|
Name |
Accession |
Description |
Interval |
E-value |
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
103-1404 |
0e+00 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 1898.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 103 SRIEKMSIQGVRSFGIEDKDKQIITFFSPLTILVGPNGAGKTTIIECLKYICTGDFPPGTKGNTFVHDPKVAQETDVRAQ 182
Cdd:TIGR00606 1 AKFLKMSILGVRSFGIEDKDKQIIDFFSPLTILVGPNGAGKTTIIECLKYICTGDFPPGTKGNTFVHDPKVAQETDVRAQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 183 IRLQFRDVNGELVAVQRSMLCTQKSKKTEFKTLEGVITRTKHGEKVSLSSKCAEIDREMISSLGVSKSVLNNVIFCHQED 262
Cdd:TIGR00606 81 IRLQFRDVNGEECAVVRSMVCTQKTKKTEFKTLEGVITRYKHGEKVSLSSKCAEIDREMISHLGVSKAVLNNVIFCHQED 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 263 SNWPLSEGKALKQKFDEIFSATRYIKALETLRQVRQTQGQKVKECQTELKYLKQNKEKACEIRDQITSKEAQLTSSREIV 342
Cdd:TIGR00606 161 SNWPLSEGKALKQKFDEIFSATRYIKALETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 343 KSYENELDPLKNRLKEIEQNLSKIMRLDNEIKALESRKKQMEKDNSELEQKMEKVFQGSDEQLNDLYHNHQRTVREKERR 422
Cdd:TIGR00606 241 KSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVREKERE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 423 LVDCQRELEKLNKESRLLNQEKSELLVEQGRLQLQADRHQEHMQARDSLIQSLATQLELDGFELGPFSERQIKNFHKLVR 502
Cdd:TIGR00606 321 LVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVI 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 503 ERQEKESETASQLLNDFTRKEALKQKQIDEIRDKKTGLGRIIELKSEILTKKQNELKNVKYELQQLEGSSDRILELDQEL 582
Cdd:TIGR00606 401 ERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQEL 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 583 TKAERELSKAEKNSNVETLKTEVISLQNEKADLDRTLRKLDQEMEQLNHHTAARTQMEMLNKDKADKDEQIRKIKYRHSD 662
Cdd:TIGR00606 481 RKAERELSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSD 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 663 ELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASAEQNKNHINIELKRKEEQLSSYEDKLFDVCGSQDFESD 742
Cdd:TIGR00606 561 ELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSQDEESD 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 743 LDRLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRGFQTEAELQEVISDLQSKLRLAPDKLKSTESELKK 822
Cdd:TIGR00606 641 LERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKK 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 823 KEKRRDEMLGLVPMRQSIIDLKEKEIPELRNKLQNVNRDIQRLKNDIEEQETLLGAIIPEEESAKVCLTDVTIMERLQME 902
Cdd:TIGR00606 721 KEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTIMERFQME 800
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 903 LKDVERKIAQQAAKLQGLDLDRSVQQVNQEKQEKQHKLDTVSSKIELNRKLIQDQQEQIQHLKSTANELKSEKLQISTNL 982
Cdd:TIGR00606 801 LKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNL 880
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 983 QRRQQLEEQTVELSTEVQSLYREIKDAKEQLSPLETTLEKFQQEKEELVNKKNTSHKIAQDKINEIKEKVKNIHSYMKDI 1062
Cdd:TIGR00606 881 QRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDI 960
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 1063 ENYIQDGKDDYKKQKETELNKVIAQISECEKHKEKINKEMGIMRQDIDTQKIQERWLQDNLTLRKRNEELKEVEEERKQH 1142
Cdd:TIGR00606 961 ENKIQDGKDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQDNLTLRKRENELKEVEEELKQH 1040
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 1143 LKEMGQMQVLQMKNEHQKLEEKIDNIKRNHSLAIGRQKGYEEEIIHFKKELREPQFRDAEEKYREMMIIMRTTELVNKDL 1222
Cdd:TIGR00606 1041 LKEMGQMQVLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELREPQFRDAEEKYREMMIVMRTTELVNKDL 1120
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 1223 DIYYKTLDQAIMKFHSMKMEEINKIIRDLWRSTYRGQDIEYIEIRSDADENVSASDKRRNYNYRVVMLKGDTALDMRGRC 1302
Cdd:TIGR00606 1121 DIYYKTLDQAIMKFHSMKMEEINKIIRDLWRSTYRGQDIEYIEIRSDADENVSASDKRRNYNYRVVMLKGDTALDMRGRC 1200
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 1303 SAGQKVLASLIIRLALAETFCLNCGILALDEPTTNLDRENIESLAHALVEIIKSRSQQRNFQLLVITHDEDFVELLGRSE 1382
Cdd:TIGR00606 1201 SAGQKVLASLIIRLALAETFCLNCGIIALDEPTTNLDRENIESLAHALVEIIKSRSQQRNFQLLVITHDEDFVELLGRSE 1280
|
1290 1300
....*....|....*....|..
gi 2015236753 1383 YVEKFYRIKKNIEQCSEIVTCS 1404
Cdd:TIGR00606 1281 YVEKFYRLKKNEDQCSEIVKCS 1302
|
|
| IL13 |
pfam03487 |
Interleukin-13; |
1482-1657 |
5.76e-53 |
|
Interleukin-13;
Pssm-ID: 460944 Cd Length: 110 Bit Score: 181.12 E-value: 5.76e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 1482 LKELIEELVNITQNQKVsacgpssegagvrgsqgrspedckapsasvtcpptlalasftqgssltgcgtqysslspkpld 1561
Cdd:pfam03487 9 LKELIEELVNITQNQKA--------------------------------------------------------------- 25
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 1562 sgkgglgtlkvPLCNGSMVWSLNLTSSMYCAALDSLISISNCSVIHRTKRMLSALCPHKPSAKHVSSEYVRDTKIEVAQF 1641
Cdd:pfam03487 26 -----------PLCNGSMVWSVNLTAGVYCAALESLINVSNCSAIQRTQRMLSGLCTHKASAGQVSSLHVRDTKIEVAQF 94
|
170
....*....|....*.
gi 2015236753 1642 LKDLLRHSRIVFRNGS 1657
Cdd:pfam03487 95 VKDLLRHLKRLFRHGN 110
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
1296-1398 |
1.43e-43 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 157.77 E-value: 1.43e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 1296 LDMRGRCSAGQKVLASLIIRLALAETFCLNCGILALDEPTTNLDRENIEslaHALVEIIKSRSQQRNFQLLVITHDEDFV 1375
Cdd:cd03240 110 LDMRGRCSGGEKVLASLIIRLALAETFGSNCGILALDEPTTNLDEENIE---ESLAEIIEERKSQKNFQLIVITHDEELV 186
|
90 100
....*....|....*....|...
gi 2015236753 1376 ELLGrseyveKFYRIKKNIEQCS 1398
Cdd:cd03240 187 DAAD------HIYRVEKDGRQKS 203
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
105-267 |
7.33e-38 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 141.21 E-value: 7.33e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 105 IEKMSIQGVRSFgiedKDKQIITFFSPLTILVGPNGAGKTTIIECLKYICTGDFPPGTKGNtfVHDPKVAQETDVRAQIR 184
Cdd:cd03240 1 IDKLSIRNIRSF----HERSEIEFFSPLTLIVGQNGAGKTTIIEALKYALTGELPPNSKGG--AHDPKLIREGEVRAQVK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 185 LQFRDVNGELVAVQRSMlctqkskktefktlegvitrtkhgekvslsskcaeidremisslgvskSVLNNVIFCHQEDSN 264
Cdd:cd03240 75 LAFENANGKKYTITRSL------------------------------------------------AILENVIFCHQGESN 106
|
...
gi 2015236753 265 WPL 267
Cdd:cd03240 107 WPL 109
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
291-1113 |
2.96e-24 |
|
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: 111.30 E-value: 2.96e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 291 ETLRQVRQTQG--QKV----KECQTELKYLKQNKEKA---CEIRDQITSKEAQLTSSReiVKSYENELDPLKNRLKEIEQ 361
Cdd:TIGR02168 176 ETERKLERTREnlDRLedilNELERQLKSLERQAEKAeryKELKAELRELELALLVLR--LEELREELEELQEELKEAEE 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 362 nlsKIMRLDNEIKALESRKKQMEKDNSELEQKMEkvfqgsdeQLNDLYHNHQRTVREKERRLvdcqrelEKLNKESRLLN 441
Cdd:TIGR02168 254 ---ELEELTAELQELEEKLEELRLEVSELEEEIE--------ELQKELYALANEISRLEQQK-------QILRERLANLE 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 442 QEKSELLVEQGRLQLQADRHQEHMQARDSLIQSLATQLEldgfelgpfserqiknfhklvreRQEKESETASQLLNDFTR 521
Cdd:TIGR02168 316 RQLEELEAQLEELESKLDELAEELAELEEKLEELKEELE-----------------------SLEAELEELEAELEELES 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 522 KEALKQKQIDEIRDKktglgrIIELKSEIlTKKQNELKNVKYELQQLEGSSDRILELDQELTKAERELSKAEKNSNVETL 601
Cdd:TIGR02168 373 RLEELEEQLETLRSK------VAQLELQI-ASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEEL 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 602 KTEVISLQNEKADLDRTLRKLDQEMEQlnhhtaARTQMEMLNKDKADKDEQIRKIKyrhsDELTSLLGYFPNKKQLEDWl 681
Cdd:TIGR02168 446 EEELEELQEELERLEEALEELREELEE------AEQALDAAERELAQLQARLDSLE----RLQENLEGFSEGVKALLKN- 514
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 682 hskSKEINQTRDRLAKLnkelasaeqnknhINIElkrkeeqlSSYEDKLFDVCGS--QDFE-SDLDRLKEEIE---KSSK 755
Cdd:TIGR02168 515 ---QSGLSGILGVLSEL-------------ISVD--------EGYEAAIEAALGGrlQAVVvENLNAAKKAIAflkQNEL 570
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 756 QRAMLAGATAVYSQFITQLTDE---NQSCC-PVCQRGFQTEAELQEVISDLQSKLRLAPDKLKSTEselKKKEKRRDEML 831
Cdd:TIGR02168 571 GRVTFLPLDSIKGTEIQGNDREilkNIEGFlGVAKDLVKFDPKLRKALSYLLGGVLVVDDLDNALE---LAKKLRPGYRI 647
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 832 ----------------GLVPMRQSIIDlKEKEIPELRNKLQNVNRDIQRLKNDIEEQETLLGAIIPEEESAKVCLTDVTI 895
Cdd:TIGR02168 648 vtldgdlvrpggvitgGSAKTNSSILE-RRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSR 726
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 896 -MERLQMELKDVERKIAQQAAKLQGLDLDRSVQQV-----NQEKQEKQHKLDTVSSKIELNRKLIQDQQEQIQHLKSTAN 969
Cdd:TIGR02168 727 qISALRKDLARLEAEVEQLEERIAQLSKELTELEAeieelEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALD 806
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 970 ELKSE----KLQISTNLQRRQQLEEQTVELSTEVQSLYREIKDAKEQLSPLETTLEKFQQEKEELvnkkNTSHKIAQDKI 1045
Cdd:TIGR02168 807 ELRAEltllNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEEL----ESELEALLNER 882
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2015236753 1046 NEIKEKVKNIHSYMKDIENYIQDgkddykkqKETELNKVIAQISECEKHKEKINKEMGIMRQDIDTQK 1113
Cdd:TIGR02168 883 ASLEEALALLRSELEELSEELRE--------LESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQ 942
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
105-1109 |
4.88e-24 |
|
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: 110.54 E-value: 4.88e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 105 IEKMSIQGVRSFGiedkDKQIITFFSPLTILVGPNGAGKTTIIECLKyictgdFPPGTKGNT---------FVHDPKVAQ 175
Cdd:TIGR02169 2 IERIELENFKSFG----KKKVIPFSKGFTVISGPNGSGKSNIGDAIL------FALGLSSSKamraerlsdLISNGKNGQ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 176 ---ETDVRAQIRLQFRDVNGELVaVQRSMLCTQKSKKTEFKTlegvitrtkHGEKVSLSskcaEIDrEMISSLGVSKSVL 252
Cdd:TIGR02169 72 sgnEAYVTVTFKNDDGKFPDELE-VVRRLKVTDDGKYSYYYL---------NGQRVRLS----EIH-DFLAAAGIYPEGY 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 253 NNVIfchQEDSNWPLS-EGKALKQKFDEIFSATRY----IKALETLRQVRQTQGQ---KVKECQTELKYLKQNKEKAceI 324
Cdd:TIGR02169 137 NVVL---QGDVTDFISmSPVERRKIIDEIAGVAEFdrkkEKALEELEEVEENIERldlIIDEKRQQLERLRREREKA--E 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 325 RDQITSKEAQLTSSREIVKSYENeldplknRLKEIEQNLSKIMRLDNEIKALESRKKQMEKDNSELEQKMEKVfqgsDEQ 404
Cdd:TIGR02169 212 RYQALLKEKREYEGYELLKEKEA-------LERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEEL----NKK 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 405 LNDLYHNHQRTVREKerrLVDCQRELEKLNKESRLLNQEKSELLVEQGRLQLQADRHQEHMQARDSLIQSLATQLELDGF 484
Cdd:TIGR02169 281 IKDLGEEEQLRVKEK---IGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTE 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 485 ElgpFSERQiKNFHKLVRERQEKESETASqllndfTRKEALK-QKQIDEIRDKKTGLGRIIELKSEILTKKQNELKNVKy 563
Cdd:TIGR02169 358 E---YAELK-EELEDLRAELEEVDKEFAE------TRDELKDyREKLEKLKREINELKRELDRLQEELQRLSEELADLN- 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 564 elQQLEGSSDRILELDQELTKAERELSKAEKnsNVETLKTEVISLQNEKADLDRTLRKLDQEMEQLNHHTAA-------- 635
Cdd:TIGR02169 427 --AAIAGIEAKINELEEEKEDKALEIKKQEW--KLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEaeaqaras 502
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 636 -------RTQMEMLNKDKADKDEQIR---KIKYRHSDELTSLLGYFPNKKQLEDWLHSKS-----KEINQTRDRLAKLNK 700
Cdd:TIGR02169 503 eervrggRAVEEVLKASIQGVHGTVAqlgSVGERYATAIEVAAGNRLNNVVVEDDAVAKEaiellKRRKAGRATFLPLNK 582
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 701 ELAS-------AEQNKNHINIELKRKEEQlssYEDKLFDVCGSQDFESDLDRLK-------------EEIEKSSkqrAML 760
Cdd:TIGR02169 583 MRDErrdlsilSEDGVIGFAVDLVEFDPK---YEPAFKYVFGDTLVVEDIEAARrlmgkyrmvtlegELFEKSG---AMT 656
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 761 AGATAVYSQFITQLTDenqsccpvcqrgfqtEAELQEVISDLQSKLRLapdkLKSTESELKKKEKRRDEMlglvpmrQSI 840
Cdd:TIGR02169 657 GGSRAPRGGILFSRSE---------------PAELQRLRERLEGLKRE----LSSLQSELRRIENRLDEL-------SQE 710
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 841 IDLKEKEIPELRNKLQNVNRDIQRLKNDIEEQETLLGAIIPEEESAKvcltdvTIMERLQMELKDVERKIAQQAAKLQGL 920
Cdd:TIGR02169 711 LSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVK------SELKELEARIEELEEDLHKLEEALNDL 784
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 921 DLDRSVQQVnQEKQEKQHKLDTVSSKIELNRKLIQDQQEQIQHLKSTANELKSEKLQISTNLQRRQQLEEQTVE-LSTEV 999
Cdd:TIGR02169 785 EARLSHSRI-PEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIEnLNGKK 863
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 1000 QSLYREIKDAKEQLSPLETTLEKFQQEKEELVNKKntshKIAQDKINEIKEKVKNIHSYMKDIENYIQDgkddyKKQKET 1079
Cdd:TIGR02169 864 EELEEELEELEAALRDLESRLGDLKKERDELEAQL----RELERKIEELEAQIEKKRKRLSELKAKLEA-----LEEELS 934
|
1050 1060 1070
....*....|....*....|....*....|...
gi 2015236753 1080 ELNKVIAQ---ISECEKHKEKINKEMGIMRQDI 1109
Cdd:TIGR02169 935 EIEDPKGEdeeIPEEELSLEDVQAELQRVEEEI 967
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
108-316 |
3.86e-23 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 98.72 E-value: 3.86e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 108 MSIQGVRSFgiedkDKQIITFFSPLTILVGPNGAGKTTIIECLKYICTGDFP---PGTKGNTFVHDPKVAQETDVRAQIR 184
Cdd:pfam13476 1 LTIENFRSF-----RDQTIDFSKGLTLITGPNGSGKTTILDAIKLALYGKTSrlkRKSGGGFVKGDIRIGLEGKGKAYVE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 185 LQFRDVNGE-LVAVQRSMLCTQKSKKTEFKTLEGVITRtkhgekvslsskcaEIDREMISSLGVSKSVLNNVIFCHQEDS 263
Cdd:pfam13476 76 ITFENNDGRyTYAIERSRELSKKKGKTKKKEILEILEI--------------DELQQFISELLKSDKIILPLLVFLGQER 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2015236753 264 NWPLSEgkalKQKFDEIFSATRYIKALETLRQVRQTQgQKVKECQTELKYLKQ 316
Cdd:pfam13476 142 EEEFER----KEKKERLEELEKALEEKEDEKKLLEKL-LQLKEKKKELEELKE 189
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
491-1053 |
8.82e-21 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 99.75 E-value: 8.82e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 491 ERQIKNFHKLVRERQEKESEtasqlLNDFTRKEALKQKQIDEIRDKKTGLGRIIELKSEILTKKQNELKNVKYELQQLEg 570
Cdd:PRK03918 161 ENAYKNLGEVIKEIKRRIER-----LEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELE- 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 571 ssdrilELDQELTKAERELSKAEKNsnVETLKTEVISLQNEKADLDRTLRKLDQEMEQLNHHTAARTQMEMLNKDKADKD 650
Cdd:PRK03918 235 ------ELKEEIEELEKELESLEGS--KRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYL 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 651 EQIRKIKYRHSDeLTSLLGYFpnKKQLEDwLHSKSKEINQTRDRLAKLNKELASAEQNKNHINiELKRKEEQLSSYEDKL 730
Cdd:PRK03918 307 DELREIEKRLSR-LEEEINGI--EERIKE-LEEKEERLEELKKKLKELEKRLEELEERHELYE-EAKAKKEELERLKKRL 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 731 FDVcGSQDFESDLDRLKEEIEKSSKQRAMLAGATAVYSQFITQLTD------ENQSCCPVCQRGFqTEAELQEVISDLQS 804
Cdd:PRK03918 382 TGL-TPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKaieelkKAKGKCPVCGREL-TEEHRKELLEEYTA 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 805 KLRLAPDKLKSTESELKKKEKRRDEMLGLVPMRQSIIDLKE--KEIPELRNKLQNVNrdIQRLKNDIEEQETLLGAIIPE 882
Cdd:PRK03918 460 ELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKElaEQLKELEEKLKKYN--LEELEKKAEEYEKLKEKLIKL 537
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 883 EESAKVCLTDVTIMERLQMELKDVERKIAQQAAKLQGL-------------DLDRSVQQ-------------VNQEKQEK 936
Cdd:PRK03918 538 KGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELlkeleelgfesveELEERLKElepfyneylelkdAEKELERE 617
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 937 QHKLDTVSSKIELNRKLIQDQQEQIQHLKSTANELKSEklqisTNLQRRQQLEEQTVELSTEVQSLYREIKDAKEQLSPL 1016
Cdd:PRK03918 618 EKELKKLEEELDKAFEELAETEKRLEELRKELEELEKK-----YSEEEYEELREEYLELSRELAGLRAELEELEKRREEI 692
|
570 580 590
....*....|....*....|....*....|....*....
gi 2015236753 1017 ETTLEKFQQEKEELVNKKNTSHKI--AQDKINEIKEKVK 1053
Cdd:PRK03918 693 KKTLEKLKEELEEREKAKKELEKLekALERVEELREKVK 731
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
352-1392 |
6.49e-19 |
|
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: 93.88 E-value: 6.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 352 LKNRLKEIEQNLSKIMRLDNEIKALESRKKQMEKDNSELEQKMEKVFQGSDEQLNDLYHNHQRTVREKERRLVDCQRELE 431
Cdd:pfam02463 171 KKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQ 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 432 KLNKESRLLNQEKSELLVEQGRLQLQADRHQEHMQARDSLIQSLATQLELDgfelgpfsERQIKNFHKLVRERQEKEset 511
Cdd:pfam02463 251 EEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSE--------LLKLERRKVDDEEKLKES--- 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 512 asqllndftrKEALKQKQIDEIRDKKTGLGRIIELKSEILTKKQNELKNVKYELQQLEGSSDRIlELDQELTKAERELSK 591
Cdd:pfam02463 320 ----------EKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEE-ELLAKKKLESERLSS 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 592 AEKnsnvetLKTEVISLQNEKADLDRTLRKLDQemeqlnhhtaartQMEMLNKDKADKDEQIRKIKYRhsdELTSLLGYF 671
Cdd:pfam02463 389 AAK------LKEEELELKSEEEKEAQLLLELAR-------------QLEDLLKEEKKEELEILEEEEE---SIELKQGKL 446
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 672 PNKKQLEDWLHSKSKEINQTRDRLAKLNKELASAEQNKNHINIELKRKEEQLSSYEDKLFDVCGSqdfesdldrlkeeIE 751
Cdd:pfam02463 447 TEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKV-------------LL 513
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 752 KSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRGFQTEAELQEVISDLQSKLRLAPDKL----KSTESELKKKEKRR 827
Cdd:pfam02463 514 ALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLgarkLRLLIPKLKLPLKS 593
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 828 DEMLGLVPMRQSIIDLKEKEIPELRNKLQNVNRDIQRLKNDIEEQETLLGAII----PEEESAKVCLTDVTIMERLQMEL 903
Cdd:pfam02463 594 IAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESglrkGVSLEEGLAEKSEVKASLSELTK 673
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 904 KDVERKIAQQAAKLQGLDLDRSVQQVNQEKQEKQHKLDTVSSKIELNRKLIQDQQEQIQHLKSTANELKSEKLQISTNLQ 983
Cdd:pfam02463 674 ELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEE 753
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 984 --RRQQLEEQTVELSTEVQSLYREIKDAKEQLSPLETTLEKFQQEKEELVNKKNTSHK---IAQDKINEIKEKVKNIHSY 1058
Cdd:pfam02463 754 ksRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKeeaELLEEEQLLIEQEEKIKEE 833
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 1059 M--KDIENYIQDGKDDYKKQKETELNKVIAQISECEKHKEKINKEMGIMRQDIDTQKIQERWLQDNLTLRKRNEELKEVE 1136
Cdd:pfam02463 834 EleELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLE 913
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 1137 EERKQHLKEMGQMQVLQMKNEHQKLEEKIDNIKRNHSLAIGRqKGYEEEIIHF---KKELREPQFRDAEEKYREMmIIMR 1213
Cdd:pfam02463 914 EKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNK-EEEEERNKRLllaKEELGKVNLMAIEEFEEKE-ERYN 991
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 1214 TTELVNKDLDIYYKTLDQAIMKFHSMKMEEINKIIRDlwRSTYRGQDIEYIEIRSDADENVSASDKRRNYNYRV-VMLKG 1292
Cdd:pfam02463 992 KDELEKERLEEEKKKLIRAIIEETCQRLKEFLELFVS--INKGWNKVFFYLELGGSAELRLEDPDDPFSGGIEIsARPPG 1069
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 1293 DTALDMRgRCSAGQKVLASLIIRLALAE----TFCLncgilaLDEPTTNLDRENIESLAHalveIIKSRSQqrNFQLLVI 1368
Cdd:pfam02463 1070 KGVKNLD-LLSGGEKTLVALALIFAIQKykpaPFYL------LDEIDAALDDQNVSRVAN----LLKELSK--NAQFIVI 1136
|
1050 1060
....*....|....*....|....
gi 2015236753 1369 THDEDFVELlgrseyVEKFYRIKK 1392
Cdd:pfam02463 1137 SLREEMLEK------ADKLVGVTM 1154
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
104-977 |
7.37e-18 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 90.12 E-value: 7.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 104 RIEKMSIQGVRSfgiedKDKQIITFFSPLTILVGPNGAGKTTIIECLK---YICTGDFPPGTKGNTFVHDPKVaqetdvR 180
Cdd:PRK03918 2 KIEELKIKNFRS-----HKSSVVEFDDGINLIIGQNGSGKSSILEAILvglYWGHGSKPKGLKKDDFTRIGGS------G 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 181 AQIRLQFrDVNGelvavqRSMLCTQKSKKTE--FKTLEGVITRTKHGEKVslsskcaeidREMISSLgVSKSVLNNVIFC 258
Cdd:PRK03918 71 TEIELKF-EKNG------RKYRIVRSFNRGEsyLKYLDGSEVLEEGDSSV----------REWVERL-IPYHVFLNAIYI 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 259 HQEDSNWPLSEGKALKQKFDEIFSATRYIKALETLRQVRQTQGQKVKECQTELKYLKQNKEKACEIRDQITSKEAQLTSS 338
Cdd:PRK03918 133 RQGEIDAILESDESREKVVRQILGLDDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEI 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 339 REIVKSYENELDPLKNRLKEIEQNLSKIMRLDNEIKALESRKKQMEKDNSELEQKMEKVfqgsDEQLNDLyhnhqrtvRE 418
Cdd:PRK03918 213 SSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEEL----KKEIEEL--------EE 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 419 KERRLvdcqRELEKLNKESRLLNQEKSELLVEQGRLQLQADRHQEHMQArdslIQSLATQLELDGFELGPFSERQIKNFH 498
Cdd:PRK03918 281 KVKEL----KELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEING----IEERIKELEEKEERLEELKKKLKELEK 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 499 KLVR-ERQEKESETASQLLNdftRKEALKQKQIDEIRDKktgLGRIIELKSEILTKKQNELKNVKYELQQLEGSSDRILE 577
Cdd:PRK03918 353 RLEElEERHELYEEAKAKKE---ELERLKKRLTGLTPEK---LEKELEELEKAKEEIEEEISKITARIGELKKEIKELKK 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 578 LDQELTKAE-------RELSKAEKNSNVETLKTEVISLQNEKADLDRTLRKLDQEMEQLnhhtaartQMEMLNKDKADKD 650
Cdd:PRK03918 427 AIEELKKAKgkcpvcgRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELREL--------EKVLKKESELIKL 498
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 651 EQIrkikYRHSDELTSLLGYFpNKKQLEdwlhSKSKEINQTRDRLAKLNKELASAEQnknhiniELKRKEEqlssyedkl 730
Cdd:PRK03918 499 KEL----AEQLKELEEKLKKY-NLEELE----KKAEEYEKLKEKLIKLKGEIKSLKK-------ELEKLEE--------- 553
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 731 fdvcgsqdFESDLDRLKEEIEKSSKQRAMLagatavysqfITQLTdenqsccpvcQRGFQTEAELQEVISDLQSKLRlAP 810
Cdd:PRK03918 554 --------LKKKLAELEKKLDELEEELAEL----------LKELE----------ELGFESVEELEERLKELEPFYN-EY 604
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 811 DKLKSTESELKKKEKRrdemlglvpmrqsiIDLKEKEIPELRNKLQNVNRDIQRLKNDIEEqetlLGAIIPEEEsakvcl 890
Cdd:PRK03918 605 LELKDAEKELEREEKE--------------LKKLEEELDKAFEELAETEKRLEELRKELEE----LEKKYSEEE------ 660
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 891 tdvtiMERLQMELKDVERKIAQQAAKLQGLDLDRSVQQVNQEK-QEKQHKLDTVSSKIELNRKLIQDQQEQIQHLKSTAN 969
Cdd:PRK03918 661 -----YEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKlKEELEEREKAKKELEKLEKALERVEELREKVKKYKA 735
|
....*...
gi 2015236753 970 ELKSEKLQ 977
Cdd:PRK03918 736 LLKERALS 743
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
548-1203 |
7.15e-17 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 87.04 E-value: 7.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 548 SEILTKKQNELKNVKYELQQLEGSSDRILELDQELTKAERELSkaEKNSNVETLKTEVISLQNEKADLDRTLRKLdqeme 627
Cdd:PRK03918 168 GEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREIN--EISSELPELREELEKLEKEVKELEELKEEI----- 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 628 qlnhhTAARTQMEMLNKDKADKDEQIRKIKYR------HSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKE 701
Cdd:PRK03918 241 -----EELEKELESLEGSKRKLEEKIRELEERieelkkEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKR 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 702 LASAEQnknhiniELKRKEEQLSSYEDKlfdvcgsqdfESDLDRLKEEIEKSSKQRAMLAGATAVYsqfitqltdenqsc 781
Cdd:PRK03918 316 LSRLEE-------EINGIEERIKELEEK----------EERLEELKKKLKELEKRLEELEERHELY-------------- 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 782 cpvcQRGFQTEAELQEVisdlqsKLRLAPDKLKSTESELKKKEKRRDEMlglvpmrqsiidlkEKEIPELRNKLQNVNRD 861
Cdd:PRK03918 365 ----EEAKAKKEELERL------KKRLTGLTPEKLEKELEELEKAKEEI--------------EEEISKITARIGELKKE 420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 862 IQRLKNDIEEQET------LLGAIIPEEESAKvcltdvtIMERLQMELKDVERKIAQQAAKLQGLdldrsvqqvnqekqe 935
Cdd:PRK03918 421 IKELKKAIEELKKakgkcpVCGRELTEEHRKE-------LLEEYTAELKRIEKELKEIEEKERKL--------------- 478
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 936 kQHKLDTVSSKIELNRKLIQDQQ--EQIQHLKSTANELKSEKLQISTNLQRRqqLEEQTVELSTEVQSLYREIKDAKEQL 1013
Cdd:PRK03918 479 -RKELRELEKVLKKESELIKLKElaEQLKELEEKLKKYNLEELEKKAEEYEK--LKEKLIKLKGEIKSLKKELEKLEELK 555
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 1014 SPLETTLEKFQQEKEELVNKKNTSHKIAQDKINEIKEKVKNIHSY------MKDIENYIQDGKDDYKKQkETELNKVIAQ 1087
Cdd:PRK03918 556 KKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFyneyleLKDAEKELEREEKELKKL-EEELDKAFEE 634
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 1088 ISECEKHKEKINKEMGIMRQDIDTQKiQERWLQDNLTLRKRNEELKEVEEERKQHLKEMGQmQVLQMKNEHQKLEEKIDN 1167
Cdd:PRK03918 635 LAETEKRLEELRKELEELEKKYSEEE-YEELREEYLELSRELAGLRAELEELEKRREEIKK-TLEKLKEELEEREKAKKE 712
|
650 660 670
....*....|....*....|....*....|....*.
gi 2015236753 1168 IKrNHSLAIGRQKGYEEEIIHFKKELREPQFRDAEE 1203
Cdd:PRK03918 713 LE-KLEKALERVEELREKVKKYKALLKERALSKVGE 747
|
|
| IL4_13 |
smart00190 |
Interleukins 4 and 13; Interleukins-4 and -13 are cytokines involved in inflammatory and ... |
1454-1658 |
1.17e-16 |
|
Interleukins 4 and 13; Interleukins-4 and -13 are cytokines involved in inflammatory and immune responses. IL-4 stimulates B and T cells.
Pssm-ID: 197564 Cd Length: 138 Bit Score: 78.26 E-value: 1.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 1454 MALFLTVVVVLTCFGGLASP--NPVPSSSSLKELIEELVNITQNQKvsacgpssegagvrgsqgrspedckapsasvtcp 1531
Cdd:smart00190 1 MGLTPQLVPALLCLLGCTGNgpHGHSCDITLREIIETLNNVTQKGT---------------------------------- 46
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 1532 ptlalasftqgssltgcgtqysslspkpldsgkgglgtlkvPLCNGSMVWSL-----NLTSSM-YCAALDSLISIS--NC 1603
Cdd:smart00190 47 -----------------------------------------NLCTEMMVPDVlaatkNTTEKElFCRALKVLRNFYfhNC 85
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2015236753 1604 SVIHRTKRMLSALCPHKPSAKHVSSEYVRDTkiEVAQFLKDLLRHSRIVFRNGSY 1658
Cdd:smart00190 86 SAILKTLRKLDRNCSGLASQTSCTVNEAKDT--TLADFLERLKSIMREKYSKGSF 138
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
494-1169 |
2.37e-16 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 85.50 E-value: 2.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 494 IKNFHKLVRERQEKESETASQL-LNDFTRKEALKQKQIDEiRDKKTGLGRIIELkseiltkkQNELKNVKYELQQLEGSS 572
Cdd:TIGR02169 197 RQQLERLRREREKAERYQALLKeKREYEGYELLKEKEALE-RQKEAIERQLASL--------EEELEKLTEEISELEKRL 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 573 DRILELDQELTKAERELSKAEKNsnveTLKTEVISLQNEKADLDRTLRKLDQEMEQLNHHTA------ARTQMEMLNKDK 646
Cdd:TIGR02169 268 EEIEQLLEELNKKIKDLGEEEQL----RVKEKIGELEAEIASLERSIAEKERELEDAEERLAkleaeiDKLLAEIEELER 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 647 ADKDEQIRKIKYrhSDELTSLlgyfpnKKQLEDW---LHSKSKEINQTRDRLAKLNKELASAEQNKNHINIELKRKEEQL 723
Cdd:TIGR02169 344 EIEEERKRRDKL--TEEYAEL------KEELEDLraeLEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEEL 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 724 SSYEDKLFDVcgSQDFESDLDRLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSccpvcqrgfqteaelqevISDLQ 803
Cdd:TIGR02169 416 QRLSEELADL--NAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQE------------------LYDLK 475
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 804 SKLRLAPDKLKSTESELKKKEKRRDEMLGLVPMRQSIIDLKEKEIP----------------------ELRNKLQNV--- 858
Cdd:TIGR02169 476 EEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQgvhgtvaqlgsvgeryataievAAGNRLNNVvve 555
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 859 -----NRDIQRLK------------NDIEEQETLLGAIIPE----------------EESAKVCLTDVTIMERLqmelkD 905
Cdd:TIGR02169 556 ddavaKEAIELLKrrkagratflplNKMRDERRDLSILSEDgvigfavdlvefdpkyEPAFKYVFGDTLVVEDI-----E 630
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 906 VERKIAQQA--AKLQGLDLDRSVQQVNQEKQEKQHKLDTVSSKIELnrkliQDQQEQIQHLKSTANELKSEKLQISTNL- 982
Cdd:TIGR02169 631 AARRLMGKYrmVTLEGELFEKSGAMTGGSRAPRGGILFSRSEPAEL-----QRLRERLEGLKRELSSLQSELRRIENRLd 705
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 983 ---QRRQQLEEQTVELSTEVQSLYREIKDAKEQLSPLETTLEKFQQEKEELVNKKNTSHKIAQD---KINEIKEKVKNIh 1056
Cdd:TIGR02169 706 elsQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEEleeDLHKLEEALNDL- 784
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 1057 sYMKDIENYIQDGKDDYKKQKEtELNKVIAQISECEKHKEKINKEMGIMRQDIDTQKIQERWLQDNLTLRKRNEELKEVE 1136
Cdd:TIGR02169 785 -EARLSHSRIPEIQAELSKLEE-EVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGK 862
|
730 740 750
....*....|....*....|....*....|...
gi 2015236753 1137 EERKQHLKEMGQMQVLQMKNEHQKLEEKIDNIK 1169
Cdd:TIGR02169 863 KEELEEELEELEAALRDLESRLGDLKKERDELE 895
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
1298-1399 |
9.95e-16 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 76.24 E-value: 9.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 1298 MRGRCSAGQKVLASLIIRLALAEtfCLNCGILALDEPTTNLDRENieslAHALVEIIKSRSQQRNfQLLVITHDEDFVEL 1377
Cdd:cd03227 74 TRLQLSGGEKELSALALILALAS--LKPRPLYILDEIDRGLDPRD----GQALAEAILEHLVKGA-QVIVITHLPELAEL 146
|
90 100
....*....|....*....|..
