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Conserved domains on  [gi|1370488827|ref|XP_024301785|]
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ankycorbin isoform X3 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
49-249 1.05e-45

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 166.28  E-value: 1.05e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  49 FHLAAAKGHVECLRVMITHGVDVTAQDTTGHSALHLAAKNSHHECIRKLLQSKCPAESVDSSGKTALHYAAAQGCLQAVQ 128
Cdd:COG0666    58 LLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVK 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 129 ILCEHKSPINLKDLDGNIPLLLAVQNGHSEICHFLLDHGADVNSRNKSGRTALMLACEIGSSNAVEALIKKGADLNLVDS 208
Cdd:COG0666   138 LLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDN 217
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1370488827 209 LGYNALHYSKLSENAGIQSLLLSKISQDADLKTPTKPKQHD 249
Cdd:COG0666   218 DGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLL 258
PRK03918 super family cl35229
DNA double-strand break repair ATPase Rad50;
422-938 3.43e-16

DNA double-strand break repair ATPase Rad50;


The actual alignment was detected with superfamily member PRK03918:

Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 83.57  E-value: 3.43e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 422 RIQQLQEILQDLQKRLESSEAERKQLQVELQSRRAELvclnnteisENSSDLSQKLKETQSKYEEAMKEVLSVQKQMKlg 501
Cdd:PRK03918  187 RTENIEELIKEKEKELEEVLREINEISSELPELREEL---------EKLEKEVKELEELKEEIEELEKELESLEGSKR-- 255
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 502 lvspesmdnyshfhelrvteeeinVLKQDLQNALEESERNKEKVRELEEKLVEREKgtvIKPPVEEYEEMK---SSYCSV 578
Cdd:PRK03918  256 ------------------------KLEEKIRELEERIEELKKEIEELEEKVKELKE---LKEKAEEYIKLSefyEEYLDE 308
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 579 IENMNKEKAFLFEKYQEAQEEIMKLKDtlKSQMTQEASDEAEDMKEAMNRMidelnKQVSELSQLYKEAQAELEDYRKRK 658
Cdd:PRK03918  309 LREIEKRLSRLEEEINGIEERIKELEE--KEERLEELKKKLKELEKRLEEL-----EERHELYEEAKAKKEELERLKKRL 381
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 659 sledvTAEYIHKAEHEklmqLTNVSRAKAE--DALSEMKSQYSKVLNELTQLKQLVDAQKENSVS-------ITEH--LQ 727
Cdd:PRK03918  382 -----TGLTPEKLEKE----LEELEKAKEEieEEISKITARIGELKKEIKELKKAIEELKKAKGKcpvcgreLTEEhrKE 452
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 728 VITTLRTAAKEMEEKISNLKEHLASKEVEVAKLEKQLLEEKAAMTDamvpRSSYEKLQSSLESEVSVLASKLKESVKEKE 807
Cdd:PRK03918  453 LLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKL----KELAEQLKELEEKLKKYNLEELEKKAEEYE 528
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 808 KVHSEVVQIRSEVSQVKREKENIQTLLKSKEqevnELLQKFQQAQEELAEM-KRYAESSSKLEEDKDKKINEMSKEVTKL 886
Cdd:PRK03918  529 KLKEKLIKLKGEIKSLKKELEKLEELKKKLA----ELEKKLDELEEELAELlKELEELGFESVEELEERLKELEPFYNEY 604
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1370488827 887 KEALNSLSQLSYSTSSSKRQSQQLEALQQQVKQLQNQLAECKKQHQEVISVY 938
Cdd:PRK03918  605 LELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKY 656
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
49-249 1.05e-45

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 166.28  E-value: 1.05e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  49 FHLAAAKGHVECLRVMITHGVDVTAQDTTGHSALHLAAKNSHHECIRKLLQSKCPAESVDSSGKTALHYAAAQGCLQAVQ 128
Cdd:COG0666    58 LLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVK 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 129 ILCEHKSPINLKDLDGNIPLLLAVQNGHSEICHFLLDHGADVNSRNKSGRTALMLACEIGSSNAVEALIKKGADLNLVDS 208
Cdd:COG0666   138 LLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDN 217
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1370488827 209 LGYNALHYSKLSENAGIQSLLLSKISQDADLKTPTKPKQHD 249
Cdd:COG0666   218 DGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLL 258
Ank_2 pfam12796
Ankyrin repeats (3 copies);
82-174 1.36e-23

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 95.57  E-value: 1.36e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  82 LHLAAKNSHHECIRKLLQSKCPAESVDSSGKTALHYAAAQGCLQAVQILCEHKsPINLKDlDGNIPLLLAVQNGHSEICH 161
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHA-DVNLKD-NGRTALHYAARSGHLEIVK 78
                          90
                  ....*....|...
gi 1370488827 162 FLLDHGADVNSRN 174
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
58-231 2.99e-17

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 85.49  E-value: 2.99e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  58 VECLRVMITHGVDVTAQDTTGHSALHLAAKNS--HHECIRKLLQSKCPAESVDSSGKTALHYAAAQGC--LQAVQILCEH 133
Cdd:PHA03100   86 KEIVKLLLEYGANVNAPDNNGITPLLYAISKKsnSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDK 165
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 134 KSPINLKDldgNIPLLLavqnghseichfllDHGADVNSRNKSGRTALMLACEIGSSNAVEALIKKGADLNLVDSLGYNA 213
Cdd:PHA03100  166 GVDINAKN---RVNYLL--------------SYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTP 228
                         170
                  ....*....|....*...
gi 1370488827 214 LHYSKLSENAGIQSLLLS 231
Cdd:PHA03100  229 LHIAILNNNKEIFKLLLN 246
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
422-938 3.43e-16

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 83.57  E-value: 3.43e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 422 RIQQLQEILQDLQKRLESSEAERKQLQVELQSRRAELvclnnteisENSSDLSQKLKETQSKYEEAMKEVLSVQKQMKlg 501
Cdd:PRK03918  187 RTENIEELIKEKEKELEEVLREINEISSELPELREEL---------EKLEKEVKELEELKEEIEELEKELESLEGSKR-- 255
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 502 lvspesmdnyshfhelrvteeeinVLKQDLQNALEESERNKEKVRELEEKLVEREKgtvIKPPVEEYEEMK---SSYCSV 578
Cdd:PRK03918  256 ------------------------KLEEKIRELEERIEELKKEIEELEEKVKELKE---LKEKAEEYIKLSefyEEYLDE 308
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 579 IENMNKEKAFLFEKYQEAQEEIMKLKDtlKSQMTQEASDEAEDMKEAMNRMidelnKQVSELSQLYKEAQAELEDYRKRK 658
Cdd:PRK03918  309 LREIEKRLSRLEEEINGIEERIKELEE--KEERLEELKKKLKELEKRLEEL-----EERHELYEEAKAKKEELERLKKRL 381
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 659 sledvTAEYIHKAEHEklmqLTNVSRAKAE--DALSEMKSQYSKVLNELTQLKQLVDAQKENSVS-------ITEH--LQ 727
Cdd:PRK03918  382 -----TGLTPEKLEKE----LEELEKAKEEieEEISKITARIGELKKEIKELKKAIEELKKAKGKcpvcgreLTEEhrKE 452
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 728 VITTLRTAAKEMEEKISNLKEHLASKEVEVAKLEKQLLEEKAAMTDamvpRSSYEKLQSSLESEVSVLASKLKESVKEKE 807
Cdd:PRK03918  453 LLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKL----KELAEQLKELEEKLKKYNLEELEKKAEEYE 528
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 808 KVHSEVVQIRSEVSQVKREKENIQTLLKSKEqevnELLQKFQQAQEELAEM-KRYAESSSKLEEDKDKKINEMSKEVTKL 886
Cdd:PRK03918  529 KLKEKLIKLKGEIKSLKKELEKLEELKKKLA----ELEKKLDELEEELAELlKELEELGFESVEELEERLKELEPFYNEY 604
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1370488827 887 KEALNSLSQLSYSTSSSKRQSQQLEALQQQVKQLQNQLAECKKQHQEVISVY 938
Cdd:PRK03918  605 LELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKY 656
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
516-886 1.69e-14

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 78.17  E-value: 1.69e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  516 ELRVTEEEINVLKQDLQNALEESERNKEKVRELEEKLVEREKGTVI-KPPVEEYEEMKSSYCSVIENMNKEKAFLFEKYQ 594
Cdd:TIGR02168  692 KIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARlEAEVEQLEERIAQLSKELTELEAEIEELEERLE 771
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  595 EAQEEIMKLKDTLKSQmtQEASDEAEDMKEAMNRMIDELNKQVSELSQLYKEAQAELEDYRKRKSLEDVTAEYIH--KAE 672
Cdd:TIGR02168  772 EAEEELAEAEAEIEEL--EAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEeqIEE 849
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  673 HEKLMQLTNVSRAKAEDALSEMKSQYSKVLNELTQLKQLVDAQKENSVSITEHLQvitTLRTAAKEMEEKISNLKEHLAS 752
Cdd:TIGR02168  850 LSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELR---ELESKRSELRRELEELREKLAQ 926
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  753 KEVEVAKLEKQLLEekaamtdamvprssyekLQSSLESEVSVLaskLKESVKEKEKVHSEVVQIRSEVSQVKREKENIQt 832
Cdd:TIGR02168  927 LELRLEGLEVRIDN-----------------LQERLSEEYSLT---LEEAEALENKIEDDEEEARRRLKRLENKIKELG- 985
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1370488827  833 llkskeqEVNEL-LQKFQQAQEELAEMKRYAESSSKLEEDKDKKINEMSKEVTKL 886
Cdd:TIGR02168  986 -------PVNLAaIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDREARER 1033
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
585-890 9.20e-13

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 72.66  E-value: 9.20e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 585 EKAflfEKYQEAQEEIMKLKDTLKSQMTQEASDEAEDMKEAMNRMIDELNKQVSELSQLYKE-AQAELEDYRKRKSLEDV 663
Cdd:COG1196   210 EKA---ERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAElEELRLELEELELELEEA 286
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 664 TA-EYIHKAEHEKLmqltnvsrAKAEDALSEMKSQYSKVLNELTQLKQLVDAQKEnsvsitEHLQVITTLRTAAKEMEEK 742
Cdd:COG1196   287 QAeEYELLAELARL--------EQDIARLEERRRELEERLEELEEELAELEEELE------ELEEELEELEEELEEAEEE 352
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 743 ISNLKEHLASKEVEVAKLEKQLLEEKAAMTDAMVPRSSYEKLQSSLESEVSVLASKLKESVKEKEKVHSEVVQIRSEVSQ 822
Cdd:COG1196   353 LEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAE 432
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370488827 823 VKREKENIQTLLKSKEQEVNELLQKFQQAQEELAEMKRYAESSSKLEEDKDKKINEMSKEVTKLKEAL 890
Cdd:COG1196   433 LEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAE 500
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
80-215 2.64e-10

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 64.26  E-value: 2.64e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  80 SALHLAAKNSHHECIRKLLqsKCPaeSVD-----SSGKTALHYAAAQGCLQAVQILCEH-----KSPINLKDLDGNIPLL 149
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLL--KCP--SCDlfqrgALGETALHVAALYDNLEAAVVLMEAapelvNEPMTSDLYQGETALH 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 150 LAVQNGHSEICHFLLDHGADVNS---------RNKS-----GRTALMLACEIGSSNAVEALIKKGADLNLVDSLGYNALH 215
Cdd:cd22192    95 IAVVNQNLNLVRELIARGADVVSpratgtffrPGPKnliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLH 174
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
517-891 4.33e-10

Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.


