|
Name |
Accession |
Description |
Interval |
E-value |
| CCDC73 |
pfam15818 |
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil ... |
26-1072 |
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: 1568.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 26 QLLDFKTSLLEALEELRMRREAEIHYEEQIGKIIVETQELKWQKETLQNQKETLAEQHKEAMAVFKKQLQMKMCALEEEK 105
Cdd:pfam15818 1 QLLDFKTSLLEALEELRMRREAETQYEEQIGKIIVETQELKWQKETLQNQKETLAKQHKEAMAVFKKQLQMKMCALEEEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 106 GKYQLATEIKEKEIEGLKETLKALQVSKYSLQKKVSEMEQKVQLHLLAKEDYHKQLSEIEKYYATITGQFGLVKENHEKL 185
Cdd:pfam15818 81 GKYQLATEIKEKEIEGLKETLKALQVSKYSLQKKVSEMEQKLQLHLLAKEDHHKQLNEIEKYYATITGQFGLVKENHGKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 186 EQNVREAIQSNKRLSALNKKQEAEICSLKKELKKAASDLIKSKVTCQYKMGEENINLTIKEQKFQELQERLNMELELNEK 265
Cdd:pfam15818 161 EQNVQEAIQLNKRLSALNKKQESEICSLKKELKKVTSDLIKSKVTCQYKMGEENINLTIKEQKFQELQERLNMELELNKK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 266 INEEITHIQEEKQDIIISFQHMQQLLRQQIQANTEMEAELKVLKENNQTLERDNELQREKVKENEEKFLNLQNEHEKALG 345
Cdd:pfam15818 241 INEEITHIQEEKQDIIISFQHMQQLLQQQTQANTEMEAELKALKENNQTLERDNELQREKVKENEEKFLNLQNEHEKALG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 346 TWKRHAEELNGEINKIKNELSSLKETHIKLQEHYNKLCNQKTFEEDKKFQNVPEVNNENSEMSTEKSENTIIQKYNTEQE 425
Cdd:pfam15818 321 TWKKHVEELNGEINEIKNELSSLKETHIKLQEHYNKLCNQKKFEEDKKFQNVPEVNNENSEMSTEKSENLIIQKYNSEQE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 426 IREENMENFCSDTEYReKEEKKEGSFIEEIIIDDLQLFEKSFKNEIDTVVSQDENQSEISLSKTLSLDKEVISQGQTSNV 505
Cdd:pfam15818 401 IREENTKSFCSDTEYR-ETEKKKGPPVEEIIIEDLQVLEKSFKNEIDTSVPQDKNQSEISLSKTLCTDKDLISQGQTLNV 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 506 TDNRKSVTTEIKDKICLEKDNGCTEFKSPNNHFVVLDTAIETEKIHLERTRGLDVHHTDVNLEVENNKTSFNSILNETAH 585
Cdd:pfam15818 480 TDFRKSVTTEIKDKLCLEKDNGCSEFKSPNNLFLVADQSIETEKIHLESTEGLGLHHADIHLETESNRSSFNGTLNEMAH 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 586 NTYHnnNKDVSENEPFK-QFRLLPGTREHALEKEITNSDQTKADLDSSLDIKKNPVPCQKYSLRNSSNVMLDDKQCKIKq 664
Cdd:pfam15818 560 NTNH--NKDVSENEPFKqQFRLLLCTQENATEKRITNSDQTKAGLDSSLDVKKNPVQCQKYSLQDSSNVSLDDKQCKIE- 636
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 665 iQLLTKKSECSILLSKQTSDFLQVCNDTLEKSELTVPCDIVIDHHVSYAAFSANSKLLLKNSDKNVHSMSMLVKPNSSPG 744
Cdd:pfam15818 637 -QLLNKKSECSTLPLKQTSSFQQLCNDTSEKPGLTIPCDTVVSHPISPAAFSDNLKADLKNSDNNVNIMPMLVKPNSSPG 715
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 745 GKTMCKNMSDMQNSQFNNCLGYLENtNVNISHLHLNNENSHASQAKDVKTAVHMKTCTETEFSNKKNQIDENQVTEATKN 824
Cdd:pfam15818 716 KRTTRKNLDDMQSSQFKNCLGGLEN-GVTISHLQVNNENSHASQAKDLKTAVHPKTSTEIQFSSKESQIDENQITEATKN 794
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 825 DLFLFVSINERQHTLLNNTEKTESLNDIVSGKMFSEGQLEESHSFHIEPSGDLVNRSGRSTFDLSTSDKKTEKTPVYMNF 904
Cdd:pfam15818 795 DLFLLVNVNERQHTLLNNTEKTESLNDIVSGKIYSEGQLEESHSFHIKPSGDLVNRSGRSAFDLSTSDKKTEKTPVYLNF 874
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 905 SDPGPWSKVNHIESQTASSSTPCISLLLKERPLDPSENKKIISMALCKNIGVDDVGKDIGPDTTSINRVADTLNNWSIHP 984
Cdd:pfam15818 875 LDPSPWSKVNQTEGQTVSTSTSSIPLLLKEKPIGPSENTKIISVTLCKNVGVDDVRKDIGPDTTSISRVADTLNNSSIHP 954
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 985 DPKGEPSEEKNAMAKTFYDSSFPTEHVKTKPLISTPLQSHLQAIKTT------KNTSGDDDWQSLITNQLNKSENLLSLE 1058
Cdd:pfam15818 955 DPKGEPSEERNATAKTFYDSSFPTEHVKTEPLKSTVLQSHFQTVKIKdspdllKSSPGEDDWQSLITNQITEIEKLLSLE 1034
|
1050
....*....|....
gi 83715968 1059 NDNQPKKRKAEETL 1072
Cdd:pfam15818 1035 NDNQPKKRKAEEML 1048
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
35-370 |
1.92e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 65.34 E-value: 1.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 35 LEALEelRMRREAEIHYEEQIGKIIVETQELKWQKETLQNQKETLAEQHKEAMAVfKKQLQMKMCALEEEKGKYQLATEI 114
Cdd:COG1196 202 LEPLE--RQAEKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAE-LEELEAELAELEAELEELRLELEE 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 115 KEKEIEGLKETLkalqvskYSLQKKVSEMEQKVQLHLLAKEDYHKQLSEIEkyyatitgqfglvkENHEKLEQNVREAIQ 194
Cdd:COG1196 279 LELELEEAQAEE-------YELLAELARLEQDIARLEERRRELEERLEELE--------------EELAELEEELEELEE 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 195 SNKRLSALNKKQEAEICSLKKELKKAASDLIKSkvtcqykmgeeninLTIKEQKFQELQERLNMELELNEKINEEITHIQ 274
Cdd:COG1196 338 ELEELEEELEEAEEELEEAEAELAEAEEALLEA--------------EAELAEAEEELEELAEELLEALRAAAELAAQLE 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 275 EEKQDIIISFQHMQQLLRQQIQANTEMEAELKVLKENNQTLERDNELQREKVKENEEKFLNLQNEHEKALGtWKRHAEEL 354
Cdd:COG1196 404 ELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAAL-LEAALAEL 482
|
330
....*....|....*.
gi 83715968 355 NGEINKIKNELSSLKE 370
Cdd:COG1196 483 LEELAEAAARLLLLLE 498
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
52-376 |
2.33e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 61.62 E-value: 2.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 52 EEQIGKIIVETQELKWQKETLQNQKETLAE-----------------QHKEAMAVFKKQLQMKMCALEEEKGKYQLATEI 114
Cdd:TIGR02169 183 EENIERLDLIIDEKRQQLERLRREREKAERyqallkekreyegyellKEKEALERQKEAIERQLASLEEELEKLTEEISE 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 115 KEKEIEGLKETLKAL--QVSKYS------LQKKVSEMEQKVQLHLLAKEDYHKQLSEIEKYYATITGQFGLVKENHEKLE 186
Cdd:TIGR02169 263 LEKRLEEIEQLLEELnkKIKDLGeeeqlrVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELE 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 187 QNVREaiqSNKRLSALnkkqEAEICSLKKELKKAASDLikskvtcqykmGEENINLTIKEQKFQELQERLNMeleLNEKI 266
Cdd:TIGR02169 343 REIEE---ERKRRDKL----TEEYAELKEELEDLRAEL-----------EEVDKEFAETRDELKDYREKLEK---LKREI 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 267 NEeithiqeekqdIIISFQHMQQLLRQQIQANTEMEAELKVLKENNQTLERDNELQREKVKENEEKFLNLQneheKALGT 346
Cdd:TIGR02169 402 NE-----------LKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLA----ADLSK 466
|
330 340 350
....*....|....*....|....*....|
gi 83715968 347 WKRHAEELNGEINKIKNELSSLKETHIKLQ 376
Cdd:TIGR02169 467 YEQELYDLKEEYDRVEKELSKLQRELAEAE 496
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
117-370 |
8.32e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 59.01 E-value: 8.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 117 KEIEGLKETLKALQVSKYSLQKKVSEMEQKvqlhllaKEDYHKQLSEIEKYYATITgqfglvkenhEKLEQNVREAIQSN 196
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKE-------EKALLKQLAALERRIAALA----------RRIRALEQELAALE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 197 KRLSALNKKQEAeicsLKKELKKAASDLIKSKVTcQYKMGEEN-INLTIKEQKFQELQERLNMELELNEKINEEITHIQE 275
Cdd:COG4942 83 AELAELEKEIAE----LRAELEAQKEELAELLRA-LYRLGRQPpLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 276 EKQDIiisfqhmQQLLRQQIQANTEMEAELKVLKENNQTLERDNELQREKVKENEEKflnlQNEHEKALGTWKRHAEELN 355
Cdd:COG4942 158 DLAEL-------AALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKE----LAELAAELAELQQEAEELE 226
|
250
....*....|....*
gi 83715968 356 GEINKIKNELSSLKE 370
Cdd:COG4942 227 ALIARLEAEAAAAAE 241
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
101-432 |
1.29e-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: 59.30 E-value: 1.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 101 LEEEKG--KYQLATEIKEKEIEGLKETLKALQVSKYSLQKKVSEMEQKVQLHLLAKEdYHKQLSEIEKYYATitgqfGLV 178
Cdd:TIGR02168 161 FEEAAGisKYKERRKETERKLERTRENLDRLEDILNELERQLKSLERQAEKAERYKE-LKAELRELELALLV-----LRL 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 179 KENHEKLEQNVREAIQSNKRLSALNKKQEAeicslkKELKKAASDLIKSKVtcqykmgeeninltikEQKFQELQERLNM 258
Cdd:TIGR02168 235 EELREELEELQEELKEAEEELEELTAELQE------LEEKLEELRLEVSEL----------------EEEIEELQKELYA 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 259 ELELNEKINEEITHIQEEKQDIIISFQHMQQLLRQQIQANTEMEAELKVLKENNQTLERDNELQREKVKENEEKFLNLQN 338
Cdd:TIGR02168 293 LANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELES 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 339 ---EHEKALGTWKRHAEELNGEINKIKNELSSLKETHIKLQEHYNKLCNQKTFEEDK----KFQNVPEVNNENSEM--ST 409
Cdd:TIGR02168 373 rleELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKleeaELKELQAELEELEEEleEL 452
|
330 340
....*....|....*....|...
