELEEAEAELAEAEEALLEAEAELAEAEEELEE 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020982037 272 IKEEKLEILSSLQCVQELLQRITQANVRMESELNALKEDYQALERDNELQREKAKENEEKFLNLQNEHEKALKTWKNDEE 351
Cdd:COG1196 384 LAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE 463
|
330 340
....*....|....*....|....*
gi 1020982037 352 NMRREIQTIKNELNSLKELHRHLED 376
Cdd:COG1196 464 LLAELLEEAALLEAALAELLEELAE 488
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
20-342 |
8.49e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 56.60 E-value: 8.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020982037 20 TLLSIRLLDFKTNL---LEAIEELRIRRETET----NYEDQINKIVIEKQELEWQKETLQHQTDTLQQQnKEAMAAFKKQ 92
Cdd:TIGR02168 228 ALLVLRLEELREELeelQEELKEAEEELEELTaelqELEEKLEELRLEVSELEEEIEELQKELYALANE-ISRLEQQKQI 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020982037 93 LQARMFAMEEEKGKYQLAAETKEKEIDGLKETLKALQISKYTLQKKLNEMDQKLQMHLTAKEEHHKKLNEVERcyatias 172
Cdd:TIGR02168 307 LRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEE------- 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020982037 173 rfgvvkgvhgKLEHSVQEAIQHNKKLASVNKrqetEISNLKEELkkvtTDLIRSKVNSQYRVGEENINLavKEKQFQELQ 252
Cdd:TIGR02168 380 ----------QLETLRSKVAQLELQIASLNN----EIERLEARL----ERLEDRRERLQQEIEELLKKL--EEAELKELQ 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020982037 253 QKIRMETAVSKKVQEENTHIkEEKLEILsslqcvQELLQRITQANVRMESELNALKEDYQALERdneLQREKAKENEEKF 332
Cdd:TIGR02168 440 AELEELEEELEELQEELERL-EEALEEL------REELEEAEQALDAAERELAQLQARLDSLER---LQENLEGFSEGVK 509
|
330
....*....|
gi 1020982037 333 LNLQNEHEKA 342
Cdd:TIGR02168 510 ALLKNQSGLS 519
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
91-370 |
1.62e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 55.83 E-value: 1.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020982037 91 KQLQARMFAMEEEkgkyqlaAETKEKEIDGLKETLKALQISKYTLQKKLNEMDQKLQMHLTAKEEHHKKLNEVERCYATI 170
Cdd:TIGR02168 680 EELEEKIEELEEK-------IAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQL 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020982037 171 ASRFGVVKGVHGKLEHSVQEAIQHNKKLASVNKRQETEISNLKEELKKVTTDLirSKVNSQY------------RVGEEN 238
Cdd:TIGR02168 753 SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREAL--DELRAELtllneeaanlreRLESLE 830
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020982037 239 INLAVKEKQFQELQQKIRMETAVSKKVQEENTHIKEEKLEILSSLqcvQELLQRITQANVRMESelnaLKEDYQALERDN 318
Cdd:TIGR02168 831 RRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESEL---EALLNERASLEEALAL----LRSELEELSEEL 903
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1020982037 319 ELQREKAKENEEKFLNLQNEHEKAlktwKNDEENMRREIQTIKNELNSLKEL 370
Cdd:TIGR02168 904 RELESKRSELRRELEELREKLAQL----ELRLEGLEVRIDNLQERLSEEYSL 951
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
33-357 |
2.46e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 55.07 E-value: 2.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020982037 33 LLEAIEELRIRRET----ETNYEDQINKIVIEKQELEWQKETLQHQTDTLQQQnKEAMAAFKKQLQARMFAMEEEKGKYQ 108
Cdd:TIGR02169 679 LRERLEGLKRELSSlqseLRRIENRLDELSQELSDASRKIGEIEKEIEQLEQE-EEKLKERLEELEEDLSSLEQEIENVK 757
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020982037 109 LAAETKEKEIDGLKETLKAlqiskytLQKKLNEMDQKLQMH-LTAKEEHHKKLNE-VERCYATIASRFGVVKGVHGKLEh 186
Cdd:TIGR02169 758 SELKELEARIEELEEDLHK-------LEEALNDLEARLSHSrIPEIQAELSKLEEeVSRIEARLREIEQKLNRLTLEKE- 829
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020982037 187 SVQEAIQHNK-------------------------KLASVNKRQETEISNLKEELKKVTTDliRSKVNSQYRV---GEEN 238
Cdd:TIGR02169 830 YLEKEIQELQeqridlkeqiksiekeienlngkkeELEEELEELEAALRDLESRLGDLKKE--RDELEAQLRElerKIEE 907
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020982037 239 INLAVKEKQFQELQQKIRMETAvskkvQEENTHIKEEKLEILS------SLQCVQELLQRITQANVRMESELNALKEDYQ 312
Cdd:TIGR02169 908 LEAQIEKKRKRLSELKAKLEAL-----EEELSEIEDPKGEDEEipeeelSLEDVQAELQRVEEEIRALEPVNMLAIQEYE 982
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1020982037 313 -ALERDNELQREKAKENEEKflnlqneheKALKTWKNDEENMRREI 357
Cdd:TIGR02169 983 eVLKRLDELKEKRAKLEEER---------KAILERIEEYEKKKREV 1019
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
25-256 |
2.23e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 51.98 E-value: 2.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020982037 25 RLLDFKTNLLEAIEELRIRRETetnYEDQINKIVIEKQELEWQKETLQHQTDTLQ---QQNKEAMAAFKKQLQA------ 95
Cdd:TIGR02168 744 QLEERIAQLSKELTELEAEIEE---LEERLEEAEEELAEAEAEIEELEAQIEQLKeelKALREALDELRAELTLlneeaa 820
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020982037 96 ----RMFAMEEEKGKYQLAAETKEKEIDGLKETLKALQISKYTLQKKLNEMDQKLQMHLTAKEEHHKKLNEVERCYATIA 171
Cdd:TIGR02168 821 nlreRLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELS 900
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020982037 172 SRFGVVKGVHGKLEHSVQEAiqhNKKLASVNKRQET---EISNLKEELkkvttdlirskvNSQYRVGEENI--NLAVKEK 246
Cdd:TIGR02168 901 EELRELESKRSELRRELEEL---REKLAQLELRLEGlevRIDNLQERL------------SEEYSLTLEEAeaLENKIED 965
|
250
....*....|
gi 1020982037 247 QFQELQQKIR 256