Pssm-ID: 428797 [Multi-domain]  Cd Length: 542  Bit Score: 63.33  E-value: 4.33e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 517 LRVTEEEINVLKQDLQNALEESERNKEKVRELEEKlverekgtvikppveeYEEMKSSYcsvienmnKEKAFLFEKYQEA 596
Cdd:pfam06160  95 LDDIEEDIKQILEELDELLESEEKNREEVEELKDK----------------YRELRKTL--------LANRFSYGPAIDE 150
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 597 QEEIMKLKDTLKSQMTQEASD----EAEDMKEAMNRMIDELNKQVSELSQLYKEAQAELEDyrkrkSLEDVTAEYihkae 672
Cdd:pfam06160 151 LEKQLAEIEEEFSQFEELTESgdylEAREVLEKLEEETDALEELMEDIPPLYEELKTELPD-----QLEELKEGY----- 220
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 673 HEKLMQLTNVSRAKAEDALSEMKSQYSKVLNELTQLKqlVDAQKENSVSITEHLQ----VITTLRTAAKEMEEKISNLKE 748
Cdd:pfam06160 221 REMEEEGYALEHLNVDKEIQQLEEQLEENLALLENLE--LDEAEEALEEIEERIDqlydLLEKEVDAKKYVEKNLPEIED 298
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 749 HLAskevEVAKLEKQLLEEKAAMTDAMVPRSSYEKLQSSLESEVSVLASKLKESVK---EKEKVHSEVV----QIRSEVS 821
Cdd:pfam06160 299 YLE----HAEEQNKELKEELERVQQSYTLNENELERVRGLEKQLEELEKRYDEIVErleEKEVAYSELQeeleEILEQLE 374
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370488827 822 QVKREKENIQTLLKS---KEQEVNELLQKFQQaqeELAEMKRYAESS--SKLEEDKDKKINEMSKEVTKLKEALN 891
Cdd:pfam06160 375 EIEEEQEEFKESLQSlrkDELEAREKLDEFKL---ELREIKRLVEKSnlPGLPESYLDYFFDVSDEIEDLADELN 446
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
75-219 6.90e-07

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 53.16  E-value: 6.90e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  75 DTTGHSALHLAAKNSHHECIRKLLQSKCPAESVdssGKTALHyAAAQGCLQAVQILCEHKSPINLKDLD----------- 143
Cdd:TIGR00870  49 DRLGRSALFVAAIENENLELTELLLNLSCRGAV---GDTLLH-AISLEYVDAVEAILLHLLAAFRKSGPlelandqytse 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 144 ---GNIPLLLAVQNGHSEICHFLLDHGADVNSRNKS--------------GRTALMLACEIGSSNAVEALIKKGADLNLV 206
Cdd:TIGR00870 125 ftpGITALHLAAHRQNYEIVKLLLERGASVPARACGdffvksqgvdsfyhGESPLNAAACLGSPSIVALLSEDPADILTA 204
                         170
                  ....*....|...
gi 1370488827 207 DSLGYNALHYSKL 219
Cdd:TIGR00870 205 DSLGNTLLHLLVM 217
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
143-171 1.44e-05

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 42.57  E-value: 1.44e-05
                           10        20
                   ....*....|....*....|....*....
gi 1370488827  143 DGNIPLLLAVQNGHSEICHFLLDHGADVN 171
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
687-859 2.11e-05

Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.


Pssm-ID: 439154 [Multi-domain]  Cd Length: 309  Bit Score: 47.75  E-value: 2.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 687 AEDALSEMKSQYSKVLNELTQLKQLVDaQKENSVSITEHLQVITTLRTAAKEMEEKISNLKEHLASKEVEVAKLEKQLLE 766
Cdd:cd22656    82 AQNAGGTIDSYYAEILELIDDLADATD-DEELEEAKKTIKALLDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQTALET 160
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 767 EKAAMTD------AMVPRSSYEKLQSSLESEVSVLASKLKESVKEKEKvhsevvQIRSEVSQVKREKeNIQTLLKSKEQE 840
Cdd:cd22656   161 LEKALKDlltdegGAIARKEIKDLQKELEKLNEEYAAKLKAKIDELKA------LIADDEAKLAAAL-RLIADLTAADTD 233
                         170
                  ....*....|....*....
gi 1370488827 841 VNELLQKFQQAQEELAEMK 859
Cdd:cd22656   234 LDNLLALIGPAIPALEKLQ 252
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
49-249 1.05e-45

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 166.28  E-value: 1.05e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  49 FHLAAAKGHVECLRVMITHGVDVTAQDTTGHSALHLAAKNSHHECIRKLLQSKCPAESVDSSGKTALHYAAAQGCLQAVQ 128
Cdd:COG0666    58 LLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVK 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 129 ILCEHKSPINLKDLDGNIPLLLAVQNGHSEICHFLLDHGADVNSRNKSGRTALMLACEIGSSNAVEALIKKGADLNLVDS 208
Cdd:COG0666   138 LLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDN 217
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1370488827 209 LGYNALHYSKLSENAGIQSLLLSKISQDADLKTPTKPKQHD 249
Cdd:COG0666   218 DGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLL 258
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
49-240 1.28e-45

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 165.90  E-value: 1.28e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  49 FHLAAAKGHVECLRVMITHGVDVTAQDTTGHSALHLAAKNSHHECIRKLLQSKCPAESVDSSGKTALHYAAAQGCLQAVQ 128
Cdd:COG0666    91 LHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVK 170
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 129 ILCEHKSPINLKDLDGNIPLLLAVQNGHSEICHFLLDHGADVNSRNKSGRTALMLACEIGSSNAVEALIKKGADLNLVDS 208
Cdd:COG0666   171 LLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDK 250
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1370488827 209 LGYNALHYSKLSENAGIQSLLLSKISQDADLK 240
Cdd:COG0666   251 DGLTALLLAAAAGAALIVKLLLLALLLLAAAL 282
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
49-242 2.38e-36

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 139.32  E-value: 2.38e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  49 FHLAAAKGHVECLRVMITHGVDVTAQDTTGHSALHLAAKNSHHECIRKLLQSKCPAESVDSSGKTALHYAAAQGCLQAVQ 128
Cdd:COG0666    25 LLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVK 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 129 ILCEHKSPINLKDLDGNIPLLLAVQNGHSEICHFLLDHGADVNSRNKSGRTALMLACEIGSSNAVEALIKKGADLNLVDS 208
Cdd:COG0666   105 LLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDN 184
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1370488827 209 LGYNALHYSKLSENAGIQSLLLSK----ISQDADLKTP 242
Cdd:COG0666   185 DGETPLHLAAENGHLEIVKLLLEAgadvNAKDNDGKTA 222
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
50-214 2.16e-34

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 133.54  E-value: 2.16e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  50 HLAAAKGHVECLRVMITHGVDVTAQDTTGHSALHLAAKNSHHECIRKLLQSKCPAESVDSSGKTALHYAAAQGCLQAVQI 129
Cdd:COG0666   125 HLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKL 204
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 130 LCEHKSPINLKDLDGNIPLLLAVQNGHSEICHFLLDHGADVNSRNKSGRTALMLACEIGSSNAVEALIKKGADLNLVDSL 209
Cdd:COG0666   205 LLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLD 284

                  ....*
gi 1370488827 210 GYNAL 214
Cdd:COG0666   285 LLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
61-242 1.06e-25

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 108.12  E-value: 1.06e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  61 LRVMITHGVDVTAQDTTGHSALHLAAKNSHHECIRKLLQSKCPAESVDSSGKTALHYAAAQGCLQAVQILCEHKSPINLK 140
Cdd:COG0666     4 LLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAK 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 141 DLDGNIPLLLAVQNGHSEICHFLLDHGADVNSRNKSGRTALMLACEIGSSNAVEALIKKGADLNLVDSLGYNALHYSKLS 220
Cdd:COG0666    84 DDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAAN 163
                         170       180
                  ....*....|....*....|....*.
gi 1370488827 221 ENAGIQSLLLSK----ISQDADLKTP 242
Cdd:COG0666   164 GNLEIVKLLLEAgadvNARDNDGETP 189
Ank_2 pfam12796
Ankyrin repeats (3 copies);
82-174 1.36e-23

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 95.57  E-value: 1.36e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  82 LHLAAKNSHHECIRKLLQSKCPAESVDSSGKTALHYAAAQGCLQAVQILCEHKsPINLKDlDGNIPLLLAVQNGHSEICH 161
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHA-DVNLKD-NGRTALHYAARSGHLEIVK 78
                          90
                  ....*....|...
gi 1370488827 162 FLLDHGADVNSRN 174
Cdd:pfam12796  79 LLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
115-207 1.53e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 92.87  E-value: 1.53e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 115 LHYAAAQGCLQAVQILCEHKSPINLKDLDGNIPLLLAVQNGHSEICHFLLDHgADVNSRNKsGRTALMLACEIGSSNAVE 194
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78
                          90
                  ....*....|...
gi 1370488827 195 ALIKKGADLNLVD 207
Cdd:pfam12796  79 LLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
49-141 2.23e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 92.10  E-value: 2.23e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  49 FHLAAAKGHVECLRVMITHGVDVTAQDTTGHSALHLAAKNSHHECIRKLLQsKCPAESVDsSGKTALHYAAAQGCLQAVQ 128
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVK 78
                          90
                  ....*....|...
gi 1370488827 129 ILCEHKSPINLKD 141
Cdd:pfam12796  79 LLLEKGADINVKD 91
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
49-181 4.08e-22