gi 83715968 410 EKSENTIIQKYNTEQEIREENME 432
Cdd:TIGR02168 453 QEELERLEEALEELREELEEAEQ 475
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
24-419 |
1.75e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.92 E-value: 1.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 24 SIQLLDFKTSLLEALEELRMRREaeihyEEQIGKIIVETQELKWQKETLQNQKETLaEQHKEAMAVFKKQLQMKMCALEE 103
Cdd:PRK03918 360 RHELYEEAKAKKEELERLKKRLT-----GLTPEKLEKELEELEKAKEEIEEEISKI-TARIGELKKEIKELKKAIEELKK 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 104 EKGK-------------------YQLATEIKEKEIEGLKETLKALQVSKYSLQKKVSEMEQKVQLHLLAKedyhkQLSEI 164
Cdd:PRK03918 434 AKGKcpvcgrelteehrkelleeYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAE-----QLKEL 508
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 165 EKyyatitgqfGLVKENHEKLEQNVREAIQSNKRLSALnkkqEAEICSLKKELKKAAsDLIKSKVTCQYKMGE-----EN 239
Cdd:PRK03918 509 EE---------KLKKYNLEELEKKAEEYEKLKEKLIKL----KGEIKSLKKELEKLE-ELKKKLAELEKKLDEleeelAE 574
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 240 INLTIKEQKFQELQErLNMELELNEKINEEITHIQEEKQDIiisfqhmQQLLRQQIQANTEMEAELKVLKENNQTLER-D 318
Cdd:PRK03918 575 LLKELEELGFESVEE-LEERLKELEPFYNEYLELKDAEKEL-------EREEKELKKLEEELDKAFEELAETEKRLEElR 646
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 319 NELQREKVKENEEKFLNLQNEH-----------------EKALGTWKRHAEELN---GEINKIKNELSSLKETHIKLQEH 378
Cdd:PRK03918 647 KELEELEKKYSEEEYEELREEYlelsrelaglraeleelEKRREEIKKTLEKLKeelEEREKAKKELEKLEKALERVEEL 726
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 83715968 379 YNKLCNQKTFEEDKKFQNVPEVNNE-NSEMSTEKSENTIIQK 419
Cdd:PRK03918 727 REKVKKYKALLKERALSKVGEIASEiFEELTEGKYSGVRVKA 768
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
137-382 |
3.67e-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: 57.76 E-value: 3.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 137 QKKVSEMEQKVQLHLLAKEDYHKQLSEIEKYYATITGQFGLVKENHEKLEQNVREAIQSNKRLSALNKKQEAEICSLKKE 216
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 217 LKkaasDLIKSKVTCQYKMGEENINLTIKEQKFQELQERLNMELELNEKINEEITHIQEEKQDIIISFQH----MQQLLR 292
Cdd:TIGR02168 756 LT----ELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANlrerLESLER 831
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 293 QQIQANTEMEAELKVLKENNQTLER------DNELQREKVKENEEKFLNLQNEHEKALGTWKRHAEELNGEINKIKNELS 366
Cdd:TIGR02168 832 RIAATERRLEDLEEQIEELSEDIESlaaeieELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRS 911
|
250
....*....|....*.
gi 83715968 367 SLKETHIKLQEHYNKL 382
Cdd:TIGR02168 912 ELRRELEELREKLAQL 927
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
63-408 |
8.64e-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: 8.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 63 QELKWQKETLQ-----NQKETLAEQhKEAMAVFKKQLQMKMCALEEEKGKYQLATEIKEKEIEGLKETLKALQVSKYSLQ 137
Cdd:TIGR02168 216 KELKAELRELElallvLRLEELREE-LEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALA 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 138 KKVSEMEQKVQLHLLAKEDYHKQLSEIEkyyatitgqfglvkenhEKLEQNVREAIQSNKRLSALNKKQE---AEICSLK 214
Cdd:TIGR02168 295 NEISRLEQQKQILRERLANLERQLEELE-----------------AQLEELESKLDELAEELAELEEKLEelkEELESLE 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 215 KELKKAASDLIKSKVTcqykmgeeninLTIKEQKFQELQERLNMELELNEKINEEITHIQEEKQDIiisfQHMQQLLRQQ 294
Cdd:TIGR02168 358 AELEELEAELEELESR-----------LEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERL----EDRRERLQQE 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 295 IQANtEMEAELKVLKENNQTLERDNELQREKVKENEEKFLNLqnehekalgtwkrhaEELNGEINKIKNELSSLKETHIK 374
Cdd:TIGR02168 423 IEEL-LKKLEEAELKELQAELEELEEELEELQEELERLEEAL---------------EELREELEEAEQALDAAERELAQ 486
|
330 340 350
....*....|....*....|....*....|....
gi 83715968 375 LQEHYNKLCNQKTfEEDKKFQNVPEVNNENSEMS 408
Cdd:TIGR02168 487 LQARLDSLERLQE-NLEGFSEGVKALLKNQSGLS 519
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
8-388 |
1.39e-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: 1.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 8 ESSSTFTLQSSSETLFSIQLLDFKTSLLEALEELRMRREAEIHYEEQIG----KIIVETQELKWQKETLQNQKETLAEQH 83
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISalrkDLARLEAEVEQLEERIAQLSKELTELE 760
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 84 KEAMAVFKK--QLQMKMCALEEEKGKYQLATEIKEKEIEGLKETLKALQVSKYSLQKKVSEMEQKVQLHLLAKEDYHKQL 161
Cdd:TIGR02168 761 AEIEELEERleEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRL 840
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 162 SEIEKYYATITGQFGLVKENHEKLEQNVREAIQSNKRLSALNKKQEAEICSLKKELKKAASDLikskvtcqykmGEENIN 241
Cdd:TIGR02168 841 EDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEEL-----------RELESK 909
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 242 LTIKEQKFQELQERLN-MELELnEKINEEITHIQEE-KQDIIISFQHMQQLLRQQIQANTEMEAELKVLKENNQTLERDN 319
Cdd:TIGR02168 910 RSELRRELEELREKLAqLELRL-EGLEVRIDNLQERlSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVN 988
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 83715968 320 ELQREKVKENEEKFLNLQNEHE---KALGTWKRHAEELNGEInkikneLSSLKETHIKLQEHYNKLCnQKTF 388
Cdd:TIGR02168 989 LAAIEEYEELKERYDFLTAQKEdltEAKETLEEAIEEIDREA------RERFKDTFDQVNENFQRVF-PKLF 1053
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
34-429 |
1.93e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.46 E-value: 1.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 34 LLEALEELRMRREA---EIHYEEQIGKIIVETQELKWQKETLQNQKETLAEQHKEAMAVFKKQLQmKMCALEEEKGKYQL 110
Cdd:PRK03918 167 LGEVIKEIKRRIERlekFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVK-ELEELKEEIEELEK 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 111 ATEIKEKEIEGLKETLKALQVSKYSLQKKVSEMEQKV----QLHLLAKE---------DYHKQLSEIEKYYATITGQFGL 177
Cdd:PRK03918 246 ELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVkelkELKEKAEEyiklsefyeEYLDELREIEKRLSRLEEEING 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 178 VKENHEKLEQNVREAIQSNKRLSALNKKQEA---------EICSLKKELKKaasdlIKSKVTCqYKMGEENINLTIKEQK 248
Cdd:PRK03918 326 IEERIKELEEKEERLEELKKKLKELEKRLEEleerhelyeEAKAKKEELER-----LKKRLTG-LTPEKLEKELEELEKA 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 249 FQELQERLNmelELNEKINEEITHIQEEKQDII---------------ISFQHMQQLLRQQIQANTEMEAELKVLKENNQ 313
Cdd:PRK03918 400 KEEIEEEIS---KITARIGELKKEIKELKKAIEelkkakgkcpvcgreLTEEHRKELLEEYTAELKRIEKELKEIEEKER 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 314 TLERdNELQREKVKENEEKFLNLQN------EHEKALGTW--------KRHAEELNGEINKIKNELSSLKETHIKLQEHY 379
Cdd:PRK03918 477 KLRK-ELRELEKVLKKESELIKLKElaeqlkELEEKLKKYnleelekkAEEYEKLKEKLIKLKGEIKSLKKELEKLEELK 555
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 83715968 380 NKLC----NQKTFEEDKK----------FQNVPEVNNENSEMstEKSENTIIQKYNTEQEIREE 429
Cdd:PRK03918 556 KKLAelekKLDELEEELAellkeleelgFESVEELEERLKEL--EPFYNEYLELKDAEKELERE 617
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
173-433 |
3.77e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 54.30 E-value: 3.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 173 GQFGLVKENHEKLEQNVREAIQ------SNKRLSALNKKQEAEICSLKKELKKAAS--DLIKSKVTCQYKMGEENINLTI 244
Cdd:PRK03918 135 GEIDAILESDESREKVVRQILGlddyenAYKNLGEVIKEIKRRIERLEKFIKRTENieELIKEKEKELEEVLREINEISS 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 245 KEQKFQELQERLNMELELNEKINEEITHIQEEKQDIIISFQHMQQLLRQQIQANTEMEAELKVLKENNQTLE--RDNELQ 322
Cdd:PRK03918 215 ELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKelKEKAEE 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 323 REKVKENEEKFLNLQNEHEKALGTW-----------------KRHAEELNGEINKIKNELSSLKETHIKLQEHYNKLCNQ 385
Cdd:PRK03918 295 YIKLSEFYEEYLDELREIEKRLSRLeeeingieerikeleekEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEEL 374
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 83715968 386 KTFEEDKKFQNVPEVNNENSEMSTEKSE-----NTIIQKYNTEQEIREENMEN 433
Cdd:PRK03918 375 ERLKKRLTGLTPEKLEKELEELEKAKEEieeeiSKITARIGELKKEIKELKKA 427
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
32-432 |
4.32e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 54.28 E-value: 4.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 32 TSLLEALEELRMRREAEIHYEEQIGKiivETQELKWQKETLQNQKETLAEQ------HKEAMAVFKKQLQMKMCALEEEK 105
Cdd:PRK02224 254 ETLEAEIEDLRETIAETEREREELAE---EVRDLRERLEELEEERDDLLAEaglddaDAEAVEARREELEDRDEELRDRL 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 106 GKYQLATEIKEKEIEGLKETLKALQVSKYSLQKKVSEMEQKVQLHLLAKEDYHKQLSEIEKYYATITGQFGLVKENHEKL 185
Cdd:PRK02224 331 EECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNA 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 186 EqNVREAIQSNK-RLSALNKKQEAEICSLKKELKKAASDLIKSKV-TCQYKMGEENINLTI--KEQKFQELQERL-NMEL 260
Cdd:PRK02224 411 E-DFLEELREERdELREREAELEATLRTARERVEEAEALLEAGKCpECGQPVEGSPHVETIeeDRERVEELEAELeDLEE 489
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 261 E---LNEKINE---------EITHIQEEKQDIiisfqhmQQLLRQQIQANTEMEAELKVLKENNQTLERDNELQREKVKE 328
Cdd:PRK02224 490 EveeVEERLERaedlveaedRIERLEERREDL-------EELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAE 562
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 329 NEEkflnlqnEHEKALGTwkrhAEELNGEINKIKNELSSLKETHIKLQEHYNklCNQKTFEEDKKFQNVPEVNNENSEMS 408
Cdd:PRK02224 563 AEE-------EAEEAREE----VAELNSKLAELKERIESLERIRTLLAAIAD--AEDEIERLREKREALAELNDERRERL 629
|
410 420
....*....|....*....|....