Cdd:TIGR02168 966 DEEEARRRLK 975
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
33-376 |
2.82e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.60 E-value: 2.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020982037 33 LLEAIEELRIRRETETnyedqINKIVIEKQELEWQKETLQHQTDTLqqqnKEAMAAFKKQLQARMFAMEEEKG------- 105
Cdd:PRK03918 370 KKEELERLKKRLTGLT-----PEKLEKELEELEKAKEEIEEEISKI----TARIGELKKEIKELKKAIEELKKakgkcpv 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020982037 106 ---------------KYQLAAETKEKEIDGLKETLKALQISKYTLQKKLNEMDQKLQMHLTAK-----EEHHKKLN--EV 163
Cdd:PRK03918 441 cgrelteehrkelleEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEqlkelEEKLKKYNleEL 520
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020982037 164 ERC---YATIASRFGVVKGVHGKLEHSVQEAIQHNKKLASVNKrqetEISNLKEELKKVTTDLIRSKVNSQYRVGEENIN 240
Cdd:PRK03918 521 EKKaeeYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEK----KLDELEEELAELLKELEELGFESVEELEERLKE 596
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020982037 241 LAVKEKQFQELQQkirmetaVSKKVQEENTHIKEEKLEILSSLQCVQELLQRITqanvRMESELNALKEDYQalerdnel 320
Cdd:PRK03918 597 LEPFYNEYLELKD-------AEKELEREEKELKKLEEELDKAFEELAETEKRLE----ELRKELEELEKKYS-------- 657
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1020982037 321 qREKAKENEEKFLNLQNEH---EKALKTWKNDEENMRREIQTIKNELNSLKELHRHLED 376
Cdd:PRK03918 658 -EEEYEELREEYLELSRELaglRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEK 715
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
32-378 |
3.46e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 51.31 E-value: 3.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020982037 32 NLLEAIEELRIRRETETNYEDQINKIVIEKQELEWQKETLQHQTDTLQQQNKEAMAAFKKQLQARMFAMEEEKGKYQLAA 111
Cdd:COG4717 143 ELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEEL 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020982037 112 ETKEKEIDGLKETLKALQiskytLQKKLNEMDQKLQMH---LTAKEEHHKKLNEVERCYATIASRFGVVKGVHGKLEHSV 188
Cdd:COG4717 223 EELEEELEQLENELEAAA-----LEERLKEARLLLLIAaalLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREK 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020982037 189 QEAIQHNKKLASVNKRQETEISNLKEELKK--VTTDLIRSKVNSQYRVGEENINLAVKEKQFQELQQKIRMETAVSKKVQ 266
Cdd:COG4717 298 ASLGKEAEELQALPALEELEEEELEELLAAlgLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLA 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020982037 267 EENTHIKEEKLEILSSLQCVQELLQRITQANVRMESELNALKE-----DYQALERDNELQREKAKENEEKFLNLQNE--- 338
Cdd:COG4717 378 EAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEEllealDEEELEEELEELEEELEELEEELEELREElae 457
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1020982037 339 HEKALKTWKNDEE--NMRREIQTIKNELNSLKE-----------LHRHLEDYH 378
Cdd:COG4717 458 LEAELEQLEEDGElaELLQELEELKAELRELAEewaalklalelLEEAREEYR 510
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
22-347 |
9.67e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.94 E-value: 9.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020982037 22 LSIRLLDFKTNLLEAIEELRIRRETETNYEDQINKIVIEKQELEWQKETLQHQTDTLQqqnkeamaafkkQLQARMFAME 101
Cdd:COG1196 227 AELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELE------------EAQAEEYELL 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020982037 102 EEkgkyqlaAETKEKEIDGLKETLKALQISKYTLQKKLNEMDQKLQMHLTAKEEHHKKLNEVERcyatiasrfgvvkgvh 181
Cdd:COG1196 295 AE-------LARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEE---------------- 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020982037 182 gKLEHSVQEAIQHNKKLASVNKRQETEISNLKEELkkvttdliRSKVNSQYRVGEENINLAVKEKQFQELQQKIRMETAV 261
Cdd:COG1196 352 -ELEEAEAELAEAEEALLEAEAELAEAEEELEELA--------EELLEALRAAAELAAQLEELEEAEEALLERLERLEEE 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020982037 262 SKKVQEENTHIKEEKLEILSSLQCVQELLQRITQANVRMESELNALK---EDYQALERDNELQREKAKENEEKFLNLQNE 338
Cdd:COG1196 423 LEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLeeaALLEAALAELLEELAEAAARLLLLLEAEAD 502
|
....*....
gi 1020982037 339 HEKALKTWK 347
Cdd:COG1196 503 YEGFLEGVK 511
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
103-375 |
1.31e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 49.68 E-value: 1.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020982037 103 EKGKYQLAAETKEKEIDgLKETLKALQISKYTLQKKLNEMDQKLQMHLTAKEEHHKKLNEVERcyatiasrfgvvkgvhg 182
Cdd:TIGR02169 662 PRGGILFSRSEPAELQR-LRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEK----------------- 723
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020982037 183 KLEHSVQEAIQHNKKLASVnkrqETEISNLKEELkkvtTDLIRSKVNSQYRVGEENINLAVKEKQFQELQQKIRMETAvs 262
Cdd:TIGR02169 724 EIEQLEQEEEKLKERLEEL----EEDLSSLEQEI----ENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRI-- 793
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020982037 263 KKVQEENTHIKEEKLEILSSLQCVQELLQRITQANVRMESELNALKEDYQALErDNELQREKAKEN----EEKFLNLQNE 338
Cdd:TIGR02169 794 PEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLK-EQIKSIEKEIENlngkKEELEEELEE 872
|
250 260 270
....*....|....*....|....*....|....*..