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 97.72  E-value: 4.08e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  49 FHLAAAKGHVECLRVMITHGVDVTAQDTTGHSALHLAAKNSHHECIRKLLQSKCPAESVDSSGKTALHYAAAQGCLQAVQ 128
Cdd:COG0666   157 LHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVK 236
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1370488827 129 ILCEHKSPINLKDLDGNIPLLLAVQNGHSEICHFLLDHGADVNSRNKSGRTAL 181
Cdd:COG0666   237 LLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
PHA03100 PHA03100
ankyrin repeat protein; Provisional
58-231 2.99e-17

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 85.49  E-value: 2.99e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  58 VECLRVMITHGVDVTAQDTTGHSALHLAAKNS--HHECIRKLLQSKCPAESVDSSGKTALHYAAAQGC--LQAVQILCEH 133
Cdd:PHA03100   86 KEIVKLLLEYGANVNAPDNNGITPLLYAISKKsnSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDK 165
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 134 KSPINLKDldgNIPLLLavqnghseichfllDHGADVNSRNKSGRTALMLACEIGSSNAVEALIKKGADLNLVDSLGYNA 213
Cdd:PHA03100  166 GVDINAKN---RVNYLL--------------SYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTP 228
                         170
                  ....*....|....*...
gi 1370488827 214 LHYSKLSENAGIQSLLLS 231
Cdd:PHA03100  229 LHIAILNNNKEIFKLLLN 246
Ank_2 pfam12796
Ankyrin repeats (3 copies);
148-232 3.84e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 77.46  E-value: 3.84e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 148 LLLAVQNGHSEICHFLLDHGADVNSRNKSGRTALMLACEIGSSNAVEALIKKgADLNLVDSlGYNALHYSKLSENAGIQS 227
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78

                  ....*
gi 1370488827 228 LLLSK 232
Cdd:pfam12796  79 LLLEK 83
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
422-938 3.43e-16

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 83.57  E-value: 3.43e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 422 RIQQLQEILQDLQKRLESSEAERKQLQVELQSRRAELvclnnteisENSSDLSQKLKETQSKYEEAMKEVLSVQKQMKlg 501
Cdd:PRK03918  187 RTENIEELIKEKEKELEEVLREINEISSELPELREEL---------EKLEKEVKELEELKEEIEELEKELESLEGSKR-- 255
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 502 lvspesmdnyshfhelrvteeeinVLKQDLQNALEESERNKEKVRELEEKLVEREKgtvIKPPVEEYEEMK---SSYCSV 578
Cdd:PRK03918  256 ------------------------KLEEKIRELEERIEELKKEIEELEEKVKELKE---LKEKAEEYIKLSefyEEYLDE 308
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 579 IENMNKEKAFLFEKYQEAQEEIMKLKDtlKSQMTQEASDEAEDMKEAMNRMidelnKQVSELSQLYKEAQAELEDYRKRK 658
Cdd:PRK03918  309 LREIEKRLSRLEEEINGIEERIKELEE--KEERLEELKKKLKELEKRLEEL-----EERHELYEEAKAKKEELERLKKRL 381
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 659 sledvTAEYIHKAEHEklmqLTNVSRAKAE--DALSEMKSQYSKVLNELTQLKQLVDAQKENSVS-------ITEH--LQ 727
Cdd:PRK03918  382 -----TGLTPEKLEKE----LEELEKAKEEieEEISKITARIGELKKEIKELKKAIEELKKAKGKcpvcgreLTEEhrKE 452
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 728 VITTLRTAAKEMEEKISNLKEHLASKEVEVAKLEKQLLEEKAAMTDamvpRSSYEKLQSSLESEVSVLASKLKESVKEKE 807
Cdd:PRK03918  453 LLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKL----KELAEQLKELEEKLKKYNLEELEKKAEEYE 528
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 808 KVHSEVVQIRSEVSQVKREKENIQTLLKSKEqevnELLQKFQQAQEELAEM-KRYAESSSKLEEDKDKKINEMSKEVTKL 886
Cdd:PRK03918  529 KLKEKLIKLKGEIKSLKKELEKLEELKKKLA----ELEKKLDELEEELAELlKELEELGFESVEELEERLKELEPFYNEY 604
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1370488827 887 KEALNSLSQLSYSTSSSKRQSQQLEALQQQVKQLQNQLAECKKQHQEVISVY 938
Cdd:PRK03918  605 LELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKY 656
PHA02875 PHA02875
ankyrin repeat protein; Provisional
49-206 9.55e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 80.81  E-value: 9.55e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  49 FHLAAAKGHVECLRVMITHGV---DVTAQDttGHSALHLAAKNSHHECIRKLLQSKCPAESVDSSGKTALHYAAAQGCLQ 125
Cdd:PHA02875   72 LHDAVEEGDVKAVEELLDLGKfadDVFYKD--GMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIK 149
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 126 AVQILCEHKSPINLKDLDGNIPLLLAVQNGHSEICHFLLDHGADVNSRNKSGRTALM-LACEIGSSNAVEALIKKGADLN 204
Cdd:PHA02875  150 GIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALcYAIENNKIDIVRLFIKRGADCN 229

                  ..
gi 1370488827 205 LV 206
Cdd:PHA02875  230 IM 231
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
516-886 1.69e-14

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 78.17  E-value: 1.69e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  516 ELRVTEEEINVLKQDLQNALEESERNKEKVRELEEKLVEREKGTVI-KPPVEEYEEMKSSYCSVIENMNKEKAFLFEKYQ 594
Cdd:TIGR02168  692 KIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARlEAEVEQLEERIAQLSKELTELEAEIEELEERLE 771
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  595 EAQEEIMKLKDTLKSQmtQEASDEAEDMKEAMNRMIDELNKQVSELSQLYKEAQAELEDYRKRKSLEDVTAEYIH--KAE 672
Cdd:TIGR02168  772 EAEEELAEAEAEIEEL--EAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEeqIEE 849
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  673 HEKLMQLTNVSRAKAEDALSEMKSQYSKVLNELTQLKQLVDAQKENSVSITEHLQvitTLRTAAKEMEEKISNLKEHLAS 752
Cdd:TIGR02168  850 LSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELR---ELESKRSELRRELEELREKLAQ 926
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  753 KEVEVAKLEKQLLEekaamtdamvprssyekLQSSLESEVSVLaskLKESVKEKEKVHSEVVQIRSEVSQVKREKENIQt 832
Cdd:TIGR02168  927 LELRLEGLEVRIDN-----------------LQERLSEEYSLT---LEEAEALENKIEDDEEEARRRLKRLENKIKELG- 985
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1370488827  833 llkskeqEVNEL-LQKFQQAQEELAEMKRYAESSSKLEEDKDKKINEMSKEVTKL 886
Cdd:TIGR02168  986 -------PVNLAaIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDREARER 1033
PHA02874 PHA02874
ankyrin repeat protein; Provisional
38-214 1.91e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 76.93  E-value: 1.91e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  38 VRARPRKLKHCFHLAAAKGHVECLRVMITHGVDVTAQDTTGHSALHLAAKNSHHECIRKLLQSKCPAESVDSSGKTALHY 117
Cdd:PHA02874  117 VNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHN 196
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 118 AAAQGCLQAVQILCEHKSPINLKDLDGNIPLLLAVQNGHSEIChfLLDHGADVNSRNKSGRTALMLA----CEIgssNAV 193
Cdd:PHA02874  197 AAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRSAIE--LLINNASINDQDIDGSTPLHHAinppCDI---DII 271
                         170       180
                  ....*....|....*....|.
gi 1370488827 194 EALIKKGADLNLVDSLGYNAL 214
Cdd:PHA02874  272 DILLYHKADISIKDNKGENPI 292
PHA03095 PHA03095
ankyrin-like protein; Provisional
58-216 2.14e-14

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 76.99  E-value: 2.14e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  58 VECLRVMITHGVDVTAQDTTGHSALHLAAKNSH--HECIRKLLQSKCPAESVDSSGKTALHYAAAQGCLQAVQI--LCEH 133
Cdd:PHA03095  167 VELLRLLIDAGADVYAVDDRFRSLLHHHLQSFKprARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVlpLLIA 246
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 134 KSPINLKDLDGNIPLLLAVQNGHSEICHFLLDHGADVNSRNKSGRTALMLACEIGSSNAVEALIKKGADLNLVDslgyNA 213
Cdd:PHA03095  247 GISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETVA----AT 322

                  ...
gi 1370488827 214 LHY 216
Cdd:PHA03095  323 LNT 325
PHA02874 PHA02874
ankyrin repeat protein; Provisional
52-242 1.54e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 73.84  E-value: 1.54e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  52 AAAKGHVECLRVMITHGVDVTAQDTTGHSALHLAAKNSHH-----------------------ECIRKLLQSKCPAESVD 108
Cdd:PHA02874   42 AIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHdiikllidngvdtsilpipciekDMIKTILDCGIDVNIKD 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 109 SSGKTALHYAAAQGCLQAVQILCEHKSPINLKDLDGNIPLLLAVQNGHSEICHFLLDHGADVNSRNKSGRTALMLACEIG 188
Cdd:PHA02874  122 AELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYG 201
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1370488827 189 SSNAVEALIKKGADLNLVDSLGYNALHYSKLSENAGIQsLLLSKIS---QDADLKTP 242
Cdd:PHA02874  202 DYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRSAIE-LLINNASindQDIDGSTP 257
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
50-174 6.75e-13

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 72.98  E-value: 6.75e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  50 HLAAAKGHVECLRVMITHGVDVTAQDTTGHSALHLAAKNSHHECIRKLLQskCPAESVDSSGKTALHYAAAQGCLQAVQI 129
Cdd:PLN03192  563 HIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYH--FASISDPHAAGDLLCTAAKRNDLTAMKE 640
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1370488827 130 LCEHKSPINLKDLDGNIPLLLAVQNGHSEICHFLLDHGADVNSRN 174
Cdd:PLN03192  641 LLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKAN 685
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
422-911 8.62e-13