gi 83715968 409 TEKSEntiiQKYNTEQEIREENME 432
Cdd:PRK02224 630 AEKRE----RKRELEAEFDEARIE 649
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
34-324 |
4.84e-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: 4.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 34 LLEALEELRMRREAEihyEEQIGKIIVETQELKWQKETLQNQKETLAEQHKEAMAvfkkqlqmkmcALEEEKGKYQLAT- 112
Cdd:COG1196 230 LLLKLRELEAELEEL---EAELEELEAELEELEAELAELEAELEELRLELEELEL-----------ELEEAQAEEYELLa 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 113 --EIKEKEIEGLKETLKALQVSKYSLQKKVSEMEQKVQLHLLAKEDYHKQLSEIEKYYATITGQFGLVKENHEKLEQNVR 190
Cdd:COG1196 296 elARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 191 EAIQSNKRLSALNKKQEAEICSLKKELKKAASDLikskvtcQYKMGEENINLTIKEQKFQELQERLNMELELNEKINEEI 270
Cdd:COG1196 376 EAEEELEELAEELLEALRAAAELAAQLEELEEAE-------EALLERLERLEEELEELEEALAELEEEEEEEEEALEEAA 448
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 83715968 271 THIQEEKQDIIISFQHMQQLLRQQIQANTEMEAELKVLKENNQTLERDNELQRE 324
Cdd:COG1196 449 EEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEAD 502
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
30-382 |
7.94e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 53.53 E-value: 7.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 30 FKTSLLEALEELR-----MRREAEI------HYEEQIGKIIVETQELKWQKETLQNQKETLAEQHkEAMAVFKKQLQMKM 98
Cdd:TIGR02169 668 FSRSEPAELQRLRerlegLKRELSSlqselrRIENRLDELSQELSDASRKIGEIEKEIEQLEQEE-EKLKERLEELEEDL 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 99 CALEEEKGKYQLATEIKEKEIEGLKETLKALQVSKYSLQKKVSEME-QKVQLHLLAKEDYHkqlSEIEKYYATITGQFGL 177
Cdd:TIGR02169 747 SSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRiPEIQAELSKLEEEV---SRIEARLREIEQKLNR 823
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 178 VKENHEKLEQNVREAIQSNKRLSALNKKQEAEICSLKKELKKAASDLIKSKVTcQYKMGEENINLTIK----EQKFQELQ 253
Cdd:TIGR02169 824 LTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAA-LRDLESRLGDLKKErdelEAQLRELE 902
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 254 ERLNmelELNEKINEEITHIQEEKQDIIISFQHMQQLLR--QQIQANTEMEAELKVLKENNQTLERD-------NELQRE 324
Cdd:TIGR02169 903 RKIE---ELEAQIEKKRKRLSELKAKLEALEEELSEIEDpkGEDEEIPEEELSLEDVQAELQRVEEEiralepvNMLAIQ 979
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 83715968 325 KVKENEEKFLNLQNEHEKaLGTWKRHAEELNGEINKIKNElsSLKETHIKLQEHYNKL 382
Cdd:TIGR02169 980 EYEEVLKRLDELKEKRAK-LEEERKAILERIEEYEKKKRE--VFMEAFEAINENFNEI 1034
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
110-377 |
1.03e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.02 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 110 LATEIkEKEIEGLKEtlKALQVSKY-SLQKKvsEMEQKVQLHLLAKEDYHKQLSEIEkyyatitgqfglvkenhEKLEQN 188
Cdd:COG1196 194 ILGEL-ERQLEPLER--QAEKAERYrELKEE--LKELEAELLLLKLRELEAELEELE-----------------AELEEL 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 189 VREAIQSNKRLSALnkkqEAEICSLKKELKKAasdlikskvtcqykmgeeninltikEQKFQELQERLNMELELNEKINE 268
Cdd:COG1196 252 EAELEELEAELAEL----EAELEELRLELEEL-------------------------ELELEEAQAEEYELLAELARLEQ 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 269 EITHIQEEKQDIIISFQHMQQLLRQQIQANTEMEAELKVLKENNQTLERDNELQREKVKENEEKFLNLQNEHEKALGTWK 348
Cdd:COG1196 303 DIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELE 382
|
250 260
....*....|....*....|....*....
gi 83715968 349 RHAEELNGEINKIKNELSSLKETHIKLQE 377
Cdd:COG1196 383 ELAEELLEALRAAAELAAQLEELEEAEEA 411
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
102-427 |
1.66e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 52.38 E-value: 1.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 102 EEEKGKYQLATEIKEKEIEGL-KETLKALqvsKY-SLQKKVSEMEQKvqLHLLAKEDYHKQLSEIEKYYATITGQfglVK 179
Cdd:TIGR02169 183 EENIERLDLIIDEKRQQLERLrREREKAE---RYqALLKEKREYEGY--ELLKEKEALERQKEAIERQLASLEEE---LE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 180 ENHEKLEQNVREAIQSNKRLSALNKKQEA----EICSLKKELKKAASDLIKSKVtcqykmgeeniNLTIKEQKFQELQER 255
Cdd:TIGR02169 255 KLTEEISELEKRLEEIEQLLEELNKKIKDlgeeEQLRVKEKIGELEAEIASLER-----------SIAEKERELEDAEER 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 256 LNMELELNEKINEEITHIQEEKQDiiisfqhmQQLLRQQIQAntemeaELKVLKENNQTLERDNElqrekvkeneekfln 335
Cdd:TIGR02169 324 LAKLEAEIDKLLAEIEELEREIEE--------ERKRRDKLTE------EYAELKEELEDLRAELE--------------- 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 336 lqnEHEKALGTWKRHAEELNGEINKIKNELSSLKETHIKLQEHYNKLCNQKTF---------EEDKKFQNVPEVNNENSE 406
Cdd:TIGR02169 375 ---EVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADlnaaiagieAKINELEEEKEDKALEIK 451
|
330 340
....*....|....*....|.
gi 83715968 407 MSTEKSENTIIQKYNTEQEIR 427
Cdd:TIGR02169 452 KQEWKLEQLAADLSKYEQELY 472
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
26-224 |
2.37e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.86 E-value: 2.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 26 QLLDFKTSLLEALEELRMRREAEIHYEEQIGKIIVETQELKWQKETLQNQKETLAEQHKEAMAVFKKQLQmkmcALEEEK 105
Cdd:COG1196 289 EEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEA----ELAEAE 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 106 GKYQLATEIKEKEIEGLKETLKALQvskySLQKKVSEMEQKVQLHLLAKEDYHKQLSEIEKYYATITGQFGLVKENHEKL 185
Cdd:COG1196 365 EALLEAEAELAEAEEELEELAEELL----EALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEE 440
|
170 180 190
....*....|....*....|....*....|....*....