gi 1020982037 339 HEKALKTWKNDEENMRREIQTIKNELNSLKELHRHLE 375
Cdd:TIGR02169 873 LEAALRDLESRLGDLKKERDELEAQLRELERKIEELE 909
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
31-486 |
2.05e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 48.96 E-value: 2.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020982037 31 TNLLEAIEELRIR-RETETNYEDQINKIviEKQELEWQKETLQHQTDtlQQQNKEAMAAFKKQLQARMFAMEEEKGKYQL 109
Cdd:pfam15921 320 SDLESTVSQLRSElREAKRMYEDKIEEL--EKQLVLANSELTEARTE--RDQFSQESGNLDDQLQKLLADLHKREKELSL 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020982037 110 AAETKEKEIDglKETLKALQISKytLQKKLNEMDQKLQmHLTAKEEHHKklnevERCYATIASRFGVVKGVHGKLEhsvq 189
Cdd:pfam15921 396 EKEQNKRLWD--RDTGNSITIDH--LRRELDDRNMEVQ-RLEALLKAMK-----SECQGQMERQMAAIQGKNESLE---- 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020982037 190 eaiqhnkKLASVNKRQETEisnlKEELKKVTTDLIRSKV---NSQYRVGEENINLAVKEKQFQELQQKI-RMETAVSKKV 265
Cdd:pfam15921 462 -------KVSSLTAQLEST----KEMLRKVVEELTAKKMtleSSERTVSDLTASLQEKERAIEATNAEItKLRSRVDLKL 530
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020982037 266 QE------ENTHI----------------KEEKLEILSslQCVQELLQRITQ----------ANVRMESELNALKEDYQA 313
Cdd:pfam15921 531 QElqhlknEGDHLrnvqtecealklqmaeKDKVIEILR--QQIENMTQLVGQhgrtagamqvEKAQLEKEINDRRLELQE 608
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020982037 314 LERDNELQREKAKENEE----------KFLNLQNEHEKALKTWKNDEENMRREIQTIKNELNSLKELHRHLEDYHPPQGN 383
Cdd:pfam15921 609 FKILKDKKDAKIRELEArvsdlelekvKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSE 688
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020982037 384 QHSEHVENLQMQ----------------------SPAQPIPTNVSGQEHSKDSEILAIQKENEFMQSGISKcgncGNEEE 441
Cdd:pfam15921 689 EMETTTNKLKMQlksaqseleqtrntlksmegsdGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTN----ANKEK 764
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1020982037 442 TEVKTTRDKSSstEELKTEQNPQvleNSFKDEINVASPRELKQRE 486
Cdd:pfam15921 765 HFLKEEKNKLS--QELSTVATEK---NKMAGELEVLRSQERRLKE 804
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
17-331 |
2.86e-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: 48.51 E-value: 2.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020982037 17 PSETLLSIRLLDFKTNLLEAIEELRIRRETETNYEDQINKIVIEKQELEWQKETLQHQTDTLQQQNKEAMA------AFK 90
Cdd:TIGR02168 691 EKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAeieeleERL 770
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020982037 91 KQLQARMFAMEEEKGKYQLAAETKEKEIDGLKETLKALQISKYTLQKKLNEMDQKLQMHLTAKEEHHKKLNEVERcyati 170
Cdd:TIGR02168 771 EEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEE----- 845
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020982037 171 asRFGVVKGVHGKLEHSVQEaiqhnkklasvnkrQETEISNLKEELKKVTtdlirskvnSQYRVGEENINLAvkEKQFQE 250
Cdd:TIGR02168 846 --QIEELSEDIESLAAEIEE--------------LEELIEELESELEALL---------NERASLEEALALL--RSELEE 898
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020982037 251 LQQKIR-METAVSK---KVQEENTHIKEEKLEiLSSLQcvQELLQRITQANVRMESELNALKEDYQALERDNELQREKAK 326
Cdd:TIGR02168 899 LSEELReLESKRSElrrELEELREKLAQLELR-LEGLE--VRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLK 975
|
....*
gi 1020982037 327 ENEEK 331
Cdd:TIGR02168 976 RLENK 980
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
101-376 |
4.62e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 47.76 E-value: 4.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020982037 101 EEEKGKYQLAAETKEKEIDGL-KETLKALQISKytLQKKLNEMDQKLqmHLTAKEEHHKKLNEVERcyaTIASRFGVVKG 179
Cdd:TIGR02169 183 EENIERLDLIIDEKRQQLERLrREREKAERYQA--LLKEKREYEGYE--LLKEKEALERQKEAIER---QLASLEEELEK 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020982037 180 VHGKLEHSVQEAIQHNKKLASVNKR----QETEISNLKEELKKVTTDLIRSKVNsqyrvgeeninLAVKEKQFQELQQKI 255
Cdd:TIGR02169 256 LTEEISELEKRLEEIEQLLEELNKKikdlGEEEQLRVKEKIGELEAEIASLERS-----------IAEKERELEDAEERL 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020982037 256 RmetavskKVQEENTHIKEEkleilsslqcVQELLQRITQANVRMESelnaLKEDYQALERDNELQREKAKENEEKFlnl 335
Cdd:TIGR02169 325 A-------KLEAEIDKLLAE----------IEELEREIEEERKRRDK----LTEEYAELKEELEDLRAELEEVDKEF--- 380
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1020982037 336 qnehekalKTWKNDEENMRREIQTIKNELNSLKELHRHLED 376
Cdd:TIGR02169 381 --------AETRDELKDYREKLEKLKREINELKRELDRLQE 413
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
32-375 |
6.77e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.98 E-value: 6.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020982037 32 NLLEAIEELRIRREtetNYEDQI-------NKIVIEKQELEWQKETLQHQTDTLQQQNKEaMAAFKKQLQaRMFAMEEEK 104
Cdd:PRK03918 166 NLGEVIKEIKRRIE---RLEKFIkrtenieELIKEKEKELEEVLREINEISSELPELREE-LEKLEKEVK-ELEELKEEI 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020982037 105 GKYQLAAETKEKEIDGLKETLKALQISKYTLQKKLNEMDQKLQmHLTAKEEHHKKLNEVERCYATIASRFGVVKGVHGKL 184
Cdd:PRK03918 241 EELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVK-ELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRL 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020982037 185 EHSVQEAIQHNKKLASVNKRQEtEISNLKEELKKvttdlirskvnsqyRVGEeninLAVKEKQFQELQQKI-RMETAVSK 263