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 72.40  E-value: 8.62e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 422 RIQQLQEILQDLQKRLESSEAERKQLQVELQSRRAELvclnnteisenssdlsQKLKETQSKYEEAMKEVLSVQKQMKLG 501
Cdd:PRK03918  232 ELEELKEEIEELEKELESLEGSKRKLEEKIRELEERI----------------EELKKEIEELEEKVKELKELKEKAEEY 295
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 502 LVSPESMDNY-SHFHELRVTEEEINVLKQDLQNALEESERNKEKVRELEEKLVE-REKGTVIKPPVEEYEEMKSsycsVI 579
Cdd:PRK03918  296 IKLSEFYEEYlDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKElEKRLEELEERHELYEEAKA----KK 371
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 580 ENMNKEKAFLFEKYQEAQEEIMKLKDTLKSQMTQEASdEAEDMKEAMNRMIDELNKQVSELsqlyKEAQ-------AELE 652
Cdd:PRK03918  372 EELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEIS-KITARIGELKKEIKELKKAIEEL----KKAKgkcpvcgRELT 446
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 653 DYRKRKSLEDVTAEyIHKAEHEKLMQLTNVSRAKAEDALSEMK-SQYSKVLNELTQLKQLVDAQKENSVSITEHLQVIT- 730
Cdd:PRK03918  447 EEHRKELLEEYTAE-LKRIEKELKEIEEKERKLRKELRELEKVlKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAe 525
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 731 ---TLRTAAKEMEEKISNLKEHLASKEV---EVAKLEKQL--LEEKAAMTDAMVPRSSYEKLQSsLESEVSVLAS----- 797
Cdd:PRK03918  526 eyeKLKEKLIKLKGEIKSLKKELEKLEElkkKLAELEKKLdeLEEELAELLKELEELGFESVEE-LEERLKELEPfyney 604
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 798 -KLKESVKEKEKVHSEVVQIRSEVSQVKREKENIQTLLKSKEQEVNELLQKFqqAQEELAEMKRYAESSSKLEEDKDKKI 876
Cdd:PRK03918  605 lELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKY--SEEEYEELREEYLELSRELAGLRAEL 682
                         490       500       510
                  ....*....|....*....|....*....|....*
gi 1370488827 877 NEMSKEVTKLKEALNSLSQLSYSTSSSKRQSQQLE 911
Cdd:PRK03918  683 EELEKRREEIKKTLEKLKEELEEREKAKKELEKLE 717
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
585-890 9.20e-13

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 72.66  E-value: 9.20e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 585 EKAflfEKYQEAQEEIMKLKDTLKSQMTQEASDEAEDMKEAMNRMIDELNKQVSELSQLYKE-AQAELEDYRKRKSLEDV 663
Cdd:COG1196   210 EKA---ERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAElEELRLELEELELELEEA 286
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 664 TA-EYIHKAEHEKLmqltnvsrAKAEDALSEMKSQYSKVLNELTQLKQLVDAQKEnsvsitEHLQVITTLRTAAKEMEEK 742
Cdd:COG1196   287 QAeEYELLAELARL--------EQDIARLEERRRELEERLEELEEELAELEEELE------ELEEELEELEEELEEAEEE 352
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 743 ISNLKEHLASKEVEVAKLEKQLLEEKAAMTDAMVPRSSYEKLQSSLESEVSVLASKLKESVKEKEKVHSEVVQIRSEVSQ 822
Cdd:COG1196   353 LEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAE 432
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370488827 823 VKREKENIQTLLKSKEQEVNELLQKFQQAQEELAEMKRYAESSSKLEEDKDKKINEMSKEVTKLKEAL 890
Cdd:COG1196   433 LEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAE 500
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
422-926 9.60e-13

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 72.66  E-value: 9.60e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 422 RIQQLQEILQDLQKRLESSEAERKQLQVELQSRRAELvclnnTEISENSSDLSQKLKETQSKYEEAMKEVLSVQKQMKLG 501
Cdd:COG1196   233 KLRELEAELEELEAELEELEAELEELEAELAELEAEL-----EELRLELEELELELEEAQAEEYELLAELARLEQDIARL 307
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 502 LvspESMDNYShfHELRVTEEEINVLKQDLQNALEESERNKEKVRELEEKLVEREKGtvikppVEEYEEMKSSYCSVIEN 581
Cdd:COG1196   308 E---ERRRELE--ERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAE------LAEAEEALLEAEAELAE 376
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 582 MNKEKAFLFEKYQEAQEEIMKLKDTLKSQMTQEASDEAEDmkEAMNRMIDELNKQVSELSQLYKEAQAELEDYRKR--KS 659
Cdd:COG1196   377 AEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERL--ERLEEELEELEEALAELEEEEEEEEEALEEAAEEeaEL 454
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 660 LEDVTAEYIHKAEHEKLMQLTNVSRAKAEDALSEMKSQYSKVLNELTQ---------LKQLVDAQKENSVSITEHLQVIT 730
Cdd:COG1196   455 EEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADyegflegvkAALLLAGLRGLAGAVAVLIGVEA 534
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 731 TLRTAAkemEEKISNLKEHLASKEVEVAKLEKQLLEEKAA-------MTDAMVPRSSYEKLQSSLESEVSVLASKLKESV 803
Cdd:COG1196   535 AYEAAL---EAALAAALQNIVVEDDEVAAAAIEYLKAAKAgratflpLDKIRARAALAAALARGAIGAAVDLVASDLREA 611
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 804 KEKEKVHSEVVQIRSEVSQVKREKENIQTLLKSKEQEVNELLQKFQQAQEELAEMKRYAESSSKLEEDKDKKINEMSKEV 883
Cdd:COG1196   612 DARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEE 691
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|...
gi 1370488827 884 TKLKEALNSLSQLSYSTSSSKRQSQQLEALQQQVKQLQNQLAE 926
Cdd:COG1196   692 ELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAER 734
PHA03095 PHA03095
ankyrin-like protein; Provisional
94-238 1.10e-12

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 71.59  E-value: 1.10e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  94 IRKLLQSKCPAESVDSSGKTALHY---AAAQGCLQAVQILCEHKSPINLKDLDGNIPLLLAVQNGHSE-ICHFLLDHGAD 169
Cdd:PHA03095   30 VRRLLAAGADVNFRGEYGKTPLHLylhYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLdVIKLLIKAGAD 109
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370488827 170 VNSRNKSGRTALMLACEIGSSNA--VEALIKKGADLNLVDSLGYNALHYSKLSENAGIQ--SLLLSKISQDAD 238
Cdd:PHA03095  110 VNAKDKVGRTPLHVYLSGFNINPkvIRLLLRKGADVNALDLYGMTPLAVLLKSRNANVEllRLLIDAGADVYA 182
PHA03095 PHA03095
ankyrin-like protein; Provisional
47-222 1.22e-12

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 71.21  E-value: 1.22e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  47 HCFHLAAAKghVECLRVMITHGVDVTAQDTTGHSALH--LAAKNSHHECIRKLLQSKCPAESVDSSGKTALH-YAAAQGC 123
Cdd:PHA03095   88 HLYLYNATT--LDVIKLLIKAGADVNAKDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAvLLKSRNA 165
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 124 -LQAVQILCEHKSPINLKDLDGNIPLLLAVQNGHS--EICHFLLDHGADVNSRNKSGRTALMLACEIGSSNA--VEALIK 198
Cdd:PHA03095  166 nVELLRLLIDAGADVYAVDDRFRSLLHHHLQSFKPraRIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRslVLPLLI 245
                         170       180
                  ....*....|....*....|....
gi 1370488827 199 KGADLNLVDSLGYNALHYSKLSEN 222
Cdd:PHA03095  246 AGISINARNRYGQTPLHYAAVFNN 269
PHA02874 PHA02874
ankyrin repeat protein; Provisional
59-217 1.25e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 71.15  E-value: 1.25e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  59 ECLRVMITHGVDVTAQDTTGHSALHLAAKNSHHECIRKLLQSKCPAESVDSSGKTALHYAAAQGCLQAVQILCEHKSPIN 138
Cdd:PHA02874  105 DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYAN 184
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370488827 139 LKDLDGNIPLLLAVQNGHSEICHFLLDHGADVNSRNKSGRTALMLACeIGSSNAVEALIKKgADLNLVDSLGYNALHYS 217
Cdd:PHA02874  185 VKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAI-IHNRSAIELLINN-ASINDQDIDGSTPLHHA 261
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
52-203 1.33e-12

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 71.82  E-value: 1.33e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  52 AAAKGHVECLRVMITHGVDVTAQDTTGHSALHLAAKNSHHECIRKLLQSKCPAESVDSSGKTALHYAAAQGCLQAVQILc 131
Cdd:PLN03192  532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRIL- 610
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370488827 132 EHKSPINLKDLDGNIpLLLAVQNGHSEICHFLLDHGADVNSRNKSGRTALMLACEIGSSNAVEALIKKGADL 203
Cdd:PLN03192  611 YHFASISDPHAAGDL-LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADV 681
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
420-891 2.14e-12

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: 71.64  E-value: 2.14e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  420 DVRIQQLQEILQDLQKRLESSEAERKQLQVELQSRRAELvclnnteisensSDLSQKLKETQSKYEEAMKEVLSVQKqmk 499
Cdd:TIGR02169  328 EAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEEL------------EDLRAELEEVDKEFAETRDELKDYRE--- 392
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  500 lglvspesmdnyshfhELRVTEEEINVLKQDLQNALEESERNKEKVRELEEKLverekgTVIKPPVEEYEEMKssycsvi 579
Cdd:TIGR02169  393 ----------------KLEKLKREINELKRELDRLQEELQRLSEELADLNAAI------AGIEAKINELEEEK------- 443
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  580 enmnKEKAflfEKYQEAQEEIMKLKDTLKSqmtqeASDEAEDMKEAMNRMIDELNKQVSELSQLYKEAQAELEDYRKRKS 659
Cdd:TIGR02169  444 ----EDKA---LEIKKQEWKLEQLAADLSK-----YEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRA 511
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  660 LEDVTAEYIhKAEHEKLMQLTNVSRAKA-----------------EDALSEMKSQYSKV----------LNELTQLKQLV 712
Cdd:TIGR02169  512 VEEVLKASI-QGVHGTVAQLGSVGERYAtaievaagnrlnnvvveDDAVAKEAIELLKRrkagratflpLNKMRDERRDL 590
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  713 DAQKENSVsITEHLQVIttlrtaakEMEEKISN-----LKEHLASKEVEVAK----------LEKQLLEEKAAMTDAMVP 777
Cdd:TIGR02169  591 SILSEDGV-IGFAVDLV--------EFDPKYEPafkyvFGDTLVVEDIEAARrlmgkyrmvtLEGELFEKSGAMTGGSRA 661
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  778 RSSYEKLQSSLESEVSVLASKLKESVKEKEKVHSEVVQIRSEVSQVKREKENIQTLLKSKEQEVNELLQKFQQAQEELAE 857
Cdd:TIGR02169  662 PRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEE 741
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|.
gi 1370488827  858 MKRYAES-SSKLEEDK------DKKINEMSKEVTKLKEALN 891
Cdd:TIGR02169  742 LEEDLSSlEQEIENVKselkelEARIEELEEDLHKLEEALN 782
PHA02878 PHA02878
ankyrin repeat protein; Provisional
59-208 3.48e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 69.91  E-value: 3.48e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  59 ECLRVMITHGVDVTAQDT-TGHSALHLAAKNSHHECIRKLLQSKCPAESVDSSGKTALHYAAAQGCLQAVQILCEHKSPI 137
Cdd:PHA02878  148 EITKLLLSYGADINMKDRhKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGAST 227
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370488827 138 NLKDLDGNIPLLLAVQNGHS-EICHFLLDHGADVNSRNK-SGRTALMLAceIGSSNAVEALIKKGADLNLVDS 208
Cdd:PHA02878  228 DARDKCGNTPLHISVGYCKDyDILKLLLEHGVDVNAKSYiLGLTALHSS--IKSERKLKLLLEYGADINSLNS 298
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
579-891 1.59e-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: 68.54  E-value: 1.59e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  579 IENMNKEKAFLFEKYQEAQEEIMKLKDTLksqmtqeasDEAEDMKEAMNRMIDELNKQVSELSQLYKEAQAELEDYRKRK 658
Cdd:TIGR02168  679 IEELEEKIEELEEKIAELEKALAELRKEL---------EELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERI 749
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  659 SLEDVTAEyihkaEHEKLMQLTNVSRAKAEDALSEMKSqyskvlnELTQLKQLVDAQKENSVSITEHLQ----VITTLRT 734
Cdd:TIGR02168  750 AQLSKELT-----ELEAEIEELEERLEEAEEELAEAEA-------EIEELEAQIEQLKEELKALREALDelraELTLLNE 817
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  735 AAKEMEEKISNLKEHLASKEVEVAKLEKQLLEEKAAMtdamvprSSYEKLQSSLESEVSVLASKLKESVKEKEKVHSEVV 814
Cdd:TIGR02168  818 EAANLRERLESLERRIAATERRLEDLEEQIEELSEDI-------ESLAAEIEELEELIEELESELEALLNERASLEEALA 890
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  815 QIRS--------------EVSQVKREKENIQTLLKSKEQEVNELLQKFQQAQEELAEM-KRYAESSSKLEEDKDKKINEM 879
Cdd:TIGR02168  891 LLRSeleelseelrelesKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEySLTLEEAEALENKIEDDEEEA 970
                          330
                   ....*....|..
gi 1370488827  880 SKEVTKLKEALN 891
Cdd:TIGR02168  971 RRRLKRLENKIK 982
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
422-774 2.87e-11