gi 83715968 186 EQNVREAIQSNKRLSALNKKQEAEICSLKKELKKAASDL 224
Cdd:COG1196 441 EEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAAL 479
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
31-435 |
3.00e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 51.68 E-value: 3.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 31 KTSLLEALEELRMRREAEIhyeEQIGKIIVETQELKWQKETLQNQKETLAEQHKEAMAVFKKQLQMKMCALEEEKGKYQL 110
Cdd:PTZ00121 1576 KNMALRKAEEAKKAEEARI---EEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEEL 1652
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 111 ATEIKEKEIEGLKETLKALQVSKYSLQ-KKVSEMEQKVQLHLLAKEDYHKQLSEIEKYYAtitgqfglvkENHEKLEQNV 189
Cdd:PTZ00121 1653 KKAEEENKIKAAEEAKKAEEDKKKAEEaKKAEEDEKKAAEALKKEAEEAKKAEELKKKEA----------EEKKKAEELK 1722
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 190 REAIQSNKRLSALNKKQEAEicslKKELKKAASDLIKSKVTCQYKMGEENINLTIKEQKFQELQErlnmelELNEKINEE 269
Cdd:PTZ00121 1723 KAEEENKIKAEEAKKEAEED----KKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEE------ELDEEDEKR 1792
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 270 ITHIQEEKQDIIISFQHMQQLLRQ-QIQANTEMEAELKVLKENNQTlerdNELQREKVKENEEKFLNLQNEHEKALGTwk 348
Cdd:PTZ00121 1793 RMEVDKKIKDIFDNFANIIEGGKEgNLVINDSKEMEDSAIKEVADS----KNMQLEEADAFEKHKFNKNNENGEDGNK-- 1866
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 349 rhaeelNGEINKIKNELSSLKETHIKLQEhyNKLCNQKTFEEDKKFQNVPEVNNENSEMSTEKSENTIIQKYNTEQEIRE 428
Cdd:PTZ00121 1867 ------EADFNKEKDLKEDDEEEIEEADE--IEKIDKDDIEREIPNNNMAGKNNDIIDDKLDKDEYIKRDAEETREEIIK 1938
|
....*..
gi 83715968 429 ENMENFC 435
Cdd:PTZ00121 1939 ISKKDMC 1945
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
29-342 |
3.81e-06 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 51.13 E-value: 3.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 29 DFKTSLLEALEELRMRREAEIHYEeqigKIIVETQELK---WQKETLQNQKETLAEQHKEAMAVFKKQLQMKMCALEEEK 105
Cdd:pfam02463 153 ERRLEIEEEAAGSRLKRKKKEALK----KLIEETENLAeliIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLY 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 106 GKYQLATEIKEKEIEGLKETLKALQVSKYSLQKKVSEMEQKVQ----LHLLAKEDYHKQLSEIEKYYATITGQFGLVKEN 181
Cdd:pfam02463 229 LDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLkenkEEEKEKKLQEEELKLLAKEEEELKSELLKLERR 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 182 HEKLEQNVREAIQSNKRLSALNKKQEAEICSLKKELKKAASDLIKSKVTCQYKMGEENINLTIKEQ---KFQELQERLNM 258
Cdd:pfam02463 309 KVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEEllaKKKLESERLSS 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 259 ELELNEKINEEITHIQEEKQDIIisfQHMQQLLRQQIQANTEMEAELKVLKENNQTLERDNELQREKVKENEEKFLNLQN 338
Cdd:pfam02463 389 AAKLKEEELELKSEEEKEAQLLL---ELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDEL 465
|
....
gi 83715968 339 EHEK 342
Cdd:pfam02463 466 ELKK 469
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
24-377 |
4.01e-06 |
|
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: 51.27 E-value: 4.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 24 SIQLLDFKtSLLEALEELRMRREAEIHYEEqiGKIIVETQELKWQKETLQNQKETLAEQHKEAMAvfkkqlqmkmcalee 103
Cdd:pfam15921 209 SMSTMHFR-SLGSAISKILRELDTEISYLK--GRIFPVEDQLEALKSESQNKIELLLQQHQDRIE--------------- 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 104 ekgkyQLATEiKEKEIEGLKETLKALQVSKYSLQKKVSEMEQKVQLHllaKEDYHKQLSEIEkyyATITgqfglvkenhe 183
Cdd:pfam15921 271 -----QLISE-HEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQ---NSMYMRQLSDLE---STVS----------- 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 184 KLEQNVREAiqsnKRLsalnkkQEAEICSLKKELKKAASDLIKSKvTCQYKMGEENINLTIKEQK----FQELQERLNME 259
Cdd:pfam15921 328 QLRSELREA----KRM------YEDKIEELEKQLVLANSELTEAR-TERDQFSQESGNLDDQLQKlladLHKREKELSLE 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 260 LELNEKINEE-------ITHIQEEKQDIIISFQHMQQLLRQ-QIQANTEMEAELKVLKENNQTLER----------DNEL 321
Cdd:pfam15921 397 KEQNKRLWDRdtgnsitIDHLRRELDDRNMEVQRLEALLKAmKSECQGQMERQMAAIQGKNESLEKvssltaqlesTKEM 476
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 83715968 322 QREKVKENEEKFLNLQNEHEK------ALGTWKRHAEELNGEINKIKNELSslkethIKLQE 377
Cdd:pfam15921 477 LRKVVEELTAKKMTLESSERTvsdltaSLQEKERAIEATNAEITKLRSRVD------LKLQE 532
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
61-438 |
4.14e-06 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 50.89 E-value: 4.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 61 ETQELKWQKETLQNQKETLAEQHKEAMAvfkkqlqmkmcalEEEKGKYQLATEIkEKEIEGLKETLKALQVskysLQKKV 140
Cdd:pfam05557 3 ELIESKARLSQLQNEKKQMELEHKRARI-------------ELEKKASALKRQL-DRESDRNQELQKRIRL----LEKRE 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 141 SEMEQKvqlhllakedYHKQLSEIEKYYATITGQFGLVKENHEKLEQnVREAIQS-NKRLSALN---KKQEAEICSLKKE 216
Cdd:pfam05557 65 AEAEEA----------LREQAELNRLKKKYLEALNKKLNEKESQLAD-AREVISClKNELSELRrqiQRAELELQSTNSE 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 217 LKKAasdlikskvtcQYKMGEENINLTIKEQKFQELQERLNMELELNEKINEEITHIQEEKQDIIISFQHMQQLLRQqiq 296
Cdd:pfam05557 134 LEEL-----------QERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIKELEFEIQSQEQDSEIVKNSKSELARI--- 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 297 anTEMEAELKVLKENNQ---TLERDNELQREKVK------ENEEKF------LNLQNEH-EKALGTWKRHA--------- 351
Cdd:pfam05557 200 --PELEKELERLREHNKhlnENIENKLLLKEEVEdlkrklEREEKYreeaatLELEKEKlEQELQSWVKLAqdtglnlrs 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 352 -EELNGEINKIKNELSSLKETHIKLQEHYNKLCNQKTFEEDKKFQNVPEVNNENSEMSTEKSENTIIQK----YNTEQEI 426
Cdd:pfam05557 278 pEDLSRRIEQLQQREIVLKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRrvllLTKERDG 357
|
410
....*....|..
gi 83715968 427 REENMENFCSDT 438
Cdd:pfam05557 358 YRAILESYDKEL 369
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
169-377 |
1.50e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.61 E-value: 1.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 169 ATITGQFGLVKENHEKLEQNVREAIQSNKRLSALNKKQEA---EICSLKKELKKAASDLIKSKVtcQYKMGEENINLTIK 245
Cdd:COG4942 13 LAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKAllkQLAALERRIAALARRIRALEQ--ELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 246 EQkfQELQERLNmelELNEKINEEITHIQ--------------EEKQDIIISFQHMQQLLRQQIQANTEMEAELKVLKEN 311
Cdd:COG4942 91 EI--AELRAELE---AQKEELAELLRALYrlgrqpplalllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAAL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 83715968 312 NQTLERDNELQREKVKENEEKFLNLQNEHEKAlgtwKRHAEELNGEINKIKNELSSLKETHIKLQE 377
Cdd:COG4942 166 RAELEAERAELEALLAELEEERAALEALKAER----QKLLARLEKELAELAAELAELQQEAEELEA 227
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
213-393 |
3.08e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.23 E-value: 3.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 213 LKKELKKAASDLIKSK------VTCQYKMGEENIN-LTIKEQKFQELQERL---NMELELNEKINEEITHIQEEKQDIII 282
Cdd:COG4717 47 LLERLEKEADELFKPQgrkpelNLKELKELEEELKeAEEKEEEYAELQEELeelEEELEELEAELEELREELEKLEKLLQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 283 SFQHMQQL--LRQQIQANTE----MEAELKVLKENNQTLERDNELQREKVKENEEKFLNLQNEHEKALGTWKRHAEELNG 356
Cdd:COG4717 127 LLPLYQELeaLEAELAELPErleeLEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQ 206
|
170 180 190
....*....|....*....|....*....|....*..