Cdd:PRK03918 320 EEEINGIEERIKELEEKEERLE-ELKKKLKELEK--------------RLEE----LEERHELYEEAKAKKeELERLKKR 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020982037 264 KVQEENTHIKEEKLEILSSLQCVQELLQRITQANVRMESELNALKEDYQALER--------DNELQREKAKENEEKFLNL 335
Cdd:PRK03918 381 LTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKakgkcpvcGRELTEEHRKELLEEYTAE 460
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1020982037 336 QNEHEKALKTWKNDEENMRREIQTIKNELNSLKELHRHLE 375
Cdd:PRK03918 461 LKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKE 500
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
18-375 |
8.99e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 46.64 E-value: 8.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020982037 18 SETLLSIRLLDFKTNLLEAIEELRIRRETETNYEDQINKIViekqeLEWQKETLQHQTDTLQQQNKEA-MAAFKKQLQAR 96
Cdd:pfam05483 343 AKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIIT-----MELQKKSSELEEMTKFKNNKEVeLEELKKILAED 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020982037 97 MFAMEEEKGKYQLAAE-------------TKEKEIDGLKETLKALQISKYTLQKKLNEMDQKLQMHLTAKEE---HHKKL 160
Cdd:pfam05483 418 EKLLDEKKQFEKIAEElkgkeqelifllqAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIEltaHCDKL 497
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020982037 161 NEVERCYATIASRFGVVKGVHgklehsvQEAIQHNKK-----LASVNKRQETEIsNLKEELKKVTTDLI--RSKVNSQYR 233
Cdd:pfam05483 498 LLENKELTQEASDMTLELKKH-------QEDIINCKKqeermLKQIENLEEKEM-NLRDELESVREEFIqkGDEVKCKLD 569
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020982037 234 VGEENINLAVKEKQFQELQQKIRMETAVSKKVQEENthikeeKLEILSSLQCVQELLQRITQANVRmesELNALKEDYQA 313
Cdd:pfam05483 570 KSEENARSIEYEVLKKEKQMKILENKCNNLKKQIEN------KNKNIEELHQENKALKKKGSAENK---QLNAYEIKVNK 640
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1020982037 314 LErdneLQREKAKEneeKFLNLQNEHEKALKTWKNDEENMRREIQTIKNELNSLKELHRHLE 375
Cdd:pfam05483 641 LE----LELASAKQ---KFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEID 695
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
48-392 |
1.72e-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: 45.78 E-value: 1.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020982037 48 TNYEDQINKIVIEKQELEWQKETLQHQTDTLQQQNKEaMAAFKKQLQARMFAMEEEKGKYQLAAETKEKEIDGLKETLKA 127
Cdd:TIGR04523 394 NDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIER-LKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKV 472
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020982037 128 LQIS----KYTLQKKLNEMDQKLQMHLTAKEEHHKKLNEVErcyatiasrfgvvkgvhgKLEHSVQEAIQHNKKLASVNK 203
Cdd:TIGR04523 473 LSRSinkiKQNLEQKQKELKSKEKELKKLNEEKKELEEKVK------------------DLTKKISSLKEKIEKLESEKK 534
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020982037 204 RQETEISNLKEELKKVTTDLIRSKVNSQYRVGEENI--------NLAVKEKQFQELqqkirmetavSKKVQEENTHIKEE 275
Cdd:TIGR04523 535 EKESKISDLEDELNKDDFELKKENLEKEIDEKNKEIeelkqtqkSLKKKQEEKQEL----------IDQKEKEKKDLIKE 604
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020982037 276 KLEILSSLQCVQELLQRITQANVRMESELNALKEDYQALERDNELQREKAKENEEKFlnlqNEHEKALKTWKNDEENMRR 355
Cdd:TIGR04523 605 IEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKW----PEIIKKIKESKTKIDDIIE 680
|
330 340 350
....*....|....*....|....*....|....*....
gi 1020982037 356 EIQTIKNELNSL--KELHRHLEDYHPPQGNQHSEHVENL 392
Cdd:TIGR04523 681 LMKDWLKELSLHykKYITRMIRIKDLPKLEEKYKEIEKE 719
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
70-296 |
1.92e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.14 E-value: 1.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020982037 70 TLQHQTDTLQQQNKEAMAAFK--KQLQARMFAMEEEKGKYQLAAETKEKEIDGLKETLKALQISKYTLQKKLNEMDQKLQ 147
Cdd:COG4942 14 AAAAQADAAAEAEAELEQLQQeiAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020982037 148 MHLTAKEEHHKKLNEVERCYATIASRFGVVKGVHGKlehSVQEAIQHNKKLASVNKRQETEIsnlkEELKKVTTDLIRSK 227
Cdd:COG4942 94 ELRAELEAQKEELAELLRALYRLGRQPPLALLLSPE---DFLDAVRRLQYLKYLAPARREQA----EELRADLAELAALR 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1020982037 228 VNSQYRVGEENINLAVKEKQFQELQQKIRMETAVSKKVQEENTHIKEEKLEILSSLQCVQELLQRITQA 296
Cdd:COG4942 167 AELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
32-369 |
2.64e-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: 45.01 E-value: 2.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020982037 32 NLLEAIEELRIRRETETNYEDQINKIVIEKQELEWQKETLQHQTDTLQQQNKEAMAAFKKqLQARMFAMEEEKGKYQLAA 111
Cdd:TIGR04523 104 DLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYND-LKKQKEELENELNLLEKEK 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020982037 112 ETKEKEIDGLKETLKALQISKYTLQKKlNEMDQKLQMHLTAKEEHHKKLNEvercyatiasrfgvvkgvhgklehSVQEA 191
Cdd:TIGR04523 183 LNIQKNIDKIKNKLLKLELLLSNLKKK-IQKNKSLESQISELKKQNNQLKD------------------------NIEKK 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020982037 192 IQHNKKLASVNKRQETEISNLKEELKKVTTDLIrskvNSQYRVGEENINLAVKEKQFQELQQKIrmETAVSKKVQEENTH 271
Cdd:TIGR04523 238 QQEINEKTTEISNTQTQLNQLKDEQNKIKKQLS----EKQKELEQNNKKIKELEKQLNQLKSEI--SDLNNQKEQDWNKE 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020982037 272 IKEEKLEILSSLQCVQELLQRITQANVRMESELNALKEDYQALERDNELQREKAKENEEKFLNLQNEHEKALKTWKNDE- 350
Cdd:TIGR04523 312 LKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLEs 391
|
330 340
....*....|....*....|.