gi 2015236753 1378 LgrseyvEKFYRIKKNIEQCSE 1399
Cdd:cd03227 147 A------DKLIHIKKVITGVYK 162
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
305-1061 |
1.29e-14 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 79.29 E-value: 1.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 305 KECQTELKYLKQNKEKACEIRDQITSKEAQLTSSREIVKSYENELDPLKNRLKEIEQNLSK----IMRLDNEIKALESRK 380
Cdd:TIGR04523 40 KKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKlnsdLSKINSEIKNDKEQK 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 381 KQMEKDNSELEQKMEKVFQGSDEQLNDLYHNHQrtvrekerrlvdcqrELEKLNKESRLLNQEKSELLVEQGRLQLQADR 460
Cdd:TIGR04523 120 NKLEVELNKLEKQKKENKKNIDKFLTEIKKKEK---------------ELEKLNNKYNDLKKQKEELENELNLLEKEKLN 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 461 HQEHMQardsliqslatqleldgfelgpfserQIKNfhklvrerQEKESETASQLLNDFTRKEALKQKQIDEIRDKKTGL 540
Cdd:TIGR04523 185 IQKNID--------------------------KIKN--------KLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 541 GRIIELKSEILTKKQNELKNVKYELQQLEGSSDRIL----ELDQELTKAERELSkaEKNSNVETLKTEVISLQNEK-ADL 615
Cdd:TIGR04523 231 KDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKkqlsEKQKELEQNNKKIK--ELEKQLNQLKSEISDLNNQKeQDW 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 616 DRTLRK-LDQEMEQLnhhTAARTQMEMLNKDKADKDEQIRKIKyrhsdeltsllgyfPNKKQLEDWLHSKSKEINQTRDR 694
Cdd:TIGR04523 309 NKELKSeLKNQEKKL---EEIQNQISQNNKIISQLNEQISQLK--------------KELTNSESENSEKQRELEEKQNE 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 695 LAKLNKELASAEQNKNHINIELKRKEEQLSSYEDKlfdvcgSQDFESDLDRLKEEIEKSSKQRAMLAGATAVYSQFITQL 774
Cdd:TIGR04523 372 IEKLKKENQSYKQEIKNLESQINDLESKIQNQEKL------NQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDL 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 775 TDENQSCCPVCQRGFQTEAELQEVISDLQSKLRLAPDKLKSTESELKKKEKRRDEMlglvpmrqsiidlkEKEIPELRNK 854
Cdd:TIGR04523 446 TNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKL--------------NEEKKELEEK 511
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 855 LQNVNRDIQRLKNDIEEqetllgaiipeeesakvcltdvtimerLQMELKDVERKIAQQAAKLQGLDLDRSVQQVNQEKQ 934
Cdd:TIGR04523 512 VKDLTKKISSLKEKIEK---------------------------LESEKKEKESKISDLEDELNKDDFELKKENLEKEID 564
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 935 EKQHKLdtvsSKIELNRKLIQDQQEQIQHL-KSTANELKSEKLQISTNLQRRQQLEEQTVELSTEVQSLYREIKDAKEQL 1013
Cdd:TIGR04523 565 EKNKEI----EELKQTQKSLKKKQEEKQELiDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKK 640
|
730 740 750 760
....*....|....*....|....*....|....*....|....*...
gi 2015236753 1014 SPLETTLEKFQQEKEELVNKKNtshkIAQDKINEIKEKVKNIHSYMKD 1061
Cdd:TIGR04523 641 NKLKQEVKQIKETIKEIRNKWP----EIIKKIKESKTKIDDIIELMKD 684
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
105-1145 |
2.43e-14 |
|
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: 78.86 E-value: 2.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 105 IEKMSIQGVRSFGiedkdKQIITFFSP-LTILVGPNGAGKTTIIECLKY---ICTGDFPPGTKGNTFVHdpKVAQETDVR 180
Cdd:pfam02463 2 LKRIEIEGFKSYA-----KTVILPFSPgFTAIVGPNGSGKSNILDAILFvlgERSAKSLRSERLSDLIH--SKSGAFVNS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 181 AQIRLQFRDVNGELvavqrsmlctqKSKKTEFktlegVITRTK----------HGEKVSLSskcaEIdREMISSLGVSKS 250
Cdd:pfam02463 75 AEVEITFDNEDHEL-----------PIDKEEV-----SIRRRVyrggdseyyiNGKNVTKK----EV-AELLESQGISPE 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 251 VLNNVIFCHQEDsNWPLSEGKALKQKFDEIFSATRYIKALETLRQVRQTQGQKVKE----CQTELKYLKQNKEKACEIRD 326
Cdd:pfam02463 134 AYNFLVQGGKIE-IIAMMKPERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELiidlEELKLQELKLKEQAKKALEY 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 327 QITSKEAQLTSSREIVKSYENELDPLKNRLKEI-----EQNLSKIMRLDNEIKALESRKKQMEKDNSElEQKMEKVFQGS 401
Cdd:pfam02463 213 YQLKEKLELEEEYLLYLDYLKLNEERIDLLQELlrdeqEEIESSKQEIEKEEEKLAQVLKENKEEEKE-KKLQEEELKLL 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 402 DEQLNDLYHNHQRTVREKERRLVDCQRELEKLNKESRLLNQEKSELLVEQGRLQLQADRHQEHMQARDSLIQSLATQLEL 481
Cdd:pfam02463 292 AKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQL 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 482 DGFELGPFSERQ--------IKNFHKLVRERQEKESETASQLLNdftRKEALKQKQIDEIRDKKTGLGRIIELKSEILTK 553
Cdd:pfam02463 372 EEELLAKKKLESerlssaakLKEEELELKSEEEKEAQLLLELAR---QLEDLLKEEKKEELEILEEEEESIELKQGKLTE 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 554 KQNELKNVKYELQQLEGSSDRI--LELDQELTKAERELSKAEKNSNVETLKTEVISLQNEKADLDRTLRKLDQEMEQLNH 631
Cdd:pfam02463 449 EKEELEKQELKLLKDELELKKSedLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAH 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 632 HTAARTQMEMLNKDKADKDEQIRKIKYRHSDELTSLLGYFPNKKQLedwlhsksKEINQTRDRLAKLNKELASAEQNKNH 711
Cdd:pfam02463 529 GRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELP--------LGARKLRLLIPKLKLPLKSIAVLEID 600
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 712 INIELKRKEEQLSSYEDKLFDVCGSQDFESDLDRLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSccpvcqrgFQT 791
Cdd:pfam02463 601 PILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLS--------ELT 672
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 792 EAELQEVISDLQSKLRLAPDKLKSTESELKKKEKRRDEMlglvpMRQSIIDLKEKEIPELRNKLQNVNRDIQRLKNDIEE 871
Cdd:pfam02463 673 KELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEE-----LKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDE 747
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 872 QETLLGAIIPEEESAKVCLTDVTimerLQMELKDVERKIAQQAAKLQGLDLDRSVQQVNQEKQEKQHKLDTVSSKIELNR 951
Cdd:pfam02463 748 EEEEEEKSRLKKEEKEEEKSELS----LKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLL 823
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 952 KLIQDQQEQIQHLKSTANELKSEKLQISTNLQRRQQLEEQTVELSTEVQSLYREIKDAKEQLSPLETTLEKFQQEKEELV 1031
Cdd:pfam02463 824 IEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELE 903
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 1032 NKKNTSHKIAQDKI-NEIKEKVKNIHSYMKDIENYIQDGKDDYKKQKE---TELNKVIAQISECEKHKEKINKEMGIMRQ 1107
Cdd:pfam02463 904 EESQKLNLLEEKENeIEERIKEEAEILLKYEEEPEELLLEEADEKEKEennKEEEEERNKRLLLAKEELGKVNLMAIEEF 983
|
1050 1060 1070
....*....|....*....|....*....|....*...
gi 2015236753 1108 DIDTQKIQERWLQDNLTLRKRNEELKEVEEERKQHLKE 1145
Cdd:pfam02463 984 EEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKE 1021
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
528-1070 |
5.01e-14 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 77.63 E-value: 5.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 528 KQIDEIRDKKTGLGRIIELKSEILTKKQNELKNVKYELQQLEGSSDRILELDQELTKAERELSKAEKNSN---------- 597
Cdd:PRK01156 204 KQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEIKTAESDLSMELEKNNyykeleerhm 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 598 ----------------VETLKTEVISLQNEKADLDRTLRKLDQEMEQLNHHTAARTQMEMLNKDKADKDEQIRKIKYRHS 661
Cdd:PRK01156 284 kiindpvyknrnyindYFKYKNDIENKKQILSNIDAEINKYHAIIKKLSVLQKDYNDYIKKKSRYDDLNNQILELEGYEM 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 662 DeltsLLGYFPNKKQLEDWLHSKSKEInqtRDRLAKLNKELASAEQNKNHINIELKRKEEQLSSYEDKLfdvcgsQDFES 741
Cdd:PRK01156 364 D----YNSYLKSIESLKKKIEEYSKNI---ERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKV------SSLNQ 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 742 DLDRLKEEIEKSSKQRAMLAGatavysqfitqltdenQSCCPVCQRGFQTEaELQEVISDLQSKLRLAPDKLKSTESELK 821
Cdd:PRK01156 431 RIRALRENLDELSRNMEMLNG----------------QSVCPVCGTTLGEE-KSNHIINHYNEKKSRLEEKIREIEIEVK 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 822 K-KEKRRDemlgLVPMRQSIIDLKEKEIPELRNKLQNVNRDIQRLKND---IEEQETLLGAIIPEEESAKVCLTDVTIME 897
Cdd:PRK01156 494 DiDEKIVD----LKKRKEYLESEEINKSINEYNKIESARADLEDIKIKineLKDKHDKYEEIKNRYKSLKLEDLDSKRTS 569
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 898 RL----QMELKDVERKIAQQAAKLQGL-DLDRSVQQVNQEKQEKQHKLDTVSSKI--ELN-----RKLIQDQQEQIQHLK 965
Cdd:PRK01156 570 WLnalaVISLIDIETNRSRSNEIKKQLnDLESRLQEIEIGFPDDKSYIDKSIREIenEANnlnnkYNEIQENKILIEKLR 649
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 966 STANELKSEKLQISTNLQRRQQLEEQTVELSTEVQSLYREIKDAKEQLSPLETTLEKFQQEKEELvnkkntshkiaQDKI 1045
Cdd:PRK01156 650 GKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINEL-----------SDRI 718
|
570 580
....*....|....*....|....*
gi 2015236753 1046 NEIKEKVKNihsyMKDIENYIQDGK 1070
Cdd:PRK01156 719 NDINETLES----MKKIKKAIGDLK 739
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
104-1026 |
5.14e-14 |
|
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: 77.70 E-value: 5.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 104 RIEKMSIQGVRSFgiedKDKQIITF--FSPLTILVGPNGAGKTTIIECLKYICTGDFPpgTKGNTFVHDPKVAQETDVRA 181
Cdd:TIGR00618 2 KPLRLTLKNFGSY----KGTHTIDFtaLGPIFLICGKTGAGKTTLLDAITYALYGKLP--RRSEVIRSLNSLYAAPSEAA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 182 QIRLQFrDVNGELVAVQRSMLCTQKSKKTEfkTLEGVITRTKHGEKVSLSSKCAEIDREMISSLGVSKSVLNNVIFCHQ- 260
Cdd:TIGR00618 76 FAELEF-SLGTKIYRVHRTLRCTRSHRKTE--QPEQLYLEQKKGRGRILAAKKSETEEVIHDLLKLDYKTFTRVVLLPQg 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 261 EDSNWPLSEGKALKQKFDEIFSATRY----------IKALE----------------------TLRQVRQTQGQKVKECQ 308
Cdd:TIGR00618 153 EFAQFLKAKSKEKKELLMNLFPLDQYtqlalmefakKKSLHgkaelltlrsqlltlctpcmpdTYHERKQVLEKELKHLR 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 309 TELKYLKQNKEKACEIR---DQITSKEAQLTSSREIVKSYENELDPLKNRLKEIEQNlSKIMRLDNEIKALESRKKQMEK 385
Cdd:TIGR00618 233 EALQQTQQSHAYLTQKReaqEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRA-RKAAPLAAHIKAVTQIEQQAQR 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 386 DNSELEQKMEKVFQgsdEQLNDLYHNHQRTVREKERRLVDC----QRELEKLNKESRLLNQEKSELLVEQGRLQLQADRH 461
Cdd:TIGR00618 312 IHTELQSKMRSRAK---LLMKRAAHVKQQSSIEEQRRLLQTlhsqEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQK 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 462 QEHMQARDSLIQSLATQLELDGFELGPFSERQIKNFHKLVRERQEKESETASQLLNDFTRKEAlkQKQIDEIRDKKTGLG 541
Cdd:TIGR00618 389 TTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTA--QCEKLEKIHLQESAQ 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 542 RIIELKsEILTKKQNELKNVKYELQQLEGSSDRILELDQELTKAERELS-KAEKNSNVETLKTEVISLQNEKADLDRTLR 620
Cdd:TIGR00618 467 SLKERE-QQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNpARQDIDNPGPLTRRMQRGEQTYAQLETSEE 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 621 KLDQEM-EQLNHHTAARTQMEmlnkdKADKDEQIRKIKYRHSDELtsllgyFPNKKQLEDWLHSKSKEINQTRDRLAKLN 699
Cdd:TIGR00618 546 DVYHQLtSERKQRASLKEQMQ-----EIQQSFSILTQCDNRSKED------IPNLQNITVRLQDLTEKLSEAEDMLACEQ 614
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 700 KElasaeqnknhiniELKRKEEQLSSYEDKLFDVCGSQDFESDLDRLKEEIEKSSKQRAMLAGATAvySQFITQLTDENQ 779
Cdd:TIGR00618 615 HA-------------LLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSI--RVLPKELLASRQ 679
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 780 SCCPVCQRGFQTEAELQEVISDLQSKLRlapdklkSTESELKKKEKRRDEMLGLVPMRQSIIDLKEKEIPELRNKLQnvn 859
Cdd:TIGR00618 680 LALQKMQSEKEQLTYWKEMLAQCQTLLR-------ELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELM--- 749
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 860 rdiqrlkndiEEQETLLGAIIPEEESAKvclTDVTIMERLQMELKDVERKIAQQAAKLQgldldRSVQQVNQEKQEKQHK 939
Cdd:TIGR00618 750 ----------HQARTVLKARTEAHFNNN---EEVTAALQTGAELSHLAAEIQFFNRLRE-----EDTHLLKTLEAEIGQE 811
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 940 LDTVSSKIELNRKLIQDQQEQ----IQHLKSTANELKSEKLQISTNLQRRQQLEEQTVELSTEVQSL--YREIKDAKEql 1013
Cdd:TIGR00618 812 IPSDEDILNLQCETLVQEEEQflsrLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKLngINQIKIQFD-- 889
|
970
....*....|...
gi 2015236753 1014 splETTLEKFQQE 1026
Cdd:TIGR00618 890 ---GDALIKFLHE 899
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
291-941 |
2.87e-13 |
|
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: 75.15 E-value: 2.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 291 ETLRQVRQTQGQKVKECQTELKYLKQNKEKA-CEIRDQITSKEAQLTSSREIVKSYENELDPLKNRLKEIEQN------- 362
Cdd:pfam15921 127 DAMADIRRRESQSQEDLRNQLQNTVHELEAAkCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSILVDFEEAsgkkiye 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 363 ---------------LSKIMR-LDNEIKALESR----KKQMEKDNSELEQKMEKVFQGSDEQLNDLYHNHQrtvrekerr 422
Cdd:pfam15921 207 hdsmstmhfrslgsaISKILReLDTEISYLKGRifpvEDQLEALKSESQNKIELLLQQHQDRIEQLISEHE--------- 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 423 lVDCQRELEKLNKESRLLNQEKSELLVeqgrLQLQAdRHQEHMQARD-SLIQSLATQLELDGFELGPFSERQIKNFHK-- 499
Cdd:pfam15921 278 -VEITGLTEKASSARSQANSIQSQLEI----IQEQA-RNQNSMYMRQlSDLESTVSQLRSELREAKRMYEDKIEELEKql 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 500 ------LVRERQEKES---------ETASQLLNDFTRKE---ALKQKQIDEIRDKKTGLGRIIE---------------- 545
Cdd:pfam15921 352 vlanseLTEARTERDQfsqesgnldDQLQKLLADLHKREkelSLEKEQNKRLWDRDTGNSITIDhlrrelddrnmevqrl 431
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 546 ------LKSEI----------LTKKQNELKNVKYELQQLEGSSDRILELDQELT-------KAERELSK-----AEKNSN 597
Cdd:pfam15921 432 eallkaMKSECqgqmerqmaaIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTakkmtleSSERTVSDltaslQEKERA 511
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 598 VETLKTEVISLQNeKADLD-RTLRKLDQEMEQLNHhtaARTQMEMLNKDKADKDEQIrKIKYRHSDELTSLLGYFP---- 672
Cdd:pfam15921 512 IEATNAEITKLRS-RVDLKlQELQHLKNEGDHLRN---VQTECEALKLQMAEKDKVI-EILRQQIENMTQLVGQHGrtag 586
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 673 ----NKKQLEdwlhsksKEINQTRDRLaklnKELASAEQNKNHINIELKRKEEQLSSYEDKLFDVcGSQ------DFESD 742
Cdd:pfam15921 587 amqvEKAQLE-------KEINDRRLEL----QEFKILKDKKDAKIRELEARVSDLELEKVKLVNA-GSErlravkDIKQE 654
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 743 LDRLKEEIEKSSKQramlagatavysqfITQLTDENQsccpVCQRGFQTEAELQEVISD-LQSKLRLAPDKLKSTESELK 821
Cdd:pfam15921 655 RDQLLNEVKTSRNE--------------LNSLSEDYE----VLKRNFRNKSEEMETTTNkLKMQLKSAQSELEQTRNTLK 716
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 822 KKEKRRDEMLGLVPMRQSIIDLKEKEIPELRNKLQ-------NVNRDIQRLKNDIEEQETLLGAIIPEEESAKVCLTDVT 894
Cdd:pfam15921 717 SMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQfleeamtNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLR 796
|
730 740 750 760
....*....|....*....|....*....|....*....|....*....
gi 2015236753 895 IMERlQMELKDVERKIAQQAAKLQGLDLDRSVQQVNQE--KQEKQHKLD 941
Cdd:pfam15921 797 SQER-RLKEKVANMEVALDKASLQFAECQDIIQRQEQEsvRLKLQHTLD 844
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
521-1272 |
3.40e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 75.09 E-value: 3.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 521 RKEALKQkqideIRDKKTGLGRIIELKSEIltKKQneLKNVKYELQQLEgssdRILELDQELTKAERELSKAEKNS---N 597
Cdd:TIGR02168 174 RKETERK-----LERTRENLDRLEDILNEL--ERQ--LKSLERQAEKAE----RYKELKAELRELELALLVLRLEElreE 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 598 VETLKTEVISLQNEKADLDRTLRKLDQEMEQLNHhtaARTQMEM-----------LNKDKADKDEQIRKIKYRhsdelts 666
Cdd:TIGR02168 241 LEELQEELKEAEEELEELTAELQELEEKLEELRL---EVSELEEeieelqkelyaLANEISRLEQQKQILRER------- 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 667 llgyfpnKKQLEDWLHSKSKEINQTRDRLAKLNKELASAEQNKNHINIELKRKEEQLSSYEDKLFD-VCGSQDFESDLDR 745
Cdd:TIGR02168 311 -------LANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEElESRLEELEEQLET 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 746 LKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQsccpvcqrgfQTEAELQEVISDLQS-KLRLAPDKLKSTESELKKKE 824
Cdd:TIGR02168 384 LRSKVAQLELQIASLNNEIERLEARLERLEDRRE----------RLQQEIEELLKKLEEaELKELQAELEELEEELEELQ 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 825 KRRDEMLGLVPMRQSIIDLKEKEIPELRNKLQNVNRDIQRLKNDIEEQET--------------------LLGAIIPEEE 884
Cdd:TIGR02168 454 EELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGfsegvkallknqsglsgilgVLSELISVDE 533
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 885 SAKVCLtDVTIMERLQM----ELKDVERKIAQQAAKLQG----LDLDRSVQQVNQEKQEKQHK-----------LDTVSS 945
Cdd:TIGR02168 534 GYEAAI-EAALGGRLQAvvveNLNAAKKAIAFLKQNELGrvtfLPLDSIKGTEIQGNDREILKniegflgvakdLVKFDP 612
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 946 KIE------LNRKLIQDQQEQIQHLkstANELKSEKLQISTN---------------------LQRRQ---QLEEQTVEL 995
Cdd:TIGR02168 613 KLRkalsylLGGVLVVDDLDNALEL---AKKLRPGYRIVTLDgdlvrpggvitggsaktnssiLERRReieELEEKIEEL 689
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 996 STEVQSLYREIKDAKEQLSPLETTLEKFQQEKEElvnkKNTSHKIAQDKINEIKEKVKNIHSYMKDIENYIQDgKDDYKK 1075
Cdd:TIGR02168 690 EEKIAELEKALAELRKELEELEEELEQLRKELEE----LSRQISALRKDLARLEAEVEQLEERIAQLSKELTE-LEAEIE 764
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 1076 QKETELNKVIAQISECEKHKEKINKEMGIMRQDIDTQKIQERWLQDNLTLRKRNEELKEVEEERKQHLKEMGQMQVLQMK 1155
Cdd:TIGR02168 765 ELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLE 844
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 1156 NEHQKLEEKIDNIKRNH-SLAIGRQKgYEEEIIHFKKELR--EPQFRDAEEKYREMMIIMRTTELVNKDLDIYYKTLDQA 1232
Cdd:TIGR02168 845 EQIEELSEDIESLAAEIeELEELIEE-LESELEALLNERAslEEALALLRSELEELSEELRELESKRSELRRELEELREK 923
|
810 820 830 840
....*....|....*....|....*....|....*....|....*.
gi 2015236753 1233 IMKFH------SMKMEEINKIIRDLWRSTYRGQDIEYIEIRSDADE 1272
Cdd:TIGR02168 924 LAQLElrleglEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEE 969
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
266-1250 |
4.55e-13 |
|
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: 75.09 E-value: 4.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 266 PLSEGKALKQKFDEIFsatryiKALETLRQVRQTQGQKVKECQTELKYLKQNKEkaceIRDQITSKEaqltssreivkSY 345
Cdd:TIGR01612 457 PKSKLKALEKRFFEIF------EEEWGSYDIKKDIDENSKQDNTVKLILMRMKD----FKDIIDFME-----------LY 515
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 346 ENELDPLKNR-LKEIEQNLSKIMRLDNEIKALESR------KKQMEKDNSELEQKMEKVFQgSDEQLNDLYHNHQRTV-- 416
Cdd:TIGR01612 516 KPDEVPSKNIiGFDIDQNIKAKLYKEIEAGLKESYelaknwKKLIHEIKKELEEENEDSIH-LEKEIKDLFDKYLEIDde 594
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 417 -----------REKERRLVDCQRELEKLNKESRLL--NQEKSELLVEQGRLQLQadrhqEHMQARDSLIQSLATQLeldg 483
Cdd:TIGR01612 595 iiyinklklelKEKIKNISDKNEYIKKAIDLKKIIenNNAYIDELAKISPYQVP-----EHLKNKDKIYSTIKSEL---- 665
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 484 felgpfSERQIKNFHKLVRERQEKESETASQLLNDFTRKEALKQKqIDEIRDKKTGL-GRIIELKSEILTKKQNELKNVK 562
Cdd:TIGR01612 666 ------SKIYEDDIDALYNELSSIVKENAIDNTEDKAKLDDLKSK-IDKEYDKIQNMeTATVELHLSNIENKKNELLDII 738
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 563 YELQQLEGSsdrilELDQELTKAERELSKAEKNsnvetLKTEVISLQNEKADLDRTLRKLDQEMEQLNHHTAARTQMEML 642
Cdd:TIGR01612 739 VEIKKHIHG-----EINKDLNKILEDFKNKEKE-----LSNKINDYAKEKDELNKYKSKISEIKNHYNDQINIDNIKDED 808
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 643 NKDKADKDEQIRKIKYRHSDELTSLLGYFPNKKqlEDWLHSKSKEINQTRDRLAKLNKELASAEQNKNHINIELKrkEEQ 722
Cdd:TIGR01612 809 AKQNYDKSKEYIKTISIKEDEIFKIINEMKFMK--DDFLNKVDKFINFENNCKEKIDSEHEQFAELTNKIKAEIS--DDK 884
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 723 LSSYEDKLfdvcgsQDFESDLDRLKEEIEKSSkqramlagatavysQFITQLTDENQSCcPVCQRGFQTEAELQEVISDL 802
Cdd:TIGR01612 885 LNDYEKKF------NDSKSLINEINKSIEEEY--------------QNINTLKKVDEYI-KICENTKESIEKFHNKQNIL 943
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 803 QSKLRLAPDKLKSTESELKKKEKRRDEMLglvpmRQSIIDLkEKEIPELR-NKLQNVNRDIQRLKNDIEE-----QETLL 876
Cdd:TIGR01612 944 KEILNKNIDTIKESNLIEKSYKDKFDNTL-----IDKINEL-DKAFKDASlNDYEAKNNELIKYFNDLKAnlgknKENML 1017
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 877 GAIIPEEESAkvcltdvtimerlqmeLKDVERKIAQQAAKLQGLDL--DRSVQQVNQEKQEKqhkldtVSSKIE-LNRKL 953
Cdd:TIGR01612 1018 YHQFDEKEKA----------------TNDIEQKIEDANKNIPNIEIaiHTSIYNIIDEIEKE------IGKNIElLNKEI 1075
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 954 IQDQQEQIQHLkstaNELKsEKLQIstnLQRRQQLEEQTVELSTEVQSLYREIKDAKEQLSPLETTLEKFQQEKEELVNK 1033
Cdd:TIGR01612 1076 LEEAEINITNF----NEIK-EKLKH---YNFDDFGKEENIKYADEINKIKDDIKNLDQKIDHHIKALEEIKKKSENYIDE 1147
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 1034 ---------KNTSHKIAQDKINEIKEKVKNIHSymkdienyiqdgKDDYKKQKETELNKVIAQISECEKHKEKINKEMGI 1104
Cdd:TIGR01612 1148 ikaqindleDVADKAISNDDPEEIEKKIENIVT------------KIDKKKNIYDEIKKLLNEIAEIEKDKTSLEEVKGI 1215
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 1105 -----------MRQDIDTQKIQ--------ERWLQDNLTLRKRNEELKEVEEERKQHLKEMGQMQVLQMKNE-----HQK 1160
Cdd:TIGR01612 1216 nlsygknlgklFLEKIDEEKKKsehmikamEAYIEDLDEIKEKSPEIENEMGIEMDIKAEMETFNISHDDDKdhhiiSKK 1295
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 1161 LEEKIDNIkRNHSLAIGRQKGYEEEIIHFKKELREpQFRDAEEKYREM-MIIMRTTELVN-KDLDIYYKTLDQaiMKFHS 1238
Cdd:TIGR01612 1296 HDENISDI-REKSLKIIEDFSEESDINDIKKELQK-NLLDAQKHNSDInLYLNEIANIYNiLKLNKIKKIIDE--VKEYT 1371
|
1050
....*....|..
gi 2015236753 1239 MKMEEINKIIRD 1250
Cdd:TIGR01612 1372 KEIEENNKNIKD 1383
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
550-1169 |
4.76e-13 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 74.29 E-value: 4.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 550 ILTKKQNELKNVKYELQ----QLEGSSDRILELDQELTKaeRELSKAEKNSNVETLKTEVISLQNEKADLDRTLRKLDQE 625
Cdd:TIGR04523 27 IANKQDTEEKQLEKKLKtiknELKNKEKELKNLDKNLNK--DEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 626 MEQLNHHTAARTQMEMLNKDKADK-DEQIRKIKYRHSDELTSLLgyfpNKKQLEDWLHSK----SKEINQTRDRLAKLNK 700
Cdd:TIGR04523 105 LSKINSEIKNDKEQKNKLEVELNKlEKQKKENKKNIDKFLTEIK----KKEKELEKLNNKyndlKKQKEELENELNLLEK 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 701 ELASAEQNKNHINIELKRKEEQLSSYEDKlfdvcgsqdfESDLDRLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQS 780
Cdd:TIGR04523 181 EKLNIQKNIDKIKNKLLKLELLLSNLKKK----------IQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISN 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 781 CCPVCQRGFQTEAELQEVISDLQSKLRLAPDKLKSTESELK---------KKEKRRDEMLGLvpmrQSIIDLKEKEIPEL 851
Cdd:TIGR04523 251 TQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNqlkseisdlNNQKEQDWNKEL----KSELKNQEKKLEEI 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 852 RNKLQNVNRDIQRLKNDIEEQETllgaiipeeesakvcltdvtimERLQMELKDVERKIaqqaaklqglDLDRSVQQVNQ 931
Cdd:TIGR04523 327 QNQISQNNKIISQLNEQISQLKK----------------------ELTNSESENSEKQR----------ELEEKQNEIEK 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 932 EKQEKQHKLDTV----SSKIELNRKlIQDQQEQIQHLKSTANELKSEKLQISTNLQRRQQ-----------LEEQTVELS 996
Cdd:TIGR04523 375 LKKENQSYKQEIknleSQINDLESK-IQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKEtiiknnseikdLTNQDSVKE 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 997 TEVQSLYREIKDAKEQLSPLE-------TTLEKFQQEKEELVN--------KKNTSHKIA--QDKINEIKEKVKNIHSYM 1059
Cdd:TIGR04523 454 LIIKNLDNTRESLETQLKVLSrsinkikQNLEQKQKELKSKEKelkklneeKKELEEKVKdlTKKISSLKEKIEKLESEK 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 1060 KDIENYIQDGKDDYKKqKETELNKviaqiSECEKHKEKINKEMGIMRQDIDTQKIQERWLQDNLTLRKRNEELKEVEEER 1139
Cdd:TIGR04523 534 KEKESKISDLEDELNK-DDFELKK-----ENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEE 607
|
650 660 670
....*....|....*....|....*....|
gi 2015236753 1140 KQHLKEMGQMQVLQMKNEHQKLEEKIDNIK 1169
Cdd:TIGR04523 608 KEKKISSLEKELEKAKKENEKLSSIIKNIK 637
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
413-1169 |
5.32e-13 |
|
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: 74.38 E-value: 5.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 413 QRTVREKERRLVDCQReleKLNKESRLlnQEKSELLVEQGRLQLQAdRHQEHMQARDSLIQslatqleldgfelgpfser 492
Cdd:pfam15921 77 ERVLEEYSHQVKDLQR---RLNESNEL--HEKQKFYLRQSVIDLQT-KLQEMQMERDAMAD------------------- 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 493 qiknfhklVRERQEKESET-ASQLLNDFTRKEALKQKQIDEIRDKKTglgRIIELKSEILTKKQ--NELKNVKYELQqlE 569
Cdd:pfam15921 132 --------IRRRESQSQEDlRNQLQNTVHELEAAKCLKEDMLEDSNT---QIEQLRKMMLSHEGvlQEIRSILVDFE--E 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 570 GSSDRILELDQELTKAERELSKAeKNSNVETLKTEVISLQNEKADLDRTLRKLDQEmeqlnhhtaARTQMEMLNKDKADK 649
Cdd:pfam15921 199 ASGKKIYEHDSMSTMHFRSLGSA-ISKILRELDTEISYLKGRIFPVEDQLEALKSE---------SQNKIELLLQQHQDR 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 650 DEQIRKikyRHSDELTSLLGYFPNKKQLEDWLHSKSKEIN-QTRDRLAKLNKELASAEQNKNHINIELKrkeEQLSSYED 728
Cdd:pfam15921 269 IEQLIS---EHEVEITGLTEKASSARSQANSIQSQLEIIQeQARNQNSMYMRQLSDLESTVSQLRSELR---EAKRMYED 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 729 KLfdvcgsqdfesdldrlkEEIEKsskqRAMLAGatavySQFITQLTDENQsccpVCQRGFQTEAELQEVISDLQSKlrl 808
Cdd:pfam15921 343 KI-----------------EELEK----QLVLAN-----SELTEARTERDQ----FSQESGNLDDQLQKLLADLHKR--- 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 809 apDKLKSTESELKKKEKRRDemlglvpMRQSIIdlkekeIPELRNKLQNVNRDIQRL-------KNDIEEQ-ETLLGAII 880
Cdd:pfam15921 390 --EKELSLEKEQNKRLWDRD-------TGNSIT------IDHLRRELDDRNMEVQRLeallkamKSECQGQmERQMAAIQ 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 881 PEEESakvcLTDVTIMERLQMELKDVERKIAQQ--AAKLQGLDLDRSVQQVNQEKQEKQHKLDTVSSKIELNRKLIQDQQ 958
Cdd:pfam15921 455 GKNES----LEKVSSLTAQLESTKEMLRKVVEEltAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKL 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 959 EQIQHLKSTANELKSE-------KLQISTNLQ----RRQQLEEQTV----------ELSTEVQSLYREIKDAKEQLS--- 1014
Cdd:pfam15921 531 QELQHLKNEGDHLRNVqtecealKLQMAEKDKvieiLRQQIENMTQlvgqhgrtagAMQVEKAQLEKEINDRRLELQefk 610
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 1015 -----------PLETTLEKFQQEKEELVNKKNTSHKIAQD-------KINEIKEKVKNIHSYMKDIENYIQDGKDDyKKQ 1076
Cdd:pfam15921 611 ilkdkkdakirELEARVSDLELEKVKLVNAGSERLRAVKDikqerdqLLNEVKTSRNELNSLSEDYEVLKRNFRNK-SEE 689
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 1077 KETELNKVIAQI----SECEK-------------HKEKI----NKEMGIMRQDIDTQKIQERWLQDNLT---------LR 1126
Cdd:pfam15921 690 METTTNKLKMQLksaqSELEQtrntlksmegsdgHAMKVamgmQKQITAKRGQIDALQSKIQFLEEAMTnankekhflKE 769
|
810 820 830 840
....*....|....*....|....*....|....*....|...