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 67.65  E-value: 2.87e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 422 RIQQLQEILQDLQKRLESSEAERKQ------LQVELQSRRAELVCLNNTEISENSSDLSQKLKETQSKYEEAMKevlsvq 495
Cdd:COG1196   187 NLERLEDILGELERQLEPLERQAEKaeryreLKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEA------ 260
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 496 kqmklglvspesmdnyshfhELRVTEEEINVLKQDLQNALEESERNKEKVRELEEKLVEREKGtvikppVEEYEEMKSSY 575
Cdd:COG1196   261 --------------------ELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQD------IARLEERRREL 314
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 576 CSVIENMNKEKAFLFEKYQEAQEEIMKLkdtlksqmtQEASDEAEDMKEAMNRMIDELNKQVSELSQLYKEAQAELEDyR 655
Cdd:COG1196   315 EERLEELEEELAELEEELEELEEELEEL---------EEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEE-L 384
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 656 KRKSLEDVTAEYIHKAEHEKLMQLTNVSRAKAEDALSEMKSQYSKVLNELTQLKQLVDAQKENSVSITEHLQVITTLRTA 735
Cdd:COG1196   385 AEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLEL 464
                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 1370488827 736 AKEMEEKISNLKEHLASKEVEVAKLEKQLLEEKAAMTDA 774
Cdd:COG1196   465 LAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADY 503
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
420-891 3.76e-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: 67.39  E-value: 3.76e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  420 DVRIQQLQEILQDLQKRLESSEAERKQLQVELQSRRAELvclnnTEISENSSDLSQKLKETQSKYEEAMKEVLSVQKQMK 499
Cdd:TIGR02168  322 EAQLEELESKLDELAEELAELEEKLEELKEELESLEAEL-----EELEAELEELESRLEELEEQLETLRSKVAQLELQIA 396
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  500 LglvspesmdnyshfhelrvTEEEINVLKQDLQNALEESERNKEKVRELEEKLVEREKGTViKPPVEEYEEMKSSYCSVI 579
Cdd:TIGR02168  397 S-------------------LNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKEL-QAELEELEEELEELQEEL 456
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  580 ENMNKEKAFLFEKYQEAQEEIMKLKDTLKS---------QMTQEASDEAEDMKEAMNRMID------------------- 631
Cdd:TIGR02168  457 ERLEEALEELREELEEAEQALDAAERELAQlqarldsleRLQENLEGFSEGVKALLKNQSGlsgilgvlselisvdegye 536
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  632 ---------ELNKQVSELSQLYKEAQAELEDYRKRKS----LEDVTAEYIHKAEHEKLMQLTNVSRAKAEdaLSEMKSQY 698
Cdd:TIGR02168  537 aaieaalggRLQAVVVENLNAAKKAIAFLKQNELGRVtflpLDSIKGTEIQGNDREILKNIEGFLGVAKD--LVKFDPKL 614
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  699 SKVLN----------------------------------------------------------ELTQLKQLVDAQKEnsv 720
Cdd:TIGR02168  615 RKALSyllggvlvvddldnalelakklrpgyrivtldgdlvrpggvitggsaktnssilerrrEIEELEEKIEELEE--- 691
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  721 SITEHLQVITTLRTAAKEMEEKISNLKEHLASKEVEVAKLEKQLLEEKAAMTDAMVPRSSYEKLQSSLESEVSVLASKLK 800
Cdd:TIGR02168  692 KIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLE 771
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  801 ESVKEKEKVHSEVVQIRSEVSQVKREKENIQTLLKSKEQEVNELLQKFQQAQEELAEMKRYAESSSKLEEDKDKKINEMS 880
Cdd:TIGR02168  772 EAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELS 851
                          570
                   ....*....|.
gi 1370488827  881 KEVTKLKEALN 891
Cdd:TIGR02168  852 EDIESLAAEIE 862
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
620-856 4.53e-11

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 66.96  E-value: 4.53e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 620 EDMKEAMNRMIDELNKQVSELSQLYKEAQAELEDYRKRKSLEDVTAEyihkaeheklMQLTNVSRAKAEDALSEMKSQYS 699
Cdd:COG3206   167 ELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVDLSEE----------AKLLLQQLSELESQLAEARAELA 236
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 700 KVLNELTQLKQLVDAQKENSVSITEHlQVITTLRTAAKEMEEKISNLKEHLASKEVEVAKLEKQLLEEKAAMtdamvpRS 779
Cdd:COG3206   237 EAEARLAALRAQLGSGPDALPELLQS-PVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQL------QQ 309
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 780 SYEKLQSSLESEVSVLASKLKESVKEKEKVHSEVVQI---RSEVSQVKREKENIQTLLkskeqevNELLQKFQQAQEELA 856
Cdd:COG3206   310 EAQRILASLEAELEALQAREASLQAQLAQLEARLAELpelEAELRRLEREVEVARELY-------ESLLQRLEEARLAEA 382
PTZ00121 PTZ00121
MAEBL; Provisional
431-890 7.23e-11

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 66.70  E-value: 7.23e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  431 QDLQKRLESSEAERKQLQVElQSRRAElvclnntEISENSSDLSQKLKETQSKYEEAMKEVLSVQKQMKLGLVSPESMDN 510
Cdd:PTZ00121  1293 DEAKKAEEKKKADEAKKKAE-EAKKAD-------EAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEE 1364
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  511 YSHFHELRVTEEEINV--------LKQDLQNALEESERNKEKVRELEEKLVEREKGTVIKPPVEEYEEMKSSYCSVIENM 582
Cdd:PTZ00121  1365 KAEAAEKKKEEAKKKAdaakkkaeEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAK 1444
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  583 N----KEKAFLFEKYQEAQ---EEIMKLKDTLKSQMTQEASDEAEDMKEAMNRMIDELNKQVSELSQLYKEAQAE----- 650
Cdd:PTZ00121  1445 KadeaKKKAEEAKKAEEAKkkaEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEeakka 1524
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  651 -----LEDYRK----RKSLEDVTAEYIHKAEH-EKLMQLTNVSRAKAEDALSEMKSQYSKVLN--ELTQLKQLVDAQKEN 718
Cdd:PTZ00121  1525 deakkAEEAKKadeaKKAEEKKKADELKKAEElKKAEEKKKAEEAKKAEEDKNMALRKAEEAKkaEEARIEEVMKLYEEE 1604
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  719 SVSITEHLQVITTLRTAAKEM--EEKISNLKEHLASKEVEVAKLEKQL--LEEKAAMTDAMVPRSSYEKLQSSLESEVSV 794
Cdd:PTZ00121  1605 KKMKAEEAKKAEEAKIKAEELkkAEEEKKKVEQLKKKEAEEKKKAEELkkAEEENKIKAAEEAKKAEEDKKKAEEAKKAE 1684
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  795 LASKLK-ESVKEKEKVHSEVVQIRSEVSQVKREKENIQtllksKEQEVNELlqKFQQAQEELAEMKRYAESSSKLEEDKd 873
Cdd:PTZ00121  1685 EDEKKAaEALKKEAEEAKKAEELKKKEAEEKKKAEELK-----KAEEENKI--KAEEAKKEAEEDKKKAEEAKKDEEEK- 1756
                          490
                   ....*....|....*..
gi 1370488827  874 KKINEMSKEVTKLKEAL 890
Cdd:PTZ00121  1757 KKIAHLKKEEEKKAEEI 1773
Ank_4 pfam13637
Ankyrin repeats (many copies);
113-164 7.97e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 58.05  E-value: 7.97e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1370488827 113 TALHYAAAQGCLQAVQILCEHKSPINLKDLDGNIPLLLAVQNGHSEICHFLL 164
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
416-891 1.47e-10