gi 83715968 357 EINKIKNELSSLKETHIKLQEHYNKLCNQKTFEEDKK 393
Cdd:COG4717 207 RLAELEEELEEAQEELEELEEELEQLENELEAAALEE 243
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
14-429 |
4.95e-05 |
|
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: 47.66 E-value: 4.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 14 TLQSSSETLfsIQLLDFKTSLLEALEELRMRREAEIHYE--EQIGKIIVETQElKWQKETLQNQKETLAEQHKEAMAvfK 91
Cdd:TIGR00618 383 TLQQQKTTL--TQKLQSLCKELDILQREQATIDTRTSAFrdLQGQLAHAKKQQ-ELQQRYAELCAAAITCTAQCEKL--E 457
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 92 KQLQMKMC-ALEEEKGKYQLATEIKEKEIEGLKETLKALQVSKYS---LQKKVSEMEQKVQL---------HLLAKEDYH 158
Cdd:TIGR00618 458 KIHLQESAqSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEpcpLCGSCIHPNPARQDidnpgpltrRMQRGEQTY 537
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 159 KQLSEIEKyyaTITGQFGLVKENHEKLEQNVREAIQSNKRLSALNKKQEAEICSLKKELKKAaSDLIKSKVTCQYKMGEE 238
Cdd:TIGR00618 538 AQLETSEE---DVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRL-QDLTEKLSEAEDMLACE 613
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 239 NINLTIKEQKFQELQERLNMELELNEKINEEITHIQEEKQDIiisfqhMQQLLRQQIQANTEMEAELKVLKENNQTLERD 318
Cdd:TIGR00618 614 QHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTL------TQERVREHALSIRVLPKELLASRQLALQKMQS 687
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 319 NELQREKVKENEEKFLNLQNEHEKALGTWKRHAEEL----NGEINKIKNELSSLKETHIKLQEHYNKLCNQKTFEEDKKF 394
Cdd:TIGR00618 688 EKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIenasSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNN 767
|
410 420 430
....*....|....*....|....*....|....*
gi 83715968 395 QNVPevnnenSEMSTEKSENTIIQKYNTEQEIREE 429
Cdd:TIGR00618 768 EEVT------AALQTGAELSHLAAEIQFFNRLREE 796
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
16-429 |
7.01e-05 |
|
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: 47.04 E-value: 7.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 16 QSSSETLFSIQLLDFKTSLLEALEELR-MRREAEIHYEeqiGKIIVETQELKWQKETLQNQKETLAEQHKEAmavFKKQL 94
Cdd:pfam17380 224 QGMPHTLAPYEKMERRKESFNLAEDVTtMTPEYTVRYN---GQTMTENEFLNQLLHIVQHQKAVSERQQQEK---FEKME 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 95 QMKMCALEEEKGKyQLATEIKEKEIEGLKETLKALQVSKYSLQKKVSeMEQKVQLHLLAKEDYHKQLSEIEKYyatitgQ 174
Cdd:pfam17380 298 QERLRQEKEEKAR-EVERRRKLEEAEKARQAEMDRQAAIYAEQERMA-MERERELERIRQEERKRELERIRQE------E 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 175 FGLVKENHEKLEQNVREAIQSNKRLsalnkkqeaeicslKKELKKAAsdlikskvtcQYKMGEENINLTIKEQKFQELQE 254
Cdd:pfam17380 370 IAMEISRMRELERLQMERQQKNERV--------------RQELEAAR----------KVKILEEERQRKIQQQKVEMEQI 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 255 RLNMElelnEKINEEITHIQEEKQDIIISFQHMQQLLRQQIQANTEMEAELKVLKENNQTLERDN---ELQREKVKENEE 331
Cdd:pfam17380 426 RAEQE----EARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRkraEEQRRKILEKEL 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 332 KflnlqnEHEKALGTWKRHAEELNGEINKIKNELSSLKETHIKLQEHYnklcNQKTFEEDKKFQ-NVPEVNNENSEMSTE 410
Cdd:pfam17380 502 E------ERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERR----KQQEMEERRRIQeQMRKATEERSRLEAM 571
|
410
....*....|....*....
gi 83715968 411 KSENTIIQKYNTEQEIREE 429
Cdd:pfam17380 572 EREREMMRQIVESEKARAE 590
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
116-343 |
8.95e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.55 E-value: 8.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 116 EKEIEGLKETLKALQ--VSKYSLQKKVSEMEQKVQLHLlakedyhKQLSEIEKYYATITGQFGLVKENHEKLEQNVREAI 193
Cdd:COG3206 181 EEQLPELRKELEEAEaaLEEFRQKNGLVDLSEEAKLLL-------QQLSELESQLAEARAELAEAEARLAALRAQLGSGP 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 194 QSNKRLSalnkkQEAEICSLKKELKKAasdlikskvtcqykmgeeninltikEQKFQELQERLNME----LELNEKINEE 269
Cdd:COG3206 254 DALPELL-----QSPVIQQLRAQLAEL-------------------------EAELAELSARYTPNhpdvIALRAQIAAL 303
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 83715968 270 ITHIQEEKQDIIISFQHMQQLLRQQIQANTEMEAELKV-LKENNQTLERDNELQREkVKENEEKFLNLQNEHEKA 343
Cdd:COG3206 304 RAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEArLAELPELEAELRRLERE-VEVARELYESLLQRLEEA 377
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
81-393 |
9.35e-05 |
|
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: 46.50 E-value: 9.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 81 EQHKEAMA---VFKKQLQMKMCALEEEKGKYQLATEIKEKEIEGLKETLKALQVSKYSLQKKVSEMEQKVQLHLLAKEdy 157
Cdd:TIGR00618 187 AKKKSLHGkaeLLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQ-- 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 158 hkQLSEIEKYyatiTGQFGLVKENHEKLEQNVREA--IQSNKRLSALNKKQEAEICSLKKELKKAASDLIKSKVTCQYKm 235
Cdd:TIGR00618 265 --LRARIEEL----RAQEAVLEETQERINRARKAAplAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQ- 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 236 geeninLTIKEQkfQELQERLNMELELNEKINEEITHIQEEKQDIIISFQHMQQlLRQQIQANTEMEAEL--KVLKENNQ 313
Cdd:TIGR00618 338 ------SSIEEQ--RRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHT-LQQQKTTLTQKLQSLckELDILQRE 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 314 TLERDNELQREKVKENEEKFLNLQNEHEKALGTWKRHAeelngeinkIKNELSSLKETHIKLQEHYNKLCNQKTFEEDKK 393
Cdd:TIGR00618 409 QATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAA---------ITCTAQCEKLEKIHLQESAQSLKEREQQLQTKE 479
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
70-433 |
2.18e-04 |
|
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: 45.81 E-value: 2.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 70 ETLQNQKETLAEQHKEAMAVFKKQLQMKMCALEEEKGK-YQLATEIKEKEIEGLKEtlKALQVSK-YSLQKKVSEMEQKV 147
Cdd:TIGR01612 1250 EDLDEIKEKSPEIENEMGIEMDIKAEMETFNISHDDDKdHHIISKKHDENISDIRE--KSLKIIEdFSEESDINDIKKEL 1327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 148 QLHLLakeDYHKQLSEIEKYYATITGQFGLVKENheKLEQNVREAIQSNKRLSALNKKQEAEICSLKKELKKAASDLikS 227
Cdd:TIGR01612 1328 QKNLL---DAQKHNSDINLYLNEIANIYNILKLN--KIKKIIDEVKEYTKEIEENNKNIKDELDKSEKLIKKIKDDI--N 1400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 228 KVTCQYKMgEENINLTIKEQKFQELQERLNMELELNEKINEEITHIQEEKQDIIISFQHMQQllrqqiqANTEMEAELKV 307
Cdd:TIGR01612 1401 LEECKSKI-ESTLDDKDIDECIKKIKELKNHILSEESNIDTYFKNADENNENVLLLFKNIEM-------ADNKSQHILKI 1472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 308 lKENNQTLERD---NELQREKVKENEEKFLNLQNEH--EKALGTWKRHAEELNGEINK-----IKNELSSLKETHIKLQE 377
Cdd:TIGR01612 1473 -KKDNATNDHDfniNELKEHIDKSKGCKDEADKNAKaiEKNKELFEQYKKDVTELLNKysalaIKNKFAKTKKDSEIIIK 1551
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 83715968 378 HYNKLCNQKTFEEDKKFQNVPEVNNENSEMSTEKSENTIIQKYNTEQEIREENMEN 433
Cdd:TIGR01612 1552 EIKDAHKKFILEAEKSEQKIKEIKKEKFRIEDDAAKNDKSNKAAIDIQLSLENFEN 1607
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
60-322 |
2.51e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 45.21 E-value: 2.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 60 VETQELKWQKETLQNQKETLAEQHKEAMAVFKKQLQMKMCALEEEKGKYQLATEIKEKEIEGLKETLKALQVSKYSLQKK 139
Cdd:pfam12128 265 FGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLDADIETAAA 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 140 VSEMEQKVQlhllakedyhKQLSEIEKYYATITGQFGLVKENHEKLEQNVREaiQSNKRLSALNKKQEA--EICSLKKEL 217
Cdd:pfam12128 345 DQEQLPSWQ----------SELENLEERLKALTGKHQDVTAKYNRRRSKIKE--QNNRDIAGIKDKLAKirEARDRQLAV 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 218 KKAASDLIKSKVTCQYKMGEENIN-------LTIKEQKFQELQERLNMELELNEKINEEITHIQEEKQDiiISFQHMQQL 290
Cdd:pfam12128 413 AEDDLQALESELREQLEAGKLEFNeeeyrlkSRLGELKLRLNQATATPELLLQLENFDERIERAREEQE--AANAEVERL 490
|
250 260 270
....*....|....*....|....*....|...
gi 83715968 291 LRQQIQANTEMEAELKVLKENNQTL-ERDNELQ 322
Cdd:pfam12128 491 QSELRQARKRRDQASEALRQASRRLeERQSALD 523
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
63-224 |
3.82e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.98 E-value: 3.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 63 QELKWQKETLQNQKETLAEQHKEAMAVFK--KQLQMKMCALEEEKGKYQLATEIKEKEIEGLKETLKALQVSKYSLQKKV 140
Cdd:COG4942 27 AELEQLQQEIAELEKELAALKKEEKALLKqlAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEEL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 141 SEMEQKVQLH--------LLAKED---------YHKQLS--------EIEKYYATITGQFGLVKENHEKLEQNVREAIQS 195
Cdd:COG4942 107 AELLRALYRLgrqpplalLLSPEDfldavrrlqYLKYLAparreqaeELRADLAELAALRAELEAERAELEALLAELEEE 186
|
170 180
....*....|....*....|....*....