gi 2015236753 1127 KRNEELKEVEEERKQHLKEMGQMQVLqmKNEHQKLEEKIDNIK 1169
Cdd:pfam15921 770 EKNKLSQELSTVATEKNKMAGELEVL--RSQERRLKEKVANME 810
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
273-1013 |
9.35e-13 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 73.56 E-value: 9.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 273 LKQKFDEIFSATRYIKALEtlRQVRQTQGQKVKeCQTELKYLKQNKEkacEIRDQITSKEAQLTSSREIVKSYENELDPL 352
Cdd:TIGR02169 324 LAKLEAEIDKLLAEIEELE--REIEEERKRRDK-LTEEYAELKEELE---DLRAELEEVDKEFAETRDELKDYREKLEKL 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 353 KNRLKEIEQNL-----------SKIMRLDNEIKALESRKKQMEKDNSELEQKMEKVFQGSDEQLNDL------YHNHQRT 415
Cdd:TIGR02169 398 KREINELKRELdrlqeelqrlsEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLskyeqeLYDLKEE 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 416 VREKERRLVDCQRELEKLNKESRLLNQEK------SELLVE--QGRLQLQAD------RHQEHMQA-----------RDS 470
Cdd:TIGR02169 478 YDRVEKELSKLQRELAEAEAQARASEERVrggravEEVLKAsiQGVHGTVAQlgsvgeRYATAIEVaagnrlnnvvvEDD 557
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 471 LIQSLATQLeLDGFELGPFS---ERQIKNFHKLVRERQEKESETASQLLNDFTRKEALKQKQIdeIRDkkTGLGRIIELK 547
Cdd:TIGR02169 558 AVAKEAIEL-LKRRKAGRATflpLNKMRDERRDLSILSEDGVIGFAVDLVEFDPKYEPAFKYV--FGD--TLVVEDIEAA 632
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 548 SEILtkkqnelknVKYELQQLEGSsdrILELDQELTKAERELSKAEKNS-----NVETLKTEVISLQNEKADLDRTLRKL 622
Cdd:TIGR02169 633 RRLM---------GKYRMVTLEGE---LFEKSGAMTGGSRAPRGGILFSrsepaELQRLRERLEGLKRELSSLQSELRRI 700
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 623 DQEMEQLnhhtaaRTQMEmlnkdkaDKDEQIRKIKYRHSdeltsllgyfpnkkQLEDWLHSKSKEINQTRDRLAKLNKEL 702
Cdd:TIGR02169 701 ENRLDEL------SQELS-------DASRKIGEIEKEIE--------------QLEQEEEKLKERLEELEEDLSSLEQEI 753
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 703 ASAEQNKNHINIELKRKEEQLSSYEDKLFDVCGSQDfESDLDRLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQScc 782
Cdd:TIGR02169 754 ENVKSELKELEARIEELEEDLHKLEEALNDLEARLS-HSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEY-- 830
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 783 pvcqrgfqteaeLQEVISDLQSKLRLAPDKLKSTESELKKKEKRRDEMlglvpmrQSIIDLKEKEIPELRNKLQNVNRDI 862
Cdd:TIGR02169 831 ------------LEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEEL-------EEELEELEAALRDLESRLGDLKKER 891
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 863 QRLKNDIEEQETLLGAIIPEEESAKVCLTDVTI-MERLQMELKDVERKIAQQAAKLQGLDLDRSVQQVNQEKQEKQHKLD 941
Cdd:TIGR02169 892 DELEAQLRELERKIEELEAQIEKKRKRLSELKAkLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALE 971
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 942 TVsskielNRKLIQDQQE---QIQHLKSTANELKSEKLQI-----STNLQRRQQLEEQTVELSTEVQSLYREIKDAKEQL 1013
Cdd:TIGR02169 972 PV------NMLAIQEYEEvlkRLDELKEKRAKLEEERKAIlerieEYEKKKREVFMEAFEAINENFNEIFAELSGGTGEL 1045
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
319-912 |
1.07e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 73.43 E-value: 1.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 319 EKACEIRDQITSKEAQLTSSReiVKSYENELDPLKNRLKEIEQNLSkimRLDNEIKALESRKKQMEKDNSELEQKMEKvf 398
Cdd:COG1196 213 ERYRELKEELKELEAELLLLK--LRELEAELEELEAELEELEAELE---ELEAELAELEAELEELRLELEELELELEE-- 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 399 qgsdeqlndlyhnHQRTVREKERRLVDCQRELEKLNKESRLLNQEKSELLVEQGRLQLQADRHQEHMQARDSLIQSLATQ 478
Cdd:COG1196 286 -------------AQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEE 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 479 LELDGFELGpFSERQIKNFHKLVRERQEKESETASQLLNDFTRKEALKQKQIDEIRDKKTGLGRIIELKSEILTKKQNEL 558
Cdd:COG1196 353 LEEAEAELA-EAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALA 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 559 KNVKYELQQLEGSSDRILELDQELTKAERELSKAEKNSNVETLKTEVISLQNEKADLDRTLRKLDQEMEQLNHH----TA 634
Cdd:COG1196 432 ELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGflegVK 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 635 ARTQMEMLNKDKADKDEQIRKIKYRHSDELTSLLGYFPNK--------KQLEDWLhSKSKEINQTRDRLAKLNKELASAE 706
Cdd:COG1196 512 AALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIvveddevaAAAIEYL-KAAKAGRATFLPLDKIRARAALAA 590
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 707 QNKNHINIELKRKEEQLSSYEDKLFDVCGSQDFESDLDRLKEEieksskqRAMLAGATAVYSQFITQLTDENQSccpvcQ 786
Cdd:COG1196 591 ALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLE-------AALRRAVTLAGRLREVTLEGEGGS-----A 658
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 787 RGFQTEAELQEVISDLQSKLRLAPDKLKSTESELKKKEKRRDEmlglvpMRQSIIDLKEKEIPELRNKLQNVNRDIQRLK 866
Cdd:COG1196 659 GGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLA------EEEEERELAEAEEERLEEELEEEALEEQLEA 732
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 2015236753 867 NDIEEQETLLGAIIPEEESAKVCLTDVTIMERLQMELKDVERKIAQ 912
Cdd:COG1196 733 EREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEA 778
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
320-1103 |
4.37e-12 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 71.71 E-value: 4.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 320 KACEIRDQITSKEAQLTSSREIVKSYENELDPLKNRLKEIEQNLSKIMRLDneikalESRKKQMEKDNSELEQKMEKVfQ 399
Cdd:PTZ00121 1183 KAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAE------EAKKDAEEAKKAEEERNNEEI-R 1255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 400 GSDEQLNDLYHNHQRTVREKERRLVDCQRELEKLNKESRLLNQEKSElLVEQGRLQLQADRHQEHMQARDSLIQSLATQL 479
Cdd:PTZ00121 1256 KFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKK-KADEAKKKAEEAKKADEAKKKAEEAKKKADAA 1334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 480 ELDGFElgpfserqiknfHKLVRERQEKESETASQLLNDFTRKEALKQKQIDEIRDKKTGLGRIIE--LKSEILTKKQNE 557
Cdd:PTZ00121 1335 KKKAEE------------AKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEekKKADEAKKKAEE 1402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 558 LKNVKYELQQLEGSSDRILELD---QELTKAERELSKAEKNSNVETLKtevislqnEKADLDRTLRKLDQEMEQLNHHTA 634
Cdd:PTZ00121 1403 DKKKADELKKAAAAKKKADEAKkkaEEKKKADEAKKKAEEAKKADEAK--------KKAEEAKKAEEAKKKAEEAKKADE 1474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 635 ARTQMEmlNKDKADKDEQIRKIKYRHSDELtsllgyfpnKKQLEDwlHSKSKEINQTRDrlAKLNKELASAEQNKNhiNI 714
Cdd:PTZ00121 1475 AKKKAE--EAKKADEAKKKAEEAKKKADEA---------KKAAEA--KKKADEAKKAEE--AKKADEAKKAEEAKK--AD 1537
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 715 ELKRKEEQLSSYEDKlfdvcGSQDFESDLDRLKEEIEKSSKQRAMLAGATAVYSQFItqltdenqsccpvcqrgfqTEAE 794
Cdd:PTZ00121 1538 EAKKAEEKKKADELK-----KAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKA-------------------EEAR 1593
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 795 LQEVISDLQSKLRLAPDKLKSTESELKKKEKRRDEmlglvpmrqsiiDLKEKEIPELRNKLQNVNRDIQRLKNDIEEQEt 874
Cdd:PTZ00121 1594 IEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKA------------EEEKKKVEQLKKKEAEEKKKAEELKKAEEENK- 1660
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 875 llgaiIPEEESAKVCLTDVTIMERLQMELKDvERKIAQQAAKLQglDLDRSVQQVNQEKQEKQHKLDTVSSKIELNRKLI 954
Cdd:PTZ00121 1661 -----IKAAEEAKKAEEDKKKAEEAKKAEED-EKKAAEALKKEA--EEAKKAEELKKKEAEEKKKAEELKKAEEENKIKA 1732
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 955 QDQQEQIQHLKSTANELKSEKlqistnlqrrqqleeqtvELSTEVQSLYREikdakEQLSPLETTLEKFQQEKEELVNKK 1034
Cdd:PTZ00121 1733 EEAKKEAEEDKKKAEEAKKDE------------------EEKKKIAHLKKE-----EEKKAEEIRKEKEAVIEEELDEED 1789
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2015236753 1035 NTSHKIAQDKINEIKEKVKNIHSYMKDIENYIQDGK---DDYKKQKETELNKVIAQISECEKHKEKINKEMG 1103
Cdd:PTZ00121 1790 EKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKemeDSAIKEVADSKNMQLEEADAFEKHKFNKNNENG 1861
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
503-1185 |
4.94e-12 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 70.91 E-value: 4.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 503 ERQEKESETASQLLNDFTRKEALKQKQIDEIRDKKTGLG---RIIELKSEILTKKQNELKNVKYELQQ-LEGSSDRILEL 578
Cdd:pfam05483 71 ENSEGLSRLYSKLYKEAEKIKKWKVSIEAELKQKENKLQenrKIIEAQRKAIQELQFENEKVSLKLEEeIQENKDLIKEN 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 579 D--QELTKAEREL--SKAEKNSNVETLKTEVislQNEKADLDRTLRKLDQEMEQLNHHtAARTQMEMLNKDKADKdEQIR 654
Cdd:pfam05483 151 NatRHLCNLLKETcaRSAEKTKKYEYEREET---RQVYMDLNNNIEKMILAFEELRVQ-AENARLEMHFKLKEDH-EKIQ 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 655 KIKYRHSDELTSllgyfpNKKQLEDWLHSKSKEINQTRDrlakLNKELASAEQNKNHINIELKRKEEQLSSYEDKlfdvc 734
Cdd:pfam05483 226 HLEEEYKKEIND------KEKQVSLLLIQITEKENKMKD----LTFLLEESRDKANQLEEKTKLQDENLKELIEK----- 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 735 gSQDFESDLDRLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRGFQTEA-----------ELQEVISDLQ 803
Cdd:pfam05483 291 -KDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSfvvtefeattcSLEELLRTEQ 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 804 SKLRLAPDKLKSTESELKKKEKRRDEMLGLVPMRQsiIDLKE-KEIPELRNKLQNVNRDIQRLKNDIE--EQET--LLGA 878
Cdd:pfam05483 370 QRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKE--VELEElKKILAEDEKLLDEKKQFEKIAEELKgkEQELifLLQA 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 879 IIPEEESAKVCLTDVTIMErlQMELKDVER-KIAQQAAKLQGLDLDRSVQQVNQEkqekqhkldtvsskielNRKLIQDQ 957
Cdd:pfam05483 448 REKEIHDLEIQLTAIKTSE--EHYLKEVEDlKTELEKEKLKNIELTAHCDKLLLE-----------------NKELTQEA 508
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 958 QEQIQHLKSTANELKSEKLQISTNLQRRQQLEEQTVELSTEVQSLYREIKDAKEQLSPLETTLEKFQQEKEELVNKKNTS 1037
Cdd:pfam05483 509 SDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQ 588
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 1038 HKIAQDKINEIKEKVKNIHSYMKDIEnyiQDGKDDYKK--QKETELN----KVIAQISECEKHKEKINKEMGIMRQDIDT 1111
Cdd:pfam05483 589 MKILENKCNNLKKQIENKNKNIEELH---QENKALKKKgsAENKQLNayeiKVNKLELELASAKQKFEEIIDNYQKEIED 665
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2015236753 1112 QKIQERWLQDNLTLRK----RNEELKEVEEERKQHlkEMGQMQVLQMKNEHQkleekIDNIKRNHSLAIGRQKGYEEE 1185
Cdd:pfam05483 666 KKISEEKLLEEVEKAKaiadEAVKLQKEIDKRCQH--KIAEMVALMEKHKHQ-----YDKIIEERDSELGLYKNKEQE 736
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
271-780 |
1.25e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 69.41 E-value: 1.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 271 KALKQKFDEIFSAT-----RYIKALETLRQVRQTQGQKVKECQTELKYLKQNKEKACEIRDQITSKEAQLTSSREIVKSY 345
Cdd:COG4717 49 ERLEKEADELFKPQgrkpeLNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 346 E--NELDPLKNRLKEIEQNLSKIMRLDNEIKALESRKKQMEKDNSELEQKMEKVFQGSD----EQLNDL---YHNHQRTV 416
Cdd:COG4717 129 PlyQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSlateEELQDLaeeLEELQQRL 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 417 REKERRLVDCQRELEKLNKEsrllnqeksellVEQGRLQLQADRHQEHMQARDSLIQSLATQLELDGFELGPFSER---- 492
Cdd:COG4717 209 AELEEELEEAQEELEELEEE------------LEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLIltia 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 493 -------QIKNFHKLVRERQEKESETASQLLNDFTRKEALKQKQIDEIRDKktgLGRIIELKSEILTKKQNELKNVKYEL 565
Cdd:COG4717 277 gvlflvlGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAA---LGLPPDLSPEELLELLDRIEELQELL 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 566 QQLEgssdrilELDQELTKAERELSKAEknsnvetlkteviSLQNEKADLDRTLRKLDQEMEQLNHHTAARTQMEmlnkd 645
Cdd:COG4717 354 REAE-------ELEEELQLEELEQEIAA-------------LLAEAGVEDEEELRAALEQAEEYQELKEELEELE----- 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 646 kadkdEQIRkikyRHSDELTSLLGYFpNKKQLEDWLHSKSKEINQTRDRLAKLNKELASAEQnknhiniELKRKEEQlSS 725
Cdd:COG4717 409 -----EQLE----ELLGELEELLEAL-DEEELEEELEELEEELEELEEELEELREELAELEA-------ELEQLEED-GE 470
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 2015236753 726 YEDKlfdvcgsqdfESDLDRLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQS 780
Cdd:COG4717 471 LAEL----------LQELEELKAELRELAEEWAALKLALELLEEAREEYREERLP 515
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
588-1373 |
1.61e-11 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 69.55 E-value: 1.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 588 ELSKAEKNSNVetLKTEVISLQNEKADLDRTLRKLDQEMEQLNHhtaartqmemlNKDKADKDEQIRKIKYRHSDELTSL 667
Cdd:PRK01156 160 EINSLERNYDK--LKDVIDMLRAEISNIDYLEEKLKSSNLELEN-----------IKKQIADDEKSHSITLKEIERLSIE 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 668 LGYFPNKKqleDWLHSKSKEINQTRDRLAKLNKELASAEQNKNHI---NIELKRKEEQLSSYEDKlfDVCGSQDFESDLD 744
Cdd:PRK01156 227 YNNAMDDY---NNLKSALNELSSLEDMKNRYESEIKTAESDLSMElekNNYYKELEERHMKIIND--PVYKNRNYINDYF 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 745 RLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRGFQTEaELQEVISDLQSKLRLAPDKLKSTESELKKKE 824
Cdd:PRK01156 302 KYKNDIENKKQILSNIDAEINKYHAIIKKLSVLQKDYNDYIKKKSRYD-DLNNQILELEGYEMDYNSYLKSIESLKKKIE 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 825 KRRDEMLGLVPMRQSIIDLKEKEIPELRNKLQNVNRDIQRLKNDIEEQETLLGAIIPEEESAKvcltdvtimerlqmelK 904
Cdd:PRK01156 381 EYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELS----------------R 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 905 DVERKIAQQAAKLQGLDL-DRSVQQVNQEKQEKQHKLDTVSSKIELNRKLIQDQQEQIQHLKSTANELKSEKLQISTNL- 982
Cdd:PRK01156 445 NMEMLNGQSVCPVCGTTLgEEKSNHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKi 524
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 983 -QRRQQLEEQTVELStEVQSLYREIKDAKEQLSPLEttLEKFQQEKEELVNKKNTSHKIAQDKI----NEIKEKVKNIHS 1057
Cdd:PRK01156 525 eSARADLEDIKIKIN-ELKDKHDKYEEIKNRYKSLK--LEDLDSKRTSWLNALAVISLIDIETNrsrsNEIKKQLNDLES 601
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 1058 YMKDIENYIQDGK---DDYKKQKETELNKVIAQISECEKHKEKINKemgiMRQDIDTQKIQerwlqdnltlrkrneelKE 1134
Cdd:PRK01156 602 RLQEIEIGFPDDKsyiDKSIREIENEANNLNNKYNEIQENKILIEK----LRGKIDNYKKQ-----------------IA 660
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 1135 VEEERKQHLKEMgQMQVLQMKNEHQKLEEKIDNIKRNHslaigrqkgYEEEIIHFKKELREPQFRDAEEKYREMMIIMRT 1214
Cdd:PRK01156 661 EIDSIIPDLKEI-TSRINDIEDNLKKSRKALDDAKANR---------ARLESTIEILRTRINELSDRINDINETLESMKK 730
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 1215 TELVNKDLDIYYKTLDQAIMKfhSMKMEEINKIIRDLWRSTYRGQDIEYIEIRSDADENVSAsdkrrnynYRVVMLKGDT 1294
Cdd:PRK01156 731 IKKAIGDLKRLREAFDKSGVP--AMIRKSASQAMTSLTRKYLFEFNLDFDDIDVDQDFNITV--------SRGGMVEGID 800
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2015236753 1295 ALdmrgrcSAGQKVLASLIIRLALAETFCLNCGILALDEPTTNLDRENIESLAHALVEIIKSRSQQRnfQLLVITHDED 1373
Cdd:PRK01156 801 SL------SGGEKTAVAFALRVAVAQFLNNDKSLLIMDEPTAFLDEDRRTNLKDIIEYSLKDSSDIP--QVIMISHHRE 871
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
271-629 |
2.35e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 68.93 E-value: 2.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 271 KALKQKFDEIfsatryIKALETLRQVRQTQGQKVKECQTELKYLKQNKEKACEIRDQItskEAQLTSSREIVKSYENELD 350
Cdd:TIGR02168 701 AELRKELEEL------EEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQL---SKELTELEAEIEELEERLE 771
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 351 PLKNRLKEIEQnlsKIMRLDNEIKALESRKKQMEKDNSELEQKMEkvfqgsdeQLNDLYHNHQRTVREKERRLVDCQREL 430
Cdd:TIGR02168 772 EAEEELAEAEA---EIEELEAQIEQLKEELKALREALDELRAELT--------LLNEEAANLRERLESLERRIAATERRL 840
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 431 EKLNKESRLLNQEKSELLVEQGRLQLQADRHQEHMQARDSLIQSLATQLELDGFELGPFSERQIKNFHKLVRERQEKESe 510
Cdd:TIGR02168 841 EDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEE- 919
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 511 tASQLLNDF-TRKEALKQkQIDEIRDKKTGLGRI----IELKSEILTKKQNELKNvkyELQQLEGSSDRILELDQEltkA 585
Cdd:TIGR02168 920 -LREKLAQLeLRLEGLEV-RIDNLQERLSEEYSLtleeAEALENKIEDDEEEARR---RLKRLENKIKELGPVNLA---A 991
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 2015236753 586 ERELSkaEKNSNVETLKTEVISLQNEKADLDRTLRKLDQEMEQL 629
Cdd:TIGR02168 992 IEEYE--ELKERYDFLTAQKEDLTEAKETLEEAIEEIDREARER 1033
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
427-1033 |
2.58e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 68.81 E-value: 2.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 427 QRELEKLNKESRLLnqEKSELLVEQGRLQLQADRHQEHMQARDSLIQSLATQLELdgfelgpfserqiknfHKLVRERQE 506
Cdd:COG1196 219 KEELKELEAELLLL--KLRELEAELEELEAELEELEAELEELEAELAELEAELEE----------------LRLELEELE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 507 KESETASQLLNDFTRKEALKQKQIDEIRDKKTGLGRIIELKSEILTKKQNELKNVKYELQQLEgssDRILELDQELTKAE 586
Cdd:COG1196 281 LELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELE---EELEEAEEELEEAE 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 587 RELSKAEknsnvETLKTEVISLQNEKADLDRTLRKLDQEMEQLNHHTAARTQMEMLNKDKADKDEQIRKIKYRHSDELTS 666
Cdd:COG1196 358 AELAEAE-----EALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAE 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 667 LLgyfpnkkqledwlhsksKEINQTRDRLAKLNKELASAEQNKNHINIELKRKEEQLSSYEDKLfdvcgsqdfesdlDRL 746
Cdd:COG1196 433 LE-----------------EEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAAL-------------AEL 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 747 KEEIEKSSKQRAMLAGATAVYSQFI-----TQLTDENQSCCPVCQRGFQTEAELQEVISD-----LQSKLRLAPDKLKST 816
Cdd:COG1196 483 LEELAEAAARLLLLLEAEADYEGFLegvkaALLLAGLRGLAGAVAVLIGVEAAYEAALEAalaaaLQNIVVEDDEVAAAA 562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 817 ESELKKKEKRRDEMLGLVPMRQSiidlKEKEIPELRNKLQNVNRDIQRLKNDIEEQETLLGAIIPEEESAkvclTDVTIM 896
Cdd:COG1196 563 IEYLKAAKAGRATFLPLDKIRAR----AALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLV----AARLEA 634
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 897 ERLQMELKDVERKIAQQAAKLQGLDLDRSVQQVNQEKQE----KQHKLDTVSSKIELNRKLIQDQQEQIQHLKSTANELK 972
Cdd:COG1196 635 ALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAAlleaEAELEELAERLAEEELELEEALLAEEEEERELAEAEE 714
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2015236753 973 SEKLQISTNLQRRQQLEEQTVELSTEVQSLYREIKDAKEQLSPLETTLEKFQQEKEELVNK 1033
Cdd:COG1196 715 ERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLERE 775
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
107-186 |
5.54e-11 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 62.76 E-value: 5.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 107 KMSIQGVRSFGIEdkdkQIITFFSP-LTILVGPNGAGKTTIIECLKYICTGDFPPGTKGNTFVHDPKVAQETDVRAQIRL 185
Cdd:cd03227 1 KIVLGRFPSYFVP----NDVTFGEGsLTIITGPNGSGKSTILDAIGLALGGAQSATRRRSGVKAGCIVAAVSAELIFTRL 76
|
.
gi 2015236753 186 Q 186
Cdd:cd03227 77 Q 77
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
527-1054 |
6.60e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 67.10 E-value: 6.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 527 QKQIDEIRDKKTGLGRIIELKSEILTKKQNELKNVKYELQQ----LEGSSDRILELDQELTKAERELSKAEKNSNVETLK 602
Cdd:COG4717 52 EKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAElqeeLEELEEELEELEAELEELREELEKLEKLLQLLPLY 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 603 TEVISLQNEKADLDRTLRKLDQEMEQLNHhtaARTQMEMLNKDKADKDEQIRKIkyrhsdeltsllgyfpnkkqLEDWLH 682
Cdd:COG4717 132 QELEALEAELAELPERLEELEERLEELRE---LEEELEELEAELAELQEELEEL--------------------LEQLSL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 683 SKSKEINQTRDRLAKLNKELASAEQNKNHINIELKRKEEQLSSYEDKLFDvcgsqdfESDLDRLKEEiekssKQRAMLAG 762
Cdd:COG4717 189 ATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEA-------AALEERLKEA-----RLLLLIAA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 763 ATAVYSQFITQLTDENQSCCPVcqrgFQTEAELQEVISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLglvpmrQSIID 842
Cdd:COG4717 257 ALLALLGLGGSLLSLILTIAGV----LFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEEL------EELLA 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 843 LKEKEIPELRNKLQNVNRDIQRLKNDIEEQETLlgaiipeeesakvcltdvtimeRLQMELKDVERKIAQQAAKLQGLDL 922
Cdd:COG4717 327 ALGLPPDLSPEELLELLDRIEELQELLREAEEL----------------------EEELQLEELEQEIAALLAEAGVEDE 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 923 D--RSVQQVNQEKQEKQHKLDTVSSKIELNRKLIQDQQEQIqhlksTANELKseklqistnlQRRQQLEEQTVELSTEVQ 1000
Cdd:COG4717 385 EelRAALEQAEEYQELKEELEELEEQLEELLGELEELLEAL-----DEEELE----------EELEELEEELEELEEELE 449
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2015236753 1001 SLYREIKDAKEQLSPLET--TLEKFQQEKEELVNKKNT------SHKIAQDKINEIKEKVKN 1054
Cdd:COG4717 450 ELREELAELEAELEQLEEdgELAELLQELEELKAELRElaeewaALKLALELLEEAREEYRE 511
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
108-866 |
7.41e-11 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 67.23 E-value: 7.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 108 MSIQGVRSFGIEDKDKQIITFFSPLTILVGPNGAGKTTIIECLKYICTGDfppgtKGNTFVHDpkVAQETDVRAQIRLQF 187
Cdd:PRK01156 1 MIIKRIRLKNFLSHDDSEIEFDTGINIITGKNGAGKSSIVDAIRFALFTD-----KRTEKIED--MIKKGKNNLEVELEF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 188 RdVNGELVAVQRSMLCTQKSKKTEFKTLegvitrtKHGEKVSLSSKCAEIDREMiSSLGVSKSVLNNVIFCHQEDSNWPL 267
Cdd:PRK01156 74 R-IGGHVYQIRRSIERRGKGSRREAYIK-------KDGSIIAEGFDDTTKYIEK-NILGISKDVFLNSIFVGQGEMDSLI 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 268 SEGKALKQK-FDEIFSATRYIKALETLRQVRQTQGQKVKECQTELKYLKQNKEKACEIRDQITSKEAQLT-------SSR 339
Cdd:PRK01156 145 SGDPAQRKKiLDEILEINSLERNYDKLKDVIDMLRAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHSitlkeieRLS 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 340 EIVKSYENELDPLKNRLKEIEQNLSKIMRLDNEIKALESRKKQMEKDNSELeqkmekvfQGSDEQLNDLYHNHQRTVREK 419
Cdd:PRK01156 225 IEYNNAMDDYNNLKSALNELSSLEDMKNRYESEIKTAESDLSMELEKNNYY--------KELEERHMKIINDPVYKNRNY 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 420 ERRLVDCQRELEKLNKESRLLNQEKSELLVEQGRLQ-LQADRHQ-EHMQARDSLIQSLatQLELDGFELGPFSE-RQIKN 496
Cdd:PRK01156 297 INDYFKYKNDIENKKQILSNIDAEINKYHAIIKKLSvLQKDYNDyIKKKSRYDDLNNQ--ILELEGYEMDYNSYlKSIES 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 497 FHKLVRERQEKESETASQLLNDFTRKEALKQ---KQIDEIRDKKTGL-GRIIELKSEILTKKQNELKnVKYELQQLEGSS 572
Cdd:PRK01156 375 LKKKIEEYSKNIERMSAFISEILKIQEIDPDaikKELNEINVKLQDIsSKVSSLNQRIRALRENLDE-LSRNMEMLNGQS 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 573 DRIL---ELDQELTKAERELSKAEKN---SNVETLKTEVISLQNEKADLDRTLRKLdqEMEQLNHHTAARTQMEMLNKDK 646
Cdd:PRK01156 454 VCPVcgtTLGEEKSNHIINHYNEKKSrleEKIREIEIEVKDIDEKIVDLKKRKEYL--ESEEINKSINEYNKIESARADL 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 647 ADKDEQIRKIKYRHS------DELTSL-LGYFPNKKqlEDWLHSKSK----EINQTRDRLAKLNKELASAEQNKNHINIE 715
Cdd:PRK01156 532 EDIKIKINELKDKHDkyeeikNRYKSLkLEDLDSKR--TSWLNALAVisliDIETNRSRSNEIKKQLNDLESRLQEIEIG 609
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 716 -----------LKRKEEQLSSYEDKLFDVcgsQDFESDLDRLKEEIEKSSKQramlagatavysqfitqltdenqsccpv 784
Cdd:PRK01156 610 fpddksyidksIREIENEANNLNNKYNEI---QENKILIEKLRGKIDNYKKQ---------------------------- 658
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 785 cqrgfqtEAELQEVISDLQSklrlAPDKLKSTESELKKKEKRRDEMLGLVPMRQSIIDLKEKEIPELRNKLQNVNRDIQR 864
Cdd:PRK01156 659 -------IAEIDSIIPDLKE----ITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRINDINETLES 727
|
..
gi 2015236753 865 LK 866
Cdd:PRK01156 728 MK 729
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
547-1376 |
1.27e-10 |
|
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: 66.53 E-value: 1.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 547 KSEILTKKQNELKNVKYELQQLEGSSDRILELDQELTKAERELSKAEKNSNVETLKTEVISLQNEKADLDRTLRKLDQEM 626
Cdd:TIGR00618 220 RKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHI 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 627 EQLNHHTAARTQMEMLNKDKADKDEQIRKIKYRHSDELTSLlgyfPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASAE 706
Cdd:TIGR00618 300 KAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSI----EEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQH 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 707 QNKNHINIE------LKRKEEQLSSYEDKLFDVCGSQDFES--------DLDRLKEEIEKSSKQRAMLAgatavysQFIT 772
Cdd:TIGR00618 376 TLTQHIHTLqqqkttLTQKLQSLCKELDILQREQATIDTRTsafrdlqgQLAHAKKQQELQQRYAELCA-------AAIT 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 773 QLTDENQSCCPVCQRGFQTEAELQEVISDLQS---------------KLRLA--PDKLKSTESELKKKEKRRDEMLGLVP 835
Cdd:TIGR00618 449 CTAQCEKLEKIHLQESAQSLKEREQQLQTKEQihlqetrkkavvlarLLELQeePCPLCGSCIHPNPARQDIDNPGPLTR 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 836 MRQSIID---LKEKEIPELRNKLQNVNRDIQRLKNDIEEqetllgaIIPEEESAKVCLTDVT-IMERLQMELKDVERKIA 911
Cdd:TIGR00618 529 RMQRGEQtyaQLETSEEDVYHQLTSERKQRASLKEQMQE-------IQQSFSILTQCDNRSKeDIPNLQNITVRLQDLTE 601
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 912 QQAAKLQGLDLDRSVQQVnqEKQEKQHKLDtvssKIELNRKLIQDQQEQIQHLKSTANELKSEKLQISTNLQRRQQLE-- 989
Cdd:TIGR00618 602 KLSEAEDMLACEQHALLR--KLQPEQDLQD----VRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKEll 675
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 990 EQTVELSTEVQSLYREIKDAKEQLS-------PLETTLEKFQQEKEELvnkKNTSHKIAQDKINEIKEKVKNIHSYMKDI 1062
Cdd:TIGR00618 676 ASRQLALQKMQSEKEQLTYWKEMLAqcqtllrELETHIEEYDREFNEI---ENASSSLGSDLAAREDALNQSLKELMHQA 752
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 1063 ENYIQDGKDDY--KKQKETELNKVIAQISECEKHKEKINKEMGIMRQDIDTQKIQERwlqdnltlrkrneelkeveeerk 1140
Cdd:TIGR00618 753 RTVLKARTEAHfnNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIG----------------------- 809
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 1141 QHLKEMGQMQVLQMKNEHQKLEEKIDNIKRNHSL--AIGRQKGYEEEIIHFKKELREPQFRDAEEK-----YREMMIIMR 1213
Cdd:TIGR00618 810 QEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATlgEITHQLLKYEECSKQLAQLTQEQAKIIQLSdklngINQIKIQFD 889
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 1214 TTELVNKDLDI-YYKTLDQAIMKFHSMKMEEINKIIRdlwRSTYRGQDIEYIEIRSDADENVSAsdkrrnynyrvvmlkg 1292
Cdd:TIGR00618 890 GDALIKFLHEItLYANVRLANQSEGRFHGRYADSHVN---ARKYQGLALLVADAYTGSVRPSAT---------------- 950
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 1293 dtaldmrgrCSAGQKVLASLIIRLALAETFCLNCGI----LALDEPTTNLDRENIESLAHALVEIIKSrsqqrNFQLLVI 1368
Cdd:TIGR00618 951 ---------LSGGETFLASLSLALALADLLSTSGGTvldsLFIDEGFGSLDEDSLDRAIGILDAIREG-----SKMIGII 1016
|
....*...
gi 2015236753 1369 THDEDFVE 1376
Cdd:TIGR00618 1017 SHVPEFRE 1024
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
283-728 |
1.66e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 66.09 E-value: 1.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 283 ATRYIKALETLRQVRQTQGQKVKECQtELKYLK------QNKEKACEIRDQITSKEAQLTSSREIVKSYENELDPLKNRL 356
Cdd:COG4913 247 AREQIELLEPIRELAERYAAARERLA-ELEYLRaalrlwFAQRRLELLEAELEELRAELARLEAELERLEARLDALREEL 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 357 KEIEQNLS-----KIMRLDNEIKALESRKKQMEKDNSELEQKMEKV---FQGSDEQLNDLYHNHQRTVREKERRLVDCQR 428
Cdd:COG4913 326 DELEAQIRgnggdRLEQLEREIERLERELEERERRRARLEALLAALglpLPASAEEFAALRAEAAALLEALEEELEALEE 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 429 ELEKLNKESRLLNQEKSELLVEQGRLQLQADR-HQEHMQARDSLIQSL---ATQL----EL-----------DGFE--LG 487
Cdd:COG4913 406 ALAEAEAALRDLRRELRELEAEIASLERRKSNiPARLLALRDALAEALgldEAELpfvgELievrpeeerwrGAIErvLG 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 488 PFSerqiknFHKLVRERQEKEsetasqlLNDFTRKEALKQK-QIDEIRDKKTGLGRIIELKSEILTK---KQNELKN-VK 562
Cdd:COG4913 486 GFA------LTLLVPPEHYAA-------ALRWVNRLHLRGRlVYERVRTGLPDPERPRLDPDSLAGKldfKPHPFRAwLE 552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 563 YELQQlegSSDRIL-ELDQELTKAERELSKA----------EKN-------------SN---VETLKTEVISLQNEKADL 615
Cdd:COG4913 553 AELGR---RFDYVCvDSPEELRRHPRAITRAgqvkgngtrhEKDdrrrirsryvlgfDNrakLAALEAELAELEEELAEA 629
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 616 DRTLRKLDQEMEQLNHHTAARTQMEMLNKDKADKDEQIRKIkYRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRL 695
Cdd:COG4913 630 EERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREI-AELEAELERLDASSDDLAALEEQLEELEAELEELEEEL 708
|
490 500 510
....*....|....*....|....*....|...
gi 2015236753 696 AKLNKELASAEQNKNHINIELKRKEEQLSSYED 728
Cdd:COG4913 709 DELKGEIGRLEKELEQAEEELDELQDRLEAAED 741
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
505-830 |
3.12e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 65.46 E-value: 3.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 505 QEKESETASQLLNDFTRKEALKQKQIDEIRDKKTGLGRIIELKSEILTKKQNELKNVKYELQQLEGS-----------SD 573
Cdd:TIGR02168 675 RRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEveqleeriaqlSK 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 574 RILELDQELTKAERELSKAEKN-----SNVETLKTEVISLQNEKADLDRTLRKLDQEMEQLN-HHTAARTQMEMLNKDKA 647
Cdd:TIGR02168 755 ELTELEAEIEELEERLEEAEEElaeaeAEIEELEAQIEQLKEELKALREALDELRAELTLLNeEAANLRERLESLERRIA 834
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 648 DKDEQIRKIKYRhsdeltsllgyfpnKKQLEDWLHSKSKEINQTRDRLAKLNKELASAEQNKNHINIELKRKEEQLSSYE 727
Cdd:TIGR02168 835 ATERRLEDLEEQ--------------IEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELS 900
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 728 DKLFDVCGS-QDFESDLDRLKEEIEKSskqRAMLAGATAVYSQFITQLTDE---NQSCCPVCQRGFQTE-AELQEVISDL 802
Cdd:TIGR02168 901 EELRELESKrSELRRELEELREKLAQL---ELRLEGLEVRIDNLQERLSEEyslTLEEAEALENKIEDDeEEARRRLKRL 977
|
330 340
....*....|....*....|....*....
gi 2015236753 803 QSKL-RLAPDKLKSTEsELKKKEKRRDEM 830
Cdd:TIGR02168 978 ENKIkELGPVNLAAIE-EYEELKERYDFL 1005
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
820-1206 |
3.89e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 65.08 E-value: 3.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 820 LKKKEKRRDEMLGLVPMRQSIIDLkEKEIPELRNKLQNVNR------DIQRLKNDIEEQETLLGAIIPEEESAKvcltdv 893
Cdd:TIGR02168 168 SKYKERRKETERKLERTRENLDRL-EDILNELERQLKSLERqaekaeRYKELKAELRELELALLVLRLEELREE------ 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 894 tiMERLQMELKDVERKIAQQAAKLQGLD-----LDRSVQQVNQEKQEKQHKLDTVSSKIElnrkliqDQQEQIQHLKsta 968
Cdd:TIGR02168 241 --LEELQEELKEAEEELEELTAELQELEekleeLRLEVSELEEEIEELQKELYALANEIS-------RLEQQKQILR--- 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 969 nelkseklqistnlQRRQQLEEQTVELSTEVQSLYREIKDAKEQLSPLETTLEKFQQEKEELvnkkntshkiaQDKINEI 1048
Cdd:TIGR02168 309 --------------ERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESL-----------EAELEEL 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 1049 KEKVKNIHSYMKDIENYIQDGKDDYkKQKETELNKVIAQISECEKHKEKINKEmgimrqdidtqkiQERWLQDNLTLRKR 1128
Cdd:TIGR02168 364 EAELEELESRLEELEEQLETLRSKV-AQLELQIASLNNEIERLEARLERLEDR-------------RERLQQEIEELLKK 429
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2015236753 1129 NEELKEVEEERKQHLKEMGQMQVLQMKNEHQKLEEKIDNIKRNHSLAIgRQKGYEEEIIHFKKELREPQFRDAEEKYR 1206
Cdd:TIGR02168 430 LEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQAL-DAAERELAQLQARLDSLERLQENLEGFSE 506
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1303-1384 |
5.38e-10 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 59.57 E-value: 5.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 1303 SAGQKVlasliiRLALAETFCLNCGILALDEPTTNLDRENIESLAHALVEIiksrsQQRNFQLLVITHDEDFVELLGRSE 1382
Cdd:cd00267 82 SGGQRQ------RVALARALLLNPDLLLLDEPTSGLDPASRERLLELLREL-----AEEGRTVIIVTHDPELAELAADRV 150
|
..