gi 1020982037 351 --ENMRREIQTIKNELNSLKE 369
Cdd:TIGR04523 392 qiNDLESKIQNQEKLNQQKDE 412
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
30-395 |
3.48e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.76 E-value: 3.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020982037 30 KTNLLEAIEELRIRRETETNYEDQINKIVIEKQELEWQKETLQHQTDTLQQQnkeaMAAFKKQLQARMFAMEEEKGKYQL 109
Cdd:COG4717 66 PELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREE----LEKLEKLLQLLPLYQELEALEAEL 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020982037 110 AAETK-----EKEIDGLKETLKALQISKYTLQKKLNEMDQKLQMHLTAKEEHHKKL-NEVERCYATIASRfgvvkgvHGK 183
Cdd:COG4717 142 AELPErleelEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLaEELEELQQRLAEL-------EEE 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020982037 184 LEHSVQEAIQHNKKLASVNKRQETEisNLKEELKKVTTDLI------------RSKVNSQYRVGE-----------ENIN 240
Cdd:COG4717 215 LEEAQEELEELEEELEQLENELEAA--ALEERLKEARLLLLiaaallallglgGSLLSLILTIAGvlflvlgllalLFLL 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020982037 241 LAVKEKQFQELQQKIRMETAVSKKVQEENTHIKEE-KLEILSSLQCVQELLQRITQ---ANVRMESELNALKEDYQALER 316
Cdd:COG4717 293 LAREKASLGKEAEELQALPALEELEEEELEELLAAlGLPPDLSPEELLELLDRIEElqeLLREAEELEEELQLEELEQEI 372
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1020982037 317 DNELQREKAkENEEKFLNLQNEHEKAlktwkndeENMRREIQTIKNELNSLKELHRHLEDYHPPQgnQHSEHVENLQMQ 395
Cdd:COG4717 373 AALLAEAGV-EDEEELRAALEQAEEY--------QELKEELEELEEQLEELLGELEELLEALDEE--ELEEELEELEEE 440
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
30-376 |
3.90e-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: 44.63 E-value: 3.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020982037 30 KTNLLEAIEELRIRRETETNYEDQINKIVIEKQELEWQKET---------LQHQTDTLQQ------QNKEAMAAFKKQ-- 92
Cdd:TIGR04523 266 KKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQdwnkelkseLKNQEKKLEEiqnqisQNNKIISQLNEQis 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020982037 93 --------LQARMFAMEEEKGKYQLAAETKEKEIDGLKETLKALQISKYTLQKKL-------NEMDQKLQmhlTAKEEHH 157
Cdd:TIGR04523 346 qlkkeltnSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIqnqeklnQQKDEQIK---KLQQEKE 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020982037 158 KKLNEVERCYATIASRFGVVKGVhgKLEHSVQEAIQhnKKLASVNKRQETEISNLKEELKKVTTDL------IRSKVNSQ 231
Cdd:TIGR04523 423 LLEKEIERLKETIIKNNSEIKDL--TNQDSVKELII--KNLDNTRESLETQLKVLSRSINKIKQNLeqkqkeLKSKEKEL 498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020982037 232 YRVGEENINLavkEKQFQELQQKIrmeTAVSKKVQEENTHIKEEKLEILSSLQCVQELLQRITQANVRME-----SELNA 306
Cdd:TIGR04523 499 KKLNEEKKEL---EEKVKDLTKKI---SSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEKEideknKEIEE 572
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020982037 307 LKEDYQALERDNELQREKAKENEEKFLNLQNEHE----------KALKTWKNDEENMRREIQTIKNELNSLKELHRHLED 376
Cdd:TIGR04523 573 LKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEekekkissleKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKE 652
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
30-376 |
4.57e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.26 E-value: 4.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020982037 30 KTNLLEAIEELRIRRETETNYEDQINKIVIEKQELEWQKETLQHQTDTLQQQ--------------------NKEAMAAF 89
Cdd:PRK02224 236 RDEADEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERleeleeerddllaeaglddaDAEAVEAR 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020982037 90 KKQLQARMFAMEEEKGKYQLAAETKEKEIDGLKETLKALQISKYTLQKKLNEMDQKLQMHLTAKEEHHKKLNEVERCYAT 169
Cdd:PRK02224 316 REELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEE 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020982037 170 IASRFGVVKGVHGKLEHSVQEAIQHNKKLASVNKRQETEISNLKEELKKVTTDLIRSKVNS--QYRVGEENIN-LAVKEK 246
Cdd:PRK02224 396 LRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKCPEcgQPVEGSPHVEtIEEDRE 475
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020982037 247 QFQELQ---QKIRMETAVSKKVQEENTHIKEEKLEILSSLQCVQELLQRITQANVRMESE---LNALKEDYQALERDNEL 320
Cdd:PRK02224 476 RVEELEaelEDLEEEVEEVEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKrerAEELRERAAELEAEAEE 555
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1020982037 321 QREKAKENEEkflnlqnEHEKALKTWKNDEenmrREIQTIKNELNSLKELHRHLED 376
Cdd:PRK02224 556 KREAAAEAEE-------EAEEAREEVAELN----SKLAELKERIESLERIRTLLAA 600
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
6-344 |
9.13e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 43.42 E-value: 9.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020982037 6 KAQALDSTLPSPSETLLSIRLLDFKTNLLEAIEELRIRRETETNYEDQINKIVIEK--------QELEWQKETLQHQTDT 77
Cdd:TIGR00618 165 KKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERkqvlekelKHLREALQQTQQSHAY 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020982037 78 LQQQNKEAMAAFKKQLQARMFAMEEEKGKYQLAA-ETKEKEIDGLKETLKALQIskytlQKKLNEMDQKLQMHLTAKEEH 156
Cdd:TIGR00618 245 LTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVlEETQERINRARKAAPLAAH-----IKAVTQIEQQAQRIHTELQSK 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020982037 157 HKKLNEVERCYATiasrfgvvkgvHGKLEHSVQEAIQHNKKLAS---VNKRQETEISNLKEELKKVTTDLIR-SKVNSQY 232
Cdd:TIGR00618 320 MRSRAKLLMKRAA-----------HVKQQSSIEEQRRLLQTLHSqeiHIRDAHEVATSIREISCQQHTLTQHiHTLQQQK 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020982037 233 RVGEENINLAVKEK-QFQELQQKIRMETAVSKKVQEENTHIK-EEKLEILSSLQC---VQELLQRITQANVRMESELNAL 307
Cdd:TIGR00618 389 TTLTQKLQSLCKELdILQREQATIDTRTSAFRDLQGQLAHAKkQQELQQRYAELCaaaITCTAQCEKLEKIHLQESAQSL 468
|
330 340 350
....*....|....*....|....*....|....*....