gi 83715968 196 NKRLSALNKKQEAEICSLKKELKKAASDL 224
Cdd:COG4942 187 RAALEALKAERQKLLARLEKELAELAAEL 215
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
34-382 |
3.86e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.37 E-value: 3.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 34 LLEALEELRMRREAEIHYEEQIGKIIVETQELKWQKETLQNQKETLAEQHKEAMAVFkkqlqmkmcALEEEKGKYQLATE 113
Cdd:COG4717 130 LYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQL---------SLATEEELQDLAEE 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 114 IKE--KEIEGLKETLKALQVSKYSLQKKVSEMEQKvqlhlLAKEDYHKQLSEIEKYYATITGQFGLVKENHEKLEQNVRE 191
Cdd:COG4717 201 LEElqQRLAELEEELEEAQEELEELEEELEQLENE-----LEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTI 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 192 A---------------IQSNKRLSALNKKQEAEICSLKKELKKAASDLIKSKVtcQYKMGEENINLTIKEQKFQELQERL 256
Cdd:COG4717 276 AgvlflvlgllallflLLAREKASLGKEAEELQALPALEELEEEELEELLAAL--GLPPDLSPEELLELLDRIEELQELL 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 257 NMELELNEKIneEITHIQEEKqdiiisfqhmQQLLRqqiQANTEMEAELkvlkenNQTLERDNELQ--REKVKENEEKFL 334
Cdd:COG4717 354 REAEELEEEL--QLEELEQEI----------AALLA---EAGVEDEEEL------RAALEQAEEYQelKEELEELEEQLE 412
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 83715968 335 NLQNEHEKALGTWKRhaEELNGEINKIKNELSSLKETHIKLQEHYNKL 382
Cdd:COG4717 413 ELLGELEELLEALDE--EELEEELEELEEELEELEEELEELREELAEL 458
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
31-518 |
4.79e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.36 E-value: 4.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 31 KTSLLEALEELRMRREAEIHYEEQIGKIIVETQELKWQKETLQNQKETLAEQHK--------EAMAVFKKQLQMKMCALE 102
Cdd:PTZ00121 1523 KADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKnmalrkaeEAKKAEEARIEEVMKLYE 1602
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 103 EEKGKYQLATEIKEKEIEGLKETLKALQVSKYSLQKKVSEMEQKVQLHLLAKEDyhkqlseiekyyatitgqfglvKENH 182
Cdd:PTZ00121 1603 EEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAE----------------------EENK 1660
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 183 EKLEQNVREAIQSNKRLSALNKKQE----AEICSLKKELKKAASDLIKSKVTCQYKMGEEninLTIKEQKFQELQERLNM 258
Cdd:PTZ00121 1661 IKAAEEAKKAEEDKKKAEEAKKAEEdekkAAEALKKEAEEAKKAEELKKKEAEEKKKAEE---LKKAEEENKIKAEEAKK 1737
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 259 ELELNEKINEEITHIQEEKQDIiisfqhmQQLLRQQIQANTEMEAELK-VLKENNQTLERDNELQREK-VKENEEKFLNL 336
Cdd:PTZ00121 1738 EAEEDKKKAEEAKKDEEEKKKI-------AHLKKEEEKKAEEIRKEKEaVIEEELDEEDEKRRMEVDKkIKDIFDNFANI 1810
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 337 QNEHEKALGTWKRHAEELNGEINKIKNELSSLKETHIKLQEHYNKLCNQKTFEEDKKFQNVPEVNN--ENSEMSTEKSEN 414
Cdd:PTZ00121 1811 IEGGKEGNLVINDSKEMEDSAIKEVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEKDLkeDDEEEIEEADEI 1890
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 415 TIIQKYNTEQEIREENMENFCSDTEYREKEekkegsfIEEIIIDDLQlfekSFKNEIDTVVSQDENQSEISlSKTLSLDK 494
Cdd:PTZ00121 1891 EKIDKDDIEREIPNNNMAGKNNDIIDDKLD-------KDEYIKRDAE----ETREEIIKISKKDMCINDFS-SKFCDYMK 1958
|
490 500
....*....|....*....|....
gi 83715968 495 EVISQGQTSNVtdNRKSVTTEIKD 518
Cdd:PTZ00121 1959 DNISSGNCSDE--ERKELCCSISD 1980
|
|
| HlpA |
COG2825 |
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ... |
181-281 |
4.93e-04 |
|
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 442073 [Multi-domain] Cd Length: 171 Bit Score: 42.13 E-value: 4.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 181 NHEKLEQNVREAIQSNKRLSALNKKQEAEICSLKKELKKAASDLIKSKVTcqykMGEENIN-----LTIKEQKFQELQER 255
Cdd:COG2825 30 DVQRILQESPEGKAAQKKLEKEFKKRQAELQKLEKELQALQEKLQKEAAT----LSEEERQkkereLQKKQQELQRKQQE 105
|
90 100
....*....|....*....|....*.
gi 83715968 256 LNMelELNEKINEEITHIQEEKQDII 281
Cdd:COG2825 106 AQQ--DLQKRQQELLQPILEKIQKAI 129
|
|
| OmpH |
pfam03938 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
181-281 |
5.37e-04 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 461098 [Multi-domain] Cd Length: 140 Bit Score: 41.41 E-value: 5.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 181 NHEKLEQNVREAIQSNKRLSALNKKQEAEICSLKKELKKAASDLIKSKVTCQYKMGEENINLTIKEQKFQELQERLNMel 260
Cdd:pfam03938 6 DMQKILEESPEGKAAQAQLEKKFKKRQAELEAKQKELQKLYEELQKDGALLEEEREEKEQELQKKEQELQQLQQKAQQ-- 83
|
90 100
....*....|....*....|.
gi 83715968 261 ELNEKINEEITHIQEEKQDII 281
Cdd:pfam03938 84 ELQKKQQELLQPIQDKINKAI 104
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
179-337 |
8.43e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 43.28 E-value: 8.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 179 KENHEKLEQNVREAIQSnkrLSALNKKQEAEICSLKKELKKAasDLIKSKVtcqykmgeeninltikEQKFQELQERL-N 257
Cdd:PRK00409 508 KKLIGEDKEKLNELIAS---LEELERELEQKAEEAEALLKEA--EKLKEEL----------------EEKKEKLQEEEdK 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 258 MELELNEKINEEITHIQEEKQDIIISFQHMQQLLRQQIQANtEMEAELKVLKENNQTLErdnelqrEKVKENEEKFLNLQ 337
Cdd:PRK00409 567 LLEEAEKEAQQAIKEAKKEADEIIKELRQLQKGGYASVKAH-ELIEARKRLNKANEKKE-------KKKKKQKEKQEELK 638
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
31-282 |
8.46e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.22 E-value: 8.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 31 KTSLLEALEEL---RMRREAEIHYEEQIGKIIVETQELKWQKETLQnqketlaeqhkeamavfkkqlqmkmcALEEEKGK 107
Cdd:COG4717 36 KSTLLAFIRAMlleRLEKEADELFKPQGRKPELNLKELKELEEELK--------------------------EAEEKEEE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 108 YQLATEikekEIEGLKETLKALQVSKYSLQKKVSEMEQKVQLHllakeDYHKQLSEIEKYYATITGQFGLVKENHEKLEQ 187
Cdd:COG4717 90 YAELQE----ELEELEEELEELEAELEELREELEKLEKLLQLL-----PLYQELEALEAELAELPERLEELEERLEELRE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 188 NVREAIQSNKRLSALNKKQEAEICSLKKELKKAASDLIKSKVTCQYKMGEENINLTIKEQKFQELQERLNmELELNEKIN 267
Cdd:COG4717 161 LEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELE-QLENELEAA 239
|
250
....*....|....*
gi 83715968 268 EEITHIQEEKQDIII 282
Cdd:COG4717 240 ALEERLKEARLLLLI 254
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
100-680 |
8.85e-04 |
|
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: 43.50 E-value: 8.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 100 ALEEEKGKYQLATEIKEKEIEGLKET--LKALQVSKY--SLQKKVSEMEQKVQLhlLAKEDYHKQLSEIEKYYATITGQF 175
Cdd:TIGR01612 932 SIEKFHNKQNILKEILNKNIDTIKESnlIEKSYKDKFdnTLIDKINELDKAFKD--ASLNDYEAKNNELIKYFNDLKANL 1009
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 176 GLVKEN--------HEKLEQNVREAIQS-NKRLSALNKKQEAEICSLKKELKKAASDLIKSKVTCQYKmgEENINLTike 246
Cdd:TIGR01612 1010 GKNKENmlyhqfdeKEKATNDIEQKIEDaNKNIPNIEIAIHTSIYNIIDEIEKEIGKNIELLNKEILE--EAEINIT--- 1084
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 247 qKFQELQERLNMeLELNEKINEEITHIQEEKQDIIISFQHMQQLLRQQIQANTEM----EAELKVLKENNQTLER--DNE 320
Cdd:TIGR01612 1085 -NFNEIKEKLKH-YNFDDFGKEENIKYADEINKIKDDIKNLDQKIDHHIKALEEIkkksENYIDEIKAQINDLEDvaDKA 1162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 321 LQREKVKENEEKFLNLQNEHEKALGTWKRHAEELN--GEINKIKNELSSLKETHIKLQEHYNKLCNQKTFEEDKKFQNV- 397
Cdd:TIGR01612 1163 ISNDDPEEIEKKIENIVTKIDKKKNIYDEIKKLLNeiAEIEKDKTSLEEVKGINLSYGKNLGKLFLEKIDEEKKKSEHMi 1242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 398 -----------------PEVNNE-------NSEMSTEKSENTIIQKYNTEQEIREENMenfcsdTEYREKEEKKEGSFIE 453
Cdd:TIGR01612 1243 kameayiedldeikeksPEIENEmgiemdiKAEMETFNISHDDDKDHHIISKKHDENI------SDIREKSLKIIEDFSE 1316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 454 EIIIDDLqlfeksfKNEIDTVVSQDE-NQSEIS--LSKTLSLdKEVISQGQTSNVTDNRKSVTTEIKD---KICLEKDNG 527
Cdd:TIGR01612 1317 ESDINDI-------KKELQKNLLDAQkHNSDINlyLNEIANI-YNILKLNKIKKIIDEVKEYTKEIEEnnkNIKDELDKS 1388
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 528 CTEFKSPNNhfvvlDTAIETEKIHLERTrgldVHHTDVNLEVENNKTSFNSILN-ETAHNTYHNNNKDVSENEP--FKQF 604
Cdd:TIGR01612 1389 EKLIKKIKD-----DINLEECKSKIEST----LDDKDIDECIKKIKELKNHILSeESNIDTYFKNADENNENVLllFKNI 1459
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 83715968 605 RLLPGTREHALEKEitnSDQTKADLDSSL-DIKKNPVPCQKYSLRNSSNVmlddKQCKIKQIQLLTKKSECSILLSK 680
Cdd:TIGR01612 1460 EMADNKSQHILKIK---KDNATNDHDFNInELKEHIDKSKGCKDEADKNA----KAIEKNKELFEQYKKDVTELLNK 1529
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
245-434 |
1.38e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.44 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 245 KEQKFQELQERLNMELELNEKINEEITHIQEEKQDIIISFQHMQQLLRQQIQANTEMEAELKVLKENNQTLERDNELQRE 324
Cdd:COG4942 25 AEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 325 KVKE-----------NEEKFLNLQ---NEHEKALGTWKRHAEELNGEINKIKNELSSLKETHIKLQEHYNKLCNQKTFEE 390
Cdd:COG4942 105 ELAEllralyrlgrqPPLALLLSPedfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELE 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 83715968 391 DKKFQNVPEVNNENSEMSTEKSENTIIQKYNTEQEIREENMENF 434
Cdd:COG4942 185 EERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEAL 228
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
35-296 |
1.75e-03 |
|
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.