gi 2015236753 1383 YV 1384
Cdd:cd00267 151 IV 152
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
1303-1376 |
7.00e-10 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 59.00 E-value: 7.00e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2015236753 1303 SAGQKVlasliiRLALAETFCLNCGILALDEPTTNLDRENIESLAHALveiiksrsqqRNFQ--LLVITHDEDFVE 1376
Cdd:cd03221 72 SGGEKM------RLALAKLLLENPNLLLLDEPTNHLDLESIEALEEAL----------KEYPgtVILVSHDRYFLD 131
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
809-1037 |
1.32e-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: 62.09 E-value: 1.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 809 APDKLKSTESELKKKEKRRDEMLGLVPMRQSIIDLKEKEIPELRNKLQNVNRDIQRLKNDIEEQETLLGAIIPEEEsakv 888
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA---- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 889 cltdvtimeRLQMELKDVERKIAQQAAKLQGL----------------DLDRSVQQVNQEKQEKQHKLDTVSSKIELNRK 952
Cdd:COG4942 94 ---------ELRAELEAQKEELAELLRALYRLgrqpplalllspedflDAVRRLQYLKYLAPARREQAEELRADLAELAA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 953 LIQDQQEQIQHLKSTANELKSEKLQISTNLQRRQQLEEQtveLSTEVQSLYREIKDAKEQLSPLETTLEKFQQEKEELVN 1032
Cdd:COG4942 165 LRAELEAERAELEALLAELEEERAALEALKAERQKLLAR---LEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
....*
gi 2015236753 1033 KKNTS 1037
Cdd:COG4942 242 RTPAA 246
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
354-728 |
1.41e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 63.15 E-value: 1.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 354 NRLKEIEQNLSKIMRLDNEIKALESRKKQMEKDNSELEQKMEKVFQGSDEqLNDLYHNHQRTVREKERRLVDCQRELEKL 433
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEE-LSRQISALRKDLARLEAEVEQLEERIAQL 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 434 NKESRLLNQEKSELLVEQGRLQLQADRHQEHMQARDSLIQSLATQLELdgfelgpfSERQIKNFHKLVRErqekesetas 513
Cdd:TIGR02168 753 SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKA--------LREALDELRAELTL---------- 814
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 514 qllndfTRKEALKQKQideirdKKTGLGRIIELKSEILTKKQNELKNVKYELQQLEGSsdrILELDQELTKAEREL---- 589
Cdd:TIGR02168 815 ------LNEEAANLRE------RLESLERRIAATERRLEDLEEQIEELSEDIESLAAE---IEELEELIEELESELeall 879
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 590 -SKAEKNSNVETLKTEVISLQNEKADLDRTLRKLDQEMEQLNHHtaaRTQMEM-LNKDKADKDEQIRKIKYRHSDELTSL 667
Cdd:TIGR02168 880 nERASLEEALALLRSELEELSEELRELESKRSELRRELEELREK---LAQLELrLEGLEVRIDNLQERLSEEYSLTLEEA 956
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2015236753 668 LGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNkeLASAEQNKNhiniELKRKEEQLSSYED 728
Cdd:TIGR02168 957 EALENKIEDDEEEARRRLKRLENKIKELGPVN--LAAIEEYEE----LKERYDFLTAQKED 1011
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
674-1373 |
2.12e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 62.39 E-value: 2.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 674 KKQLEDWLHSKSkeinQTRDRLAKLNKELASAEQNKNHINIELKRKEEQLSSYEDKLfdvcgsqdfeSDLDRLKEEIEKS 753
Cdd:PRK03918 178 IERLEKFIKRTE----NIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEV----------KELEELKEEIEEL 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 754 SKQRAMLAGATAVYSQFItqltdenqsccpvcqrgfqteAELQEVISDLQSKLRlapdKLKSTESELKKKEKRRDEMLGL 833
Cdd:PRK03918 244 EKELESLEGSKRKLEEKI---------------------RELEERIEELKKEIE----ELEEKVKELKELKEKAEEYIKL 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 834 VPMRQSIIDLK---EKEIPELRNKLQNVNRDIQRLKNDIEEQETLLGAIIPEEESAKVCLTDVTIMERLqMELKDVERKI 910
Cdd:PRK03918 299 SEFYEEYLDELreiEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEA-KAKKEELERL 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 911 AQQAAKLQGLDLDRSVQQVNQEKQEKQHKLDTVSSKIELNRKLIQDQQEQIQHLKSTANELKSEKLQIsTNLQRRQQLEE 990
Cdd:PRK03918 378 KKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGREL-TEEHRKELLEE 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 991 QTVELStEVQSLYREIKDAKEQLSPLETTLEKFQQEKEELVNKKNTShkiaqDKINEIKEKVKNIhsymkDIENYIQDGK 1070
Cdd:PRK03918 457 YTAELK-RIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELA-----EQLKELEEKLKKY-----NLEELEKKAE 525
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 1071 DdYKKQKEtELNKVIAQISECEKHKEKIN---KEMGIMRQDIDtqKIQERWLQDNLTLRKRNEELKEVEEERKQHLKEM- 1146
Cdd:PRK03918 526 E-YEKLKE-KLIKLKGEIKSLKKELEKLEelkKKLAELEKKLD--ELEEELAELLKELEELGFESVEELEERLKELEPFy 601
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 1147 --------GQMQVLQMKNEHQKLEEKIDNIKRNHSLAIGRQKGYEEEIIHFKKELREPQFRDAEEKYREM-MIIMRTTEL 1217
Cdd:PRK03918 602 neylelkdAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLELsRELAGLRAE 681
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 1218 VN-------------KDLDIYYKTLDQAIMKFHSM-----KMEEINKIIRDLWRSTYRGQDIEYIEIRSD-----ADENV 1274
Cdd:PRK03918 682 LEelekrreeikktlEKLKEELEEREKAKKELEKLekaleRVEELREKVKKYKALLKERALSKVGEIASEifeelTEGKY 761
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 1275 SASDKRRNYNYRVVMLKGDTALDMRGRCSAGQKVLASLIIRLALAETFCLNCGILALDEPTTNLDRENieslAHALVEII 1354
Cdd:PRK03918 762 SGVRVKAEENKVKLFVVYQGKERPLTFLSGGERIALGLAFRLALSLYLAGNIPLLILDEPTPFLDEER----RRKLVDIM 837
|
730
....*....|....*....
gi 2015236753 1355 kSRSQQRNFQLLVITHDED 1373
Cdd:PRK03918 838 -ERYLRKIPQVIIVSHDEE 855
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
675-1110 |
2.92e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 61.98 E-value: 2.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 675 KQLEDWLHSKSKEINQTRDRLAKLNKELASAEQNKNHInielkrkEEQLSSYEDKLFDVcgsQDFESDLDRLKEEIEKSS 754
Cdd:PRK02224 202 KDLHERLNGLESELAELDEEIERYEEQREQARETRDEA-------DEVLEEHEERREEL---ETLEAEIEDLRETIAETE 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 755 KQRAMLAGATAVYSQFITQLTDENQSC----------------------------------CPVCQRGFQTEAE------ 794
Cdd:PRK02224 272 REREELAEEVRDLRERLEELEEERDDLlaeaglddadaeavearreeledrdeelrdrleeCRVAAQAHNEEAEslreda 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 795 --LQEVISDLQSKLRLAPDKLKSTESELKKKEKRRDEM----------LGLVPMR----QSIIDLKEKEIPELRNKLQNV 858
Cdd:PRK02224 352 ddLEERAEELREEAAELESELEEAREAVEDRREEIEELeeeieelrerFGDAPVDlgnaEDFLEELREERDELREREAEL 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 859 NRDIQRLKNDIEEQETLLGA-IIPE-----EESAKVCLT--DVTIMERLQMELKDVERKIAQQAAKlqgldLDRSVQQVN 930
Cdd:PRK02224 432 EATLRTARERVEEAEALLEAgKCPEcgqpvEGSPHVETIeeDRERVEELEAELEDLEEEVEEVEER-----LERAEDLVE 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 931 QEKQ--EKQHKLDTVSSKIELNRKLIQDQQEQIQHLKSTANELKSEKLQISTNLQRRQQLEEQTVELSTEVQSLYREIKD 1008
Cdd:PRK02224 507 AEDRieRLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKE 586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 1009 AKEQLSPLETTLEKFQ---------QEKEELVNKKNTSHKiaqDKINEIKEKVKNIHSYMKdiENYIQDGKDDyKKQKET 1079
Cdd:PRK02224 587 RIESLERIRTLLAAIAdaedeierlREKREALAELNDERR---ERLAEKRERKRELEAEFD--EARIEEARED-KERAEE 660
|
490 500 510
....*....|....*....|....*....|.
gi 2015236753 1080 ELNKVIAQISECEKHKEKINKEMGIMRQDID 1110
Cdd:PRK02224 661 YLEQVEEKLDELREERDDLQAEIGAVENELE 691
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
899-1185 |
3.59e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 61.88 E-value: 3.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 899 LQMELKdvERKIAQQAAKLQGLD-----LDRSVQQVNQEKQEKQHKLDTVSSKIELNRKLIQDQQEQIQHLKSTANELKS 973
Cdd:COG1196 218 LKEELK--ELEAELLLLKLRELEaeleeLEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 974 EKLQISTNL----QRRQQLEEQTVELSTEVQSLYREIKDAKEQLSPLETTLEKFQQEKEELVNKKNTSHKIAQDKINEIK 1049
Cdd:COG1196 296 ELARLEQDIarleERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 1050 EKVKNIHSYMKDIENYIQDgkddyKKQKETELNKVIAQISECEKHKEKINKEMGIMRQDIDTQKIQERWLQDNLTLRKRN 1129
Cdd:COG1196 376 EAEEELEELAEELLEALRA-----AAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEE 450
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 2015236753 1130 EELKEVEEERKQHLKEMGQMQVLQMKNEHQKLEEKIDNIKRNHSLAIGRQKGYEEE 1185
Cdd:COG1196 451 EAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGF 506
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
104-199 |
5.01e-09 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 58.10 E-value: 5.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 104 RIEKMSIQGVRSFgiedKDKQIITFFSPLTILVGPNGAGKTTIIECLKYICTGDFPPGTK-GNTFVHDPkvaqetDVRAQ 182
Cdd:COG0419 1 KLLRLRLENFRSY----RDTETIDFDDGLNLIVGPNGAGKSTILEAIRYALYGKARSRSKlRSDLINVG------SEEAS 70
|
90
....*....|....*..
gi 2015236753 183 IRLQFrDVNGELVAVQR 199
Cdd:COG0419 71 VELEF-EHGGKRYRIER 86
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
492-1022 |
5.25e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 61.47 E-value: 5.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 492 RQIKNFHKLVRERQEKEsETASQLLNDFTRKEALKQkQIDEIRDKKTGL-----GRIIELKSEILTKKQNELKNVKYELQ 566
Cdd:COG4913 235 DDLERAHEALEDAREQI-ELLEPIRELAERYAAARE-RLAELEYLRAALrlwfaQRRLELLEAELEELRAELARLEAELE 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 567 QLEgssDRILELDQELTKAERELSKAeKNSNVETLKTEVISLQNEKADLDRTLRKLDQEMEQLNHHTAArtqmemlnkDK 646
Cdd:COG4913 313 RLE---ARLDALREELDELEAQIRGN-GGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPA---------SA 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 647 ADKDEQIRKIKyRHSDELTSLLgyfpnkKQLEDWLHSKSKEINQTRDRLAKLNKELASAEQNKNHI--NIELKRKE--EQ 722
Cdd:COG4913 380 EEFAALRAEAA-ALLEALEEEL------EALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIpaRLLALRDAlaEA 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 723 LSSYEDKLFDVCgsqdfesdldrlkEEIEKSSKQRA-------MLAGA-------TAVYSQFITQltdenqsccpVCQRG 788
Cdd:COG4913 453 LGLDEAELPFVG-------------ELIEVRPEEERwrgaierVLGGFaltllvpPEHYAAALRW----------VNRLH 509
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 789 FQTEAELQEVISDLQSKLRLAPD------KLKS-----------------------TESELK------------------ 821
Cdd:COG4913 510 LRGRLVYERVRTGLPDPERPRLDpdslagKLDFkphpfrawleaelgrrfdyvcvdSPEELRrhpraitragqvkgngtr 589
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 822 -----KKEKRRDEMLGLVPMRQsiIDLKEKEIPELRNKLQNVNRDIQRLKNDIEEQETLLGAiipeeesakvcLTDVTIM 896
Cdd:COG4913 590 hekddRRRIRSRYVLGFDNRAK--LAALEAELAELEEELAEAEERLEALEAELDALQERREA-----------LQRLAEY 656
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 897 ERLQMELKDVERKIAQQAAKLQGLD--------LDRSVQQVNQEKQEKQHKLDTVSSKIELNRKLIQDQQEQIQHLKSTA 968
Cdd:COG4913 657 SWDEIDVASAEREIAELEAELERLDassddlaaLEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRL 736
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*
gi 2015236753 969 NEL-KSEKLQISTNLQRRQQLEEQTVELSTEVQSLYREIKDAKEQLSPLETTLEK 1022
Cdd:COG4913 737 EAAeDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELER 791
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
1302-1374 |
6.41e-09 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 57.65 E-value: 6.41e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2015236753 1302 CSAGQKVlasliiRLALAETFCLNCGILALDEPTTNLDRENIESLAhalvEIIKSRSQQRNfQLLVITHDEDF 1374
Cdd:cd03226 127 LSGGQKQ------RLAIAAALLSGKDLLIFDEPTSGLDYKNMERVG----ELIRELAAQGK-AVIVITHDYEF 188
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1303-1392 |
8.60e-09 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 57.48 E-value: 8.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 1303 SAGQKVlasliiRLALAETFCLNCGILALDEPTTNLDRENIEslahALVEIIKsRSQQRNFQLLVITHDEDFVEllgrsE 1382
Cdd:cd03225 136 SGGQKQ------RVAIAGVLAMDPDILLLDEPTAGLDPAGRR----ELLELLK-KLKAEGKTIIIVTHDLDLLL-----E 199
|
90
....*....|
gi 2015236753 1383 YVEKFYRIKK 1392
Cdd:cd03225 200 LADRVIVLED 209
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
790-1015 |
1.17e-08 |
|
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: 1.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 790 QTEAELQEV---ISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLVPMRQSIIDLKEKEIPELRNKLQNVNRDIQRLK 866
Cdd:COG4942 24 EAEAELEQLqqeIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 867 NDIEEQetlLGAIIPEEESAKVCL----TDVTIMERLQMELKDVERKIAQQAAKLQGlDLDRSVQQVNQEKQEKQHKLDT 942
Cdd:COG4942 104 EELAEL---LRALYRLGRQPPLALllspEDFLDAVRRLQYLKYLAPARREQAEELRA-DLAELAALRAELEAERAELEAL 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2015236753 943 VSSKIELNRKLIQDQQEQIQHLKSTANELKSEKlqistnlQRRQQLEEQTVELSTEVQSLYREIKDAKEQLSP 1015
Cdd:COG4942 180 LAELEEERAALEALKAERQKLLARLEKELAELA-------AELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
314-755 |
1.20e-08 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 60.03 E-value: 1.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 314 LKQNKEKACEIRDQITSKEAQLTSSREIVKSYENEL----DPLKNRLKEIEQNLSKIMRLDNEIKALESRKKQMEKDNSE 389
Cdd:TIGR04523 330 ISQNNKIISQLNEQISQLKKELTNSESENSEKQRELeekqNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQ 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 390 LEQKMEKVfqgsdeqlndlyhnhqrtvrEKERRLVDcqRELEKLNKESRLLNQEKSELLVEQGRLQLQADRHqehmqarD 469
Cdd:TIGR04523 410 KDEQIKKL--------------------QQEKELLE--KEIERLKETIIKNNSEIKDLTNQDSVKELIIKNL-------D 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 470 SLIQSLATQLELdgfelgpfSERQIKNFhKLVRERQEKESETASQLLNDFTR-KEALKQKQIDEIRDKKTGLGRIIELKS 548
Cdd:TIGR04523 461 NTRESLETQLKV--------LSRSINKI-KQNLEQKQKELKSKEKELKKLNEeKKELEEKVKDLTKKISSLKEKIEKLES 531
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 549 EIlTKKQNELKNVKyelqqlegssDRILELDQELTKAERELSKAEKNSNVETLKTEVISLQNEKADLDRTLRKLDQEMEQ 628
Cdd:TIGR04523 532 EK-KEKESKISDLE----------DELNKDDFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKD 600
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 629 LnhhtaaRTQMEMLNKDKADKDEQIRKIKYRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKEL-ASAEQ 707
Cdd:TIGR04523 601 L------IKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIkESKTK 674
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 2015236753 708 NKNHINIELKRKEEQLSSYEDKLFDVCGSQDFESdLDRLKEEIEKSSK 755
Cdd:TIGR04523 675 IDDIIELMKDWLKELSLHYKKYITRMIRIKDLPK-LEEKYKEIEKELK 721
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
592-1232 |
1.49e-08 |
|
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: 59.85 E-value: 1.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 592 AEKNSNVETLKTEVISLQNEKADLDRTLRKLDQEMEQ-LNHHTAARTQMEmlNKDKADKDEQIRKIKYRHSDELTSLLGY 670
Cdd:pfam12128 189 HSKEGKFRDVKSMIVAILEDDGVVPPKSRLNRQQVEHwIRDIQAIAGIMK--IRPEFTKLQQEFNTLESAELRLSHLHFG 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 671 FPN---------------KKQLEDWLHSKSKEINQTRDRLaklNKELASAEQNKNHINIELKRKEEQLSSYED-KLFDVC 734
Cdd:pfam12128 267 YKSdetliasrqeerqetSAELNQLLRTLDDQWKEKRDEL---NGELSAADAAVAKDRSELEALEDQHGAFLDaDIETAA 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 735 GSQD----FESDLDRLKEEIE-----KSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRGFQTEAELQEVISDLQSK 805
Cdd:pfam12128 344 ADQEqlpsWQSELENLEERLKaltgkHQDVTAKYNRRRSKIKEQNNRDIAGIKDKLAKIREARDRQLAVAEDDLQALESE 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 806 LRlapDKLKSTESELKKKEKRRDEMLGLVPMRQSIIDLKEKEIPELRNKLQNVNRdiqrlkndieEQETLlgaiipEEES 885
Cdd:pfam12128 424 LR---EQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPELLLQLENFDERIER----------AREEQ------EAAN 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 886 AKVcltdvtimERLQMELKDVERKIAQQAAKLQglDLDRSVQQVNQEKQEKQHKLDTVS-SKIELNRKLIQDQQEQIQHL 964
Cdd:pfam12128 485 AEV--------ERLQSELRQARKRRDQASEALR--QASRRLEERQSALDELELQLFPQAgTLLHFLRKEAPDWEQSIGKV 554
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 965 KSTA-----------------------------------------NELKSEKLQISTNLQ----RRQQLEEQTVELSTEV 999
Cdd:pfam12128 555 ISPEllhrtdldpevwdgsvggelnlygvkldlkridvpewaaseEELRERLDKAEEALQsareKQAAAEEQLVQANGEL 634
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 1000 QSLYREIKDAKEQLSPLETTLEKFQQEKEELVNKKNTSHKIAQDKINeikEKVKNIHSYMKDIENYIQDGKDDYKKQKET 1079
Cdd:pfam12128 635 EKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSAN---ERLNSLEAQLKQLDKKHQAWLEEQKEQKRE 711
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 1080 ELNKVIAQISECEkhkEKINKEMGIMRQDIDTQKIQERWLQDNLtlrkrneelkevEEERKQHLKEMG--QMQVLQMKNE 1157
Cdd:pfam12128 712 ARTEKQAYWQVVE---GALDAQLALLKAAIAARRSGAKAELKAL------------ETWYKRDLASLGvdPDVIAKLKRE 776
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2015236753 1158 HQKLEEKIDNIKRNHSlAIGRQKGYEEEIIHFKKELREPQFRDAEEKYREMMI----IMRTTELVNKDLDIYYKTLDQA 1232
Cdd:pfam12128 777 IRTLERKIERIAVRRQ-EVLRYFDWYQETWLQRRPRLATQLSNIERAISELQQqlarLIADTKLRRAKLEMERKASEKQ 854
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
289-514 |
1.19e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 55.93 E-value: 1.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 289 ALETLRQVRQTQGQKVKECQTELKYLKQNKEKACEIRDQITSKEAQLTSSREIVKSYENELDPLKNRLKEIEQNLSKI-M 367
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELrA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 368 RLDNEIKALESRKKQMEKdNSELEQKMEKVFQGSDEQLNDLYHNHQRTVREKERRLVDCQRELEKLNKESRLLNQEKSEL 447
Cdd:COG4942 98 ELEAQKEELAELLRALYR-LGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAEL 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 448 LVEQGRLQLQADRHQEHMQARDSLIQSLATQLELDGFELGPF--SERQIKNFH-KLVRERQEKESETASQ 514
Cdd:COG4942 177 EALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELqqEAEELEALIaRLEAEAAAAAERTPAA 246
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
302-875 |
1.43e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 56.59 E-value: 1.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 302 QKVKECQTELKYLKQNKEKACEIRDQITSKEAQLTSSREIVKSYENELDPLKNRLKEIEqnlSKIMRLDNEIKALESRKK 381
Cdd:PRK02224 213 SELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETE---REREELAEEVRDLRERLE 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 382 QMEKDNSELEQKMEkVFQGSDEQLNDLYHNHQRTVREKERRLVDCQRELEKLNKESRLLNQEKSELLVEQGRLQLQADRH 461
Cdd:PRK02224 290 ELEEERDDLLAEAG-LDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAEL 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 462 QEHMQARDSLIQSLATQLEldgfELgpfserqiknfhklvrerqEKESETASQLLNDFTRKEALKQKQIDEIRDKKTGL- 540
Cdd:PRK02224 369 ESELEEAREAVEDRREEIE----EL-------------------EEEIEELRERFGDAPVDLGNAEDFLEELREERDELr 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 541 GRIIELKSEIltkkqNELKNVKYELQQL--EGssdRILELDQELTKAERELSKAEKNSNVETLKTEVISLQNEKADLDRT 618
Cdd:PRK02224 426 EREAELEATL-----RTARERVEEAEALleAG---KCPECGQPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEER 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 619 LRKLDQEMEQLNHHTAARTQMEMLNKDKADKDEQIRkikyRHSDELTSLLgyfPNKKQLEDWLHSKSKEINQTRDRLAKL 698
Cdd:PRK02224 498 LERAEDLVEAEDRIERLEERREDLEELIAERRETIE----EKRERAEELR---ERAAELEAEAEEKREAAAEAEEEAEEA 570
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 699 NKELASAEQNKNhiniELKRKEEQLSSYEDKLFDVcgsQDFESDLDRLKEeieksskQRAMLAgatAVYSQFITQLTDEN 778
Cdd:PRK02224 571 REEVAELNSKLA----ELKERIESLERIRTLLAAI---ADAEDEIERLRE-------KREALA---ELNDERRERLAEKR 633
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 779 qsccpvcQRGFQTEAELQEV-ISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLVPMRQSIIdlkeKEIPELRNKLQN 857
Cdd:PRK02224 634 -------ERKRELEAEFDEArIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENEL----EELEELRERREA 702
|
570
....*....|....*...
gi 2015236753 858 VNRDIQRLKNDIEEQETL 875
Cdd:PRK02224 703 LENRVEALEALYDEAEEL 720
|
|
| RloC |
COG4694 |
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis]; |
102-562 |
1.67e-07 |
|
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 443729 [Multi-domain] Cd Length: 692 Bit Score: 56.28 E-value: 1.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 102 MSRIEKmsIQGVRSFgiedKDKQIITFFSPLTILVGPNGAGKTTIIECLKYICTGDFPPGTKGNTFVHDPKVAQETDVR- 180
Cdd:COG4694 2 ITKIKK--LKNVGAF----KDFGWLAFFKKLNLIYGENGSGKSTLSRILRSLELGDTSSEVIAEFEIEAGGSAPNPSVRv 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 181 -----AQIRLQFRD-VNGELVAVQRSmlctqKSKKTEFKTLEGVITRTK---HGEKVSLSSKCAEIDREMISSLGVSKSV 251
Cdd:COG4694 76 fnrdfVEENLRSGEeIKGIFTLGEEN-----IELEEEIEELEKEIEDLKkelDKLEKELKEAKKALEKLLEDLAKSIKDD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 252 LNNVIFCHQEDSNWPLSEGKALKQKFDeifSATRYIKALETLRQVRQTQGQKV----------KECQTELKYLKQNKEKA 321
Cdd:COG4694 151 LKKLFASSGRNYRKANLEKKLSALKSS---SEDELKEKLKLLKEEEPEPIAPItplpdlkallSEAETLLEKSAVSSAIE 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 322 cEIRDQITSKEAQ--LTSSREIVKSYENELDPL------KNRLKEIEQnlskimRLDNEIKALesrKKQMEKDNSELEQK 393
Cdd:COG4694 228 -ELAALIQNPGNSdwVEQGLAYHKEEEDDTCPFcqqelaAERIEALEA------YFDDEYEKL---LAALKDLLEELESA 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 394 MEKVFQGSDEQLNDLYHnhqrtvrEKERRLVDCQRELEKLNKESRLLNQEKSELLVEQGRLQLqadrhQEHMQARDSLIQ 473
Cdd:COG4694 298 INALSALLLEILRTLLP-------SAKEDLKAALEALNALLETLLAALEEKIANPSTSIDLDD-----QELLDELNDLIA 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 474 SLATQLELdgfelgpfSERQIKNFHKLVRE-RQEKESETASQLLNDFTRKEALKQKQIDEIRDKKTGLGRIIELKSEIlT 552
Cdd:COG4694 366 ALNALIEE--------HNAKIANLKAEKEEaRKKLEAHELAELKEDLSRYKAEVEELIEELKTIKALKKALEDLKTEI-S 436
|
490
....*....|
gi 2015236753 553 KKQNELKNVK 562
Cdd:COG4694 437 ELEAELSSVD 446
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
288-830 |
2.72e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 55.71 E-value: 2.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 288 KALETLRQVRQTQGQKVKECQTELKYLKQNKEkacEIRDQITSKEAQLTSSREIVKSYENELDPLKNRLKEIEQNLS--- 364
Cdd:COG1196 267 AELEELRLELEELELELEEAQAEEYELLAELA---RLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEele 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 365 -KIMRLDNEIKALESRKKQMEKDNSELEQKMEkvfqgsdeqlndlyhnhqrtvrEKERRLVDC-QRELEKLNKESRLLNQ 442
Cdd:COG1196 344 eELEEAEEELEEAEAELAEAEEALLEAEAELA----------------------EAEEELEELaEELLEALRAAAELAAQ 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 443 EKSELLVEQGRLQLQADRHQEHMQARDSLIQSLATQLEldgfELGPFSERQIKnfhklvRERQEKESETASQLLNDFTRK 522
Cdd:COG1196 402 LEELEEAEEALLERLERLEEELEELEEALAELEEEEEE----EEEALEEAAEE------EAELEEEEEALLELLAELLEE 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 523 EALKQKQIDEIRDKKTGLGRIIELKSEILTKKQNELKNVKyELQQLEGSSDRILELDQELTKAERELSKAEknsnvetlK 602
Cdd:COG1196 472 AALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVK-AALLLAGLRGLAGAVAVLIGVEAAYEAALE--------A 542
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 603 TEVISLQNEKADLDRTLRKLDQEMEQLNHHTAARTQMEMLNKDKADKDEQIRKIKYRHSDELTSLLGYFPNKKQL----- 677
Cdd:COG1196 543 ALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVlgdtl 622
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 678 ------EDWLHSKSKEINQTRDRLAK-------LNKELASAEQNKNHINIELKRKEEQLSSYEDKLFDvcGSQDFESDLD 744
Cdd:COG1196 623 lgrtlvAARLEAALRRAVTLAGRLREvtlegegGSAGGSLTGGSRRELLAALLEAEAELEELAERLAE--EELELEEALL 700
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 745 RLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENqsccpvcQRGFQTEAELQEVISDLQSKLRLAPDKLKSTESELKKKE 824
Cdd:COG1196 701 AEEEEERELAEAEEERLEEELEEEALEEQLEAER-------EELLEELLEEEELLEEEALEELPEPPDLEELERELERLE 773
|
....*.
gi 2015236753 825 KRRDEM 830
Cdd:COG1196 774 REIEAL 779
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
104-617 |
3.69e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.16 E-value: 3.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 104 RIEKMSIQGVRSFgiedkDKQIITFFSPLTILVGPNGAGKTTIIECLKYICTGdfppgtkgntfvhdpKVAQETDVRAQI 183
Cdd:COG4717 2 KIKELEIYGFGKF-----RDRTIEFSPGLNVIYGPNEAGKSTLLAFIRAMLLE---------------RLEKEADELFKP 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 184 RLQFRDVNGELVAVQRSMLCTQKSKKTEFKTLEgvitrtkhGEKVSLSSKCAEIDREmisslgvsksvlnnvifchqeds 263
Cdd:COG4717 62 QGRKPELNLKELKELEEELKEAEEKEEEYAELQ--------EELEELEEELEELEAE----------------------- 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 264 nwpLSEGKALKQKFDEIFSATRYIKALETLRQVRQTQGQKVKECQTELKYLKQNKEKACEIRDQITSKEAQLTSSREIVK 343
Cdd:COG4717 111 ---LEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLS 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 344 -SYENELDPLKNRLKEIEQnlsKIMRLDNEIKALESRKKQMEKDNSELEQKMEK---------------------VFQGS 401
Cdd:COG4717 188 lATEEELQDLAEELEELQQ---RLAELEEELEEAQEELEELEEELEQLENELEAaaleerlkearlllliaaallALLGL 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 402 DEQLNDLYHN---------------HQRTVREKERRLVDcQRELEKLNKESRLLNQEKSELLVEQGRLQ-------LQAD 459
Cdd:COG4717 265 GGSLLSLILTiagvlflvlgllallFLLLAREKASLGKE-AEELQALPALEELEEEELEELLAALGLPPdlspeelLELL 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 460 RHQEHMQARDSLIQSLATQLELDGFElgpfserqiKNFHKLVRERQEKESETASQLLNDFTRKEALKQKqIDEIRDKKTG 539
Cdd:COG4717 344 DRIEELQELLREAEELEEELQLEELE---------QEIAALLAEAGVEDEEELRAALEQAEEYQELKEE-LEELEEQLEE 413
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 540 LGRIIELKSEILTKKQ--NELKNVKYELQQLEgssDRILELDQELTKAERELSKAEKNSNVETLKTEVISLQNEKADLDR 617
Cdd:COG4717 414 LLGELEELLEALDEEEleEELEELEEELEELE---EELEELREELAELEAELEQLEEDGELAELLQELEELKAELRELAE 490
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
104-159 |
4.08e-07 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 53.46 E-value: 4.08e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 2015236753 104 RIEKMSIQGVRsfGIEDKDkqiITF--FSPLTILVGPNGAGKTTIIECLKYICTGDFP 159
Cdd:COG3950 2 RIKSLTIENFR--GFEDLE---IDFdnPPRLTVLVGENGSGKTTLLEAIALALSGLLS 54
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
792-1379 |
5.61e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.39 E-value: 5.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 792 EAELQEVISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLvpmrqsiidlkEKEIPELRNKLQNVNRDIQRLKNDIEE 871
Cdd:COG4717 52 EKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAEL-----------QEELEELEEELEELEAELEELREELEK 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 872 QETLLGAIIPEEEsakvcltdvtiMERLQMELKDVERKIAQQAAKLQGL-DLDRSVQQVNQEKQEKQHKLDTVSSKIEL- 949
Cdd:COG4717 121 LEKLLQLLPLYQE-----------LEALEAELAELPERLEELEERLEELrELEEELEELEAELAELQEELEELLEQLSLa 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 950 NRKLIQDQQEQIQHLKSTANELKSEKLQISTNLQRRQQlEEQTVELSTEVQSLYREIKDAKEQL---------------- 1013
Cdd:COG4717 190 TEEELQDLAEELEELQQRLAELEEELEEAQEELEELEE-ELEQLENELEAAALEERLKEARLLLliaaallallglggsl 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 1014 --------------------SPLETTLEKFQQEKE-ELVNKKNTSHKIAQDKINEIKEKVKNIHSYMKD-IENYIQDGKD 1071
Cdd:COG4717 269 lsliltiagvlflvlgllalLFLLLAREKASLGKEaEELQALPALEELEEEELEELLAALGLPPDLSPEeLLELLDRIEE 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 1072 dyKKQKETELNKVIAQ--ISECEKHKEKINKEMGImrQDIDT-QKIQERWLQDNLTLRKRNEELKEVEEERKQHLKEMGQ 1148
Cdd:COG4717 349 --LQELLREAEELEEElqLEELEQEIAALLAEAGV--EDEEElRAALEQAEEYQELKEELEELEEQLEELLGELEELLEA 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 1149 MQVLQMKNEHQKLEEKIDNIKRNHSLAIGRQKGYEEEIIHFKKELREPQFRDAEEKYREmmiimRTTELVNKD--LDIYY 1226
Cdd:COG4717 425 LDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGELAELLQELEELKA-----ELRELAEEWaaLKLAL 499
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 1227 KTLDQAIMKFHSMKMEEINKIIRDLWRSTYRGqdiEYIEIRSDADENVSASDKRRNYnYRVVMLkgdtaldmrgrcSAGQ 1306
Cdd:COG4717 500 ELLEEAREEYREERLPPVLERASEYFSRLTDG---RYRLIRIDEDLSLKVDTEDGRT-RPVEEL------------SRGT 563
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2015236753 1307 KVLASLIIRLALAETFCLNCGILALDEPTTNLDRENIESLAHALVEIIKSRsqqrnfQLLVITHDEDFVELLG 1379
Cdd:COG4717 564 REQLYLALRLALAELLAGEPLPLILDDAFVNFDDERLRAALELLAELAKGR------QVIYFTCHEELVELFQ 630
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
1293-1376 |
6.34e-07 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 53.99 E-value: 6.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 1293 DTALDMRGRC-SAGQKVlasliiRLALAETFCLNCGILALDEPTTNLDRENIESLAHALVEIIKSRSqqrnfqLLVITHD 1371
Cdd:COG4988 464 DTPLGEGGRGlSGGQAQ------RLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRT------VILITHR 531
|
....*
gi 2015236753 1372 EDFVE 1376
Cdd:COG4988 532 LALLA 536
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
348-866 |
6.76e-07 |
|
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: 53.98 E-value: 6.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 348 ELDPLKNRLKEIEQNLSKIMRLDNEIKALESRKKQMEKDNSELEQKMEKVFQGSDEQLNDLYHNHQRTVREKERRLVDCQ 427
Cdd:pfam05557 3 ELIESKARLSQLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAELNRLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 428 RELEKLN-----KESRL--LNQEKSELLVEQGRLQLQADRHQEHMQARDSLIQSLATQLELdgfelgpfSERQIKNFHKL 500
Cdd:pfam05557 83 KYLEALNkklneKESQLadAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDL--------LKAKASEAEQL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 501 VR--ERQEKESETASQLLNDFTRKEALKQKQIDEIRDKKTGLGRIIELKSEI-----LTKKQNELK-----------NVK 562
Cdd:pfam05557 155 RQnlEKQQSSLAEAEQRIKELEFEIQSQEQDSEIVKNSKSELARIPELEKELerlreHNKHLNENIenklllkeeveDLK 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 563 YELQQLEGSSDRILELDQELTKAERELSKAEK---------------NSNVETLKTEVISLQNEKADLDRTLRKLDQEME 627
Cdd:pfam05557 235 RKLEREEKYREEAATLELEKEKLEQELQSWVKlaqdtglnlrspedlSRRIEQLQQREIVLKEENSSLTSSARQLEKARR 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 628 QLNHHTAA-RTQMEMLNKDKADKDEQIRKIKYRHS------DELTSLLGYFPNKKQLEDWLHSKSKEINQTRD------- 693
Cdd:pfam05557 315 ELEQELAQyLKKIEDLNKKLKRHKALVRRLQRRVLlltkerDGYRAILESYDKELTMSNYSPQLLERIEEAEDmtqkmqa 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 694 -------RLAKLNKELASAEQNKNHINIELKRKEEQLSSYEdklfdvcgSQDFESDLDRLKEEIEKSSKQRAMLAGATAV 766
Cdd:pfam05557 395 hneemeaQLSVAEEELGGYKQQAQTLERELQALRQQESLAD--------PSYSKEEVDSLRRKLETLELERQRLREQKNE 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 767 YSQFITQLT---DENQSCCPVCQRGFQTEAELQEVISDLQSKLRLAPDKLKstesELKKKEKRRDEMLGLVPMRQSIIDl 843
Cdd:pfam05557 467 LEMELERRClqgDYDPKKTKVLHLSMNPAAEAYQQRKNQLEKLQAEIERLK----RLLKKLEDDLEQVLRLPETTSTMN- 541
|
570 580
....*....|....*....|...
gi 2015236753 844 kEKEIPELRNKLQNVNRDIQRLK 866
Cdd:pfam05557 542 -FKEVLDLRKELESAELKNQRLK 563
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
283-936 |
7.06e-07 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 54.06 E-value: 7.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 283 ATRYIKALETLRQVRQTQGQKVKECQTELKYLKQNKEKACEIRDQITSKEAQLTSSREIVKSYENELDPLK-NRLKEIEQ 361
Cdd:pfam10174 190 AEMQLGHLEVLLDQKEKENIHLREELHRRNQLQPDPAKTKALQTVIEMKDTKISSLERNIRDLEDEVQMLKtNGLLHTED 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 362 NLSKImrldneikalesrkKQMEkdnseleqkmekvfqgsdeqlndLYHNHQRTVREKerrlvdcqreLEKLNKEsrlLN 441
Cdd:pfam10174 270 REEEI--------------KQME-----------------------VYKSHSKFMKNK----------IDQLKQE---LS 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 442 QEKSELLVEQGRLQLQADRHQEHMQARDSLIQSLAT--------QLELDGFELGPFSERQIKN-FHKLVRERQEKESETA 512
Cdd:pfam10174 300 KKESELLALQTKLETLTNQNSDCKQHIEVLKESLTAkeqraailQTEVDALRLRLEEKESFLNkKTKQLQDLTEEKSTLA 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 513 SQLLNdftrkealkQKQIDEIRDKKTG-LGRIIELKSEILTKKQNELKNVKYELQQLEGSSDRIlelDQELTKAERELSk 591
Cdd:pfam10174 380 GEIRD---------LKDMLDVKERKINvLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNT---DTALTTLEEALS- 446
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 592 aEKNSNVETLKTEVISLQNEKADLDRTLRKLDQEMEQlnhhtaartQMEMLNKDKADKDEQIRKIKYRHSDELTSLLGYF 671
Cdd:pfam10174 447 -EKERIIERLKEQREREDRERLEELESLKKENKDLKE---------KVSALQPELTEKESSLIDLKEHASSLASSGLKKD 516
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 672 PNKKQLEDWLHSKSKEINQTRDRLAKLnKELASAEQNKNHINIELKRKEEQLSSYEDKlfdvcgSQDFESDLDRLKE--- 748
Cdd:pfam10174 517 SKLKSLEIAVEQKKEECSKLENQLKKA-HNAEEAVRTNPEINDRIRLLEQEVARYKEE------SGKAQAEVERLLGilr 589
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 749 --EIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRGFQTEAELQEVISDLQSKLRLAPD-KLKSTESELKKKEK 825
Cdd:pfam10174 590 evENEKNDKDKKIAELESLTLRQMKEQNKKVANIKHGQQEMKKKGAQLLEEARRREDNLADNSQQlQLEELMGALEKTRQ 669
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 826 RRDEMLGLVPMRQSIIDLKEKEIPELRNKLQNVNRDIQRLKndieeQETLLGAIipEEESAKVCLtdvtimerlqMELKD 905
Cdd:pfam10174 670 ELDATKARLSSTQQSLAEKDGHLTNLRAERRKQLEEILEMK-----QEALLAAI--SEKDANIAL----------LELSS 732
|
650 660 670
....*....|....*....|....*....|.