gi 1020982037 308 KEDYQAL-ERDNELQREKAKEN-EEKFLNLQNEHEKALK 344
Cdd:TIGR00618 469 KEREQQLqTKEQIHLQETRKKAvVLARLLELQEEPCPLC 507
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
196-375 |
1.50e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.74 E-value: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020982037 196 KKLASVNKRQETEISNLKEELKKVTT--DLIRSKVNSQYRVGEENINLAVKEKQFQELQQKIRMETAVSKKVQEENTHIK 273
Cdd:PRK03918 165 KNLGEVIKEIKRRIERLEKFIKRTENieELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELE 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020982037 274 EEKLEILSSLQCVQELLQRITQANVRMESELNALKEDYQALE--RDNELQREKAKENEEKFLNLQNEHEKALKTWKNDEE 351
Cdd:PRK03918 245 KELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKelKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEIN 324
|
170 180
....*....|....*....|....
gi 1020982037 352 NMRREIQTIKNELNSLKELHRHLE 375
Cdd:PRK03918 325 GIEERIKELEEKEERLEELKKKLK 348
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
65-379 |
1.74e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.59 E-value: 1.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020982037 65 EWQKETLQHQTDTLQQQNKEAmAAFKKQLQARMFAMEEEKGKYQLAAETKEKEIDgLKETLKALQiskyTLQKKLNEMDQ 144
Cdd:COG4913 609 RAKLAALEAELAELEEELAEA-EERLEALEAELDALQERREALQRLAEYSWDEID-VASAEREIA----ELEAELERLDA 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020982037 145 KLQMHLTAKEEhhkkLNEVERCYATIASRFGVVKGVHGKLEHSVQEAiqhnkklasvnkrqETEISNLKEELKKVtTDLI 224
Cdd:COG4913 683 SSDDLAALEEQ----LEELEAELEELEEELDELKGEIGRLEKELEQA--------------EEELDELQDRLEAA-EDLA 743
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020982037 225 RSKVNSQYrvgeeninlavkEKQFQELQQKiRMETAVSKKVQEENTHIKEEKleilssLQCVQELLQRITQANVRMESEL 304
Cdd:COG4913 744 RLELRALL------------EERFAAALGD-AVERELRENLEERIDALRARL------NRAEEELERAMRAFNREWPAET 804
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020982037 305 NALKEDYQA----LERDNELQREKAKENEEKFLNLQNEHEKALKTWKNDEenMRREIQTIKNELNSL-KELHRHleDYHP 379
Cdd:COG4913 805 ADLDADLESlpeyLALLDRLEEDGLPEYEERFKELLNENSIEFVADLLSK--LRRAIREIKERIDPLnDSLKRI--PFGP 880
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
33-375 |
1.95e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.36 E-value: 1.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020982037 33 LLEAIEELRIRRETETNYEDQINKIVIEKQELEWQKE---TLQHQTDTLQQqNKEAMAAFKKQLQARMFAME------EE 103
Cdd:PRK03918 202 LEEVLREINEISSELPELREELEKLEKEVKELEELKEeieELEKELESLEG-SKRKLEEKIRELEERIEELKkeieelEE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020982037 104 KGKYQLAAETKEKEIDGLKETLKALQISKYTLQKKLNEMDQK---LQMHLTAKEEHHKKLNEVERCYATIASRFGVVKGV 180
Cdd:PRK03918 281 KVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEingIEERIKELEEKEERLEELKKKLKELEKRLEELEER 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020982037 181 HGKLEHSVQ---EAIQHNKKLASVN----KRQETEISNLKEELKKVTTDLIRSKVNSQYRVGEENINLAVKEKQF----- 248
Cdd:PRK03918 361 HELYEEAKAkkeELERLKKRLTGLTpeklEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKgkcpv 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020982037 249 --QELQQKIRME-----TAVSKKVQEENTHIKEEKLEILSSLQCVQELLQRitqanvrmESELNALKEDYQAL----ERD 317
Cdd:PRK03918 441 cgRELTEEHRKElleeyTAELKRIEKELKEIEEKERKLRKELRELEKVLKK--------ESELIKLKELAEQLkeleEKL 512
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1020982037 318 NELQREKAKENEEKFLNLQnehEKALKtwkndeenMRREIQTIKNELNSLKELHRHLE 375
Cdd:PRK03918 513 KKYNLEELEKKAEEYEKLK---EKLIK--------LKGEIKSLKKELEKLEELKKKLA 559
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
11-376 |
2.05e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 42.33 E-value: 2.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020982037 11 DSTLPSPSETLLSIRLLDFKTNLLEAIEELRIRRETETNYEDQINKIVIEKQELEWQKETLQHQTDTLQ---QQNKEAMA 87