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: 65.04  E-value: 1.47e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 416 TTDNDVRIQQLQEILQDLQKRLESSEAERKQLQVELQSRRAELVCLNNT--EISENSSDLSQKLKETQSKYEEAMKEVLS 493
Cdd:TIGR04523  28 ANKQDTEEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKikILEQQIKDLNDKLKKNKDKINKLNSDLSK 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 494 VQKQMK--------------------------LGLVSPESMDNYSHFHELRVTEEEINVLKQDLQNALEESERNKEKVRE 547
Cdd:TIGR04523 108 INSEIKndkeqknklevelnklekqkkenkknIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQK 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 548 LEEKL-VEREKGTVIKPPVEEYEEMKSSYCSVIENMNKEKAFLFEKYQEAQEEIMKLKDTLKSQMTQ--EASDEAEDMKE 624
Cdd:TIGR04523 188 NIDKIkNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQlnQLKDEQNKIKK 267
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 625 AMNRMIDEL---NKQVSELSQLYKEAQAELEDYRKRKSLEDVTAEYIHKAEHEKLMQLTNVSRAKAEDALSEMKSQYSKV 701
Cdd:TIGR04523 268 QLSEKQKELeqnNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQL 347
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 702 LNELTQL---------------KQLVDAQKENSvsitEHLQVITTLRTAAKEMEEKISNLKEHLASKEVEVAKLEKQLLE 766
Cdd:TIGR04523 348 KKELTNSesensekqreleekqNEIEKLKKENQ----SYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKEL 423
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 767 EKAAMTDAMVPRSSYEKLQSSLESEVSVLASKLKESVKEKEKVHSEVVQIRSEVSQVKREKENIQTLLKSKEQEVNELLQ 846
Cdd:TIGR04523 424 LEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNE 503
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*
gi 1370488827 847 KFQQAQEELAEMKRYAESSSKLEEDKDKKINEMSKEVTKLKEALN 891
Cdd:TIGR04523 504 EKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELN 548
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
422-891 2.47e-10

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 64.57  E-value: 2.47e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 422 RIQQLQEILQDLQKRLESSEAERKQLQVELQSRRAELvclnnTEISENSSDLSQKLKETQSKYEEAMKEVLSVQKQMklg 501
Cdd:COG1196   303 DIARLEERRRELEERLEELEEELAELEEELEELEEEL-----EELEEELEEAEEELEEAEAELAEAEEALLEAEAEL--- 374
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 502 lvSPESMDNYSHFHELRVTEEEINVLKQDLQNALEESERNKEKVRELEEKLVEREkgtvikppvEEYEEMKSSYCSVIEN 581
Cdd:COG1196   375 --AEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELE---------EALAELEEEEEEEEEA 443
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 582 MNKEKAFLFEKYQEAQEEIMKLKDTLKSQMTQEASDEAEDMKEAMNRMIDELNKQVSELSQLYKEAQAELEDYRKRKSL- 660
Cdd:COG1196   444 LEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLa 523
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 661 ---------EDVTAEYIHKAEHEKLMQLTNVSRAKAEDALSEMKSQYSKVLNELTQLKQLVDAQKENSVSITEHLQVITT 731
Cdd:COG1196   524 gavavligvEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDL 603
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 732 LRTAAKEMEEKISNLKEHLASKEVEVA----------KLEKQLLEEKAAMTDAMVPRSSYE----KLQSSLESEVSVLAS 797
Cdd:COG1196   604 VASDLREADARYYVLGDTLLGRTLVAArleaalrravTLAGRLREVTLEGEGGSAGGSLTGgsrrELLAALLEAEAELEE 683
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 798 KLKESVKEKEKVHSEVVQIRSEVSQVKREKENIQTLLKSKEQEVNELLQKFQQAQEELAEMKRYAESSSKLEEDKDKKIN 877
Cdd:COG1196   684 LAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLE 763
                         490
                  ....*....|....
gi 1370488827 878 EMSKEVTKLKEALN 891
Cdd:COG1196   764 ELERELERLEREIE 777
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
80-215 2.64e-10

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 64.26  E-value: 2.64e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  80 SALHLAAKNSHHECIRKLLqsKCPaeSVD-----SSGKTALHYAAAQGCLQAVQILCEH-----KSPINLKDLDGNIPLL 149
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLL--KCP--SCDlfqrgALGETALHVAALYDNLEAAVVLMEAapelvNEPMTSDLYQGETALH 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 150 LAVQNGHSEICHFLLDHGADVNS---------RNKS-----GRTALMLACEIGSSNAVEALIKKGADLNLVDSLGYNALH 215
Cdd:cd22192    95 IAVVNQNLNLVRELIARGADVVSpratgtffrPGPKnliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLH 174
PHA03095 PHA03095
ankyrin-like protein; Provisional
58-231 3.98e-10

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 63.12  E-value: 3.98e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  58 VECLRVMITHGVDVTAQDTTGHSALHLaaknshhecirkLLQSKCPAESVDssgktalhyaaaqgclqavqILCEHKSPI 137
Cdd:PHA03095   63 KDIVRLLLEAGADVNAPERCGFTPLHL------------YLYNATTLDVIK--------------------LLIKAGADV 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 138 NLKDLDGNIPL--LLAVQNGHSEICHFLLDHGADVNSRNKSGRTAlmLACEIGSSNA----VEALIKKGADLNLVDSLGY 211
Cdd:PHA03095  111 NAKDKVGRTPLhvYLSGFNINPKVIRLLLRKGADVNALDLYGMTP--LAVLLKSRNAnvelLRLLIDAGADVYAVDDRFR 188
                         170       180
                  ....*....|....*....|..
gi 1370488827 212 NALHYSKLS--ENAGIQSLLLS 231
Cdd:PHA03095  189 SLLHHHLQSfkPRARIVRELIR 210
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
528-891 4.23e-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: 63.92  E-value: 4.23e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  528 KQDLQNALEESERNKEKV----RELEEKLVEREKGTVIkppVEEYEEMKSsycsviENMNKEKAFLFEKYQEAQEEIMKL 603
Cdd:TIGR02168  174 RKETERKLERTRENLDRLedilNELERQLKSLERQAEK---AERYKELKA------ELRELELALLVLRLEELREELEEL 244
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  604 KDTLKSQMTQEASDEAE-DMKEAMnrmIDELNKQVSELSQLYKEAQAELEDYRKRksledvtaeyIHKAEHEKlmqltnv 682
Cdd:TIGR02168  245 QEELKEAEEELEELTAElQELEEK---LEELRLEVSELEEEIEELQKELYALANE----------ISRLEQQK------- 304
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  683 srakaedalsemksqysKVLNEltQLKQLVDAQKENSVSITEHLQVITTLRTAAKEMEEKISNLKEHLASKEVEVAKLEK 762
Cdd:TIGR02168  305 -----------------QILRE--RLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEA 365
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  763 QLLEEKAAMTDAMVPRSSYEKLQSSLESEVSVLASKLKESVKEKEKVHSEVVQIRSEVSQVKREKEN-----IQTLLKSK 837
Cdd:TIGR02168  366 ELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEaelkeLQAELEEL 445
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1370488827  838 EQEVNELLQKFQQAQEELAEMKRYAESSSKLEEDKDKKINEMSKEVTKLKEALN 891
Cdd:TIGR02168  446 EEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQE 499
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
517-891 4.33e-10

Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.


Pssm-ID: 428797 [Multi-domain]  Cd Length: 542  Bit Score: 63.33  E-value: 4.33e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 517 LRVTEEEINVLKQDLQNALEESERNKEKVRELEEKlverekgtvikppveeYEEMKSSYcsvienmnKEKAFLFEKYQEA 596
Cdd:pfam06160  95 LDDIEEDIKQILEELDELLESEEKNREEVEELKDK----------------YRELRKTL--------LANRFSYGPAIDE 150
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 597 QEEIMKLKDTLKSQMTQEASD----EAEDMKEAMNRMIDELNKQVSELSQLYKEAQAELEDyrkrkSLEDVTAEYihkae 672
Cdd:pfam06160 151 LEKQLAEIEEEFSQFEELTESgdylEAREVLEKLEEETDALEELMEDIPPLYEELKTELPD-----QLEELKEGY----- 220
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 673 HEKLMQLTNVSRAKAEDALSEMKSQYSKVLNELTQLKqlVDAQKENSVSITEHLQ----VITTLRTAAKEMEEKISNLKE 748
Cdd:pfam06160 221 REMEEEGYALEHLNVDKEIQQLEEQLEENLALLENLE--LDEAEEALEEIEERIDqlydLLEKEVDAKKYVEKNLPEIED 298
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 749 HLAskevEVAKLEKQLLEEKAAMTDAMVPRSSYEKLQSSLESEVSVLASKLKESVK---EKEKVHSEVV----QIRSEVS 821
Cdd:pfam06160 299 YLE----HAEEQNKELKEELERVQQSYTLNENELERVRGLEKQLEELEKRYDEIVErleEKEVAYSELQeeleEILEQLE 374
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370488827 822 QVKREKENIQTLLKS---KEQEVNELLQKFQQaqeELAEMKRYAESS--SKLEEDKDKKINEMSKEVTKLKEALN 891
Cdd:pfam06160 375 EIEEEQEEFKESLQSlrkDELEAREKLDEFKL---ELREIKRLVEKSnlPGLPESYLDYFFDVSDEIEDLADELN 446
PHA02875 PHA02875
ankyrin repeat protein; Provisional
52-230 1.01e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 61.93  E-value: 1.01e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  52 AAAKGHVECLRVMITHGVDVTAQDTTGHSALHLAAKNSHHECIrKLLQSKCPAESVDSSG-KTALHYAAAQGCLQAVQIL 130
Cdd:PHA02875    9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAI-KLLMKHGAIPDVKYPDiESELHDAVEEGDVKAVEEL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 131 CEHKSPINlkDL---DGNIPLLLAVQNGHSEICHFLLDHGADVNSRNKSGRTALMLACEIGSSNAVEALIKKGADLNLVD 207
Cdd:PHA02875   88 LDLGKFAD--DVfykDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIED 165
                         170       180
                  ....*....|....*....|...
gi 1370488827 208 SLGYNALHYSKLSENAGIQSLLL 230
Cdd:PHA02875  166 CCGCTPLIIAMAKGDIAICKMLL 188
Ank_4 pfam13637
Ankyrin repeats (many copies);
47-98 2.54e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 53.82  E-value: 2.54e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1370488827  47 HCFHLAAAKGHVECLRVMITHGVDVTAQDTTGHSALHLAAKNSHHECIRKLL 98
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
163-216 2.68e-09

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 53.89  E-value: 2.68e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1370488827 163 LLDHG-ADVNSRNKSGRTALMLACEIGSSNAVEALIKKGADLNLVDSLGYNALHY 216
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDL 55
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
430-859 2.86e-09