gi 2015236753 906 VERKIAQQAAKLQGLDLDRSVQQVNQEKQEK 936
Cdd:pfam10174 733 SKKKKTQEEVMALKREKDRLVHQLKQQTQNR 763
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
850-1274 |
7.95e-07 |
|
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: 54.29 E-value: 7.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 850 ELRNKLQNVNRDIQRLKNDIEEQETL---------LGAIIPEEESAKVCLTDvTIMERLQMELKdverKIAQQAAKLQGL 920
Cdd:TIGR01612 604 ELKEKIKNISDKNEYIKKAIDLKKIIennnayideLAKISPYQVPEHLKNKD-KIYSTIKSELS----KIYEDDIDALYN 678
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 921 DLDRSVQQVNQEKQEKQHKLDTVSSKIElnrkliqDQQEQIQHLkstanELKSEKLQISTNLQRRQQLEEQTVELStevQ 1000
Cdd:TIGR01612 679 ELSSIVKENAIDNTEDKAKLDDLKSKID-------KEYDKIQNM-----ETATVELHLSNIENKKNELLDIIVEIK---K 743
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 1001 SLYREIKDakeqlsPLETTLEKFQQEKEELVNKKNTSHKiAQDKINEIKEKVKNIHSYMKDIENyIQDGKDDYKKQKETE 1080
Cdd:TIGR01612 744 HIHGEINK------DLNKILEDFKNKEKELSNKINDYAK-EKDELNKYKSKISEIKNHYNDQIN-IDNIKDEDAKQNYDK 815
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 1081 LNKVIAQISECEKHKEKINKEMGIMRQDIdtqkiqerwlqdnltLRKRNEELKEVEEERKQHLKEMGQMQVL--QMKNE- 1157
Cdd:TIGR01612 816 SKEYIKTISIKEDEIFKIINEMKFMKDDF---------------LNKVDKFINFENNCKEKIDSEHEQFAELtnKIKAEi 880
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 1158 -HQKLEEKIDNIKRNHSLAIGRQKGYEEEI--IHFKKELRE-----PQFRDAEEKYREMMIIMRttELVNKDLDIYYKTl 1229
Cdd:TIGR01612 881 sDDKLNDYEKKFNDSKSLINEINKSIEEEYqnINTLKKVDEyikicENTKESIEKFHNKQNILK--EILNKNIDTIKES- 957
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 2015236753 1230 dQAIMKFHSMKME--------EINKIIRDLWRSTYRGQDIEYIEIRSDADENV 1274
Cdd:TIGR01612 958 -NLIEKSYKDKFDntlidkinELDKAFKDASLNDYEAKNNELIKYFNDLKANL 1009
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
104-157 |
1.06e-06 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 52.70 E-value: 1.06e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 2015236753 104 RIEKMSIQGVRSFGiedkdKQIITFFSPLTILVGPNGAGKTTIIECLKYICTGD 157
Cdd:COG3593 2 KLEKIKIKNFRSIK-----DLSIELSDDLTVLVGENNSGKSSILEALRLLLGPS 50
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
926-1293 |
1.33e-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: 53.53 E-value: 1.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 926 VQQVNQEKQEKQHKLDTVSSKIELNRKLIQDQQEQIQHLKSTAN------ELKSEK--LQISTNLQRRQQLEEQTVELST 997
Cdd:TIGR02169 165 VAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREkaeryqALLKEKreYEGYELLKEKEALERQKEAIER 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 998 EVQSLYREIKDAKEQLSPLETTLEKFQQEKEELVNKKNtshKIAQDKINEIKEKVKNIHSYMKDIENYIQDgKDDYKKQK 1077
Cdd:TIGR02169 245 QLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIK---DLGEEEQLRVKEKIGELEAEIASLERSIAE-KERELEDA 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 1078 ETELNKVIAQISECEKHKEKINKEmgIMRQDIDTQKIQERW--LQDNL-TLRKRNEELKEVEEERKQHLKemgqmqvlQM 1154
Cdd:TIGR02169 321 EERLAKLEAEIDKLLAEIEELERE--IEEERKRRDKLTEEYaeLKEELeDLRAELEEVDKEFAETRDELK--------DY 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 1155 KNEHQKLEEKIDNIKRNHSLAIGRQKGYEEEIIHFKKELrepqfRDAEEKYREMmiimrTTELVNKDLDIyyKTLDQAIM 1234
Cdd:TIGR02169 391 REKLEKLKREINELKRELDRLQEELQRLSEELADLNAAI-----AGIEAKINEL-----EEEKEDKALEI--KKQEWKLE 458
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2015236753 1235 KFhSMKMEEINKIIRDLwRSTYRGQDIEYIEIRSDADE---NVSASDKRRNYNYRVVMLKGD 1293
Cdd:TIGR02169 459 QL-AADLSKYEQELYDL-KEEYDRVEKELSKLQRELAEaeaQARASEERVRGGRAVEEVLKA 518
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
271-593 |
1.45e-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: 53.53 E-value: 1.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 271 KALKQKFDEIFSATRYIK-ALETLRQVRQTQGQKVKECQTELKYLKQNKEKACEirdQITSKEAQLTSSREIVKSYENEL 349
Cdd:TIGR02169 684 EGLKRELSSLQSELRRIEnRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKE---RLEELEEDLSSLEQEIENVKSEL 760
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 350 DPLKNRLKEIEQNLSKIMRLDNEIKALESRKKqmekdnseleqkmekvFQGSDEQLNDLyhnhQRTVREKERRLVDCQRE 429
Cdd:TIGR02169 761 KELEARIEELEEDLHKLEEALNDLEARLSHSR----------------IPEIQAELSKL----EEEVSRIEARLREIEQK 820
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 430 LEKLNKESRLLNQEKSELLVEQGRLQLQadrhqehmqardslIQSLATQLELDGFELGPFsERQIKNFHKLVRERQEKES 509
Cdd:TIGR02169 821 LNRLTLEKEYLEKEIQELQEQRIDLKEQ--------------IKSIEKEIENLNGKKEEL-EEELEELEAALRDLESRLG 885
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 510 ETASQLLNdftrkealKQKQIDEIRDKKTGLGRIIELKSEILTKKQNELKNVKYELQQLEGSSDRILE----------LD 579
Cdd:TIGR02169 886 DLKKERDE--------LEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEipeeelsledVQ 957
|
330
....*....|....
gi 2015236753 580 QELTKAERELSKAE 593
Cdd:TIGR02169 958 AELQRVEEEIRALE 971
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
1293-1380 |
1.46e-06 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 53.06 E-value: 1.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 1293 DTALDMRGR-CSAGQKVlasliiRLALAETFCLNCGILALDEPTTNLDREniesLAHALVEIIKSRSQQRNfqLLVITHD 1371
Cdd:TIGR02857 449 DTPIGEGGAgLSGGQAQ------RLALARAFLRDAPLLLLDEPTAHLDAE----TEAEVLEALRALAQGRT--VLLVTHR 516
|
....*....
gi 2015236753 1372 EDFVELLGR 1380
Cdd:TIGR02857 517 LALAALADR 525
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1300-1376 |
1.92e-06 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 50.56 E-value: 1.92e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2015236753 1300 GRCSAGQKVlasliiRLALAETFCLNCGILALDEPTTNLDRENIEslahALVEIIKSRSQQRnfQLLVI-THDEDFVE 1376
Cdd:COG4133 130 RQLSAGQKR------RVALARLLLSPAPLWLLDEPFTALDAAGVA----LLAELIAAHLARG--GAVLLtTHQPLELA 195
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
896-1052 |
1.93e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 50.69 E-value: 1.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 896 MERLQMELKDVERKIAQQAAKLQGLDldRSVQQVNQEKQEKQHKLDTVSSKIELNRKLIQDQQEQIQHLKsTANELKSEK 975
Cdd:COG1579 19 LDRLEHRLKELPAELAELEDELAALE--ARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVR-NNKEYEALQ 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2015236753 976 LQISTNLQRRQQLEEQTVELSTEVQSLYREIKDAKEQLSPLETTLEKFQQEKEELVNKKNTSHKIAQDKINEIKEKV 1052
Cdd:COG1579 96 KEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKI 172
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
273-1176 |
2.88e-06 |
|
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: 52.36 E-value: 2.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 273 LKQKFDEIFSATRYIKA--LETLRQVRQTQGQKVKECQTELK---YLKQNKEKACEIRDqITSKEAQLTSSREIVKSYEN 347
Cdd:TIGR01612 701 LKSKIDKEYDKIQNMETatVELHLSNIENKKNELLDIIVEIKkhiHGEINKDLNKILED-FKNKEKELSNKINDYAKEKD 779
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 348 ELDPLKNRLKEIEQNLSKIMRLDN----EIKALESRKKQMEKDNSELEQKMEKVFQG----SDEQLN--DLYHNHQRTVR 417
Cdd:TIGR01612 780 ELNKYKSKISEIKNHYNDQINIDNikdeDAKQNYDKSKEYIKTISIKEDEIFKIINEmkfmKDDFLNkvDKFINFENNCK 859
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 418 EKerrlVDCQREleklnKESRLLNQEKSELLVEqgrlqlQADRHQEHMQARDSLI-----------QSLATQLELDGF-E 485
Cdd:TIGR01612 860 EK----IDSEHE-----QFAELTNKIKAEISDD------KLNDYEKKFNDSKSLIneinksieeeyQNINTLKKVDEYiK 924
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 486 LGPFSERQIKNFHKLVRERQEKESETASQLLNDFTRKEALKQKQIDEIRDKKTGLGRII--------ELKSEILTKKQNE 557
Cdd:TIGR01612 925 ICENTKESIEKFHNKQNILKEILNKNIDTIKESNLIEKSYKDKFDNTLIDKINELDKAFkdaslndyEAKNNELIKYFND 1004
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 558 LK--------NVKYelQQLEGSSDRILELDQELTKAERELSKAEK-----------------NSNVETLKTEV------- 605
Cdd:TIGR01612 1005 LKanlgknkeNMLY--HQFDEKEKATNDIEQKIEDANKNIPNIEIaihtsiyniideiekeiGKNIELLNKEIleeaein 1082
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 606 ------------------------ISLQNE----KADLDRTLRKLDQEMEQL--------NHHTAARTQMEMLNK--DKA 647
Cdd:TIGR01612 1083 itnfneikeklkhynfddfgkeenIKYADEinkiKDDIKNLDQKIDHHIKALeeikkkseNYIDEIKAQINDLEDvaDKA 1162
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 648 DKDEQIRKIKYRHSDELTSLlgyfPNKKQLEDwlhskskEINQTRDRLAKLNKELASAEQNKN---------------HI 712
Cdd:TIGR01612 1163 ISNDDPEEIEKKIENIVTKI----DKKKNIYD-------EIKKLLNEIAEIEKDKTSLEEVKGinlsygknlgklfleKI 1231
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 713 NIELKRKEEQLSSYEdklfdvcgsqDFESDLDRLKEEIEKSSKQRAMLAGATAVYSQFITQLTDEnqsccpvcQRGFQTE 792
Cdd:TIGR01612 1232 DEEKKKSEHMIKAME----------AYIEDLDEIKEKSPEIENEMGIEMDIKAEMETFNISHDDD--------KDHHIIS 1293
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 793 AELQEVISDLQSK-LRLAPDklKSTESELKKKEKRRDEMLGLVPMRQSIIDLKEKEIPELRN--KLQNVNRDIQRLK--- 866
Cdd:TIGR01612 1294 KKHDENISDIREKsLKIIED--FSEESDINDIKKELQKNLLDAQKHNSDINLYLNEIANIYNilKLNKIKKIIDEVKeyt 1371
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 867 NDIEEQETLLGAIIPEEESAKVCLTDvtimerlQMELKDVERKIaqqAAKLQGLDLDRSVQQVNQEKQ---EKQHKLDTV 943
Cdd:TIGR01612 1372 KEIEENNKNIKDELDKSEKLIKKIKD-------DINLEECKSKI---ESTLDDKDIDECIKKIKELKNhilSEESNIDTY 1441
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 944 -------SSKIELNRKLIQDQQEQIQH-LKSTANELKSEklqISTNLQRRQQLEEQTVELSTEVQSLYREIKDAKEqlsp 1015
Cdd:TIGR01612 1442 fknadenNENVLLLFKNIEMADNKSQHiLKIKKDNATND---HDFNINELKEHIDKSKGCKDEADKNAKAIEKNKE---- 1514
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 1016 letTLEKFQQEKEELVNK------KNTSHKIAQDK---INEIKEKVKNI-------HSYMKDIENYIQDGKDDYKKQK-- 1077
Cdd:TIGR01612 1515 ---LFEQYKKDVTELLNKysalaiKNKFAKTKKDSeiiIKEIKDAHKKFileaeksEQKIKEIKKEKFRIEDDAAKNDks 1591
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 1078 --------------ETELNKVI---AQISECEKHKEKINKEMGIMrqDIDTQKIQERWLQDNL-TLRKRNEELKEVEEER 1139
Cdd:TIGR01612 1592 nkaaidiqlslenfENKFLKISdikKKINDCLKETESIEKKISSF--SIDSQDTELKENGDNLnSLQEFLESLKDQKKNI 1669
|
1050 1060 1070
....*....|....*....|....*....|....*..
gi 2015236753 1140 KQHLKEMGQMQvlqmkNEHQKLEEKIDNIKRNHSLAI 1176
Cdd:TIGR01612 1670 EDKKKELDELD-----SEIEKIEIDVDQHKKNYEIGI 1701
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
897-1029 |
2.95e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 52.22 E-value: 2.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 897 ERLQMELKDVERKIAQQAAKLQglDLDRSVQQVNQEKQEKQHKLDTVSSKIELN--RKLIQDQQEQIQHLKSTANELKSE 974
Cdd:COG4913 613 AALEAELAELEEELAEAEERLE--ALEAELDALQERREALQRLAEYSWDEIDVAsaEREIAELEAELERLDASSDDLAAL 690
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 2015236753 975 KLQISTNLQRRQQLEEQTVELSTEVQSLYREIKDAKEQLSPLETTLEKFQQEKEE 1029
Cdd:COG4913 691 EEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARL 745
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
681-945 |
3.42e-06 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 51.94 E-value: 3.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 681 LHSKSKEINQtrdRLAKLNKELASAEQN----KNHINIELKRKEEQLSSYEDKLFD-VCGSQDFESDLDRLKEEIEKSSK 755
Cdd:PHA02562 172 NKDKIRELNQ---QIQTLDMKIDHIQQQiktyNKNIEEQRKKNGENIARKQNKYDElVEEAKTIKAEIEELTDELLNLVM 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 756 QRAMLAGATAVYSQFITQLTDENQSC------------CPVCQRGFQTEaelQEVISDLQsklrlapDKLKSTESELKKK 823
Cdd:PHA02562 249 DIEDPSAALNKLNTAAAKIKSKIEQFqkvikmyekggvCPTCTQQISEG---PDRITKIK-------DKLKELQHSLEKL 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 824 EKRRDEMLGLVPMRQSIIdlkeKEIPELRNKLQNVNRDIQRLKNDIEEQEtllgaiipeeesakvcltdvTIMERLQMEL 903
Cdd:PHA02562 319 DTAIDELEEIMDEFNEQS----KKLLELKNKISTNKQSLITLVDKAKKVK--------------------AAIEELQAEF 374
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 2015236753 904 KDVERKIAQQAAKLQGLDLDRSvqqvnqEKQEKQHKLDTVSS 945
Cdd:PHA02562 375 VDNAEELAKLQDELDKIVKTKS------ELVKEKYHRGIVTD 410
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
274-979 |
3.53e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.07 E-value: 3.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 274 KQKFDEIFSATRYIKALETLRQVRQTQGQKVKECQTELKYLKQNKEKACEIRDQITS--KEAQLTSSREIVKSYENELDP 351
Cdd:PTZ00121 1277 ARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAakKKAEEAKKAAEAAKAEAEAAA 1356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 352 LKNRLKEIEQNLSKIMRLDNEIKALESRKKQMEKDNS-ELEQKMEKVFQGSDEQLNdlyhnhqrtvREKERRLVDcqrEL 430
Cdd:PTZ00121 1357 DEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKAdEAKKKAEEDKKKADELKK----------AAAAKKKAD---EA 1423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 431 EKLNKESRLLNQEKSEllVEQGRLQLQADRHQEHMQARDSLIQSLATQLELDGFELGPFSERQIKNFHKLVRERQEKESE 510
Cdd:PTZ00121 1424 KKKAEEKKKADEAKKK--AEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADE 1501
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 511 tasqllndfTRKEALKQKQIDEIRdKKTGLGRIIELKSEILTKKQNELKNVKYELQQLEGSSDRILELDQELTKAErELS 590
Cdd:PTZ00121 1502 ---------AKKAAEAKKKADEAK-KAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAE-EAK 1570
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 591 KAEKNSNVETLKTEVISlQNEKADLDRTLrKLDQEMEQLNHHTAARTQMEMLNKDKADKDEQIRKIKYRHSDELTSLLGY 670
Cdd:PTZ00121 1571 KAEEDKNMALRKAEEAK-KAEEARIEEVM-KLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKK 1648
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 671 FPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASAEQNKnhinielKRKEEQLSSYEDKLFDVCGSQDFESDLDRLKEEI 750
Cdd:PTZ00121 1649 AEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDE-------KKAAEALKKEAEEAKKAEELKKKEAEEKKKAEEL 1721
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 751 EKSSKQRAMLAgatavysqfiTQLTDENQSCCPVCQRGFQTEAELQEVISDLQSKLRLAPDKLKSTESELKKKEKRRDEm 830
Cdd:PTZ00121 1722 KKAEEENKIKA----------EEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDE- 1790
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 831 lglvpMRQSIIDLKEKEIPELRNKLQNVNRDIQRLKNDieEQETLLGAIIPEEESAKVCLTDVTIMERLQMELKDVERKI 910
Cdd:PTZ00121 1791 -----KRRMEVDKKIKDIFDNFANIIEGGKEGNLVIND--SKEMEDSAIKEVADSKNMQLEEADAFEKHKFNKNNENGED 1863
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2015236753 911 AQQAAKL--QGLDLDRSVQQVNQEKQEKQHKLDTVSSKIE------LNRKLIQDQQEQIQHLKSTANELKSEKLQIS 979
Cdd:PTZ00121 1864 GNKEADFnkEKDLKEDDEEEIEEADEIEKIDKDDIEREIPnnnmagKNNDIIDDKLDKDEYIKRDAEETREEIIKIS 1940
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
291-730 |
4.73e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 51.58 E-value: 4.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 291 ETLRQVRQTQGQKVKECQTELKYLKQNKEKACEIRDQITSKEAQLTSSREIVKSYENELDplknrlkeieqnlskimRLD 370
Cdd:PRK02224 328 DRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIE-----------------ELE 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 371 NEIKALESRKKQMEKDnseleqkmekvFQGSDEQLNDLYHNHQRTV-REKERRlVDCQRELEKLNKESRLLNQEKSEllv 449
Cdd:PRK02224 391 EEIEELRERFGDAPVD-----------LGNAEDFLEELREERDELReREAELE-ATLRTARERVEEAEALLEAGKCP--- 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 450 EQGRlQLQADRHQEHMQARDSLIQSLATQLEldgfELgpfserqiknfhKLVRERQEKESETASQLlndftrKEAlkQKQ 529
Cdd:PRK02224 456 ECGQ-PVEGSPHVETIEEDRERVEELEAELE----DL------------EEEVEEVEERLERAEDL------VEA--EDR 510
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 530 IDEIRDKKTGLGRIIELKSEILTKKQNELKNVKYELQQLEGSSDRILELDQEL-TKAERELSK-AEKNSNVETLKTEVIS 607
Cdd:PRK02224 511 IERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAeEEAEEAREEvAELNSKLAELKERIES 590
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 608 LQNEKADLDRtLRKLDQEMEQLNHHTAARTQMEMLNKDK-ADKDEQIRKIKYRHSDELTSLLGyfPNKKQLEDWLHSKSK 686
Cdd:PRK02224 591 LERIRTLLAA-IADAEDEIERLREKREALAELNDERRERlAEKRERKRELEAEFDEARIEEAR--EDKERAEEYLEQVEE 667
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 2015236753 687 EINQTRDRLAKLNKELASAEQNKNHINiELKRKEEQLSSYEDKL 730
Cdd:PRK02224 668 KLDELREERDDLQAEIGAVENELEELE-ELRERREALENRVEAL 710
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
897-1123 |
5.14e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.92 E-value: 5.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 897 ERLQMELKDVERKIAQQAAKLQgldldrsvqQVNQEKQEKQHKLDTVSSKIELNRKLIQDQQEQIQHLKSTANELKSEKL 976
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELA---------ALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 977 QIstnlqrRQQLEEQTVELSTEVQSLYReikdaKEQLSPLETTLEkfQQEKEELVNKKNTSHKIA---QDKINEIKEKVK 1053
Cdd:COG4942 94 EL------RAELEAQKEELAELLRALYR-----LGRQPPLALLLS--PEDFLDAVRRLQYLKYLAparREQAEELRADLA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 1054 NIHSYMKDIENYIQDgKDDYKKQKETELNKVIAQISECEKHKEKINKEMGIMRQDIDTQKIQERWLQDNL 1123
Cdd:COG4942 161 ELAALRAELEAERAE-LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALI 229
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
762-1118 |
5.59e-06 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 51.28 E-value: 5.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 762 GATAVYSQFITQLTDENQSCCPVCQRGFQTEAElqevisdlqsklRLAPDKLKSTESELKKKEKRRDEMLGLVPMRQSII 841
Cdd:pfam17380 262 GQTMTENEFLNQLLHIVQHQKAVSERQQQEKFE------------KMEQERLRQEKEEKAREVERRRKLEEAEKARQAEM 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 842 DLKEKEIPELRNKLQNVNRDIQRLKNDIEEQETllgAIIPEEESAkVCLTDVTIMERLQMELKDVERKIAQQ-----AAK 916
Cdd:pfam17380 330 DRQAAIYAEQERMAMERERELERIRQEERKREL---ERIRQEEIA-MEISRMRELERLQMERQQKNERVRQEleaarKVK 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 917 LQGLDLDRSVQQVNQE-----------KQEKQHKLDTVSSK-IELNRKLIQDQQEQIQHLKSTANELKSEKLQISTNLQR 984
Cdd:pfam17380 406 ILEEERQRKIQQQKVEmeqiraeqeeaRQREVRRLEEERAReMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRD 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 985 RQQLEEQTvelstevqslyREIkdakeqlspLETTLEKFQQEKEELVNKKNTSHKIAQDKINEIKEkvknihsymkdiEN 1064
Cdd:pfam17380 486 RKRAEEQR-----------RKI---------LEKELEERKQAMIEEERKRKLLEKEMEERQKAIYE------------EE 533
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 2015236753 1065 YIQDGKDDYKKQKETELNKVIAQ----ISECEKHKEKINKEMGIMRQDIDTQKIQERW 1118
Cdd:pfam17380 534 RRREAEEERRKQQEMEERRRIQEqmrkATEERSRLEAMEREREMMRQIVESEKARAEY 591
|
|
| Rad50_zn_hook |
pfam04423 |
Rad50 zinc hook motif; The Mre11 complex (Mre11 Rad50 Nbs1) is central to chromosomal ... |
760-813 |
5.84e-06 |
|
Rad50 zinc hook motif; The Mre11 complex (Mre11 Rad50 Nbs1) is central to chromosomal maintenance and functions in homologous recombination, telomere maintenance and sister chromatid association. The Rad50 coiled-coil region contains a dimer interface at the apex of the coiled coils in which pairs of conserved Cys-X-X-Cys motifs form interlocking hooks that bind one Zn ion. This alignment includes the zinc hook motif and a short stretch of coiled-coil on either side.
Pssm-ID: 427940 [Multi-domain] Cd Length: 52 Bit Score: 44.88 E-value: 5.84e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 2015236753 760 LAGATAVYSQFITQLTDENQsCCPVCQRGFQTEaELQEVISDLQSKLRLAPDKL 813
Cdd:pfam04423 1 LHQETLELNKKIEELKEAEG-CCPLCGRPLDEE-HRSELIKELQSKLERLPEEL 52
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
308-724 |
6.41e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 51.26 E-value: 6.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 308 QTELKYLKQNKEKACEIRDQITSKEAQLTSSREIVKSYENELDPLKNRLKEIEQNLSKimrldneikalesrKKQMEKDN 387
Cdd:pfam05483 366 RTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDE--------------KKQFEKIA 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 388 SEL---EQKMEKVFQGSDEQLNDLYHNHQRTVREKE---RRLVDCQRELEK-------LNKESRLLNQEKSELLVEQGRL 454
Cdd:pfam05483 432 EELkgkEQELIFLLQAREKEIHDLEIQLTAIKTSEEhylKEVEDLKTELEKeklknieLTAHCDKLLLENKELTQEASDM 511
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 455 QLQADRHQEHMQARDSLIQSLATQLE-LDGFELGPFSE-----RQIKNFHKLVRERQEKESETASQLLNDFTRKEalkqK 528
Cdd:pfam05483 512 TLELKKHQEDIINCKKQEERMLKQIEnLEEKEMNLRDElesvrEEFIQKGDEVKCKLDKSEENARSIEYEVLKKE----K 587
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 529 QIDEIRDKKTGLGRIIELKSEILTKKQNELKNVK----YELQQLEGSSDRILELDQELTKAERELSKAEKNSNVEtLKTE 604
Cdd:pfam05483 588 QMKILENKCNNLKKQIENKNKNIEELHQENKALKkkgsAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKE-IEDK 666
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 605 VISLQN-------EKADLDRTLrKLDQEMEQLNHHTAARtQMEMLNKDKADKDEQIrkikyrhsDELTSLLGYFPNKKQL 677
Cdd:pfam05483 667 KISEEKlleevekAKAIADEAV-KLQKEIDKRCQHKIAE-MVALMEKHKHQYDKII--------EERDSELGLYKNKEQE 736
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 2015236753 678 EDWLH-SKSKEINQTRDRLAKLNKELASAEQNKNHINIELKRKEEQLS 724
Cdd:pfam05483 737 QSSAKaALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTAILK 784
|
|
| SbcC_Walker_B |
pfam13558 |
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from ... |
1278-1352 |
8.08e-06 |
|
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from eukaryotes and the prokaryotic homolog SbcCD complex subunit C. RAD50-ATPase forms a complex with Mre11-nuclease that detects and processes diverse and obstructed DNA ends. This domain is separated of the Walker A domain by a long coiled-coil domain and forms the nucleotide-binding domain (NBD) when the coiled coils fold back on themselves and bring together Walker A and B domains. Two RAD50-NBDs forms heterotetramers with a Mre11 nuclease dimer that assemble as catalytic head module that binds and cleaves DNA in an ATP-dependent reaction. Through secondary structural analysis, it has been suggested that there is a wide structural conservation in the Rad50/SMC protein family as seen in structural similarities between RAD50's hook and ABC-ATPase MukB's elbow region.
Pssm-ID: 463921 [Multi-domain] Cd Length: 90 Bit Score: 45.69 E-value: 8.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 1278 DKRRNYNYRVVMLKGDTA----LDMRGRCSAGQK-VLASLIIRLALAETFCLN------CGILALDEPTTNLDRENIESL 1346
Cdd:pfam13558 5 DYRNWLSFEVEVRDEDGSevetYRRSGGLSGGEKqLLAYLPLAAALAAQYGSAegrppaPRLVFLDEAFAKLDEENIRTA 84
|
....*.
gi 2015236753 1347 AHALVE 1352
Cdd:pfam13558 85 LELLRA 90
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
894-1053 |
8.72e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.21 E-value: 8.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 894 TIMERLQMELKDVERKIAQQAAKLQglDLDRSVQQVNQEKQEKQHKLDTVSSKIELNRKLIQDQQEQIQH----LKSTAN 969
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELD--ALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEErreeLGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 970 ELKSEKLQIS---------------TNLQRRQQLEEQTVELSTEVQSLYREIKDAKEQLSPLETTLEKFQQEKEELVNKK 1034
Cdd:COG3883 94 ALYRSGGSVSyldvllgsesfsdflDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170
....*....|....*....
gi 2015236753 1035 NTSHKIAQDKINEIKEKVK 1053
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEA 192
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
284-748 |
9.02e-06 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 50.85 E-value: 9.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 284 TRYIKALETLRQVRQTQGQKVK-ECQTELKYlkqnkekaceIRDQITSKEAQlTSSREIVKSYENELDplkNRLKEIEQN 362
Cdd:COG5022 849 QKFGRSLKAKKRFSLLKKETIYlQSAQRVEL----------AERQLQELKID-VKSISSLKLVNLELE---SEIIELKKS 914
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 363 LSKIMRLDNEIKALESRKKQMEKDNSELE--QKMEKVFQGSDEQLNDLYHNHQRTVREKER---RLVDCQRELEKLNKES 437
Cdd:COG5022 915 LSSDLIENLEFKTELIARLKKLLNNIDLEegPSIEYVKLPELNKLHEVESKLKETSEEYEDllkKSTILVREGNKANSEL 994
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 438 RLLNQEKSELLVEQGRLQLQADRHQEhmqaRDSLIQSLATQLELDGFElgPFSERQIKNFHKLVRERQEKESETASQLLN 517
Cdd:COG5022 995 KNFKKELAELSKQYGALQESTKQLKE----LPVEVAELQSASKIISSE--STELSILKPLQKLKGLLLLENNQLQARYKA 1068
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 518 DFTRKEalkqkqideirdkktgLGRIIELKSEILTKKQNELKNVKYELQQlegSSDRILELDQELTKAereLSKAEKNSN 597
Cdd:COG5022 1069 LKLRRE----------------NSLLDDKQLYQLESTENLLKTINVKDLE---VTNRNLVKPANVLQF---IVAQMIKLN 1126
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 598 VET-----LKTEVISLQNEKADLDRTLRKLDQEMEQLNHHTAARTQMEMLNKDKADKDEQIRKIKYRHSDELTsllgyfp 672
Cdd:COG5022 1127 LLQeiskfLSQLVNTLEPVFQKLSVLQLELDGLFWEANLEALPSPPPFAALSEKRLYQSALYDEKSKLSSSEV------- 1199
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2015236753 673 nkKQLEDWLHSKSKEINQTrDRLAKLNKELASAEQNKNHINIELKRkeeqlSSYEDKLFDVCGSQDFESDLDRLKE 748
Cdd:COG5022 1200 --NDLKNELIALFSKIFSG-WPRGDKLKKLISEGWVPTEYSTSLKG-----FNNLNKKFDTPASMSNEKLLSLLNS 1267
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
634-873 |
9.88e-06 |
|
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: 49.76 E-value: 9.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 634 AARTQMEMLNKDKADKDEQIRKIKYRHSDELTSLlgyfpnkKQLEDWLHSKSKEINQTRDRLAKLNKELASAEQNKNHIN 713
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQL-------AALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 714 IELKRKEEQLSSYEDKLFDVcGSQDFESDLDRlKEEIEKSSKQRAMLAGATAVYSQFITQLTdenqsccpvcqrgfQTEA 793
Cdd:COG4942 97 AELEAQKEELAELLRALYRL-GRQPPLALLLS-PEDFLDAVRRLQYLKYLAPARREQAEELR--------------ADLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 794 ELQEVISDLQSklrlapdKLKSTESELKKKEKRRDEMLGLVPMRQSIIDLKEKEIPELRNKLQNVNRDIQRLKNDIEEQE 873
Cdd:COG4942 161 ELAALRAELEA-------ERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLE 233
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
563-761 |
1.01e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 48.77 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 563 YELQQLEgssDRILELDQELTKAERELSKAEKNsnVETLKTEVISLQNEKADLDRTLRKLDQEMEQLNhhtaartqmEML 642
Cdd:COG1579 10 LDLQELD---SELDRLEHRLKELPAELAELEDE--LAALEARLEAAKTELEDLEKEIKRLELEIEEVE---------ARI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 643 NKDKaDKDEQIRKIKyrhsdELTSLLgyfpnkKQLEdwlhSKSKEINQTRDRLAKLNKELASAEQNKNHINIELKRKEEQ 722
Cdd:COG1579 76 KKYE-EQLGNVRNNK-----EYEALQ------KEIE----SLKRRISDLEDEILELMERIEELEEELAELEAELAELEAE 139
|
170 180 190
....*....|....*....|....*....|....*....
gi 2015236753 723 LSSYEDKLfdvcgsqdfESDLDRLKEEIEKSSKQRAMLA 761
Cdd:COG1579 140 LEEKKAEL---------DEELAELEAELEELEAEREELA 169
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
915-1103 |
1.05e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.83 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 915 AKLQGLDLDRSVQQVNQEKQEKQHKLDTVSSKIELNRKLIQDQQEQIQHLKSTANELKSEklqISTNlqrRQQLEEQTVE 994
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAE---IAEA---EAEIEERREE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 995 LSTEVQSLYRE---------------IKDAKEQLSPLET-------TLEKFQQEKEELVNKKNTshkiAQDKINEIKEKV 1052
Cdd:COG3883 88 LGERARALYRSggsvsyldvllgsesFSDFLDRLSALSKiadadadLLEELKADKAELEAKKAE----LEAKLAELEALK 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2015236753 1053 KNIHSYMKDIENYIQDgKDDYKKQKETELNKVIAQISECEKHKEKINKEMG 1103
Cdd:COG3883 164 AELEAAKAELEAQQAE-QEALLAQLSAEEAAAEAQLAELEAELAAAEAAAA 213
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
527-758 |
1.12e-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: 49.76 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 527 QKQIDEIRDKKTGLGRIIELKSEILTKKQNELKNVKYELQQLEgssDRILELDQELTKAERELSKAEKnsNVETLKTEVI 606
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALE---RRIAALARRIRALEQELAALEA--ELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 607 SLQNEKADLDRTLRKLDQEMEQLNHH------------TAARTQMEMLNKDKADKDEQIRKIKyRHSDELTSLlgyfpnK 674
Cdd:COG4942 94 ELRAELEAQKEELAELLRALYRLGRQpplalllspedfLDAVRRLQYLKYLAPARREQAEELR-ADLAELAAL------R 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 675 KQLEdwlhSKSKEINQTRDRLAKLNKELASAEQNKNHINIELKRKEEQLSSYEDKLfdvcgsQDFESDLDRLKEEIEKSS 754
Cdd:COG4942 167 AELE----AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAEL------QQEAEELEALIARLEAEA 236
|
....
gi 2015236753 755 KQRA 758
Cdd:COG4942 237 AAAA 240
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
1328-1381 |
1.17e-05 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 48.25 E-value: 1.17e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 2015236753 1328 ILAlDEPTTNLDRENieslAHALVEIIKSRSQQRNFQLLVITHDEDFVELLGRS 1381
Cdd:cd03255 162 ILA-DEPTGNLDSET----GKEVMELLRELNKEAGTTIVVVTHDPELAEYADRI 210
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
468-760 |
1.23e-05 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 49.93 E-value: 1.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 468 RDSLIQSLAtqlELDGFELGPFSERQIKNFHKLVRERQEKESEtASQLLNDFTRKEALKQKQIDEIRDKKTG-------- 539
Cdd:PRK05771 18 KDEVLEALH---ELGVVHIEDLKEELSNERLRKLRSLLTKLSE-ALDKLRSYLPKLNPLREEKKKVSVKSLEelikdvee 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 540 -----LGRIIELKSEIlTKKQNELKNVKYELQQLEG----SSDRILELDQELTKA---------ERELSKAEKNSNVETL 601
Cdd:PRK05771 94 elekiEKEIKELEEEI-SELENEIKELEQEIERLEPwgnfDLDLSLLLGFKYVSVfvgtvpedkLEELKLESDVENVEYI 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 602 KTE-------VISLQNEKADLDRTLRKLDQEMEQLNhhtaartqmemlnkDKADKDEQIRKIKyrhsDELTSLlgyfpnK 674
Cdd:PRK05771 173 STDkgyvyvvVVVLKELSDEVEEELKKLGFERLELE--------------EEGTPSELIREIK----EELEEI------E 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 675 KQLEDwLHSKSKEINQTRDRLAKLNKELASAEqnKNHINIELKRKEEqlssyeDKLFDVCGsqdF--ESDLDRLKEEIEK 752
Cdd:PRK05771 229 KERES-LLEELKELAKKYLEELLALYEYLEIE--LERAEALSKFLKT------DKTFAIEG---WvpEDRVKKLKELIDK 296
|
....*...