Cdd:PRK02224 301 EAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELEselEEAREAVE 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020982037 88 AFKKQLQARMFAMEEEKGKYQLAAETKEK----------EIDGLKETLKALQISKYTLQKKLNEMDQKLQM--------- 148
Cdd:PRK02224 381 DRREEIEELEEEIEELRERFGDAPVDLGNaedfleelreERDELREREAELEATLRTARERVEEAEALLEAgkcpecgqp 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020982037 149 -----HLTAKEEHHKKLNEVERCYATIASRfgvvkgvhgklEHSVQEAIQHNKKLasvnKRQETEISNLKEELKKVTtDL 223
Cdd:PRK02224 461 vegspHVETIEEDRERVEELEAELEDLEEE-----------VEEVEERLERAEDL----VEAEDRIERLEERREDLE-EL 524
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020982037 224 IRSKVNsqyRVGEENINLAVKEKQFQELQQKIRMETAVSKKVQEENTHIKEEKLEI----------LSSLQCVQELLQRI 293
Cdd:PRK02224 525 IAERRE---TIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELnsklaelkerIESLERIRTLLAAI 601
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020982037 294 TQAnvrmESELNALKEDYQALERDNELQREKAKE------------NEEKFLNLQNEHEKALKTWKNDEENMRR------ 355
Cdd:PRK02224 602 ADA----EDEIERLREKREALAELNDERRERLAEkrerkreleaefDEARIEEAREDKERAEEYLEQVEEKLDElreerd 677
|
410 420
....*....|....*....|....*...
gi 1020982037 356 ----EIQTIKNELNSLKEL---HRHLED 376
Cdd:PRK02224 678 dlqaEIGAVENELEELEELrerREALEN 705
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
19-375 |
3.28e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 41.50 E-value: 3.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020982037 19 ETLLSIRLLDFKTNLLEAIEELRIRRETETNYEDQINKIVIEKQELEWQKETLQHQTDTLQQQNKEAMA-AFKKQLQARM 97
Cdd:pfam02463 180 EETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDeQEEIESSKQE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020982037 98 FAMEEEKGKYQLAAETKEKEIDGLKETlKALQISKyTLQKKLNEMDQKLQMHLTAKEEHHKKLNEVERCYAtiasrfgvv 177
Cdd:pfam02463 260 IEKEEEKLAQVLKENKEEEKEKKLQEE-ELKLLAK-EEEELKSELLKLERRKVDDEEKLKESEKEKKKAEK--------- 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020982037 178 kgvhgKLEHSVQEAIQHNKKLASVNKRQETEISNLKEELKKVTTDLIRSKVNSQYRVGEENINLAVKEKQFQELQQKIRM 257
Cdd:pfam02463 329 -----ELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEE 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020982037 258 ETAVSKKVQEENTHIKEEKLEILSSLQCVQELLQRITQANVRMESELNALKEDYQALERDN-ELQREKAKENEEKFLNLQ 336
Cdd:pfam02463 404 EKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDElELKKSEDLLKETQLVKLQ 483
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1020982037 337 NEHEKALKTWKNDEENMR-REIQTIKNELNSLKELHRHLE 375
Cdd:pfam02463 484 EQLELLLSRQKLEERSQKeSKARSGLKVLLALIKDGVGGR 523
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
49-364 |
3.41e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 41.58 E-value: 3.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020982037 49 NYEDQINKIVIEKQELEWQK--------ETLQHQTDTLQQQNKEAMAAF------KKQLQARMFAMEEEKgKYQLAAETK 114
Cdd:TIGR01612 1218 SYGKNLGKLFLEKIDEEKKKsehmikamEAYIEDLDEIKEKSPEIENEMgiemdiKAEMETFNISHDDDK-DHHIISKKH 1296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020982037 115 EKEIDGLKEtlKALQISK-YTLQKKLNEMDQKLQMHLTAKEEHHKKLNEVercYATIASRFGVVKgvHGKLEHSVQEAIQ 193
Cdd:TIGR01612 1297 DENISDIRE--KSLKIIEdFSEESDINDIKKELQKNLLDAQKHNSDINLY---LNEIANIYNILK--LNKIKKIIDEVKE 1369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020982037 194 HNKKLASVNKRQETEISNLKEELKKVttdlirsKVNSQYRVGEENINLAVKEKQFQELQQKIR-METAVSKKVQEENTHI 272
Cdd:TIGR01612 1370 YTKEIEENNKNIKDELDKSEKLIKKI-------KDDINLEECKSKIESTLDDKDIDECIKKIKeLKNHILSEESNIDTYF 1442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020982037 273 KEEK------LEILSSLQCVQELLQRITQ-----ANVRMESELNALKED------YQALERDNELQREKAKENEEKFLN- 334
Cdd:TIGR01612 1443 KNADennenvLLLFKNIEMADNKSQHILKikkdnATNDHDFNINELKEHidkskgCKDEADKNAKAIEKNKELFEQYKKd 1522
|
330 340 350
....*....|....*....|....*....|....*...