Pssm-ID: 460721 [Multi-domain] Cd Length: 297 Bit Score: 41.50 E-value: 1.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 35 LEALEELRMRREAEIHYEEQIGkiivetQELKWQKETLQNQKETLAEQHKEAMAVFKKQlqmkmcALEEEKGKYQ--LAT 112
Cdd:pfam02841 36 LAQIENSAAVQKAIAHYEQQMA------QKVKLPTETLQELLDLHRDCEKEAIAVFMKR------SFKDENQEFQkeLVE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 113 EIKEKEIEGLKETLKAlqVSKYS---LQKKVSEMEQKVQLHLLAK----EDYHKQLSEIEKYYATITGQFGLVKENHEKL 185
Cdd:pfam02841 104 LLEAKKDDFLKQNEEA--SSKYCsalLQDLSEPLEEKISQGTFSKpggyKLFLEERDKLEAKYNQVPRKGVKAEEVLQEF 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 186 EQN---VREAI-QSNKRLSALNKKQEAEicSLKKELKKAASDLIKSKVTCQYKMGEEN-----INLTIKEQKFQELQERL 256
Cdd:pfam02841 182 LQSkeaVEEAIlQTDQALTAKEKAIEAE--RAKAEAAEAEQELLREKQKEEEQMMEAQersyqEHVKQLIEKMEAEREQL 259
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 83715968 257 NMElelNEKINEEitHIQEEKQDIIISFQHMQQLLRQQIQ 296
Cdd:pfam02841 260 LAE---QERMLEH--KLQEQEELLKEGFKTEAESLQKEIQ 294
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
51-416 |
1.82e-03 |
|
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: 42.41 E-value: 1.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 51 YEEQIGKIIVETQELKWQKETLQNQKETLAEQHKEAMAVFKKQLQMKMCALEEEKGKYQLATEIKEKEIEGLKetlKALQ 130
Cdd:pfam15921 276 HEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELE---KQLV 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 131 VSKYSLQKKVSEMEQKVQLHLLAKEDYHKQLSEIEKYyatiTGQFGLVKENHEKL-----------------------EQ 187
Cdd:pfam15921 353 LANSELTEARTERDQFSQESGNLDDQLQKLLADLHKR----EKELSLEKEQNKRLwdrdtgnsitidhlrrelddrnmEV 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 188 NVREAI----------QSNKRLSALNKKQE---------AEICSLKKELKKAASDLIKSKVT---CQYKMGEENINLTIK 245
Cdd:pfam15921 429 QRLEALlkamksecqgQMERQMAAIQGKNEslekvssltAQLESTKEMLRKVVEELTAKKMTlesSERTVSDLTASLQEK 508
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 246 EQKFQ-------ELQERLNMEL-ELNEKINEE--ITHIQEEKQDIIISFQHMQ---QLLRQQIQANTEMEA--------- 303
Cdd:pfam15921 509 ERAIEatnaeitKLRSRVDLKLqELQHLKNEGdhLRNVQTECEALKLQMAEKDkviEILRQQIENMTQLVGqhgrtagam 588
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 304 -------------------ELKVLKENNQTLERDNELQREKVKENEEKFLNLQNEHEKALGTWKRHAEELNGEINKIKNE 364
Cdd:pfam15921 589 qvekaqlekeindrrlelqEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNE 668
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 83715968 365 LSSLKETHIKLQEHYnklcnQKTFEEDKKFQNVPEVNNENSEMSTEKSENTI 416
Cdd:pfam15921 669 LNSLSEDYEVLKRNF-----RNKSEEMETTTNKLKMQLKSAQSELEQTRNTL 715
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
36-280 |
1.88e-03 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 42.32 E-value: 1.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 36 EALEELRMRREAEIhyeeqigkiivetQELKWQKETLQNQKETLAEQhkeamavfKKQLQMKMCALEEEKGKYQLATEIK 115
Cdd:pfam05667 324 ETEEELQQQREEEL-------------EELQEQLEDLESSIQELEKE--------IKKLESSIKQVEEELEELKEQNEEL 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 116 EKEIEGLKETLKAL-----QVSKysLQKKVSEMEQKVQlhllakedyhkQLS-EIEKYYATitgqfgLVKEnHEKLEQnv 189
Cdd:pfam05667 383 EKQYKVKKKTLDLLpdaeeNIAK--LQALVDASAQRLV-----------ELAgQWEKHRVP------LIEE-YRALKE-- 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 190 reaIQSNKRLSAlnKKQEAEICSLKKELKKAASDlikskvtcqykmgeeninLTIKEQKFQELQ---ERLNMEL---ELN 263
Cdd:pfam05667 441 ---AKSNKEDES--QRKLEEIKELREKIKEVAEE------------------AKQKEELYKQLVaeyERLPKDVsrsAYT 497
|
250
....*....|....*..
gi 83715968 264 EKINEEITHIQEEKQDI 280
Cdd:pfam05667 498 RRILEIVKNIKKQKEEI 514
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
35-328 |
2.08e-03 |
|
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.
Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 41.56 E-value: 2.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 35 LEALEELRMRREAEIHYEEQIGKIIVETQELKW--QKETLQNQ-KETLAEQHKEAMAvfKKQLQMKMCALEEE---KGKY 108
Cdd:pfam15558 64 QAEKEQRKARLGREERRRADRREKQVIEKESRWreQAEDQENQrQEKLERARQEAEQ--RKQCQEQRLKEKEEelqALRE 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 109 QLATEIKEKEIEG-----LKETLKALQVSKYSLQKKVSEMEQKVQLHLLAKEDYH-KQLSEIEKYYATITGQFGLVKENH 182
Cdd:pfam15558 142 QNSLQLQERLEEAchkrqLKEREEQKKVQENNLSELLNHQARKVLVDCQAKAEELlRRLSLEQSLQRSQENYEQLVEERH 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 183 EKLEQNVREAIQSNKRLSALNKKQEAEicslKKELKKAASDLIKSKVtcqyKMGEENINLTIKEqKFQELQErLNMELEL 262
Cdd:pfam15558 222 RELREKAQKEEEQFQRAKWRAEEKEEE----RQEHKEALAELADRKI----QQARQVAHKTVQD-KAQRARE-LNLEREK 291
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 83715968 263 NEKIN------EEITHIQEEKQDIIISFQHMQQLLRQQiqantemEAELkvlkENNQTLERDNELQREKVKE 328
Cdd:pfam15558 292 NHHILklkvekEEKCHREGIKEAIKKKEQRSEQISREK-------EATL----EEARKTARASFHMREKVRE 352
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
178-369 |
2.28e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.21 E-value: 2.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 178 VKENHEKLEQNVREAIQSNKRLSALN-KKQEAEICSLKKELKKAASDLikskvtcqykmGEENINLTIKEQKFQELQERL 256
Cdd:COG4913 257 IRELAERYAAARERLAELEYLRAALRlWFAQRRLELLEAELEELRAEL-----------ARLEAELERLEARLDALREEL 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 257 nmeLELNEKINE----EITHIQEEKQdiiisfqHMQQLLRQQIQANTEMEAELKVLKENNQTLERDNELQREKVKENEEK 332
Cdd:COG4913 326 ---DELEAQIRGnggdRLEQLEREIE-------RLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEA 395
|
170 180 190
....*....|....*....|....*....|....*..
gi 83715968 333 FLNLQNEHEKALGTWKRHAEELNGEINKIKNELSSLK 369
Cdd:COG4913 396 LEEELEALEEALAEAEAALRDLRRELRELEAEIASLE 432
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
52-375 |
2.65e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.82 E-value: 2.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 52 EEQIGKIIVETQELKWQKETLQNQKETLAEQHKeamavfkkqlqmkmcALEEEKGKYQLATEIKEKEIEglketlkalqv 131
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELD---------------ALQERREALQRLAEYSWDEID----------- 662
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 132 sKYSLQKKVSEMEQKVQlHLLAKEDYHKQLSEiekyyatitgqfgLVKENHEKLEQNVREAIQSNKRLSALNKKQEaEIC 211
Cdd:COG4913 663 -VASAEREIAELEAELE-RLDASSDDLAALEE-------------QLEELEAELEELEEELDELKGEIGRLEKELE-QAE 726
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 212 SLKKELKKAASDLIKSKVTCQYKMGEENINLTIKEQKFQELQERLNMELE-LNEKINEEITHIQEEKQDIIISFQHMQQL 290
Cdd:COG4913 727 EELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDaLRARLNRAEEELERAMRAFNREWPAETAD 806
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 291 LRQQIQANTEMEAELkvlkennqtlerdNELQREKVKENEEKFLNLQNEHEK--------ALGTWKRHAEElngEINKIK 362
Cdd:COG4913 807 LDADLESLPEYLALL-------------DRLEEDGLPEYEERFKELLNENSIefvadllsKLRRAIREIKE---RIDPLN 870
|
330
....*....|....*.