gi 2015236753 753 SSKQRAML 760
Cdd:PRK05771 297 ATGGSAYV 304
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
310-1208 |
1.33e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 50.17 E-value: 1.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 310 ELKYLKQNKEKACEIRDQITSKEAQLTSSREIVKSY---ENEL----DPLKNRLKEIEQNLSKIMRldneikALESRKKQ 382
Cdd:pfam01576 13 ELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQlqaETELcaeaEEMRARLAARKQELEEILH------ELESRLEE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 383 MEKDNSELEQ---KMEKVFQGSDEQLNDlyhnhQRTVREKerrlvdcqRELEKLNKESRLLNQEKSELLVEQGRLQLQAD 459
Cdd:pfam01576 87 EEERSQQLQNekkKMQQHIQDLEEQLDE-----EEAARQK--------LQLEKVTTEAKIKKLEEDILLLEDQNSKLSKE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 460 RHQehMQARDSLIQSLATQLELDGFELGpfserQIKNFHKLV----RERQEKESETASQLlndftrkEALKQK---QIDE 532
Cdd:pfam01576 154 RKL--LEERISEFTSNLAEEEEKAKSLS-----KLKNKHEAMisdlEERLKKEEKGRQEL-------EKAKRKlegESTD 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 533 IRDKKTGL-GRIIELKSEiLTKKQNELK--------------NVKYELQQLEGssdRILELDQELTKAERELSKAEK--- 594
Cdd:pfam01576 220 LQEQIAELqAQIAELRAQ-LAKKEEELQaalarleeetaqknNALKKIRELEA---QISELQEDLESERAARNKAEKqrr 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 595 --NSNVETLKTEVISLQNEKADLDRTLRKLDQEMEQLNhhtaartqmEMLNKDKADKDEQIRKIKYRHS---DELTSLLG 669
Cdd:pfam01576 296 dlGEELEALKTELEDTLDTTAAQQELRSKREQEVTELK---------KALEEETRSHEAQLQEMRQKHTqalEELTEQLE 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 670 YFP-NKKQLEDWLHSKSKEINQtrdrlakLNKELASAEQNKNHINIELKRKEEQLSSYEDKLfdvcgsqdfeSDLDRLKE 748
Cdd:pfam01576 367 QAKrNKANLEKAKQALESENAE-------LQAELRTLQQAKQDSEHKRKKLEGQLQELQARL----------SESERQRA 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 749 EI-EKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRGFQTEAELQEvisDLQSKLRLApDKLKSTESELKKKEKRR 827
Cdd:pfam01576 430 ELaEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQE---ETRQKLNLS-TRLRQLEDERNSLQEQL 505
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 828 DEmlglvpmrqsiidlKEKEIPELRNKLQNVNRDIQRLKNDIEEQetlLGAIIPEEESAKvcltdvtimeRLQMELKDVE 907
Cdd:pfam01576 506 EE--------------EEEAKRNVERQLSTLQAQLSDMKKKLEED---AGTLEALEEGKK----------RLQRELEALT 558
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 908 RKIAQQAAKLQGLDldrsvqqvnQEKQEKQHKLDTVSSKIELNRKLI---QDQQEQIQHLkstaneLKSEKLQISTNLQR 984
Cdd:pfam01576 559 QQLEEKAAAYDKLE---------KTKNRLQQELDDLLVDLDHQRQLVsnlEKKQKKFDQM------LAEEKAISARYAEE 623
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 985 RQQLEEQTVELSTEVQSLYREIKDAKEQLSPLETTLEKFQQEKEELVNKKN----TSHKIAQDKiNEIKEKVKNIHSYMK 1060
Cdd:pfam01576 624 RDRAEAEAREKETRALSLARALEEALEAKEELERTNKQLRAEMEDLVSSKDdvgkNVHELERSK-RALEQQVEEMKTQLE 702
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 1061 DIENYIQDGKDD----------YKKQKETELNKVIAQISECEKHKEKINKEMGIMRQDIDTQKIQERWLQDNLT--LRKR 1128
Cdd:pfam01576 703 ELEDELQATEDAklrlevnmqaLKAQFERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLEldLKEL 782
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 1129 NEELKEVEEERKQHLKEMGQMQVlQMKNEHQKLEEKidNIKRNHSLAIGRQ-----KGYEEEIIHFKKEL--REPQFRDA 1201
Cdd:pfam01576 783 EAQIDAANKGREEAVKQLKKLQA-QMKDLQRELEEA--RASRDEILAQSKEsekklKNLEAELLQLQEDLaaSERARRQA 859
|
....*..
gi 2015236753 1202 EEKYREM 1208
Cdd:pfam01576 860 QQERDEL 866
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
308-640 |
1.35e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.52 E-value: 1.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 308 QTELKYLKQNKEKACEIRDQITSKEAQLTSSREIVKSYENELDPLKNRLKEIEQNLSK----IMRLDNEIKALESRKKQM 383
Cdd:COG4372 34 RKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAaqaeLAQAQEELESLQEEAEEL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 384 EKDNSELEQKMEKVfQGSDEQLNDLYHNHQRTVREKERRLVDCQRELEKLNKESRLLNQEKSELLVEQGRLQLQADRHQE 463
Cdd:COG4372 114 QEELEELQKERQDL-EQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEA 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 464 HMQARDSLIQSLATQLELDGFELGPFSERQIKNFHKLVRERQEKESETASQLLND-FTRKEALKQKQIDEIRDKKTGLGR 542
Cdd:COG4372 193 NRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDkEELLEEVILKEIEELELAILVEKD 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 543 IIELKSEILTKKQNELKNVKYELQQLEGSSDRILELDQELTKAERELSKAEKNSNVETLKTEVISLQNEKADLDRTLRKL 622
Cdd:COG4372 273 TEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLD 352
|
330
....*....|....*...
gi 2015236753 623 DQEMEQLNHHTAARTQME 640
Cdd:COG4372 353 NDVLELLSKGAEAGVADG 370
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
792-1004 |
1.92e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.06 E-value: 1.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 792 EAELQEVISDLQSKLRLAPDKLKSTESELKKKEKRRDEMlglvpmrQSIIDLKEKEIPELRNKLQNVNRDIQRLKNDIEE 871
Cdd:COG3883 32 LEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKL-------QAEIAEAEAEIEERREELGERARALYRSGGSVSY 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 872 QETLLGAIIPEEESAKVCLTDvTIMERLQMELKDVERKIAQQAAKLQGLDLDRSVQQVNQEKQEKQHKldtvsskiELNR 951
Cdd:COG3883 105 LDVLLGSESFSDFLDRLSALS-KIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKA--------ELEA 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2015236753 952 KLIQdQQEQIQHLKS---TANELKSEKLQISTNLQRRQQLEEQTVELSTEVQSLYR 1004
Cdd:COG3883 176 QQAE-QEALLAQLSAeeaAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAA 230
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1303-1379 |
2.00e-05 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 46.80 E-value: 2.00e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2015236753 1303 SAGQKVlasliiRLALAETFCLNCGILALDEPTTNLDREniesLAHALVEIIKSRSQQRNFQLLVITHDEDFVELLG 1379
Cdd:cd03229 102 SGGQQQ------RVALARALAMDPDVLLLDEPTSALDPI----TRREVRALLKSLQAQLGITVVLVTHDLDEAARLA 168
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1303-1370 |
2.76e-05 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 46.22 E-value: 2.76e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2015236753 1303 SAGQKVlasliiRLALAETFCLNCGILALDEPTTNLDRENieslAHALVEIIKSRSQQRNfqLLVITH 1370
Cdd:cd03228 98 SGGQRQ------RIAIARALLRDPPILILDEATSALDPET----EALILEALRALAKGKT--VIVIAH 153
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
281-588 |
3.04e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.14 E-value: 3.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 281 FSATRYIKALEtlrqvrqtqgQKVKECQTELKYLKQNKEKACEIRDQItskEAQLTSSREIVKSYENELDplknrlkeie 360
Cdd:COG4913 606 FDNRAKLAALE----------AELAELEEELAEAEERLEALEAELDAL---QERREALQRLAEYSWDEID---------- 662
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 361 qnlskIMRLDNEIKALESRKKQMEKDNSELEQkmekvfqgsdeqlndLyhnhqrtvrekERRLVDCQRELEKLNKESRLL 440
Cdd:COG4913 663 -----VASAEREIAELEAELERLDASSDDLAA---------------L-----------EEQLEELEAELEELEEELDEL 711
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 441 NQEKSELLVEQGRLQLQADRHQEHMQARDSlIQSLATQLELDGFELGPFSERQIKNFHKLVRERQEKESETASQLLNDFT 520
Cdd:COG4913 712 KGEIGRLEKELEQAEEELDELQDRLEAAED-LARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELE 790
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2015236753 521 RK-EALKQKQIDEIRDKKTGLGRIIE-------LKSEILTKKQNELKnvkyelQQLEGSSDR-ILELDQELTKAERE 588
Cdd:COG4913 791 RAmRAFNREWPAETADLDADLESLPEylalldrLEEDGLPEYEERFK------ELLNENSIEfVADLLSKLRRAIRE 861
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
502-729 |
3.67e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.84 E-value: 3.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 502 RERQEKESETASQLLNDFTRKEALKQKQIDEIRDKktglgriIELKSEILTKKQNELKNVKYELQQLEgssDRILELDQE 581
Cdd:COG4942 29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERR-------IAALARRIRALEQELAALEAELAELE---KEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 582 LTKAERELSK----AEKNSNVETLKteVISLQNEKADLDRTLRKLDQEMEQLnhhtaaRTQMEMLNKDKADKDEQIRKIK 657
Cdd:COG4942 99 LEAQKEELAEllraLYRLGRQPPLA--LLLSPEDFLDAVRRLQYLKYLAPAR------REQAEELRADLAELAALRAELE 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2015236753 658 YRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASAEQNKNHINIELKRKEEQLSSYEDK 729
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
104-151 |
4.35e-05 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 47.62 E-value: 4.35e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 2015236753 104 RIEKMSIQGVRSFGIEDKDkqiitfFSPLTILVGPNGAGKTTIIECLK 151
Cdd:COG4637 1 MITRIRIKNFKSLRDLELP------LGPLTVLIGANGSGKSNLLDALR 42
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
791-1098 |
4.49e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 47.21 E-value: 4.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 791 TEAELQEVISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLVP-MRQSIIDLKEK------EIPELRNKLQNVNRDIQ 863
Cdd:COG1340 9 SLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKeLREEAQELREKrdelneKVKELKEERDELNEKLN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 864 RLKNDIEEQETLLGAIIPEEESakvcltdvtiMERLQMELKDVERKiaqqaaklqgldldrsvQQVNQEKQEKQHKLDTV 943
Cdd:COG1340 89 ELREELDELRKELAELNKAGGS----------IDKLRKEIERLEWR-----------------QQTEVLSPEEEKELVEK 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 944 SSKIELNRKLIQDQQEQIQHLKSTANELKSEKLQISTNLQRRQQLEEQTVELSTEVQSLYREIKDAKEQLSPLETTLEKF 1023
Cdd:COG1340 142 IKELEKELEKAKKALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEA 221
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2015236753 1024 QQEKEELvnkkntsHKiaqdkinEIKEKVKNIHSYMKDIENYIQDGKDDYKKQKETELNKVIAQISECEKHKEKI 1098
Cdd:COG1340 222 QEKADEL-------HE-------EIIELQKELRELRKELKKLRKKQRALKREKEKEELEEKAEEIFEKLKKGEKL 282
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
403-1063 |
6.67e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.99 E-value: 6.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 403 EQLNDLYHNHQRTVREKER--------RLVDCQRELEKLNKESRLLNQEKSELLVEQGRLQLQADRHQEHmqaRDSLIQS 474
Cdd:COG4913 255 EPIRELAERYAAARERLAEleylraalRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREE---LDELEAQ 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 475 LAtqlELDGFELGPFsERQIKNFHKLVRERQEKESETASQL----LNDFTRKEALK--QKQIDEIRDKKTG-LGRIIELK 547
Cdd:COG4913 332 IR---GNGGDRLEQL-EREIERLERELEERERRRARLEALLaalgLPLPASAEEFAalRAEAAALLEALEEeLEALEEAL 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 548 SEI---LTKKQNELKNVKYELQQLEGSSDRIlelDQELTKAERELSKAEKNSNVE--------TLKTEVISLQN------ 610
Cdd:COG4913 408 AEAeaaLRDLRRELRELEAEIASLERRKSNI---PARLLALRDALAEALGLDEAElpfvgeliEVRPEEERWRGaiervl 484
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 611 ---------EKADLDRTLRKLDQemeqlnHHTAARTQMEMLNKD-------KADKDEQIRKIKYR---HSDELTSLLGYF 671
Cdd:COG4913 485 ggfaltllvPPEHYAAALRWVNR------LHLRGRLVYERVRTGlpdperpRLDPDSLAGKLDFKphpFRAWLEAELGRR 558
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 672 P------NKKQLEDwlHSKSkeInqTRDRLAKLNKELasAEQNKNHI----------NIE-LKRKEEQLSSYEDKLfdvc 734
Cdd:COG4913 559 FdyvcvdSPEELRR--HPRA--I--TRAGQVKGNGTR--HEKDDRRRirsryvlgfdNRAkLAALEAELAELEEEL---- 626
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 735 gsQDFESDLDRLKEEIEKSSKQRAMLAGATAVYSQFITQLtdenqsccpvcqrgfQTEAELQEVISDLQSkLRLAPDKLK 814
Cdd:COG4913 627 --AEAEERLEALEAELDALQERREALQRLAEYSWDEIDVA---------------SAEREIAELEAELER-LDASSDDLA 688
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 815 STESELKKKEKRRDemlglvpmrqsiidlkekeipELRNKLQNVNRDIQRLKNDIEEQETLLgaiipeeesakvcltdvt 894
Cdd:COG4913 689 ALEEQLEELEAELE---------------------ELEEELDELKGEIGRLEKELEQAEEEL------------------ 729
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 895 imERLQMELKDVERKIAQQAAklqgLDLDRSVQQVNQEKQEkqhkldtvsskielnRKLIQDQQEQIQHLKSTANELKSE 974
Cdd:COG4913 730 --DELQDRLEAAEDLARLELR----ALLEERFAAALGDAVE---------------RELRENLEERIDALRARLNRAEEE 788
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 975 KLQISTNLQRRQQLEeqTVELSTEVQSL--YREIkdakeqLSPLETT-LEKFQQEKEELVNKKNT------SHKIAQDkI 1045
Cdd:COG4913 789 LERAMRAFNREWPAE--TADLDADLESLpeYLAL------LDRLEEDgLPEYEERFKELLNENSIefvadlLSKLRRA-I 859
|
730
....*....|....*...
gi 2015236753 1046 NEIKEKVKNIHSYMKDIE 1063
Cdd:COG4913 860 REIKERIDPLNDSLKRIP 877
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1300-1376 |
6.88e-05 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 47.37 E-value: 6.88e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2015236753 1300 GRCSAGQKVlasliiRLALAETFCLNCGILALDEPTTNLDRENIESLAHALveiiksrsqqRNFQ--LLVITHDEDFVE 1376
Cdd:COG0488 431 GVLSGGEKA------RLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEAL----------DDFPgtVLLVSHDRYFLD 493
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
326-514 |
7.79e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.13 E-value: 7.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 326 DQITSKEAQLTSSREIVKSYENELDPLknrLKEIEQNLSKIMRLDNEIKALESRKKQMEKDNSELEQKMEKVFQGSDEQL 405
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDAL---QAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 406 NDLYHNHQ------------------------RTVREKERRLVDCQREL-EKLNKESRLLNQEKSELLVEQGRLQLQADR 460
Cdd:COG3883 93 RALYRSGGsvsyldvllgsesfsdfldrlsalSKIADADADLLEELKADkAELEAKKAELEAKLAELEALKAELEAAKAE 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2015236753 461 HQEHMQARDSLIQSLATQLELDGFELGPFSERQIKNFHKLVRERQEKESETASQ 514
Cdd:COG3883 173 LEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAA 226
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
371-585 |
9.81e-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: 46.68 E-value: 9.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 371 NEIKALESRKKQMEKDNSELEQKMEKVFQGSDEQLNDLyhnhqrtvREKERRLVDCQRELEKLNKESRLLNQEKSELLVE 450
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQL--------AALERRIAALARRIRALEQELAALEAELAELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 451 QGRLQLQADRHQEHMQARDSLIQSLATQLELDgFELGPFS----ERQIKNFHKLVRERQE------KESETASQLLNDFT 520
Cdd:COG4942 92 IAELRAELEAQKEELAELLRALYRLGRQPPLA-LLLSPEDfldaVRRLQYLKYLAPARREqaeelrADLAELAALRAELE 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2015236753 521 RKEALKQKQIDEIRDKKTGLGRIIELKSEILTK-------KQNELKNVKYELQQLEGSSDRILELDQELTKA 585
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARlekelaeLAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| COG3910 |
COG3910 |
Predicted ATPase [General function prediction only]; |
126-171 |
1.06e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443116 [Multi-domain] Cd Length: 239 Bit Score: 45.53 E-value: 1.06e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 2015236753 126 ITFFSPLTILVGPNGAGKTTIIECLKYICtgDFPP--GTKGNTFVHDP 171
Cdd:COG3910 33 LEFHPPVTFFVGENGSGKSTLLEAIAVAA--GFNPegGSKNFRFSTRE 78
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
105-151 |
1.17e-04 |
|
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. SMC proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213245 [Multi-domain] Cd Length: 197 Bit Score: 44.76 E-value: 1.17e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 2015236753 105 IEKMSIQGVRSFGiedkDKQIITFFSPLTILVGPNGAGKTTIIECLK 151
Cdd:cd03278 1 LKKLELKGFKSFA----DKTTIPFPPGLTAIVGPNGSGKSNIIDAIR 43
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
403-718 |
1.17e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.22 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 403 EQLNDLyhnhQRTVREKERRLVDCQRELEKLNKESRLLNQEKSEL--LVEQGRLQLQADRHQEHMQARDSLIQSL-ATQL 479
Cdd:COG4913 610 AKLAAL----EAELAELEEELAEAEERLEALEAELDALQERREALqrLAEYSWDEIDVASAEREIAELEAELERLdASSD 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 480 ELDgfELgpfsERQIknfhklvrERQEKESETASQLLNDFTRKEALKQKQIDEIRDKKTGLGRIIELKSEILTKKQNELK 559
Cdd:COG4913 686 DLA--AL----EEQL--------EELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALL 751
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 560 NVKYELQQLEGSSDRILE-LDQELTKAERELSKAEKNsnVETLKTEVISL-QNEKADLDRTLRKLDQEMEQLNhhtaart 637
Cdd:COG4913 752 EERFAAALGDAVERELREnLEERIDALRARLNRAEEE--LERAMRAFNREwPAETADLDADLESLPEYLALLD------- 822
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 638 qmEMLNKDKADKDEQIRKIKYRHSDEltsllgyfpNKKQLEDWLHSKSKEInqtRDRLAKLNKELASAEQNKN-HINIEL 716
Cdd:COG4913 823 --RLEEDGLPEYEERFKELLNENSIE---------FVADLLSKLRRAIREI---KERIDPLNDSLKRIPFGPGrYLRLEA 888
|
..
gi 2015236753 717 KR 718
Cdd:COG4913 889 RP 890
|
|
| RecF |
COG1195 |
Recombinational DNA repair ATPase RecF [Replication, recombination and repair]; |
104-156 |
1.21e-04 |
|
Recombinational DNA repair ATPase RecF [Replication, recombination and repair];
Pssm-ID: 440808 [Multi-domain] Cd Length: 352 Bit Score: 46.30 E-value: 1.21e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 2015236753 104 RIEKMSIQGVRSFgiedkDKQIITFFSPLTILVGPNGAGKTTIIECLKYICTG 156
Cdd:COG1195 1 RLKRLSLTNFRNY-----ESLELEFSPGINVLVGPNGQGKTNLLEAIYLLATG 48
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
896-1062 |
1.31e-04 |
|
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: 1.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 896 MERLQMELKDVERKIAQQAAKLQGLDLDRSVQQVNQEKQEKQHKLDTVSSKIELNRKLIQDQQEQIQHLKSTANELkSEK 975
Cdd:COG3206 184 LPELRKELEEAEAALEEFRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPEL-LQS 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 976 LQISTNLQRRQQLEEQTVELSTEVQSLYREIKDAKEQlspLETTLEKFQQEKEELVNKKNTSHKIAQDKINEIKEKVKNI 1055
Cdd:COG3206 263 PVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQ---IAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQL 339
|
....*..
gi 2015236753 1056 HSYMKDI 1062
Cdd:COG3206 340 EARLAEL 346
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1328-1380 |
1.41e-04 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 45.03 E-value: 1.41e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 2015236753 1328 ILAlDEPTTNLDRENieslAHALVEIIKSRSQQRNFQLLVITHDEDFVELLGR 1380
Cdd:COG1136 166 ILA-DEPTGNLDSKT----GEEVLELLRELNRELGTTIVMVTHDPELAARADR 213
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
361-657 |
1.42e-04 |
|
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: 46.66 E-value: 1.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 361 QNLSKIMRLDNEIKALESRKKQMEKDNSELEQKMEKVFQGSDEQLNDLYHNHQRTVREKERRLVDCQRELEKlnKESRLL 440
Cdd:pfam17380 288 QQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRQEERK--RELERI 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 441 NQEksELLVEQGRL----QLQADRHQEHMQARDSLIQSLATQLELDgfelgpfsERQIKNFHKLVR-ERQEKESETASQL 515
Cdd:pfam17380 366 RQE--EIAMEISRMreleRLQMERQQKNERVRQELEAARKVKILEE--------ERQRKIQQQKVEmEQIRAEQEEARQR 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 516 lnDFTRKEALKQKQIDEIRDKKtgLGRiiELKSEILTKKQNELKNVKYELQQLEGSSDRILELDQELTKAERELSKA--- 592
Cdd:pfam17380 436 --EVRRLEEERAREMERVRLEE--QER--QQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQami 509
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2015236753 593 EKNSNVETLKTEVISLQNEKADLDRTL-----RKLDQEME-------QLNHHTAARTQMEMLNKDKadkdEQIRKIK 657
Cdd:pfam17380 510 EEERKRKLLEKEMEERQKAIYEEERRReaeeeRRKQQEMEerrriqeQMRKATEERSRLEAMERER----EMMRQIV 582
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
324-1116 |
1.66e-04 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 46.75 E-value: 1.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 324 IRDQITSKEAQLTSSREIVKSYENELDPLKNRL----KEIEQNLSKIMRLDNEIKALESRKKQMEKDNSELEQKMEKVfq 399
Cdd:PTZ00440 506 IINSIKEKNNIVNNNFKNIEDYYITIEGLKNEIegliELIKYYLQSIETLIKDEKLKRSMKNDIKNKIKYIEENVDHI-- 583
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 400 gsdEQLNDLYHNHQRTVREKERRLVDCQRELEKLNKESRLLNQEKSELLVE--QGRLQLQADRHQEHMQARDSLIQSlat 477
Cdd:PTZ00440 584 ---KDIISLNDEIDNIIQQIEELINEALFNKEKFINEKNDLQEKVKYILNKfyKGDLQELLDELSHFLDDHKYLYHE--- 657
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 478 qleldgfelgPFSERQIKNFHKLVRERQEKESETASQLLNDFtrkealkqkqideIRDKKTGLGRIIELKSEILTKKQNE 557
Cdd:PTZ00440 658 ----------AKSKEDLQTLLNTSKNEYEKLEFMKSDNIDNI-------------IKNLKKELQNLLSLKENIIKKQLNN 714
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 558 LKnvkyelQQLEGSSDRILELDQELTKAERELSKAE------KNSNVETLKTEVISLQNEKADLDRTLRKLDQEMEQ--- 628
Cdd:PTZ00440 715 IE------QDISNSLNQYTIKYNDLKSSIEEYKEEEeklevyKHQIINRKNEFILHLYENDKDLPDGKNTYEEFLQYkdt 788
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 629 -LNHHTAARTQMEMLNKDKA----------DKDEQIRKIKYRHSDELTSLLGYFPNK------KQLEDWLHSKSK----- 686
Cdd:PTZ00440 789 iLNKENKISNDINILKENKKnnqdllnsynILIQKLEAHTEKNDEELKQLLQKFPTEdenlnlKELEKEFNENNQivdni 868
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 687 -----EINQTRDRLAKLNKELASAEQNKNHIN------IELKRKEEQlSSYEDKLFDVCGSQDFESDLDRLKEEIEKSSK 755
Cdd:PTZ00440 869 ikdieNMNKNINIIKTLNIAINRSNSNKQLVEhllnnkIDLKNKLEQ-HMKIINTDNIIQKNEKLNLLNNLNKEKEKIEK 947
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 756 QRA--------MLAGATAVYSQFITQLTDENQSCCPVCQRGFQTEAE---------------LQEVISDLQSK------- 805
Cdd:PTZ00440 948 QLSdtkinnlkMQIEKTLEYYDKSKENINGNDGTHLEKLDKEKDEWEhfkseidklnvnyniLNKKIDDLIKKqhddiie 1027
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 806 --LRLAPDKLKSTESELKKKEKRRDEMLGLVPMRQSIIDLK-------EKEIPELRNKLQNVNRDIQRLKNDIEEQETLL 876
Cdd:PTZ00440 1028 liDKLIKEKGKEIEEKVDQYISLLEKMKTKLSSFHFNIDIKkyknpkiKEEIKLLEEKVEALLKKIDENKNKLIEIKNKS 1107
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 877 GAIIPEEESAKVCLTDV------------TIMERLQMELKDVERK--IAQQAAKLQGLDLDRSVQQVNQEKQEKQHKLDT 942
Cdd:PTZ00440 1108 HEHVVNADKEKNKQTEHynkkkkslekiyKQMEKTLKELENMNLEdiTLNEVNEIEIEYERILIDHIVEQINNEAKKSKT 1187
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 943 VSSKIELNRKLIqdqqEQIQHLKSTANELKSEKLQISTNLQRRQQLEEQTVELSTEVQSLYRE------IKDAKEQLSPL 1016
Cdd:PTZ00440 1188 IMEEIESYKKDI----DQVKKNMSKERNDHLTTFEYNAYYDKATASYENIEELTTEAKGLKGEanrstnVDELKEIKLQV 1263
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 1017 ETTLEKFQQEKEELVNK----KNTSHKIAQDKINEIkekVKNIHSYMKDIENYIQDGKDDYKKQKETeLNKVIAQISECE 1092
Cdd:PTZ00440 1264 FSYLQQVIKENNKMENAlheiKNMYEFLISIDSEKI---LKEILNSTKKAEEFSNDAKKELEKTDNL-IKQVEAKIEQAK 1339
|
890 900
....*....|....*....|....
gi 2015236753 1093 KHKEKINKEMGIMRQDIDTQKIQE 1116
Cdd:PTZ00440 1340 EHKNKIYGSLEDKQIDDEIKKIEQ 1363
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
896-1197 |
1.90e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 45.66 E-value: 1.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 896 MERLQMELKDVERKIAQQAAKLQglDLDRSVQQVNQEKQEKQHKLDTVSSKIELNRKLIQDQQEQIQHLKSTANELKSek 975
Cdd:COG4372 40 LDKLQEELEQLREELEQAREELE--QLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQE-- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 976 lQISTNLQRRQQLEEQTVELSTEVQSLYREIKDAKEQLSPLETTLEKFQQEKEEL-VNKKNTSHKIAQDKINEIKEKVKN 1054
Cdd:COG4372 116 -ELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALeQELQALSEAEAEQALDELLKEANR 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 1055 IHSYMKDIENYIQDGKDDYKKQKET---ELNKVIAQISECEKHKEKINKEMGIMRQDIDTQKIQERWLQDNLTLRKRNEE 1131
Cdd:COG4372 195 NAEKEEELAEAEKLIESLPRELAEElleAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTE 274
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2015236753 1132 LKEVEEERKQHLKEMGQMQVLQMKNEHQKLEEKIDNIKRNHSLAIGRQKGYEEEIIHFKKELREPQ 1197
Cdd:COG4372 275 EEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELA 340
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
794-1095 |
1.98e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 46.16 E-value: 1.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 794 ELQEVISDLQSKLRLAPDKLKSTESELKKKEKRRDEmlglvpmrqsIIDLKEKEIPELRNKLQNVNRDIQRLKNDIEEqe 873
Cdd:PHA02562 178 ELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGE----------NIARKQNKYDELVEEAKTIKAEIEELTDELLN-- 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 874 tllgaIIPEEESAKVCLTDVTI--------MERLQMELKDVERKIAQQAAKLQGLDLDRSVQQVNQEKQEKQHKLDTVSS 945
Cdd:PHA02562 246 -----LVMDIEDPSAALNKLNTaaakikskIEQFQKVIKMYEKGGVCPTCTQQISEGPDRITKIKDKLKELQHSLEKLDT 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 946 KIElNRKLIQDqqeQIQHLKSTANELKSeklQISTNLQRRQQLEEQTVELSTEVQSLYREIKDAKEQLSPLETTLEKFQQ 1025
Cdd:PHA02562 321 AID-ELEEIMD---EFNEQSKKLLELKN---KISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVK 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 1026 EKEELVNKKNTsHKIAQD--KINEIKEKV--KNIHSYMKDIENYIQDGKDDYKKQKETELNKVI----------AQISEC 1091
Cdd:PHA02562 394 TKSELVKEKYH-RGIVTDllKDSGIKASIikKYIPYFNKQINHYLQIMEADYNFTLDEEFNETIksrgredfsyASFSQG 472
|
....
gi 2015236753 1092 EKHK 1095
Cdd:PHA02562 473 EKAR 476
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
306-396 |
2.46e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 45.62 E-value: 2.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 306 ECQTELKYLKQNKEKACEIRDQITSKEAQLTSSREIVKSYENELDPLKNRLKEIEQNLSKIMRLDNEIKALESRKKQMEK 385
Cdd:COG2433 407 ELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEERREIRKDREISRLDREIERLERELEEERE 486
|
90
....*....|.
gi 2015236753 386 DNSELEQKMEK 396
Cdd:COG2433 487 RIEELKRKLER 497
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
944-1141 |
2.68e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.14 E-value: 2.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 944 SSKIELNRKLIQDQQEQIQHLKSTANELKSEKLQIstnLQRRQQLEEQTVELSTEVQSLYREIKDAKEQLSPLETTLEKF 1023
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKAL---LKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 1024 QQE----KEELVNKKNTSHKIAQD-------KINEIKEKVKNIHsYMKDIENYIQDGKDDYKKQKEtELNKVIAQISECE 1092
Cdd:COG4942 96 RAEleaqKEELAELLRALYRLGRQpplalllSPEDFLDAVRRLQ-YLKYLAPARREQAEELRADLA-ELAALRAELEAER 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2015236753 1093 KHKEKINKEMGIMRQDIDTQKIQERWLQDNLTLRKRNEELKEVEEERKQ 1141
Cdd:COG4942 174 AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEA 222
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
922-1057 |
2.68e-04 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 45.01 E-value: 2.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 922 LDRSVQQVNQEKQEKQHKLDTVSSKIELNRKLIQDQQEQIQH-LKSTANELKSEKLQISTNLQRRQQLEEQTVELSTEVQ 1000
Cdd:smart00787 163 LMKELELLNSIKPKLRDRKDALEEELRQLKQLEDELEDCDPTeLDRAKEKLKKLLQEIMIKVKKLEELEEELQELESKIE 242
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 2015236753 1001 SLYREIKDAKEQLSPLEttlekfqqekeelvNKKNTSHKIAQDKINEIKEKVKNIHS 1057
Cdd:smart00787 243 DLTNKKSELNTEIAEAE--------------KKLEQCRGFTFKEIEKLKEQLKLLQS 285
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
1296-1380 |
2.69e-04 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 44.12 E-value: 2.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 1296 LDM----RGR-CSAGQKVLasliirLALAETFCLNCGILALDEPTTNLDRENIESLAHALVEIIKSRSqqrnfqLLVITH 1370
Cdd:cd03245 130 LDLqigeRGRgLSGGQRQA------VALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGDKT------LIIITH 197
|
90
....*....|
gi 2015236753 1371 DEDFVELLGR 1380
Cdd:cd03245 198 RPSLLDLVDR 207
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
672-887 |
2.96e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.21 E-value: 2.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 672 PNKKQLEDWLHSKSKEINQTRDRLAKLNKELASAEQNKNHINIELKRKEEQLSSYEDKLfdvcgsQDFESDLDRLKEEIE 751
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEI------AEAEAEIEERREELG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 752 K--SSKQR--------AMLAGATAVySQFITQLTdenqsccpVCQRGFQTEAELQEVISDLQSKLRLAPDKLKSTESELK 821
Cdd:COG3883 90 EraRALYRsggsvsylDVLLGSESF-SDFLDRLS--------ALSKIADADADLLEELKADKAELEAKKAELEAKLAELE 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2015236753 822 KKEKRRDEMLGLVpmrQSIIDLKEKEIPELRNKLQNVNRDIQRLKNDIEEQETLLGAIIPEEESAK 887
Cdd:COG3883 161 ALKAELEAAKAEL---EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAA 223
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
311-1071 |
3.01e-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: 3.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 311 LKYLKQNKEKACEIRDQITSKEAQLTSSREIVKSYENELDPLKNRLKEIE--QNLSKIMRLDNE-IKALESRKKQMEKDN 387
Cdd:TIGR01612 1485 INELKEHIDKSKGCKDEADKNAKAIEKNKELFEQYKKDVTELLNKYSALAikNKFAKTKKDSEIiIKEIKDAHKKFILEA 1564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 388 SELEQKMEKV----FQGSDEQLNDLYHNhqrtvrekeRRLVDCQRELEKL-NKESRLLNQEKsellveqgrlqlqadrhq 462
Cdd:TIGR01612 1565 EKSEQKIKEIkkekFRIEDDAAKNDKSN---------KAAIDIQLSLENFeNKFLKISDIKK------------------ 1617
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 463 ehmQARDSLIQSLATqleldgfelgpfsERQIKNFHKLVRERQEKESETASQLLNDFTrkEALKQkQIDEIRDKKTGLGr 542
Cdd:TIGR01612 1618 ---KINDCLKETESI-------------EKKISSFSIDSQDTELKENGDNLNSLQEFL--ESLKD-QKKNIEDKKKELD- 1677
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 543 iiELKSEIltkkqnelKNVKYELQQLEGSSD-RILELDQELTKAERELSKAEKNSNVETLKTEVISLQN---EKADLDRT 618
Cdd:TIGR01612 1678 --ELDSEI--------EKIEIDVDQHKKNYEiGIIEKIKEIAIANKEEIESIKELIEPTIENLISSFNTndlEGIDPNEK 1747
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 619 LRKLDQEM-----EQLNHHTAARTQMEMLNKDKADKDEqirkIKYRHSDELTSLLGYFPNKKQLEDWLHS-KSKE----I 688
Cdd:TIGR01612 1748 LEEYNTEIgdiyeEFIELYNIIAGCLETVSKEPITYDE----IKNTRINAQNEFLKIIEIEKKSKSYLDDiEAKEfdriI 1823
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 689 NQTRDRLAKLNKELAS--AEQNKNHINIELKRKEEQLSSYEDKLFDVCG-SQDFESDL-----DRLKEEIEKSSKQRAML 760
Cdd:TIGR01612 1824 NHFKKKLDHVNDKFTKeySKINEGFDDISKSIENVKNSTDENLLFDILNkTKDAYAGIigkkyYSYKDEAEKIFINISKL 1903
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 761 AGATAVYSQfitqltdeNQSccpvcqrGFQTEAELQ-EVISDLQSKLRlapDKLKSTESELKKKE---KRRDEMLGLVPM 836
Cdd:TIGR01612 1904 ANSINIQIQ--------NNS-------GIDLFDNINiAILSSLDSEKE---DTLKFIPSPEKEPEiytKIRDSYDTLLDI 1965
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 837 RQSIIDLKEKEIPELrnklqNVNRDIQRLKNDIEEQETLLGAIIPEEESAKVCLTDVTIMERLQMELKDVERKIAQQAAK 916
Cdd:TIGR01612 1966 FKKSQDLHKKEQDTL-----NIIFENQQLYEKIQASNELKDTLSDLKYKKEKILNDVKLLLHKFDELNKLSCDSQNYDTI 2040
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 917 LQGLDLDRSVQQVNQEKQEKQH-----KLDTVSSKIELNRKLIQDQQEQIQHLKSTANELKSEKlqiSTNLQRRQQLEEQ 991
Cdd:TIGR01612 2041 LELSKQDKIKEKIDNYEKEKEKfgidfDVKAMEEKFDNDIKDIEKFENNYKHSEKDNHDFSEEK---DNIIQSKKKLKEL 2117
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 992 TVELSTEVQSLYREIKDAKEQLSPLETTlekfqqEKEELVNKKNTSHKIAQDKINEIKEKVKNIHSYMKDIENYIQDGKD 1071
Cdd:TIGR01612 2118 TEAFNTEIKIIEDKIIEKNDLIDKLIEM------RKECLLFSYATLVETLKSKVINHSEFITSAAKFSKDFFEFIEDISD 2191
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
674-1099 |
3.03e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 45.60 E-value: 3.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 674 KKQLEDWlHSKSKEInqTRDRLAKLNKELASAEQNKNHINI-----ELKRKEEQLSSYEdklfdvcgsQDFESDLDRLKE 748
Cdd:PRK04778 63 EEKFEEW-RQKWDEI--VTNSLPDIEEQLFEAEELNDKFRFrkakhEINEIESLLDLIE---------EDIEQILEELQE 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 749 EIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPvcqrgfqTEAELQEVISDLQSKLRLApDKLKSTESELKKKEKrrd 828
Cdd:PRK04778 131 LLESEEKNREEVEQLKDLYRELRKSLLANRFSFGP-------ALDELEKQLENLEEEFSQF-VELTESGDYVEAREI--- 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 829 emlgLVPMRQSIIDLKE--KEIPELRNKLQNVNRD-IQRLKNDIEEQEtllgaiipeeeSAKVCLTDVTIMERLQmelkD 905
Cdd:PRK04778 200 ----LDQLEEELAALEQimEEIPELLKELQTELPDqLQELKAGYRELV-----------EEGYHLDHLDIEKEIQ----D 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 906 VERKIAQQAAKLQGLDLDRsvqqVNQEKQEKQHKLDT--------VSSKIELNrKLIQDQQEQIQHLKSTANELKSEKLQ 977
Cdd:PRK04778 261 LKEQIDENLALLEELDLDE----AEEKNEEIQERIDQlydilereVKARKYVE-KNSDTLPDFLEHAKEQNKELKEEIDR 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 978 IStnlqrrqqleeQTVELSTEVQSLYREIKdakEQLSPLETTLEKFQQEkeelVNKKNTSHKIAQDKINEIKEKVKNIHS 1057
Cdd:PRK04778 336 VK-----------QSYTLNESELESVRQLE---KQLESLEKQYDEITER----IAEQEIAYSELQEELEEILKQLEEIEK 397
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 2015236753 1058 YMKDIENYIQDGKDDYKKQKETeLNKVIAQISECEKHKEKIN 1099
Cdd:PRK04778 398 EQEKLSEMLQGLRKDELEAREK-LERYRNKLHEIKRYLEKSN 438
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
285-918 |
3.07e-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: 45.60 E-value: 3.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 285 RYIKALET----LRQVRQTQGQKVKE-CQTELKYLKQNKEKACEIRDQitskeaQLTSSREIVKSYENEL----DPLKNR 355
Cdd:pfam12128 361 ERLKALTGkhqdVTAKYNRRRSKIKEqNNRDIAGIKDKLAKIREARDR------QLAVAEDDLQALESELreqlEAGKLE 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 356 LKE----IEQNLSKIMRLDNEIKALESRKKQMEKDNSELEQKMEKVFQGSDEQLNdlyhnhqrtvREKERRLVDCQRE-- 429
Cdd:pfam12128 435 FNEeeyrLKSRLGELKLRLNQATATPELLLQLENFDERIERAREEQEAANAEVER----------LQSELRQARKRRDqa 504
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 430 LEKLNKESRLLNQEKSELlvEQGRLQLQADRHqehmqardSLIQSLATQLELDGFELGPFSERQIKNFHKLVRERQEkes 509
Cdd:pfam12128 505 SEALRQASRRLEERQSAL--DELELQLFPQAG--------TLLHFLRKEAPDWEQSIGKVISPELLHRTDLDPEVWD--- 571
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 510 ETASQLLNDFTRKEALKQKQIDEIRDKKTGLGRIIELKSEILTKKQNELKNVKYELQQLEGSSDrilELDQELTKAEREL 589
Cdd:pfam12128 572 GSVGGELNLYGVKLDLKRIDVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELE---KASREETFARTAL 648
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 590 SKA-------------EKNSNVETLKTEVISLQNEKADLDRTLRKLDQEMEQLNHH---TAARTQMEMLNKDKA---DKD 650
Cdd:pfam12128 649 KNArldlrrlfdekqsEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEqkeQKREARTEKQAYWQVvegALD 728
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 651 EQIRKIKYRHSDELTSLLGYFpnkKQLEDWLHSKSKEINQTRDRLAKLNKELASAEQNKNhiNIELKRKE---------E 721
Cdd:pfam12128 729 AQLALLKAAIAARRSGAKAEL---KALETWYKRDLASLGVDPDVIAKLKREIRTLERKIE--RIAVRRQEvlryfdwyqE 803
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 722 QLSSYEDKLFDVCGS-----QDFESDLDRLKEEIEKSSKQRAMLAGAtavySQFITQLTDENQSCCPVCQRGF------Q 790
Cdd:pfam12128 804 TWLQRRPRLATQLSNieraiSELQQQLARLIADTKLRRAKLEMERKA----SEKQQVRLSENLRGLRCEMSKLatlkedA 879
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 791 TEAELQEVISDLQSKLRLAPDKLKStESELKKKEKRRDEMLGLVPMRQSIIDLKEKeipeLRNKLQNVNRDIQRLKNDIE 870
Cdd:pfam12128 880 NSEQAQGSIGERLAQLEDLKLKRDY-LSESVKKYVEHFKNVIADHSGSGLAETWES----LREEDHYQNDKGIRLLDYRK 954
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 2015236753 871 ---EQETLLGAIIPEEESA---KVCLTDVTIMERLQMeLKDVERKIAQQAAKLQ 918
Cdd:pfam12128 955 lvpYLEQWFDVRVPQSIMVlreQVSILGVDLTEFYDV-LADFDRRIASFSRELQ 1007
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
868-1059 |
3.26e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.68 E-value: 3.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 868 DIEEQETLLGAIIPEEESAKVCLTDVTIMERLQMELKDVERKIAQQAAKLQGLDLDRSVQQVNQEKQEKQHKLDTVSSKI 947
Cdd:COG4913 246 DAREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREEL 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 948 -ELNRKLIQDQQEQIQHLKSTANELKSEKLQISTNLQR---------------RQQLEEQTVELSTEVQSLYREIKDAKE 1011
Cdd:COG4913 326 dELEAQIRGNGGDRLEQLEREIERLERELEERERRRARleallaalglplpasAEEFAALRAEAAALLEALEEELEALEE 405
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2015236753 1012 QLSPLETTLEKFQQEKEELvnkkntshkiaQDKINEIKEKVKNIHSYM 1059
Cdd:COG4913 406 ALAEAEAALRDLRRELREL-----------EAEIASLERRKSNIPARL 442
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1303-1374 |
3.38e-04 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 45.06 E-value: 3.38e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2015236753 1303 SAGQKVlasliiRLALAETFCLNCGILALDEPTTNLDRENIESLAHALveiiksrsqqRNFQ--LLVITHDEDF 1374
Cdd:COG0488 154 SGGWRR------RVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFL----------KNYPgtVLVVSHDRYF 211
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
840-1099 |
3.41e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 45.30 E-value: 3.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 840 IIDLKEKE----IPELRNKLQNVNRDIQRLKNDIEEQEtllgaIIPEEESAKVCLTDVTIMERLQMELKDVERKIAQQAA 915
Cdd:PRK05771 33 IEDLKEELsnerLRKLRSLLTKLSEALDKLRSYLPKLN-----PLREEKKKVSVKSLEELIKDVEEELEKIEKEIKELEE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 916 KLQGLDldrsvqqvnQEKQEKQHKLDTVSSKIELNRKLIqdqqeqiqhlkstaNELKSEKLQISTNLQRRQQLEEQTVEL 995
Cdd:PRK05771 108 EISELE---------NEIKELEQEIERLEPWGNFDLDLS--------------LLLGFKYVSVFVGTVPEDKLEELKLES 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 996 STEVQSLYREIKD--------AKEQLSPLETTLEKFQQEKEELVNKKntshkIAQDKINEIKEKVKnihsymkDIENYIQ 1067
Cdd:PRK05771 165 DVENVEYISTDKGyvyvvvvvLKELSDEVEEELKKLGFERLELEEEG-----TPSELIREIKEELE-------EIEKERE 232
|
250 260 270
....*....|....*....|....*....|..