gi 1020982037 335 ----LQNEHEKALKT----WKNDEENMRREIQTIKNEL 364
Cdd:TIGR01612 1523 vtelLNKYSALAIKNkfakTKKDSEIIIKEIKDAHKKF 1560
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
60-387 |
3.88e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.67 E-value: 3.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020982037 60 EKQELEwQKETLQHQTDTLQQQNKEAMAAFKKQLQARMFAMEEEKGKYQLAAETKEKEIDGLKETLKALQISKYTLQKKL 139
Cdd:PTZ00121 1562 EKKKAE-EAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKK 1640
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020982037 140 NEMDQKLQMHLTAKEEHHKKLNEVERCYATIASRfgvvkgvhgKLEHSVQEAIQHNKKLASVNKRQETEISNLkEELKKV 219
Cdd:PTZ00121 1641 KEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDK---------KKAEEAKKAEEDEKKAAEALKKEAEEAKKA-EELKKK 1710
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020982037 220 TTDLIRSKvnSQYRVGEENINLAVKEKQFQELQQKIRMETAvsKKVQEENTHIKEEKLEILSSLQCVQELLQRITQANVR 299
Cdd:PTZ00121 1711 EAEEKKKA--EELKKAEEENKIKAEEAKKEAEEDKKKAEEA--KKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELD 1786
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020982037 300 MESELNALKEDyqalerdnelqrEKAKENEEKFLNLQNEHEKALKTWKNDEENMRREIQTIKNELNSLKELHRHLEDYHP 379
Cdd:PTZ00121 1787 EEDEKRRMEVD------------KKIKDIFDNFANIIEGGKEGNLVINDSKEMEDSAIKEVADSKNMQLEEADAFEKHKF 1854
|
....*...
gi 1020982037 380 PQGNQHSE 387
Cdd:PTZ00121 1855 NKNNENGE 1862
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
33-375 |
4.02e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 41.43 E-value: 4.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020982037 33 LLEAIEELRIRRETETNYEDQINKIVIEKQELEWQKETLQHQTDTLQQQNKEAmaafkKQLQARMFAMEEEKGKYQLAAE 112
Cdd:PRK01156 154 ILDEILEINSLERNYDKLKDVIDMLRAEISNIDYLEEKLKSSNLELENIKKQI-----ADDEKSHSITLKEIERLSIEYN 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020982037 113 TKEKEIDGLKETLK---ALQISKYTLQKKLNEMDQKLQM------HLTAKEEHHKKL---------NEVeRCYATIASRF 174
Cdd:PRK01156 229 NAMDDYNNLKSALNelsSLEDMKNRYESEIKTAESDLSMeleknnYYKELEERHMKIindpvyknrNYI-NDYFKYKNDI 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020982037 175 GVVKGVHGKLEHSVQEAIQHNKKLASVNK--RQETEISNLKEELKKVTTDLIRSKVNSQYRVGE-ENINLAVKEkqFQEL 251
Cdd:PRK01156 308 ENKKQILSNIDAEINKYHAIIKKLSVLQKdyNDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSiESLKKKIEE--YSKN 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020982037 252 QQKIRMETAVSKKVQEEN-THIKEEKLEILSSLQCVQELLQRITQANVRMESELNALKEDYQALERDNELQREKAKENEE 330
Cdd:PRK01156 386 IERMSAFISEILKIQEIDpDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSVCPVCGTTLGEE 465
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1020982037 331 KFLNLQNEHEKALKTWKNDEENMRREIQTIKNELNSLKELHRHLE 375
Cdd:PRK01156 466 KSNHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLE 510
|
|
| CDC37_N |
smart01071 |
Cdc37 N terminal kinase binding; Cdc37 is a molecular chaperone required for the activity of ... |
246-353 |
7.36e-03 |
|
Cdc37 N terminal kinase binding; Cdc37 is a molecular chaperone required for the activity of numerous eukaryotic protein kinases. This domain corresponds to the N terminal domain which binds predominantly to protein kinases.and is found N terminal to the Hsp (Heat shocked protein) 90-binding domain. Expression of a construct consisting of only the N-terminal domain of Saccharomyces pombe Cdc37 results in cellular viability. This indicates that interactions with the cochaperone Hsp90 may not be essential for Cdc37 function.
Pssm-ID: 198139 [Multi-domain] Cd Length: 154 Bit Score: 38.17 E-value: 7.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020982037 246 KQFQELQQKI-RMETAVSKKVQ-EENTHIKEEKLEILSSLQcVQELLQRITQANVRMESELNALKEDYQALERDNELQRE 323
Cdd:smart01071 33 KQRDIHQARVeRMEEIKNLKYElIMNDHLNKRIDKLLKGLR-EEELSPETPTYNEMLAELQDQLKKELEEANGDSEGLLE 111
|
90 100 110
....*....|....*....|....*....|
gi 1020982037 324 KAKENEEKFLNLQNEHEKALKTWKNDEENM 353
Cdd:smart01071 112 ELKKHRDKLKKEQKELRKKLDELEKEEKKK 141
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
34-371 |
8.35e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 40.27 E-value: 8.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020982037 34 LEAIEELRIRRETETnyEDQINKIVIEKQELEWQKETLQHQTDTLQQQNKEAmaafkKQLQARMfAMEEEKGKYQLAAET 113
Cdd:PRK01156 209 DEKSHSITLKEIERL--SIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEI-----KTAESDL-SMELEKNNYYKELEE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020982037 114 KEKEIDGLKETLKALQISKYTLQKK----LNEMDQKLQMHLTAKEEHHKKLNEVE----------RCYATIASRFGVVKG 179
Cdd:PRK01156 281 RHMKIINDPVYKNRNYINDYFKYKNdienKKQILSNIDAEINKYHAIIKKLSVLQkdyndyikkkSRYDDLNNQILELEG 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020982037 180 VHGKLEHSVQEAIQHNKKLASVNKRQETEISNLKEELKK--VTTDLIRSKVNsqyrvgEENINLAVKEKQFQELQQKIRm 257
Cdd:PRK01156 361 YEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIqeIDPDAIKKELN------EINVKLQDISSKVSSLNQRIR- 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020982037 258 etAVSKKVQEenthiKEEKLEILSSLQ----CVQEL-LQRITQANVRMESELNALKEDYQALERDNELQREKAKENEEKF 332
Cdd:PRK01156 434 --ALRENLDE-----LSRNMEMLNGQSvcpvCGTTLgEEKSNHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRK 506
|
330 340 350
....*....|....*....|....*....|....*....
gi 1020982037 333 LNLQNEHEKALKTWKNDEENMRREIQTIKNELNSLKELH 371
Cdd:PRK01156 507 EYLESEEINKSINEYNKIESARADLEDIKIKINELKDKH 545
|
|
| |