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: 61.19  E-value: 2.86e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 430 LQDLQKRLESSEAERKQLQVELQSRRAELVCLNNTEISENSSDLSQKLKETQSKYEEAMKEVLSVQK----------QMK 499
Cdd:TIGR04523 269 LSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKiisqlneqisQLK 348
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 500 LGLVSPESmDNYSHFHELRVTEEEINVLKQDLQNALEESERNKEKVRELEEKLverekgtvikppvEEYEEMKSSYCSVI 579
Cdd:TIGR04523 349 KELTNSES-ENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKI-------------QNQEKLNQQKDEQI 414
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 580 ENMNKEKAFLFEKYQEAQEEIMKLKDTLKSQMTQEASDEAEdmKEAMNRMIDELNKQVSELSQLYKEAQAELEDyrKRKS 659
Cdd:TIGR04523 415 KKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELI--IKNLDNTRESLETQLKVLSRSINKIKQNLEQ--KQKE 490
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 660 LEDVTAEyihkaeheklmqltnvsrakaedaLSEMKSQYSKVLNELTQLKQLVDAQKENsvsitehlqvITTLRTAAKEM 739
Cdd:TIGR04523 491 LKSKEKE------------------------LKKLNEEKKELEEKVKDLTKKISSLKEK----------IEKLESEKKEK 536
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 740 EEKISNLKEHLASKEVEVAK--LEKQLLEEKAAMTDAMVPRSSYEKLQSSLESEVSVLASKLKESVKEKEKVHSEVVQIR 817
Cdd:TIGR04523 537 ESKISDLEDELNKDDFELKKenLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLE 616
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|..
gi 1370488827 818 SEVSQVKREKENIQTLLKSKEQEVNELLQKFQQAQEELAEMK 859
Cdd:TIGR04523 617 KELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIR 658
Ank_4 pfam13637
Ankyrin repeats (many copies);
147-197 2.92e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 53.82  E-value: 2.92e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1370488827 147 PLLLAVQNGHSEICHFLLDHGADVNSRNKSGRTALMLACEIGSSNAVEALI 197
Cdd:pfam13637   4 ALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
304-891 4.47e-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: 60.46  E-value: 4.47e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  304 FKAEISSIRENKDRLSDSTTGADSLLDISSE--ADQQDLLSLLQAKVASLTLHNKELQDKLQAKSPKEAEADLSFDSYHS 381
Cdd:TIGR02168  307 LRERLANLERQLEELEAQLEELESKLDELAEelAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRS 386
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  382 tqtdlgpslgkpgetsppdsksspsvLIHSLGKSTTDNDVRIQQLQEILQDLQKRLESSEAERKQLQVELQSRRAELVCL 461
Cdd:TIGR02168  387 --------------------------KVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQA 440
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  462 NNTEISENSSDLSQKLKETQSKYEEAMKEVLSVQ----------KQMKLGLVSPESM-DNYSHFHE-------------- 516
Cdd:TIGR02168  441 ELEELEEELEELQEELERLEEALEELREELEEAEqaldaaerelAQLQARLDSLERLqENLEGFSEgvkallknqsglsg 520
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  517 --------LRVTEE-EI---NVLKQDLQNALEEserNKEKVRELEEKLVEREKGTVI----------KPPVEEYEEMKSS 574
Cdd:TIGR02168  521 ilgvlselISVDEGyEAaieAALGGRLQAVVVE---NLNAAKKAIAFLKQNELGRVTflpldsikgtEIQGNDREILKNI 597
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  575 YCSVIENMNKEKA---------------FLFEKYQEAQEEIMKLK----------DTLKSQ--MTQeASDEAEDMKEAMN 627
Cdd:TIGR02168  598 EGFLGVAKDLVKFdpklrkalsyllggvLVVDDLDNALELAKKLRpgyrivtldgDLVRPGgvITG-GSAKTNSSILERR 676
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  628 RMIDELNKQVSELSQLYKEAQAELEDYrkRKSLEDVTAEyIHKAEHEKLMQLTNVSRAKAEDALSEMKSQyskvlNELTQ 707
Cdd:TIGR02168  677 REIEELEEKIEELEEKIAELEKALAEL--RKELEELEEE-LEQLRKELEELSRQISALRKDLARLEAEVE-----QLEER 748
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  708 LKQLVDAQKENSVSITEHLQVITTLRTAAKEMEEKISNLKEHLASKEVEVAKLEKQLLEEKAAMTDamvprssyeklqss 787
Cdd:TIGR02168  749 IAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTL-------------- 814
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  788 LESEVSVLASKLKESVKEKEKVHSEVVQIRSEVSQVKREKENIQTLLKSKEQEVNELLQKFQQAQEELAEMKRYAESSSK 867
Cdd:TIGR02168  815 LNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRS 894
                          650       660
                   ....*....|....*....|....
gi 1370488827  868 LEEDKDKKINEMSKEVTKLKEALN 891
Cdd:TIGR02168  895 ELEELSEELRELESKRSELRRELE 918
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
415-697 5.44e-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: 60.46  E-value: 5.44e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  415 STTDNDVRIQQLQEILQDLQKRLESSEAERKQLQVELQSRRAELVCLNNTEIsenssDLSQKLKETQSKYEEAMKEVLSV 494
Cdd:TIGR02168  671 SILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELE-----ELSRQISALRKDLARLEAEVEQL 745
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  495 QKQMKLGLVSPESMDNY---------SHFHELRVTEEEINVLKQDLQNALEESERNKEKVRELEEKLVE--------REK 557
Cdd:TIGR02168  746 EERIAQLSKELTELEAEieeleerleEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLlneeaanlRER 825
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  558 GTVIKPPVEEYEEMKSSYCSVIENMNKEKAFLFEKYQEAQEEIMKLKDTLKS-----QMTQEASDEAEDMKEAMNRMIDE 632
Cdd:TIGR02168  826 LESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEAllnerASLEEALALLRSELEELSEELRE 905
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370488827  633 LNKQVSELSQLYKEAQAELEDYRKRKS---------LEDVTAEYIHKAE-HEKLMQLTNVSRAKAEDALSEMKSQ 697
Cdd:TIGR02168  906 LESKRSELRRELEELREKLAQLELRLEglevridnlQERLSEEYSLTLEeAEALENKIEDDEEEARRRLKRLENK 980
PHA02876 PHA02876
ankyrin repeat protein; Provisional
50-230 6.59e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 59.69  E-value: 6.59e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  50 HLAAAKGHVECLRVMITHGVDVTAQDTTGHSALHLAAKNSHHECIRKLLQSKCPAESVDSSgktaLHYAAAQGCLQAVQI 129
Cdd:PHA02876  183 HYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINKNDLS----LLKAIRNEDLETSLL 258
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 130 LCEHKSPINLKDLDGNIPLLLAVQNGH-SEICHFLLDHGADVNSRNKSGRTALMLACEIG-SSNAVEALIKKGADLNLVD 207
Cdd:PHA02876  259 LYDAGFSVNSIDDCKNTPLHHASQAPSlSRLVPKLLERGADVNAKNIKGETPLYLMAKNGyDTENIRTLIMLGADVNAAD 338
                         170       180
                  ....*....|....*....|....
gi 1370488827 208 SLGYNALHY-SKLSENAGIQSLLL 230
Cdd:PHA02876  339 RLYITPLHQaSTLDRNKDIVITLL 362
PHA02876 PHA02876
ankyrin repeat protein; Provisional
64-217 7.50e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 59.69  E-value: 7.50e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  64 MITHGVDVTAQDTTGHSALHLAAKNSHH-ECIRKLLQSKCPAESVDSSGKTALHYAAAQGCLQAVQI-LCEHKSPINLKD 141
Cdd:PHA02876  293 LLERGADVNAKNIKGETPLYLMAKNGYDtENIRTLIMLGADVNAADRLYITPLHQASTLDRNKDIVItLLELGANVNARD 372
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370488827 142 LDGNIPLLLAVQNGHSEICHFLLDHGADVNSRNKSGRTALMLA-CEIGSSNAVEALIKKGADLNLVDSLGYNALHYS 217
Cdd:PHA02876  373 YCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFAlCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYA 449
PHA02876 PHA02876
ankyrin repeat protein; Provisional
38-216 8.67e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 59.31  E-value: 8.67e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  38 VRARPRKLKHCFHLAAAKGH-VECLRVMITHGVDVTAQDTTGHSALHLAAK-NSHHECIRKLLQSKCPAESVDSSGKTAL 115
Cdd:PHA02876  300 VNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQASTlDRNKDIVITLLELGANVNARDYCDKTPI 379
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 116 HYAAAQGCLQAVQILCEHKSPINL--KDLDGNIPLLLAVQNGHSEIcHFLLDHGADVNSRNKSGRTALMLACEIGSS-NA 192
Cdd:PHA02876  380 HYAAVRNNVVIINTLLDYGADIEAlsQKIGTALHFALCGTNPYMSV-KTLIDRGANVNSKNKDLSTPLHYACKKNCKlDV 458
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1370488827 193 VEALIKKGADLNLVD---------SLGYNA-----LHY 216
Cdd:PHA02876  459 IEMLLDNGADVNAINiqnqyplliALEYHGivnilLHY 496
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
517-891 1.10e-08

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 59.08  E-value: 1.10e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 517 LRVTEEEINVLKQDLQNALEESERNKEKVRELEEKlverekgtvikppveeYEEMKSSYcsvienmnKEKAFLFEKYQEA 596
Cdd:PRK04778  114 LDLIEEDIEQILEELQELLESEEKNREEVEQLKDL----------------YRELRKSL--------LANRFSFGPALDE 169
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 597 QEEIMKLKDTLKSQMTQEASD----EAEDMKEAMNRMIDELNKQVSELSQLYKEAQAELEDyrkrkSLEDVtaeyihKAE 672
Cdd:PRK04778  170 LEKQLENLEEEFSQFVELTESgdyvEAREILDQLEEELAALEQIMEEIPELLKELQTELPD-----QLQEL------KAG 238
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 673 HEKLMQ----LTNVsraKAEDALSEMKSQYSKVLNELTQLKqlVDAQKENSVSITEHLQ----VITTLRTAAKEMEEKIS 744
Cdd:PRK04778  239 YRELVEegyhLDHL---DIEKEIQDLKEQIDENLALLEELD--LDEAEEKNEEIQERIDqlydILEREVKARKYVEKNSD 313
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 745 NLKEHL--ASKEVEVAKLEKQLLEEKAAMTDAMVprSSYEKLQSSLESEVSVLaSKLKESVKEKEKVHSEVV----QIRS 818
Cdd:PRK04778  314 TLPDFLehAKEQNKELKEEIDRVKQSYTLNESEL--ESVRQLEKQLESLEKQY-DEITERIAEQEIAYSELQeeleEILK 390
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370488827 819 EVSQVKREKENIQTLLKSKEQEVNELLQKFQQAQEELAEMKRYAESSS--KLEEDKDKKINEMSKEVTKLKEALN 891
Cdd:PRK04778  391 QLEEIEKEQEKLSEMLQGLRKDELEAREKLERYRNKLHEIKRYLEKSNlpGLPEDYLEMFFEVSDEIEALAEELE 465
Ank_4 pfam13637
Ankyrin repeats (many copies);
78-130 1.14e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 51.89  E-value: 1.14e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1370488827  78 GHSALHLAAKNSHHECIRKLLQSKCPAESVDSSGKTALHYAAAQGCLQAVQIL 130
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
422-934 1.53e-08