gi 2015236753 1068 DGKDDYKKQKETELNKVIAQISECEKHKEKIN 1099
Cdd:PRK05771 233 SLLEELKELAKKYLEELLALYEYLEIELERAE 264
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
1293-1371 |
4.04e-04 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 45.12 E-value: 4.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 1293 DTALDMRGRC-SAGQKVlasliiRLALAETFCLNCGILALDEPTTNLDRENIESLAHALVEIiksrsQQRNFQLLVITHD 1371
Cdd:COG4618 458 DTRIGEGGARlSGGQRQ------RIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRAL-----KARGATVVVITHR 526
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
303-1050 |
4.08e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 45.17 E-value: 4.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 303 KVKECQTELKYLKQNKEK----ACEIRDQITSKEAQLTSSREIVKSYENELDPLKNRLKEiEQNlskimRLDNEIKALes 378
Cdd:pfam01576 195 RLKKEEKGRQELEKAKRKlegeSTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEE-ETA-----QKNNALKKI-- 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 379 rkKQMEKDNSELEQKMEKvfqgsdeqlndlyHNHQRTVREKERRlvDCQRELEKLNKE-----------SRLLNQEKSEL 447
Cdd:pfam01576 267 --RELEAQISELQEDLES-------------ERAARNKAEKQRR--DLGEELEALKTEledtldttaaqQELRSKREQEV 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 448 LVEQGRLQLQADRH----QEHMQARDSLIQSLATQLEldgfELGPFSERQIKNFHKLVRERQE--KESETASQLLNDFTR 521
Cdd:pfam01576 330 TELKKALEEETRSHeaqlQEMRQKHTQALEELTEQLE----QAKRNKANLEKAKQALESENAElqAELRTLQQAKQDSEH 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 522 KEALKQKQIDEIRDKKTGLGRIIELKSEILTKKQNELKNVKYELQQLEGSSDRIL--------------ELDQELTKAER 587
Cdd:pfam01576 406 KRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSkdvsslesqlqdtqELLQEETRQKL 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 588 ELS------KAEKNSNVETLKTEVIS-------LQNEKADLDRTLRKLDQEMEQLNHHTAARTQM----EMLN---KDKA 647
Cdd:pfam01576 486 NLStrlrqlEDERNSLQEQLEEEEEAkrnverqLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLqrelEALTqqlEEKA 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 648 DKDEQIRKIKYRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQT--------------RDRLAKLNKE-------LASAE 706
Cdd:pfam01576 566 AAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMlaeekaisaryaeeRDRAEAEAREketralsLARAL 645
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 707 QNKNHINIELKRKEEQLSSyedKLFDVCGSQDfesDLDRLKEEIEKSskQRAMLAGATAVYSQfITQLTDENQSCCPVCQ 786
Cdd:pfam01576 646 EEALEAKEELERTNKQLRA---EMEDLVSSKD---DVGKNVHELERS--KRALEQQVEEMKTQ-LEELEDELQATEDAKL 716
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 787 R--------GFQTEAELQEVISDLQSKLRLAPDKLKSTESELkkKEKRRDEMLGLVPMRQSIIDLKEKE----------- 847
Cdd:pfam01576 717 RlevnmqalKAQFERDLQARDEQGEEKRRQLVKQVRELEAEL--EDERKQRAQAVAAKKKLELDLKELEaqidaankgre 794
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 848 --IPELRnKLQNVNRDIQRlknDIEE----QETLLGAIIPEEESAKVCLTDVTimeRLQMELKDVER------------- 908
Cdd:pfam01576 795 eaVKQLK-KLQAQMKDLQR---ELEEarasRDEILAQSKESEKKLKNLEAELL---QLQEDLAASERarrqaqqerdela 867
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 909 -KIAQQAAKLQGL-----DLDRSVQQVNQEKQEKQHKLDTVSSKielNRKLIQdQQEQIQhlkstaNELKSEKLQISTNL 982
Cdd:pfam01576 868 dEIASGASGKSALqdekrRLEARIAQLEEELEEEQSNTELLNDR---LRKSTL-QVEQLT------TELAAERSTSQKSE 937
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2015236753 983 QRRQQLEEQTVELSTEVQSLYREIKDA-KEQLSPLETTLEKFQQEKEELVNKKNTSHKIAQDKINEIKE 1050
Cdd:pfam01576 938 SARQQLERQNKELKAKLQEMEGTVKSKfKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKE 1006
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
269-720 |
4.39e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.13 E-value: 4.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 269 EGKALKQKFDEIFSATRYIKALETLRQvrqtQGQKVKECQTELKYLKQNKEKACEIR--DQITSKEAQLTSSREIVKSYE 346
Cdd:PTZ00121 1379 KADAAKKKAEEKKKADEAKKKAEEDKK----KADELKKAAAAKKKADEAKKKAEEKKkaDEAKKKAEEAKKADEAKKKAE 1454
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 347 NeldplknrlKEIEQNLSKimRLDNEIKALESRKKQMEKDNS-ELEQKMEKVFQGSDEQLNdlyhnhqrtvREKERRLVD 425
Cdd:PTZ00121 1455 E---------AKKAEEAKK--KAEEAKKADEAKKKAEEAKKAdEAKKKAEEAKKKADEAKK----------AAEAKKKAD 1513
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 426 CQRELEKLNKESRLLNQEKSELlVEQGRLQLQADRHQEHMQARDSLIQSLATQLEldgfELGPFSERQIKNFHK--LVRE 503
Cdd:PTZ00121 1514 EAKKAEEAKKADEAKKAEEAKK-ADEAKKAEEKKKADELKKAEELKKAEEKKKAE----EAKKAEEDKNMALRKaeEAKK 1588
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 504 RQEKESETASQLLNDFTRKEALKQKQIDEIRDKKTGLGRIIELKSEILTKKQNELKNVKYELQQLEGSSDRILELDQELT 583
Cdd:PTZ00121 1589 AEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAK 1668
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 584 KAERELSKAEKNSNVETLKTEVISLQNEKADLDRTLRKLDQEMEQLNHHTAARTQMEMLNKDKADKDEQIRKIKYRHSDE 663
Cdd:PTZ00121 1669 KAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEE 1748
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 2015236753 664 LTSLLGyfpNKKQLEDWLHSKSKEINQTRDRLAKLNKELASAEQNKNHINIELKRKE 720
Cdd:PTZ00121 1749 AKKDEE---EKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKD 1802
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1315-1371 |
4.54e-04 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 43.65 E-value: 4.54e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 2015236753 1315 RLALAETFCLNCGILALDEPTTNLDRenieSLAHALVEIIKSRSQQRNFQLLVITHD 1371
Cdd:cd03257 153 RVAIARALALNPKLLIADEPTSALDV----SVQAQILDLLKKLQEELGLTLLFITHD 205
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
135-206 |
4.67e-04 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 43.26 E-value: 4.67e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2015236753 135 LVGPNGAGKTTIIECLkyicTGDFPPgTKGNTFVHDpkvaqetdvraqirlqfRDVNGELVAVQRSM-LCTQK 206
Cdd:cd03263 33 LLGHNGAGKTTTLKML----TGELRP-TSGTAYING-----------------YSIRTDRKAARQSLgYCPQF 83
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
1303-1376 |
5.04e-04 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 43.41 E-value: 5.04e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2015236753 1303 SAGQKVLASLIIRLALAETFCLNCGI----LALDEPTTNLDRENIESLAHALVEIiksrsQQRNFQLLVITHDEDFVE 1376
Cdd:cd03279 125 SGGETFLASLSLALALSEVLQNRGGArleaLFIDEGFGTLDPEALEAVATALELI-----RTENRMVGVISHVEELKE 197
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
814-1012 |
5.41e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.38 E-value: 5.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 814 KSTESELKKKEKRRDemlglvpmrqSIIDLKEKEIPEL-RNKLQNVNRDIQRLKNDIEEQetllgaiipeeesakvcltd 892
Cdd:PRK12704 27 KIAEAKIKEAEEEAK----------RILEEAKKEAEAIkKEALLEAKEEIHKLRNEFEKE-------------------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 893 vtIMERLQmELKDVERKIAQQAAKL--QGLDLDRSVQQVNQEKQEKQHKLDTVSSKIELNRKLIQDQQEQIQHLKS-TAN 969
Cdd:PRK12704 77 --LRERRN-ELQKLEKRLLQKEENLdrKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGlTAE 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2015236753 970 ELKSEKLqistnlqrrQQLEEqtvELSTEVQSLYREI-KDAKEQ 1012
Cdd:PRK12704 154 EAKEILL---------EKVEE---EARHEAAVLIKEIeEEAKEE 185
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
342-1099 |
5.99e-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: 45.04 E-value: 5.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 342 VKSYENELDPLKNRLKEIEQNLSKIMRLDNEIKALESRKKQME-----KDNSELEQKME--KVFQGSDEQLNDLYHnhqR 414
Cdd:TIGR01612 1367 VKEYTKEIEENNKNIKDELDKSEKLIKKIKDDINLEECKSKIEstlddKDIDECIKKIKelKNHILSEESNIDTYF---K 1443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 415 TVREKERRLVDCQRELEKLNKESRLL-----NQEKSELLVEQGRLQLQADRHQEHMQARDSLIQSLATQLELdgfelgpf 489
Cdd:TIGR01612 1444 NADENNENVLLLFKNIEMADNKSQHIlkikkDNATNDHDFNINELKEHIDKSKGCKDEADKNAKAIEKNKEL-------- 1515
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 490 serqIKNFHKLVRERQEKESETAsqLLNDFTRKEALKQKQIDEIRDKKtglgRIIELKSEILTKKQNELKNVKYELQQLE 569
Cdd:TIGR01612 1516 ----FEQYKKDVTELLNKYSALA--IKNKFAKTKKDSEIIIKEIKDAH----KKFILEAEKSEQKIKEIKKEKFRIEDDA 1585
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 570 GSSDR----ILELDQELTKAEREL---SKAEKNSNVETLKTEVISLQNEKADLDRTLRKLDQEMEQLNhhtAARTQMEML 642
Cdd:TIGR01612 1586 AKNDKsnkaAIDIQLSLENFENKFlkiSDIKKKINDCLKETESIEKKISSFSIDSQDTELKENGDNLN---SLQEFLESL 1662
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 643 NKDKADKDEQIRKIkyrhsDELTSLLGYFPN-----KKQLEDWLHSKSKEInqtrdrlAKLNKElasaeqnknhiniELK 717
Cdd:TIGR01612 1663 KDQKKNIEDKKKEL-----DELDSEIEKIEIdvdqhKKNYEIGIIEKIKEI-------AIANKE-------------EIE 1717
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 718 RKEEQLSSYEDKLFDVCGSQDFESdLDRlKEEIEKSSKQRAMlagataVYSQFItQLTDENQSCCPVCQRGFQTEAELQE 797
Cdd:TIGR01612 1718 SIKELIEPTIENLISSFNTNDLEG-IDP-NEKLEEYNTEIGD------IYEEFI-ELYNIIAGCLETVSKEPITYDEIKN 1788
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 798 VISDLQSKLrlapdkLKSTESELKKKE-------KRRDEMLGLVPMRQSIIDLK-EKEIPELRNKLQNVNRDIQRLKNDI 869
Cdd:TIGR01612 1789 TRINAQNEF------LKIIEIEKKSKSylddieaKEFDRIINHFKKKLDHVNDKfTKEYSKINEGFDDISKSIENVKNST 1862
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 870 EEQetLLGAIIPEEESAKVcltdvTIMERLQMELKDVERKIAQQAAKLqGLDLDRSVQQ---VNQEKQEKQHKLDTVSSK 946
Cdd:TIGR01612 1863 DEN--LLFDILNKTKDAYA-----GIIGKKYYSYKDEAEKIFINISKL-ANSINIQIQNnsgIDLFDNINIAILSSLDSE 1934
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 947 IELNRKLI---QDQQEQIQHLKSTANELksekLQISTNLQRRQQLEEQTVELSTEVQSLYREIK---DAKEQLSPLETTL 1020
Cdd:TIGR01612 1935 KEDTLKFIpspEKEPEIYTKIRDSYDTL----LDIFKKSQDLHKKEQDTLNIIFENQQLYEKIQasnELKDTLSDLKYKK 2010
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 1021 EKFQQEKEELVNKKNTSHKIAQD-----------KINEIKEKVKNihsYMKDIENYIQDGKDDYKKQKETELNKVIAQIS 1089
Cdd:TIGR01612 2011 EKILNDVKLLLHKFDELNKLSCDsqnydtilelsKQDKIKEKIDN---YEKEKEKFGIDFDVKAMEEKFDNDIKDIEKFE 2087
|
810
....*....|
gi 2015236753 1090 ECEKHKEKIN 1099
Cdd:TIGR01612 2088 NNYKHSEKDN 2097
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
763-991 |
6.02e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.62 E-value: 6.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 763 ATAVYSQFITQLTDENQsccpvcqrgfqteAELQEVISDLQSKLRLAPDKLKSTESELKK-KEKrrdemlglvpmrQSII 841
Cdd:COG3206 154 ANALAEAYLEQNLELRR-------------EEARKALEFLEEQLPELRKELEEAEAALEEfRQK------------NGLV 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 842 DLKEkEIPELRNKLQNVNRDIQRLKNDIEEQETLLGAI---IPEEESAKVCLTDVTIMERLQMELKDVERKIAQQAAKLQ 918
Cdd:COG3206 209 DLSE-EAKLLLQQLSELESQLAEARAELAEAEARLAALraqLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYT 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 919 G-----LDLDRSVQQVNQE-KQEKQHKLDTVSSKIELNRKLIQDQQEQIQHLKSTANELKSE---------KLQISTN-- 981
Cdd:COG3206 288 PnhpdvIALRAQIAALRAQlQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELeaelrrlerEVEVAREly 367
|
250
....*....|...
gi 2015236753 982 ---LQRRQQLEEQ 991
Cdd:COG3206 368 eslLQRLEEARLA 380
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
587-731 |
6.27e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 44.46 E-value: 6.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 587 RELSKAEKNSNVETLKTEVISLQNEKADLDRTLRKLDQEMEQLNHHTaartqmEMLNKDKADKDEQIRKIKYRHSDElts 666
Cdd:COG2433 383 EELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEV------EELEAELEEKDERIERLERELSEA--- 453
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2015236753 667 llgyfpnkKQLEDWLHSKSKEINQTRDRLAKLNKELASAEQNKNhiniELKRKEEQLSSYEDKLF 731
Cdd:COG2433 454 --------RSEERREIRKDREISRLDREIERLERELEEERERIE----ELKRKLERLKELWKLEH 506
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
1303-1370 |
8.18e-04 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 42.20 E-value: 8.18e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2015236753 1303 SAGQKVlasliiRLALAETFCLNCGILALDEPTTNLDRENIESLAHALVEiIKSRSQQRnfqlLVITH 1370
Cdd:cd03246 98 SGGQRQ------RLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIAA-LKAAGATR----IVIAH 154
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1315-1382 |
8.19e-04 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 42.81 E-value: 8.19e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2015236753 1315 RLALAETFCLNCGILALDEPTTNLDRENieslAHALVEIIKSRSQQRNFQLLVITHDEdfvELLGRSE 1382
Cdd:COG4181 154 RVALARAFATEPAILFADEPTGNLDAAT----GEQIIDLLFELNRERGTTLVLVTHDP---ALAARCD 214
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
811-1042 |
9.04e-04 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 43.53 E-value: 9.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 811 DKLKSTESELKKKEK-------RRDEMLGLVPMRQSIIDLKEKEIPELRNKLQNVNRDIQRLKNDIEeqetllgaiipee 883
Cdd:PRK11637 47 DQLKSIQQDIAAKEKsvrqqqqQRASLLAQLKKQEEAISQASRKLRETQNTLNQLNKQIDELNASIA------------- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 884 esakvcltdvtimeRLQMELKDVERKIAQQ--AA----KLQGLDLDRSvqqvNQEKQEKQHKLDTVSSkieLNrkliQDQ 957
Cdd:PRK11637 114 --------------KLEQQQAAQERLLAAQldAAfrqgEHTGLQLILS----GEESQRGERILAYFGY---LN----QAR 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 958 QEQIQHLKSTANELKSEKLQISTNLQRRQQL--EEQTVELSTEVQSLYReikdaKEQLSPLETTLEKFQQEKEEL-VNKK 1034
Cdd:PRK11637 169 QETIAELKQTREELAAQKAELEEKQSQQKTLlyEQQAQQQKLEQARNER-----KKTLTGLESSLQKDQQQLSELrANES 243
|
....*...
gi 2015236753 1035 NTSHKIAQ 1042
Cdd:PRK11637 244 RLRDSIAR 251
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
896-1078 |
1.01e-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: 43.86 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 896 MERLQMELKDVERKIAQqaAKLQGLDLDRSVQQVNQEKQEKQHKLDTVSSKIELNRKLI---QDQQEQIQHLKSTANELK 972
Cdd:pfam05667 337 LEELQEQLEDLESSIQE--LEKEIKKLESSIKQVEEELEELKEQNEELEKQYKVKKKTLdllPDAEENIAKLQALVDASA 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 973 SEKLQIS-----------------------TNLQRRQQLEEqtvelsteVQSLYREIKDAKEQLSPLETTLEKFQQEKEE 1029
Cdd:pfam05667 415 QRLVELAgqwekhrvplieeyralkeaksnKEDESQRKLEE--------IKELREKIKEVAEEAKQKEELYKQLVAEYER 486
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2015236753 1030 LVNKKNTSHKIaqDKINEIkekVKNIHSYMKDIENYIQDGKDdykKQKE 1078
Cdd:pfam05667 487 LPKDVSRSAYT--RRILEI---VKNIKKQKEEITKILSDTKS---LQKE 527
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
1293-1370 |
1.05e-03 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 43.49 E-value: 1.05e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2015236753 1293 DTALDMRGR-CSAGQKVlasliiRLALAETFCLNCGILALDEPTTNLDRENIESLAHALVEIiksrsQQRNFQLLVITH 1370
Cdd:TIGR01842 445 DTVIGPGGAtLSGGQRQ------RIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKAL-----KARGITVVVITH 512
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
418-763 |
1.10e-03 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 43.52 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 418 EKERRLVDCQRELEKLNKESRLLNQEKSELLVEQGRLQLQADRHQEHMQARDSLIQSLATQL-----ELDGFELGPFSE- 491
Cdd:pfam19220 52 ELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVARLAKLEAALREAEAAKEELRIELrdktaQAEALERQLAAEt 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 492 RQIKNFHKLVRERQEkESETASQLLNDFTRKEALKQKQIDEIRDKKTGLGRIIELKS-EI--LTKKQNELKnvkyelQQL 568
Cdd:pfam19220 132 EQNRALEEENKALRE-EAQAAEKALQRAEGELATARERLALLEQENRRLQALSEEQAaELaeLTRRLAELE------TQL 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 569 EGSSDRILELDQEL--TKAERELSKAEKNSNVETLKTEVISLQNEKADLDRTLRKLDQEMEQLNHHTAARTQmEMLNKDK 646
Cdd:pfam19220 205 DATRARLRALEGQLaaEQAERERAEAQLEEAVEAHRAERASLRMKLEALTARAAATEQLLAEARNQLRDRDE-AIRAAER 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 647 ADKDEQI-RKIKYRHSDELtsllgyfpnKKQLEDwLHSKSKEINQTR----DRLAKLNKELASAEqnknhinIELKRKEE 721
Cdd:pfam19220 284 RLKEASIeRDTLERRLAGL---------EADLER-RTQQFQEMQRARaeleERAEMLTKALAAKD-------AALERAEE 346
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 2015236753 722 QLSSYEDKL------FDVcGSQDFESDLDRLKEEIEKSSKQRAMLAGA 763
Cdd:pfam19220 347 RIASLSDRIaeltkrFEV-ERAALEQANRRLKEELQRERAERALAQGA 393
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
272-447 |
1.40e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 43.57 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 272 ALKQKfdeIFSATRYIKALETLRQVRQTQGQKVKECQTELKYLKQNKEKACE-IRDQITSKEAQLTSSR---EIVKSYEN 347
Cdd:pfam17380 401 ARKVK---ILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMErVRLEEQERQQQVERLRqqeEERKRKKL 477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 348 ELDPLKNRLKEIEQNLSKIMRldneiKALESRKKQM---EKDNSELEQKMEkvfqgsdEQLNDLYHNHQRTVREKERRLV 424
Cdd:pfam17380 478 ELEKEKRDRKRAEEQRRKILE-----KELEERKQAMieeERKRKLLEKEME-------ERQKAIYEEERRREAEEERRKQ 545
|
170 180
....*....|....*....|...
gi 2015236753 425 DCQRELEKLNKESRLLNQEKSEL 447
Cdd:pfam17380 546 QEMEERRRIQEQMRKATEERSRL 568
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
1315-1371 |
1.61e-03 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 41.27 E-value: 1.61e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 2015236753 1315 RLALAETFCLNCGILALDEPTTNLDreniesLAH--ALVEIIKSRSQQRNFQLLVITHD 1371
Cdd:cd03214 105 RVLLARALAQEPPILLLDEPTSHLD------IAHqiELLELLRRLARERGKTVVMVLHD 157
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
936-1231 |
1.64e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 43.35 E-value: 1.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 936 KQHKLDTVSSKIELNRKLIQDQQEQIQHLKSTANELKSEKLQISTNLQRRQQLEEqtvelstEVQSLYREIKDAKEQLSP 1015
Cdd:PRK01156 136 GQGEMDSLISGDPAQRKKILDEILEINSLERNYDKLKDVIDMLRAEISNIDYLEE-------KLKSSNLELENIKKQIAD 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 1016 LETTLEKFQQEKEELVNKKNtshkIAQDKINEIKEKVKNIHSYMKDIENYIQD-GKDDYKKQKETELNKVIAQISecEKH 1094
Cdd:PRK01156 209 DEKSHSITLKEIERLSIEYN----NAMDDYNNLKSALNELSSLEDMKNRYESEiKTAESDLSMELEKNNYYKELE--ERH 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 1095 KEKINKEMGIMRqdidtQKIQERWLQDNLTLRKRNEELKEVEEERKQH--LKEMGQMQ-----VLQMKNEHQKLEEKIDN 1167
Cdd:PRK01156 283 MKIINDPVYKNR-----NYINDYFKYKNDIENKKQILSNIDAEINKYHaiIKKLSVLQkdyndYIKKKSRYDDLNNQILE 357
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2015236753 1168 IKRNHSLAIGRQKGYeEEIIHFKKELREPQFRDAEEKYREMMIIMRTTELVNKDLDIYYKTLDQ 1231
Cdd:PRK01156 358 LEGYEMDYNSYLKSI-ESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQD 420
|
|
| CagA_N |
pfam18971 |
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial ... |
921-1163 |
1.79e-03 |
|
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial virulence determinant and critical for gastric carcinogenesis. X-ray crystallographic analysis of the N-terminal CagA fragment (residues 1-876) revealed that the region has a structure comprised of three discrete domains. Domain I constitutes a mobile CagA N terminus, while Domain II tethers CagA to the plasma membrane by interacting with membrane phosphatidylserine. Domain III interacts intramolecularly with the intrinsically disordered C-terminal region, and this interaction potentiates the pathogenic scaffold/hub function of CagA.
Pssm-ID: 408741 [Multi-domain] Cd Length: 876 Bit Score: 43.22 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 921 DLDRSVQQVNQEKQEKQHKLDTVSSKielnrkliQDQQEQiqhlKSTANelkSEKLQISTNLQRRQQLEEQTVELSTEVQ 1000
Cdd:pfam18971 618 DLEKSLRKREHLEKEVEKKLESKSGN--------KNKMEA----KAQAN---SQKDEIFALINKEANRDARAIAYTQNLK 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 1001 SLYREIKDAKEQLSpleTTLEKFQQEKEELVNKKNTSHKIAQDKINEIKEKVKNIH---SYMKDIENyIQDGKDDYKKQK 1077
Cdd:pfam18971 683 GIKRELSDKLEKIS---KDLKDFSKSFDEFKNGKNKDFSKAEETLKALKGSVKDLGinpEWISKVEN-LNAALNEFKNGK 758
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 1078 ETELNKVIAQISECEKHKEKInkemgimrqdIDTQKIQERwlQDNLTLRKRNEELKEVEEERKQHLKEMGQMQVLQMKNE 1157
Cdd:pfam18971 759 NKDFSKVTQAKSDLENSVKDV----------IINQKVTDK--VDNLNQAVSVAKAMGDFSRVEQVLADLKNFSKEQLAQQ 826
|
....*.
gi 2015236753 1158 HQKLEE 1163
Cdd:pfam18971 827 AQKNED 832
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
549-1110 |
1.87e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 43.24 E-value: 1.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 549 EILTKKQNELKNVKYELQQLEGSSdrileldQELTKAERELSkAEKNSNVETLKTEViSLQNEKADLDRTLRKLDQEMEQ 628
Cdd:pfam01576 5 EEMQAKEEELQKVKERQQKAESEL-------KELEKKHQQLC-EEKNALQEQLQAET-ELCAEAEEMRARLAARKQELEE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 629 LNHHTAARTQMEmlnKDKADKDEQIRKIKYRHSDELtsllgyfpnKKQLEDWLHSKSK---EINQTRDRLAKLNKELASA 705
Cdd:pfam01576 76 ILHELESRLEEE---EERSQQLQNEKKKMQQHIQDL---------EEQLDEEEAARQKlqlEKVTTEAKIKKLEEDILLL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 706 EQNKNHINIELKRKEEQLSSYEDKlfdvcgsqdfesdldrLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVC 785
Cdd:pfam01576 144 EDQNSKLSKERKLLEERISEFTSN----------------LAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELE 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 786 QRGFQTEAE---LQEVISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLVPMRQSIIDLKEKEIPEL----------R 852
Cdd:pfam01576 208 KAKRKLEGEstdLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELqedleseraaR 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 853 NKLQNVNRDI---------------------QRLKNDIEEQETLLGAIIPEE-ESAKVCLTDV-----TIMERLQMELKD 905
Cdd:pfam01576 288 NKAEKQRRDLgeelealkteledtldttaaqQELRSKREQEVTELKKALEEEtRSHEAQLQEMrqkhtQALEELTEQLEQ 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 906 VER-----KIAQQAAKLQGLDLDRSVQQVNQEKQEKQHKLDTVSSKI-ELNRKLiQDQQEQIQHLKSTANELKSEKLQIS 979
Cdd:pfam01576 368 AKRnkanlEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLqELQARL-SESERQRAELAEKLSKLQSELESVS 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 980 TNLqrrQQLEEQTVELSTEVQSLYREIKDAKEQLSP-------LETTLEKFQQEK--------EELVNKKNTSHKI--AQ 1042
Cdd:pfam01576 447 SLL---NEAEGKNIKLSKDVSSLESQLQDTQELLQEetrqklnLSTRLRQLEDERnslqeqleEEEEAKRNVERQLstLQ 523
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2015236753 1043 DKINEIKEKVKNIHSYMKDIEnyiqdgkdDYKKQKETELNKVIAQISECEKHKEKINKEMGIMRQDID 1110
Cdd:pfam01576 524 AQLSDMKKKLEEDAGTLEALE--------EGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELD 583
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
1291-1371 |
2.03e-03 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 41.36 E-value: 2.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 1291 KGDTALDMRG------RC----SAGQKVlasliiRLALAETFCLNCGILALDEPTTNLDRENIEslahALVEIIKsRSQQ 1360
Cdd:cd03235 112 KVDEALERVGlseladRQigelSGGQQQ------RVLLARALVQDPDLLLLDEPFAGVDPKTQE----DIYELLR-ELRR 180
|
90
....*....|.
gi 2015236753 1361 RNFQLLVITHD 1371
Cdd:cd03235 181 EGMTILVVTHD 191
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
288-1029 |
2.29e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 42.85 E-value: 2.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 288 KALETLRQvRQTQGQKVKECQTELK----YLKQNKEKACEIRDQITSKEAQLTSSREIVKSYENELDPLKNRLKEIEQNL 363
Cdd:pfam01576 420 RLSESERQ-RAELAEKLSKLQSELEsvssLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLEDER 498
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 364 SKIM-RLDNEIKALESRKKQMEKDN---SELEQKMEKvFQGSDEQLNDLYHNHQRTVREKERRLVDCQRELEKLNKESRL 439
Cdd:pfam01576 499 NSLQeQLEEEEEAKRNVERQLSTLQaqlSDMKKKLEE-DAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNR 577
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 440 LNQEKSELLVEQGRLQlqadrhqehmqardSLIQSLatqleldgfelgpfsERQIKNFHKLVRErqekESETASQLLNDF 519
Cdd:pfam01576 578 LQQELDDLLVDLDHQR--------------QLVSNL---------------EKKQKKFDQMLAE----EKAISARYAEER 624
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 520 TRKEAlkqkqidEIRDKKT---GLGRIIELKSEILTKKQNELKNVKYELQQLEGSSDRILELDQELTKAERELSKAekns 596
Cdd:pfam01576 625 DRAEA-------EAREKETralSLARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQ---- 693
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 597 nVETLKTEVISLQNE-KADLDRTLRkLDQEMEqlnhhtAARTQMEMLNKDKADKDEQIRKIKYRHSDELTSLLGyfPNKK 675
Cdd:pfam01576 694 -VEEMKTQLEELEDElQATEDAKLR-LEVNMQ------ALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELE--DERK 763
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 676 QLEDWLHSKSK-EINqtrdrLAKLNKELASAEQNKNHINIELKRKEEQLSSYEDKLFDVCGSQDfesdlDRLKEEIEKSS 754
Cdd:pfam01576 764 QRAQAVAAKKKlELD-----LKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARASRD-----EILAQSKESEK 833
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 755 KQRAMLAGatavysqfITQLTDENQSCCPVCQRGFQTEAELQEVISDLQSKlrlapdklKSTESElkkkEKRRDEmlglv 834
Cdd:pfam01576 834 KLKNLEAE--------LLQLQEDLAASERARRQAQQERDELADEIASGASG--------KSALQD----EKRRLE----- 888
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 835 pmrQSIIDLKEkEIPELRNKLQNVNRDIQRLKNDIEEQETLLGAiipEEESAKVCLTDVTIMERLQMELKdverkiaqqa 914
Cdd:pfam01576 889 ---ARIAQLEE-ELEEEQSNTELLNDRLRKSTLQVEQLTTELAA---ERSTSQKSESARQQLERQNKELK---------- 951
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 915 AKLQGLDldrsvqqvNQEKQEKQHKLDTVSSKI-ELNRKLIQDQQEQIQH---LKSTANELKSEKLQISTNLQRRQQLEE 990
Cdd:pfam01576 952 AKLQEME--------GTVKSKFKSSIAALEAKIaQLEEQLEQESRERQAAnklVRRTEKKLKEVLLQVEDERRHADQYKD 1023
|
730 740 750
....*....|....*....|....*....|....*....