gi 83715968 363 NELSSLK---ETHIKL 375
Cdd:COG4913 871 DSLKRIPfgpGRYLRL 886
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
31-210 |
3.17e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 41.29 E-value: 3.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 31 KTSLLEALEELRMR---REAEIH-YEEQIGKIIVETQELKWQKETLQNQKETLAEQHKEAM-AVFKKQLQMKMCALEEEK 105
Cdd:COG4942 50 EKALLKQLAALERRiaaLARRIRaLEQELAALEAELAELEKEIAELRAELEAQKEELAELLrALYRLGRQPPLALLLSPE 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 106 GKYQLA---------TEIKEKEIEGLKETLKALQVSKYSLQKKVSEMEQKVQLHLLAKEDYHKQLSEIEKYYATITGQFg 176
Cdd:COG4942 130 DFLDAVrrlqylkylAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKEL- 208
|
170 180 190
....*....|....*....|....*....|....
gi 83715968 177 lvkenhEKLEQNVREAIQSNKRLSALNKKQEAEI 210
Cdd:COG4942 209 ------AELAAELAELQQEAEELEALIARLEAEA 236
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
116-344 |
3.82e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.97 E-value: 3.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 116 EKEIEGLKETLKALQVSKYSLQKKVSEMEQKVQLhllAKEDYHKQLSEIEKyyatitgqfglVKENHEKLEQNVREAiqs 195
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEE---LNEEYNELQAELEA-----------LQAEIDKLQAEIAEA--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 196 nkrlsalnkkqEAEICSLKKELKKAASDLIKSKVTCQYkmgeenINLTIKEQKFQELQERLNMelelnekineeITHIQE 275
Cdd:COG3883 78 -----------EAEIEERREELGERARALYRSGGSVSY------LDVLLGSESFSDFLDRLSA-----------LSKIAD 129
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 83715968 276 EKQDIIISFQHMQQLLRQQIQANTEMEAELKVLKENNQTLErdNELQReKVKENEEKFLNLQNEHEKAL 344
Cdd:COG3883 130 ADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAK--AELEA-QQAEQEALLAQLSAEEAAAE 195
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
26-382 |
4.80e-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: 41.20 E-value: 4.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 26 QLLDFKTSLLEALEELRMRREAEIHYEEQIGKIIVETQELKWQKETLQ----NQKETLAEQHKEAMAVFKKQLQMKMCAL 101
Cdd:TIGR02168 366 ELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEdrreRLQQEIEELLKKLEEAELKELQAELEEL 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 102 EEEKGKYQLATEIKEKEIEGLKETLKALQVSKYSLQKKVSEMEQKV---QLHLLAKEDYHKQLSEIEKYYATITGQFGLV 178
Cdd:TIGR02168 446 EEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLdslERLQENLEGFSEGVKALLKNQSGLSGILGVL 525
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 179 KEN---HEKLE-------------------QNVREAIQSNKR-------LSALNKKQEAEICSLKKELKK-------AAS 222
Cdd:TIGR02168 526 SELisvDEGYEaaieaalggrlqavvvenlNAAKKAIAFLKQnelgrvtFLPLDSIKGTEIQGNDREILKniegflgVAK 605
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 223 DLIKSKVTCQ-----------------------------------------------YKMGEENINLTIKEQKFQELQER 255
Cdd:TIGR02168 606 DLVKFDPKLRkalsyllggvlvvddldnalelakklrpgyrivtldgdlvrpggvitGGSAKTNSSILERRREIEELEEK 685
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 256 LNMELELNEKINEEITHIQEEKQDIIISFQHMQQLLRQQIQANTEMEAELKVLKENNQTLERDNELQREKVKENEEKFLN 335
Cdd:TIGR02168 686 IEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEE 765
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 83715968 336 LQNEHEKA---LGTWKRHAEELNGEINKIKNELSSLKETHIKLQEHYNKL 382
Cdd:TIGR02168 766 LEERLEEAeeeLAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLL 815
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
179-424 |
5.14e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 40.71 E-value: 5.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 179 KENHEKLEQNVREAIQSNKRLSALNKKQEAEICSLKKELKKAASDLIKS--KVTCQYKMGEENINLTIKEQKFQELQERL 256
Cdd:COG5185 307 IKKATESLEEQLAAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENleAIKEEIENIVGEVELSKSSEELDSFKDTI 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 257 NmelELNEKINEEITHIQEEKQDIIISFQ-HMQQLLRQQIQANTEMEAELKVLKENNQTL-ERDNELQREKVKENEEKFL 334
Cdd:COG5185 387 E---STKESLDEIPQNQRGYAQEILATLEdTLKAADRQIEELQRQIEQATSSNEEVSKLLnELISELNKVMREADEESQS 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 335 NLQNEHEKALGTWKRHAEELNGEINKIKNELSSLKETHIKLQEHYNKLCNQKTFEEDKKFQNVPEVNNENSEMSTEKSEN 414
Cdd:COG5185 464 RLEEAYDEINRSVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLERQLEGVRSKLDQVAESLKDFMRARGYAHILALEN 543
|
250
....*....|
gi 83715968 415 TIIQKYNTEQ 424
Cdd:COG5185 544 LIPASELIQA 553
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
107-328 |
5.51e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 40.65 E-value: 5.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 107 KYQLATEIKEKEIEGLKETLKALQVSKYSLQKKVSEMEQKVQLHLLAKEDYHKQLSEIEKYYATITGQFGLVKENHEKLE 186
Cdd:pfam07888 49 AQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHE 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 187 QNVREAIQSNKRLSALNKKQEAEICSLKKELKKAASDLIKSKvtcqykmgEENINLTIKEQKFQELQERLNMEL-ELNEK 265
Cdd:pfam07888 129 ARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEE--------AERKQLQAKLQQTEEELRSLSKEFqELRNS 200
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 83715968 266 INEEITHIQEEKQDIiisfQHMQQLLRQQIQANTEMEA---ELKVLKENNQTLERDNELQREKVKE 328
Cdd:pfam07888 201 LAQRDTQVLQLQDTI----TTLTQKLTTAHRKEAENEAlleELRSLQERLNASERKVEGLGEELSS 262
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
25-148 |
5.67e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.52 E-value: 5.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 25 IQLLDFKTSLLEALEELRMRREAEIHYEEQIGKIIVETQELKWQKETLQNQKETLAEQhkeamavfKKQLQMKMCALEEE 104
Cdd:COG4942 122 LALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEAL--------LAELEEERAALEAL 193
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 83715968 105 KGKYQLATEIKEKEIEGLKETLKALQVSKYSLQKKVSEMEQKVQ 148
Cdd:COG4942 194 KAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAA 237
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
108-315 |
7.88e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.15 E-value: 7.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 108 YQLATEIKEKEIEGLKETLKALqvskysLQKKVSEMEQKVQLHLL-AKEDYHKQLSEIEKYYAtitgqfglVKENH-EKL 185
Cdd:PRK12704 22 YFVRKKIAEAKIKEAEEEAKRI------LEEAKKEAEAIKKEALLeAKEEIHKLRNEFEKELR--------ERRNElQKL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 186 EQNVREAIQSNKRLSALNKKQEAEICSLKKELKKaasdlikskvtcqykmgeeninltiKEQKFQELQERLNmelELNEK 265
Cdd:PRK12704 88 EKRLLQKEENLDRKLELLEKREEELEKKEKELEQ-------------------------KQQELEKKEEELE---ELIEE 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 83715968 266 INEEITHI----QEEKQDIIIsfQHMQQLLRQQIQA---NTEMEAELKVLKENNQTL 315
Cdd:PRK12704 140 QLQELERIsgltAEEAKEILL--EKVEEEARHEAAVlikEIEEEAKEEADKKAKEIL 194
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
84-369 |
8.24e-03 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 40.01 E-value: 8.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 84 KEAMAVFKKQLQmkmcALEEEKGKYQLATEIKEKEIEGLKETLKALQVSKYSLQK-------KVSEMEQKV--QLHLLAK 154
Cdd:pfam05701 48 QEEIPEYKKQSE----AAEAAKAQVLEELESTKRLIEELKLNLERAQTEEAQAKQdselaklRVEEMEQGIadEASVAAK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 155 EdyhkQLSEIEKYYATITGQFGLVKENHEKLeQNVREAIQSNKRLsALNKKQEAEICSlkKELKKAASDL----IKSKvt 230
Cdd:pfam05701 124 A----QLEVAKARHAAAVAELKSVKEELESL-RKEYASLVSERDI-AIKRAEEAVSAS--KEIEKTVEELtielIATK-- 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 231 cqykmgeENIN------LTIKEQKFQEL----QERLNMELELNekineeitHIQEEKQDiiisfqhmqqlLRQQIQANTE 300
Cdd:pfam05701 194 -------ESLEsahaahLEAEEHRIGAAlareQDKLNWEKELK--------QAEEELQR-----------LNQQLLSAKD 247
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 83715968 301 MEAELKVLKENNQTLERD------NELQREKVKENEEKflNLQNEHEKALGTWKRHAEELNGEINKIKNELSSLK 369
Cdd:pfam05701 248 LKSKLETASALLLDLKAElaaymeSKLKEEADGEGNEK--KTSTSIQAALASAKKELEEVKANIEKAKDEVNCLR 320
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
55-226 |
9.52e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 39.76 E-value: 9.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 55 IGKIIVETQELKWQKETlqnqKETLAEQHKEAMAVFK-KQLQMKMcalEEEKGKYQLATEIKEKEIEgLKETLKALQVSK 133
Cdd:PRK12704 24 VRKKIAEAKIKEAEEEA----KRILEEAKKEAEAIKKeALLEAKE---EIHKLRNEFEKELRERRNE-LQKLEKRLLQKE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715968 134 YSLQKKVSEMEQKVQlhllakedyhkqlsEIEKYYATITGQFGLVKENHEKLEQNVREAIQSNKRLSALNKKQEAEIC-- 211
Cdd:PRK12704 96 ENLDRKLELLEKREE--------------ELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAEEAKEILle 161
|
170
....*....|....*
gi 83715968 212 SLKKELKKAASDLIK 226
Cdd:PRK12704 162 KVEEEARHEAAVLIK 176
|
|
| |