gi 2015236753 991 QTVELSTEVQSLYREIKDAKEQLSPLETTLEKFQQEKEE 1029
Cdd:pfam01576 1024 QAEKGNSRMKQLKRQLEEAEEEASRANAARRKLQRELDD 1062
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
498-1025 |
2.38e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 42.87 E-value: 2.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 498 HKLVRERQEK-ESETASQLLNDFTRKEALKQKQIDEIRDKKTGLGRIIELKSEI--LTKkQNELKnvkyelQQLEGSSDR 574
Cdd:PRK10246 193 HKSARTELEKlQAQASGVALLTPEQVQSLTASLQVLTDEEKQLLTAQQQQQQSLnwLTR-LDELQ------QEASRRQQA 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 575 ILELDQELTKAERELSKAEKNSNVETLKTEVISLQNEKADLDRTLRKLDQEMEQLNHHTAARTqmemlnkdkadkdeQIR 654
Cdd:PRK10246 266 LQQALAAEEKAQPQLAALSLAQPARQLRPHWERIQEQSAALAHTRQQIEEVNTRLQSTMALRA--------------RIR 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 655 KIKYRHSDELTSLLGyfpnkkQLEDWLHskskeinqTRDRLAKLNKELAS-----AEQNKNHinIELKRKEEQLSSYEDK 729
Cdd:PRK10246 332 HHAAKQSAELQAQQQ------SLNTWLA--------EHDRFRQWNNELAGwraqfSQQTSDR--EQLRQWQQQLTHAEQK 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 730 LfDVCGSQDFESDLDRLKEEIEKSSKQRAMLAGATAVYSQFItqltdenqsccPVCQRgfqtEAELQEVISDLQSKLRLA 809
Cdd:PRK10246 396 L-NALPAITLTLTADEVAAALAQHAEQRPLRQRLVALHGQIV-----------PQQKR----LAQLQVAIQNVTQEQTQR 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 810 PDKLksTESELKKKEKrrdemlglvpmRQSIIDLK---EKEipelrnklqnvnrdiQRLKnDIEEQETLLGA-------- 878
Cdd:PRK10246 460 NAAL--NEMRQRYKEK-----------TQQLADVKticEQE---------------ARIK-DLEAQRAQLQAgqpcplcg 510
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 879 --IIPEEESAKVCLTDVTIMERLQMElKDVErKIAQQAAKLQGlDLDRSVQQVNQEKQEKQhkldtvsskielnrKLIQD 956
Cdd:PRK10246 511 stSHPAVEAYQALEPGVNQSRLDALE-KEVK-KLGEEGAALRG-QLDALTKQLQRDESEAQ--------------SLRQE 573
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2015236753 957 QQ---EQIQHLKSTANELKSEKLQISTNLQRRQQLEEQTVELStEVQSLYREIKDAKEQLSPLETTLEKFQQ 1025
Cdd:PRK10246 574 EQaltQQWQAVCASLNITLQPQDDIQPWLDAQEEHERQLRLLS-QRHELQGQIAAHNQQIIQYQQQIEQRQQ 644
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
897-1110 |
2.43e-03 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 41.28 E-value: 2.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 897 ERLQMELKDVERKIAQQAAKLQGLDLDRSVQQVnQEKQEKQHKLdtvsskielnRKLIQDQQEQIQHLKSTANELKSEKL 976
Cdd:cd00176 3 QQFLRDADELEAWLSEKEELLSSTDYGDDLESV-EALLKKHEAL----------EAELAAHEERVEALNELGEQLIEEGH 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 977 QISTNLQRRQQ-LEEQTVELSTEVQSLYREIKDAKEQLSPLETT--LEKFQQEKEELVNKKNT--SHKIAQDKINEIKEK 1051
Cdd:cd00176 72 PDAEEIQERLEeLNQRWEELRELAEERRQRLEEALDLQQFFRDAddLEQWLEEKEAALASEDLgkDLESVEELLKKHKEL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2015236753 1052 VKNIHSYMKDIENYIQDGKDDYKKQKETELNKVIAQISECEKHKEKINKEMGIMRQDID 1110
Cdd:cd00176 152 EEELEAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLE 210
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1303-1375 |
2.44e-03 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 42.58 E-value: 2.44e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2015236753 1303 SAGQKVlasliiRLALAETFCLNCGILALDEPTTNLDreniESLAHALVEIIKSRSQQRNFQLLVITHDEDFV 1375
Cdd:COG1123 144 SGGQRQ------RVAIAMALALDPDLLIADEPTTALD----VTTQAEILDLLRELQRERGTTVLLITHDLGVV 206
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
290-479 |
2.63e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 42.64 E-value: 2.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 290 LETLRQVRQTQGQKVKECQTEL---KYLKQNKEKA----CEIRDQITSKEAQlTSSREIVKSYENE------LDPLKNRL 356
Cdd:PRK04863 444 LEEFQAKEQEATEELLSLEQKLsvaQAAHSQFEQAyqlvRKIAGEVSRSEAW-DVARELLRRLREQrhlaeqLQQLRMRL 522
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 357 KEIEQNLSKIMRLDNEIKALESRKKQMEKDNSELEQkmekVFQGSDEQLNDLyHNHQRTVREkerRLVDCQRELEKLNKE 436
Cdd:PRK04863 523 SELEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQ----LQEELEARLESL-SESVSEARE---RRMALRQQLEQLQAR 594
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2015236753 437 SRLLNQEKSELLVEQ---GRLQLQADRHQEHMQARDSLIQSLATQL 479
Cdd:PRK04863 595 IQRLAARAPAWLAAQdalARLREQSGEEFEDSQDVTEYMQQLLERE 640
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
302-468 |
2.84e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.07 E-value: 2.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 302 QKVKECQTELKYLKqnKEKACEIRDQITSKEAQLtsSREiVKSYENELDPLKNRLKEIEQNLskimrlDNEIKALESRKK 381
Cdd:PRK12704 42 RILEEAKKEAEAIK--KEALLEAKEEIHKLRNEF--EKE-LRERRNELQKLEKRLLQKEENL------DRKLELLEKREE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 382 QMEKDNSELEQKMEKVfqgsDEQlndlyhnhQRTVREKErrlvdcQRELEKLNKESRLLNQEKSELLVEQGRLQLQADR- 460
Cdd:PRK12704 111 ELEKKEKELEQKQQEL----EKK--------EEELEELI------EEQLQELERISGLTAEEAKEILLEKVEEEARHEAa 172
|
170
....*....|.
gi 2015236753 461 ---HQEHMQAR 468
Cdd:PRK12704 173 vliKEIEEEAK 183
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
1293-1370 |
3.05e-03 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 42.07 E-value: 3.05e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2015236753 1293 DTALDMRG-RCSAGQKVlasliiRLALAETFCLNCGILALDEPTTNLDRENIESLAHALVEIIKSRSqqrnfqLLVITH 1370
Cdd:COG1132 467 DTVVGERGvNLSGGQRQ------RIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRT------TIVIAH 533
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
105-153 |
3.15e-03 |
|
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural maintenance of chromosomes (SMC) proteins are essential for successful chromosome transmission during replication and segregation of the genome in all organisms. SMCs are generally present as single proteins in bacteria, and as at least six distinct proteins in eukaryotes. The proteins range in size from approximately 110 to 170 kDa, and each has five distinct domains: amino- and carboxy-terminal globular domains, which contain sequences characteristic of ATPases, two coiled-coil regions separating the terminal domains , and a central flexible hinge. SMC proteins function together with other proteins in a range of chromosomal transactions, including chromosome condensation, sister-chromatid cohesion, recombination, DNA repair, and epigenetic silencing of gene expression.
Pssm-ID: 213206 [Multi-domain] Cd Length: 178 Bit Score: 40.37 E-value: 3.15e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2015236753 105 IEKMSIQGVRSFGiedkDKQIITFFSPLTILVGPNGAGKTTIIECLKYI 153
Cdd:cd03239 1 IKQITLKNFKSYR----DETVVGGSNSFNAIVGPNGSGKSNIVDAICFV 45
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1315-1372 |
3.35e-03 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 40.92 E-value: 3.35e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 2015236753 1315 RLALAETFCLNCGILALDEPTTNLDRENIESLAHALVeiikSRSQQRNFQLLVITHDE 1372
Cdd:PRK10584 154 RVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLF----SLNREHGTTLILVTHDL 207
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
269-1183 |
3.53e-03 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 42.51 E-value: 3.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 269 EGKALKQKFDEIFSATR-YIKALETLRQVRQTqgqkVKECQTELKYLKQNKEKACEIRDQItSKEAQLTSSREIVKSYEN 347
Cdd:PTZ00440 857 EFNENNQIVDNIIKDIEnMNKNINIIKTLNIA----INRSNSNKQLVEHLLNNKIDLKNKL-EQHMKIINTDNIIQKNEK 931
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 348 EldPLKNRLKEIEQNLSKimRLDNEikALESRKKQMEKDNSELEQkmekvfqgSDEQLNDLYHNHQRTVREKERRLVDCQ 427
Cdd:PTZ00440 932 L--NLLNNLNKEKEKIEK--QLSDT--KINNLKMQIEKTLEYYDK--------SKENINGNDGTHLEKLDKEKDEWEHFK 997
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 428 RELEKLNKESRLLNQEKSELLVEQgrlqlqadrHQEHMQARDSLIQSLATQLELdgfelgpfserQIKNFHKLVRERQEK 507
Cdd:PTZ00440 998 SEIDKLNVNYNILNKKIDDLIKKQ---------HDDIIELIDKLIKEKGKEIEE-----------KVDQYISLLEKMKTK 1057
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 508 esetasqlLNDFTRKEALKQKQIDEIRDKKTGLgriiELKSEILTKKQNELKNvkyELQQLEG-SSDRILELDQELTKAE 586
Cdd:PTZ00440 1058 --------LSSFHFNIDIKKYKNPKIKEEIKLL----EEKVEALLKKIDENKN---KLIEIKNkSHEHVVNADKEKNKQT 1122
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 587 RELSKAEKN-----SNVETLKTEVISLQNE--------KADLDRTLRKLDQEMEQLNHH-TAARTQMEMLNKDKADKDEQ 652
Cdd:PTZ00440 1123 EHYNKKKKSlekiyKQMEKTLKELENMNLEditlnevnEIEIEYERILIDHIVEQINNEaKKSKTIMEEIESYKKDIDQV 1202
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 653 IRKIKYRHSDELTSLlgyfpNKKQLEDWLHSKSKEINQTrDRLAKLNKELASAEQNKNhiniELKRKEEQLSSYedklfd 732
Cdd:PTZ00440 1203 KKNMSKERNDHLTTF-----EYNAYYDKATASYENIEEL-TTEAKGLKGEANRSTNVD----ELKEIKLQVFSY------ 1266
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 733 vcgsqdfesdldrLKEEIEKSSKQRAMLAGATAVYSQFITQLTDEnqsccpVCQRGFQTEAELQEVISDLQSKLRLAPDK 812
Cdd:PTZ00440 1267 -------------LQQVIKENNKMENALHEIKNMYEFLISIDSEK------ILKEILNSTKKAEEFSNDAKKELEKTDNL 1327
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 813 LKSTESELKKKEKRRDEMLGlvpmrqsiiDLKEKEIPELRNKLQNVNRDIQRLKNDIEEQetllgaiIPEEESAKvcltd 892
Cdd:PTZ00440 1328 IKQVEAKIEQAKEHKNKIYG---------SLEDKQIDDEIKKIEQIKEEISNKRKEINKY-------LSNIKSNK----- 1386
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 893 vtimERLQMELKDVERKIAqqaaKLQGLDLDRSVQQVNQEKQEKQHKLDTvsskielnrklIQDQQEQIQHLKSTANELK 972
Cdd:PTZ00440 1387 ----EKCDLHVRNASRGKD----KIDFLNKHEAIEPSNSKEVNIIKITDN-----------INKCKQYSNEAMETENKAD 1447
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 973 SEKlqistnlqrrqqleEQTVELSTEVQSLYREIkdakeQLSPLETTLEKFQQEKEELVNKKNTSHKIAQDKINEIKEKV 1052
Cdd:PTZ00440 1448 ENN--------------DSIIKYEKEITNILNNS-----SILGKKTKLEKKKKEATNIMDDINGEHSIIKTKLTKSSEKL 1508
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 1053 KNI---HSYMKDIENYIQDGKDDYKKQKETELNKVIAQISECEKHKEKI----NKEMGIMRQDIDTQKIQErwlqdNLTL 1125
Cdd:PTZ00440 1509 NQLneqPNIKREGDVLNNDKSTIAYETIQYNLGRVKHNLLNILNIKDEIetilNKAQDLMRDISKISKIVE-----NKNL 1583
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....*...
gi 2015236753 1126 RKRNEELKEVEEERKQHLKEMGQMQvlqmkNEHQKLEEKIDNIKRNHSLAIGRQKGYE 1183
Cdd:PTZ00440 1584 ENLNDKEADYVKYLDNILKEKQLME-----AEYKKLNEIYSDVDNIEKELKKHKKNYE 1636
|
|
| ATG17_like |
pfam04108 |
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ... |
850-1071 |
3.72e-03 |
|
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ATG17 and ATG11, conserved across eukaryotes. ATG17 forms a complex with ATG29 and ATG31, critical for both PAS (preautophagosomal structure) formation and autophagy. Together with ATG13, it is required for ATG1 kinase activation. ATG11 is a scaffold protein required for the cytoplasm-to-vacuole targeting (Cvt) pathway during starvation and to recruit ATG proteins to the pre-autophagosome. It is also required for ATG1 kinase activation. In many eukaryotes, ATG11 (the orthologue in mammals is RB1-inducible coiled-coil protein 1 (RB1CC1) and in S. pombe is Taz1-interacting factor 1 (taf1)) is essential for bulk autophagy, except in S.cerevisiae. ATG17 and ATG11 are large similar proteins, both predicted to be almost entirely helical, containing conserved coiled-coil regions and lack obvious functional motifs.
Pssm-ID: 427715 [Multi-domain] Cd Length: 360 Bit Score: 41.60 E-value: 3.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 850 ELRNKLQNVNRDIQRLKNDIEE-QETLLGAIIPEEESAKVCLTD---VTIMERLQMELKDVERKIAQQAAKLQG--LDLD 923
Cdd:pfam04108 64 DFKQLLKDLDAALERLEETLDKlRNTPVEPALPPGEEKQKTLLDfidEDSVEILRDALKELIDELQAAQESLDSdlKRFD 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 924 RSVQQVNQEKQEKQHKLDTVSSKIELNRKLIQDQQEQIQHLKSTANELKSEKLQISTNLQRRQQLEEQTVELSTEVQSLY 1003
Cdd:pfam04108 144 DDLRDLQKELESLSSPSESISLIPTLLKELESLEEEMASLLESLTNHYDQCVTAVKLTEGGRAEMLEVLENDARELDDVV 223
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2015236753 1004 REIKDAKEQLSPLETTLEKFQQEKEELvnkKNTSHKIAQDkINEIKEKVKNIHSYMKDIENYIQDGKD 1071
Cdd:pfam04108 224 PELQDRLDEMENNYERLQKLLEQKNSL---IDELLSALQL-IAEIQSRLPEYLAALKEFEERWEEEKE 287
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
1301-1378 |
3.77e-03 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 40.07 E-value: 3.77e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2015236753 1301 RCSAGQKvlasliIRLALAETFCLNCGILALDEPTTNLDRENieslAHALVEIIKSRSqQRNFQLLVITHDEDFVELL 1378
Cdd:cd03230 95 KLSGGMK------QRLALAQALLHDPELLILDEPTSGLDPES----RREFWELLRELK-KEGKTILLSSHILEEAERL 161
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
132-154 |
3.77e-03 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 41.22 E-value: 3.77e-03
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
793-994 |
3.79e-03 |
|
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.
Pssm-ID: 432790 [Multi-domain] Cd Length: 238 Bit Score: 40.75 E-value: 3.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 793 AELQEVISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLVPMRQSIIDLkEKEIPELRNKLQNVNRDIQRLKNDIEEQ 872
Cdd:pfam12795 33 DASKQRAAAYQKALDDAPAELRELRQELAALQAKAEAAPKEILASLSLEEL-EQRLLQTSAQLQELQNQLAQLNSQLIEL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 873 ETLLGAIIPEEESAKVCLTDV-TIMERLQMELKDV-ERKIAQQAAKLQGLDLdrsvqQVNQEKQEkqhkLDTVSSKIELN 950
Cdd:pfam12795 112 QTRPERAQQQLSEARQRLQQIrNRLNGPAPPGEPLsEAQRWALQAELAALKA-----QIDMLEQE----LLSNNNRQDLL 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2015236753 951 RKLIQDQQEQIQHLKSTANELKSeklQIStnlQRRQQLEEQTVE 994
Cdd:pfam12795 183 KARRDLLTLRIQRLEQQLQALQE---LLN---EKRLQEAEQAVA 220
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
135-192 |
3.84e-03 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 41.18 E-value: 3.84e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 2015236753 135 LVGPNGAGKTTIIECLkyicTGDFPPgTKGntfvhdpkvaqetdvraQIRLQFRDVNG 192
Cdd:COG0411 35 LIGPNGAGKTTLFNLI----TGFYRP-TSG-----------------RILFDGRDITG 70
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
273-463 |
4.36e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.93 E-value: 4.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 273 LKQKFDEIFSATRYIKA-LETLRQvrqtqgqKVKECQTEL-KYLKQNK------------EKACEIRDQITSKEAQLTSS 338
Cdd:COG3206 166 LELRREEARKALEFLEEqLPELRK-------ELEEAEAALeEFRQKNGlvdlseeaklllQQLSELESQLAEARAELAEA 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 339 REIVKSYENELDPLKNRLKEIEQNlSKIMRLDNEIKALESRKKQMEK---DNS----ELEQKMEKVFQGSDEQLNDLYHN 411
Cdd:COG3206 239 EARLAALRAQLGSGPDALPELLQS-PVIQQLRAQLAELEAELAELSArytPNHpdviALRAQIAALRAQLQQEAQRILAS 317
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2015236753 412 HQRTVREKERRLVDCQRELEKLNKESRLLNQekseLLVEQGRLQLQADRHQE 463
Cdd:COG3206 318 LEAELEALQAREASLQAQLAQLEARLAELPE----LEAELRRLEREVEVARE 365
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
926-1279 |
4.42e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.43 E-value: 4.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 926 VQQVNQEKQEKQHKLDTVSSKIELNRKLIQDQQEQIQHLKStanELKSEKLQISTNLQRRQQLEEQTVELSTEVQSLYRE 1005
Cdd:COG4372 26 IAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEE---ELEQARSELEQLEEELEELNEQLQAAQAELAQAQEE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 1006 IKDAKEQLSPLETTLEKFQQEKEELVNKKNTSHKIAQDKINEIKEKVKNIHSYMKDIENYIQDGKDDYKKQKETELNKVI 1085
Cdd:COG4372 103 LESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAE 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 1086 AQISECEKHKEKINKEMGIMRQDIDTQKIQERWLQDNLTLRKRNEELKEVEEERKQHLKEMGQmqvlqmKNEHQKLEEKI 1165
Cdd:COG4372 183 QALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELE------EDKEELLEEVI 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 1166 DNIKRNHSLAIGRQKGYEEEIIHFKKELREPQFRDAEEKYREMMIIMRTTELVNKDLDIYYKTLDQAIMKFHSMKMEEIN 1245
Cdd:COG4372 257 LKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILL 336
|
330 340 350
....*....|....*....|....*....|....
gi 2015236753 1246 KIIRDLWRSTYRGQDIEYIEIRSDADENVSASDK 1279
Cdd:COG4372 337 AELADLLQLLLVGLLDNDVLELLSKGAEAGVADG 370
|
|
| COG4938 |
COG4938 |
Predicted ATPase [General function prediction only]; |
105-147 |
4.57e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443965 [Multi-domain] Cd Length: 277 Bit Score: 40.72 E-value: 4.57e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 2015236753 105 IEKMSIQGVRSFgiedKDKQIItfFSPLTILVGPNGAGKTTII 147
Cdd:COG4938 1 IKSISIKNFGPF----KEAELE--LKPLTLLIGPNGSGKSTLI 37
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
132-162 |
4.66e-03 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 40.87 E-value: 4.66e-03
10 20 30
....*....|....*....|....*....|.
gi 2015236753 132 LTILVGPNGAGKTTIIECLkyicTGDFPPGT 162
Cdd:COG4559 29 LTAIIGPNGAGKSTLLKLL----TGELTPSS 55
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
1293-1377 |
4.93e-03 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 41.74 E-value: 4.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 1293 DTALDMRGRC-SAGQKvlasliIRLALAETFCLNCGILALDEPTTNLDRENieslAHALVEIIKSRSQQRNfqLLVITHD 1371
Cdd:COG2274 602 DTVVGEGGSNlSGGQR------QRLAIARALLRNPRILILDEATSALDAET----EAIILENLRRLLKGRT--VIIIAHR 669
|
....*.
gi 2015236753 1372 EDFVEL 1377
Cdd:COG2274 670 LSTIRL 675
|
|
| CCDC73 |
pfam15818 |
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil ... |
931-1090 |
4.96e-03 |
|
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: 41.86 E-value: 4.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 931 QEKQEKQHKLdtvSSKIELNRKLiqdqQEQIQHLKStanelksEKLQISTNLQRRQQLEEQTVELSTEVQSlyrEIKDAK 1010
Cdd:pfam15818 222 QKFQELQERL---NMELELNKKI----NEEITHIQE-------EKQDIIISFQHMQQLLQQQTQANTEMEA---ELKALK 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 1011 EQLSPLET----TLEKFQQEKEELVNKKNTSHKIAQDKINEIKE------KVKNIHSYMKDIENYIQDGKDDYKKQKETE 1080
Cdd:pfam15818 285 ENNQTLERdnelQREKVKENEEKFLNLQNEHEKALGTWKKHVEElngeinEIKNELSSLKETHIKLQEHYNKLCNQKKFE 364
|
170
....*....|
gi 2015236753 1081 LNKVIAQISE 1090
Cdd:pfam15818 365 EDKKFQNVPE 374
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
946-1123 |
5.27e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 41.45 E-value: 5.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 946 KIELNRKLIQDQQEQIQHLKSTANELKSEKLQISTnlQRRQQLEEQTVELSTEVQSLYREIKDAKEQLSPLETTLEKFQQ 1025
Cdd:PRK05771 44 RLRKLRSLLTKLSEALDKLRSYLPKLNPLREEKKK--VSVKSLEELIKDVEEELEKIEKEIKELEEEISELENEIKELEQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 1026 EKEEL----------VNKKNTSHKIAqdKINEIKEKVKNIHSYMKDIEN--YIQDGKDDY------KKQKETELNKVIAQ 1087
Cdd:PRK05771 122 EIERLepwgnfdldlSLLLGFKYVSV--FVGTVPEDKLEELKLESDVENveYISTDKGYVyvvvvvLKELSDEVEEELKK 199
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2015236753 1088 -----------------ISECEKHKEKINKEMGIMRQDIdtQKIQERWLQDNL 1123
Cdd:PRK05771 200 lgferleleeegtpselIREIKEELEEIEKERESLLEEL--KELAKKYLEELL 250
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
1303-1386 |
5.33e-03 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 41.24 E-value: 5.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 1303 SAGQKVLasliirLALAETFCLNCGILALDEPTTNLDRENIESLAHALVEIiksrsqQRNFQLLVITH------DEDFVE 1376
Cdd:PRK10790 478 SVGQKQL------LALARVLVQTPQILILDEATANIDSGTEQAIQQALAAV------REHTTLVVIAHrlstivEADTIL 545
|
90
....*....|
gi 2015236753 1377 LLGRSEYVEK 1386
Cdd:PRK10790 546 VLHRGQAVEQ 555
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
439-774 |
5.39e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.54 E-value: 5.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 439 LLNQEKSELLVEQ----GRLQLQADRHQEHMQARdSLIQSLATQLELDGFELGPFSERQ--IKNFHKLVRERQEKES--- 509
Cdd:COG3206 60 LVEPQSSDVLLSGlsslSASDSPLETQIEILKSR-PVLERVVDKLNLDEDPLGEEASREaaIERLRKNLTVEPVKGSnvi 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 510 ---------ETASQLLNDFTR--KEALKQKQIDEIRDKKTGL-GRIIELKSEiLTKKQNELKN--VKYELQQLEG----S 571
Cdd:COG3206 139 eisytspdpELAAAVANALAEayLEQNLELRREEARKALEFLeEQLPELRKE-LEEAEAALEEfrQKNGLVDLSEeaklL 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 572 SDRILELDQELTKAERELSKAEknSNVETLKTEVISLQNEKADL--DRTLRKLDQEMEQLnhhtaaRTQMEMLNKDKADK 649
Cdd:COG3206 218 LQQLSELESQLAEARAELAEAE--ARLAALRAQLGSGPDALPELlqSPVIQQLRAQLAEL------EAELAELSARYTPN 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 650 DEQIRKIKyrhsDELTSLlgyfpnKKQLEdwlhskskeiNQTRDRLAKLNKELASAEQNKNHINIELKRKEEQLSSYEDK 729
Cdd:COG3206 290 HPDVIALR----AQIAAL------RAQLQ----------QEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPEL 349
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 2015236753 730 lfdvcgsqdfESDLDRLKEEIEKsskqramlagATAVYSQFITQL 774
Cdd:COG3206 350 ----------EAELRRLEREVEV----------ARELYESLLQRL 374
|
|
| COG1106 |
COG1106 |
ATPase/GTPase, AAA15 family [General function prediction only]; |
1242-1405 |
5.73e-03 |
|
ATPase/GTPase, AAA15 family [General function prediction only];
Pssm-ID: 440723 [Multi-domain] Cd Length: 330 Bit Score: 40.80 E-value: 5.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 1242 EEINKIIRDLwrstyrGQDIEYIEIRSDADENVSasdkrrNYNYRVVMLKGDTALDMRgRCSAGQKVLASLIirLALAET 1321
Cdd:COG1106 156 EELLELLKIA------DPGIEDIEVEEEEIEDLV------ERKLIFKHKGGNVPLPLS-EESDGTKRLLALA--GALLDA 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 1322 FCLNcGILALDEPTTNLDreniESLAHALVEIIKSRSQQRNFQLLVITHD----EDFVELLGRSEYvekfYRIKKNIEQC 1397
Cdd:COG1106 221 LAKG-GVLLIDEIEASLH----PSLLRKLLKLFLDLANKNNAQLIFTTHStellDAFLELLRRDQI----WFVEKDKDGA 291
|
....*...
gi 2015236753 1398 SEIVTCSE 1405
Cdd:COG1106 292 SELYSLED 299
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
287-597 |
6.32e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 41.16 E-value: 6.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 287 IKALETLRQVRQTQGQKVKECQTELK-----YLKQNKEKACEIRDQITSKEAQLTSSREIVKSYENELDPLKNRLKEIEQ 361
Cdd:TIGR04523 414 IKKLQQEKELLEKEIERLKETIIKNNseikdLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKS 493
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 362 NLSKIMRLDNEIKALESRKKQMEKDNSELEQKMEKVfqgsdeqlndlyhnhQRTVREKERRLVDCQRELEKLN------- 434
Cdd:TIGR04523 494 KEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKL---------------ESEKKEKESKISDLEDELNKDDfelkken 558
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 435 --KESRLLNQEKSELLVEQGRLQLQADRHQEHMQARDSLIQSLATQLELdgfelgpfSERQIKNFHKLVRERQEKESETA 512
Cdd:TIGR04523 559 leKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEE--------KEKKISSLEKELEKAKKENEKLS 630
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 513 SQLLNDFTRKEALKQ------KQIDEIRDKKTGL-GRIIELKSEI-----LTKKQNELKNVKY-----------ELQQLE 569
Cdd:TIGR04523 631 SIIKNIKSKKNKLKQevkqikETIKEIRNKWPEIiKKIKESKTKIddiieLMKDWLKELSLHYkkyitrmirikDLPKLE 710
|
330 340
....*....|....*....|....*...
gi 2015236753 570 GSSDRILELDQELTKAERELSKAEKNSN 597
Cdd:TIGR04523 711 EKYKEIEKELKKLDEFSKELENIIKNFN 738
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
135-183 |
6.36e-03 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 39.30 E-value: 6.36e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 2015236753 135 LVGPNGAGKTTIIECLkyicTGDFPPgTKGNTFV--HDPKvAQETDVRAQI 183
Cdd:cd03230 31 LLGPNGAGKTTLIKII----LGLLKP-DSGEIKVlgKDIK-KEPEEVKRRI 75
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
949-1101 |
6.84e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 41.35 E-value: 6.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 949 LNRKLIQDQQEQIQHLKSTANELkseklqISTNLQRRQQLEEQtvelSTEVQSLYREIKDAKEQLsplETTLEKFQQEKE 1028
Cdd:PRK00409 499 LPENIIEEAKKLIGEDKEKLNEL------IASLEELERELEQK----AEEAEALLKEAEKLKEEL---EEKKEKLQEEED 565
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2015236753 1029 ELvnkKNTSHKIAQDKINEIKEKVKNIhsyMKDIENYIQDGKDDYKKQKETELNKVIAQISECEKHKEKINKE 1101
Cdd:PRK00409 566 KL---LEEAEKEAQQAIKEAKKEADEI---IKELRQLQKGGYASVKAHELIEARKRLNKANEKKEKKKKKQKE 632
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
135-198 |
6.91e-03 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 40.05 E-value: 6.91e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2015236753 135 LVGPNGAGKTTIIECLkyiCTGDFPPGTKGNTFVHDpKVAQETDVRAQIRLQFRD--VNGELVAVQ 198
Cdd:cd03265 31 LLGPNGAGKTTTIKML---TTLLKPTSGRATVAGHD-VVREPREVRRRIGIVFQDlsVDDELTGWE 92
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
272-385 |
7.35e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 41.07 E-value: 7.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 272 ALKQKFDEIFSATR-----------YIKALETLRQVRQTQgQKVKECqteLKYLKQNKEKACEIRDqiTSKEAQLTSSRE 340
Cdd:PRK05771 13 TLKSYKDEVLEALHelgvvhiedlkEELSNERLRKLRSLL-TKLSEA---LDKLRSYLPKLNPLRE--EKKKVSVKSLEE 86
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 2015236753 341 IVKSYENELDPLKNRLKEIEqnlSKIMRLDNEIKALESRKKQMEK 385
Cdd:PRK05771 87 LIKDVEEELEKIEKEIKELE---EEISELENEIKELEQEIERLEP 128
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
686-872 |
7.64e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 39.91 E-value: 7.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 686 KEINQTRDRLAKLNKELASAEQNKNHINIELKRKEEQLSSYEDKLFDVCGSQDFESdldrLKEEIEKSSKQramlagata 765
Cdd:COG1579 38 DELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEYEA----LQKEIESLKRR--------- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 766 vysqfITQLTDEnqsccpvcqrgfqtEAELQEVISDLQSKLRLAPDKLKSTESELKKKEKRRDEmlglvpmrqsiidlke 845
Cdd:COG1579 105 -----ISDLEDE--------------ILELMERIEELEEELAELEAELAELEAELEEKKAELDE---------------- 149
|
170 180
....*....|....*....|....*..
gi 2015236753 846 kEIPELRNKLQNVNRDIQRLKNDIEEQ 872
Cdd:COG1579 150 -ELAELEAELEELEAEREELAAKIPPE 175
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
844-1109 |
7.72e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 40.96 E-value: 7.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 844 KEKEIPELRNKLQNVNRDIQRLKNDIEEQETLLGAiipEEESAKVCLTDVtimERLQMELKDVERKIAQQAAKLQGLDLD 923
Cdd:pfam10174 301 KESELLALQTKLETLTNQNSDCKQHIEVLKESLTA---KEQRAAILQTEV---DALRLRLEEKESFLNKKTKQLQDLTEE 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 924 RSVQQ-----VNQEKQEKQHKLDTVSSKIELNRKLIQDQQEQIQHLK-----------------STANELKSEKLQISTN 981
Cdd:pfam10174 375 KSTLAgeirdLKDMLDVKERKINVLQKKIENLQEQLRDKDKQLAGLKervkslqtdssntdtalTTLEEALSEKERIIER 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 982 LQRRQQLEEQtvELSTEVQSLYREIKDAKEQLSPLETTLekfqQEKEELVNKkntshkiAQDKINEIKEKVKNIHSYMKD 1061
Cdd:pfam10174 455 LKEQREREDR--ERLEELESLKKENKDLKEKVSALQPEL----TEKESSLID-------LKEHASSLASSGLKKDSKLKS 521
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 2015236753 1062 IENYIQDGKDDYKKQkETELNKvIAQISECEKHKEKINKEMGIMRQDI 1109
Cdd:pfam10174 522 LEIAVEQKKEECSKL-ENQLKK-AHNAEEAVRTNPEINDRIRLLEQEV 567
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1328-1375 |
8.17e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 40.65 E-value: 8.17e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 2015236753 1328 ILALDEPTTNLDRENIESLAHALveiiksrsqqRNFQ--LLVITHDEDFV 1375
Cdd:PRK15064 459 VLVMDEPTNHMDMESIESLNMAL----------EKYEgtLIFVSHDREFV 498
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
854-1068 |
8.38e-03 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 39.74 E-value: 8.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 854 KLQNVNRDIQRLKNDIEEQETLLGAIIPEEESAKVcltdvtimERLQMELKDVERKIAQQAAKLQglDLDRSVQQVNQEK 933
Cdd:cd00176 1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDLESV--------EALLKKHEALEAELAAHEERVE--ALNELGEQLIEEG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 934 QEK----QHKLDTVSSKIELNRKLIQDQQEQIQHLKSTANEL-KSEKLQISTNLQRRQQLEEQTVELSTEVQSLYREIKD 1008
Cdd:cd00176 71 HPDaeeiQERLEELNQRWEELRELAEERRQRLEEALDLQQFFrDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKE 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2015236753 1009 AKEQLSPLETTLEKFQQEKEELVNKKN-TSHKIAQDKINEIKEKVKNIHSYMKDIENYIQD 1068
Cdd:cd00176 151 LEEELEAHEPRLKSLNELAEELLEEGHpDADEEIEEKLEELNERWEELLELAEERQKKLEE 211
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
794-1010 |
9.23e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 39.52 E-value: 9.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 794 ELQEV---ISDLQSKLRLAPDKLKSTESELKKKEKRRDEmlglvpmrqsiidlKEKEIPELRNKLQNVNRDIQRLKNDIE 870
Cdd:COG1579 11 DLQELdseLDRLEHRLKELPAELAELEDELAALEARLEA--------------AKTELEDLEKEIKRLELEIEEVEARIK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 871 EQETLLGAIIPEEEsakvcltdvtiMERLQMELKDVERKIaqqaaklqgldldrsvQQVNQEKQEKQHKLDTVSSKIELN 950
Cdd:COG1579 77 KYEEQLGNVRNNKE-----------YEALQKEIESLKRRI----------------SDLEDEILELMERIEELEEELAEL 129
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2015236753 951 RKLIQDQQEQIQHLKSTANELKSE-KLQISTNLQRRQQLEEqtvELSTEVQSLYREIKDAK 1010
Cdd:COG1579 130 EAELAELEAELEEKKAELDEELAElEAELEELEAEREELAA---KIPPELLALYERIRKRK 187
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
332-541 |
9.31e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 39.52 E-value: 9.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 332 EAQLTSSREIVKSYENELDPLKNRLKEIEQNLSKImrlDNEIKALESRKKQMEKDNSELEQKMEKvfqgSDEQLNDLyhn 411
Cdd:COG1579 16 DSELDRLEHRLKELPAELAELEDELAALEARLEAA---KTELEDLEKEIKRLELEIEEVEARIKK----YEEQLGNV--- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015236753 412 hqRTVREkerrLVDCQRELEKLNKESRLLNQEKSELLVEQGRLQLQADRHQEHMQARDSLIQSLATQLELDGFELgpfsE 491
Cdd:COG1579 86 --RNNKE----YEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAEL----E 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2015236753 492 RQIKnfhKLVRERQEKESETASQLLndftrkealkqKQIDEIRDKKTGLG 541
Cdd:COG1579 156 AELE---ELEAEREELAAKIPPELL-----------ALYERIRKRKNGLA 191
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
1293-1370 |
9.50e-03 |
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ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 39.52 E-value: 9.50e-03
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gi 2015236753 1293 DTALDMRG-RCSAGQKVlasliiRLALAETFCLNCGILALDEPTTNLDRENIESLAHALVEIIKSRSqqrnfqLLVITH 1370
Cdd:cd03253 128 DTIVGERGlKLSGGEKQ------RVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSKGRT------TIVIAH 194
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