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 58.91  E-value: 1.53e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  422 RIQQLQEILQDLQKRLESSEAERKQLQVELQSRRAELVCLNnTEISEnssdLSQKLKETQSKYEEAMKEVLSVQKQMKLG 501
Cdd:TIGR02168  233 RLEELREELEELQEELKEAEEELEELTAELQELEEKLEELR-LEVSE----LEEEIEELQKELYALANEISRLEQQKQIL 307
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  502 LVSPESMDNyshfhELRVTEEEINVLKQDLQNALEESERNKEKVRELEEKLVEREKgtVIKPPVEEYEEMKSSYCSVIEN 581
Cdd:TIGR02168  308 RERLANLER-----QLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEA--ELEELEAELEELESRLEELEEQ 380
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  582 MNKEKAFLFEKYQE---AQEEIMKLKDTLKS------QMTQEASDEAEDMKEAMnrmIDELNKQVSELSQLYKEAQAELE 652
Cdd:TIGR02168  381 LETLRSKVAQLELQiasLNNEIERLEARLERledrreRLQQEIEELLKKLEEAE---LKELQAELEELEEELEELQEELE 457
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  653 DYRKRKSLEDVTAEYIHKAEHEKLMQLTNV-SRAKAEDALSEMKSQYSKVLNELTQ-----------LKQL--VDAQKEN 718
Cdd:TIGR02168  458 RLEEALEELREELEEAEQALDAAERELAQLqARLDSLERLQENLEGFSEGVKALLKnqsglsgilgvLSELisVDEGYEA 537
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  719 SVSIT--EHLQ--VITTLRTAAKEmeekISNLKEHLASK-------EVEVAKLEKQLLEEKAAMTDAMVPRSSYEKLQSS 787
Cdd:TIGR02168  538 AIEAAlgGRLQavVVENLNAAKKA----IAFLKQNELGRvtflpldSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPK 613
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  788 LESEVSVL----------------ASKLKE-----------------SVKEKEKVHSEVVQIRSEVSQVKREKENIQTLL 834
Cdd:TIGR02168  614 LRKALSYLlggvlvvddldnalelAKKLRPgyrivtldgdlvrpggvITGGSAKTNSSILERRREIEELEEKIEELEEKI 693
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  835 KSKEQEVNELLQKFQQAQEELAEMKryaesssKLEEDKDKKINEMSKEVTKL-KEALNSLSQLSYSTSSSKRQSQQLEAL 913
Cdd:TIGR02168  694 AELEKALAELRKELEELEEELEQLR-------KELEELSRQISALRKDLARLeAEVEQLEERIAQLSKELTELEAEIEEL 766
                          570       580
                   ....*....|....*....|.
gi 1370488827  914 QQQVKQLQNQLAECKKQHQEV 934
Cdd:TIGR02168  767 EERLEEAEEELAEAEAEIEEL 787
PTZ00121 PTZ00121
MAEBL; Provisional
422-911 1.72e-08

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 59.00  E-value: 1.72e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  422 RIQQLQEILQDLQKRLESSEAERKQLQVELQSRRAELVCLNNTEISENSSDLSQKLKETQSKYEEAMKEVLSVQKQMKLG 501
Cdd:PTZ00121  1225 KAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKA 1304
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  502 LVSPESMDNYSHFHELRVTEEEINVLKQDLQNALEESERNKEKVRELEEKLVEREKGTVIKppvEEYEEMKSSYCSVIEN 581
Cdd:PTZ00121  1305 DEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEK---AEAAEKKKEEAKKKAD 1381
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  582 MNKEKAFLFEKYQEAQ---EEIMKLKDTLKSQMTQEASDEAEDMKEAMNRMIDELNKQVSElSQLYKEAQAELEDYRKRK 658
Cdd:PTZ00121  1382 AAKKKAEEKKKADEAKkkaEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEE-AKKADEAKKKAEEAKKAE 1460
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  659 SLEDvTAEYIHKAEHEKLMQLTNVSRAKAEDALSEMKSQYSKVLNELTQLKQLVDAQKENSVSITEHLQVITTLRTA--A 736
Cdd:PTZ00121  1461 EAKK-KAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKAdeA 1539
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  737 KEMEEKiSNLKEHLASKEVEVAKLEKQLLEEKAAMTDAMVPRSSYEKLQSSLESEVSVLASKLKESVKEKEKVHSEVVQI 816
Cdd:PTZ00121  1540 KKAEEK-KKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEA 1618
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  817 RSEVSQVKREKENIQTLLKSKEQEVNELLQKFQQAQEELAEMKRYAESSSKLEEDKDKkinemSKEVTKLKEALNSLSQL 896
Cdd:PTZ00121  1619 KIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKK-----AEEAKKAEEDEKKAAEA 1693
                          490
                   ....*....|....*
gi 1370488827  897 SYSTSSSKRQSQQLE 911
Cdd:PTZ00121  1694 LKKEAEEAKKAEELK 1708
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
518-888 2.32e-08

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 58.13  E-value: 2.32e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 518 RVTEEEINVLKQ-DLQNALEESERNKEKVRELEEKLVErekgtvIKPPVEEYEEMKSSYCSVIENMNKekafLFEKYQEA 596
Cdd:PRK02224  180 RVLSDQRGSLDQlKAQIEEKEEKDLHERLNGLESELAE------LDEEIERYEEQREQARETRDEADE----VLEEHEER 249
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 597 QEEIMKLKDTLKSqmTQEASDEAEDMKEAMNRMIDELNKQVSELSQLYKEAQAELEdyrkrksLEDVTAEYI--HKAEHE 674
Cdd:PRK02224  250 REELETLEAEIED--LRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAG-------LDDADAEAVeaRREELE 320
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 675 KlmqltnvSRAKAEDALSEMKSQYSKVLNELTQLKQLVDAQKENSvsitehlqviTTLRTAAKEMEEKISNLKEHLASKE 754
Cdd:PRK02224  321 D-------RDEELRDRLEECRVAAQAHNEEAESLREDADDLEERA----------EELREEAAELESELEEAREAVEDRR 383
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 755 VEVAKLEKQLLEEKAAMTDAMVPRSSYEKLQSSLESEVSVLASKLKE---SVKEKEKVHSEVVQIRSE------------ 819
Cdd:PRK02224  384 EEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAEleaTLRTARERVEEAEALLEAgkcpecgqpveg 463
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 820 ------VSQVKREKENIQTLLKSKEQEVNELLQKFQQAqEELAEMKRYAES-------SSKLEEDKDKKINEMSKEVTKL 886
Cdd:PRK02224  464 sphvetIEEDRERVEELEAELEDLEEEVEEVEERLERA-EDLVEAEDRIERleerredLEELIAERRETIEEKRERAEEL 542

                  ..
gi 1370488827 887 KE 888
Cdd:PRK02224  543 RE 544
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
523-890 2.64e-08

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 58.15  E-value: 2.64e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 523 EINVLKQDLQNALEESERNKEKVRELEEKLVE-----REKGTVIKPPVEEYEEMKSSYcsvienmnKEKAFLFEKYQEAQ 597
Cdd:PRK03918  173 EIKRRIERLEKFIKRTENIEELIKEKEKELEEvlreiNEISSELPELREELEKLEKEV--------KELEELKEEIEELE 244
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 598 EEIMKLKDTLKSqmTQEASDEAEDMKEAMNRMIDELNKQVSELSQLYKEAqaelEDYRKRKSLEDVTAEYIHKAEHE--K 675
Cdd:PRK03918  245 KELESLEGSKRK--LEEKIRELEERIEELKKEIEELEEKVKELKELKEKA----EEYIKLSEFYEEYLDELREIEKRlsR 318
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 676 LMQLTNVSRAKAEDA------LSEMKSQYSKVLNELTQLKQLVDA---------------QKENSVSITEHLQVITTLRT 734
Cdd:PRK03918  319 LEEEINGIEERIKELeekeerLEELKKKLKELEKRLEELEERHELyeeakakkeelerlkKRLTGLTPEKLEKELEELEK 398
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 735 AAKEMEEKISNLKEHLASKEVEVAKLEKQLLEEKAAMTDAMVPRSSY-----EKLQSSLESEVSVLASKLKESVKEKEKV 809
Cdd:PRK03918  399 AKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELteehrKELLEEYTAELKRIEKELKEIEEKERKL 478
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 810 HSEVVQIRSEVSQVKREKENIQTL--LKSKEQEVNEL-LQKFQQAQEELAEMKRYA---ESSSKLEEDKDKKINEMSKEV 883
Cdd:PRK03918  479 RKELRELEKVLKKESELIKLKELAeqLKELEEKLKKYnLEELEKKAEEYEKLKEKLiklKGEIKSLKKELEKLEELKKKL 558

                  ....*..
gi 1370488827 884 TKLKEAL 890
Cdd:PRK03918  559 AELEKKL 565
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
579-890 2.79e-08

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 58.16  E-value: 2.79e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  579 IENMNKEKAFLFEKYQEAQEEIMKLKDTLK--SQMTQEASDEAEDMK---EAMNRMIDELNKQVSELSQLYKEAQAELED 653
Cdd:TIGR02169  683 LEGLKRELSSLQSELRRIENRLDELSQELSdaSRKIGEIEKEIEQLEqeeEKLKERLEELEEDLSSLEQEIENVKSELKE 762
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  654 YRKRKS-LEDVTAEYihKAEHEKLmqltnvsrakaEDALSEmkSQYSKVLNELTQLKQLVdaqkensvsitehlqvittl 732
Cdd:TIGR02169  763 LEARIEeLEEDLHKL--EEALNDL-----------EARLSH--SRIPEIQAELSKLEEEV-------------------- 807
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  733 rtaaKEMEEKISNLKEHLASKEVEVAKLEKQLLEEKAAMTDAMVPRSSYEKLQSSLESEVSVLASKLKES-------VKE 805
Cdd:TIGR02169  808 ----SRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELeaalrdlESR 883
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  806 KEKVHSEVVQIRSEVSQVKREKENIQTLLKSKEQEVNELLQKFQQAQEELAEMKR--YAESSSKLEEDKDKKINEMSKEV 883
Cdd:TIGR02169  884 LGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDpkGEDEEIPEEELSLEDVQAELQRV 963

                   ....*..
gi 1370488827  884 TKLKEAL 890
Cdd:TIGR02169  964 EEEIRAL 970
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
414-652 3.25e-08

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 57.77  E-value: 3.25e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  414 KSTTDNDVRIQQLQEILQDLQKRLESSEAERKQLQVELQSRRAELvclnnteiSENSSDLSQKlKETQSKYEEAmkevls 493
Cdd:TIGR02169  716 RKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSEL--------KELEARIEEL-EEDLHKLEEA------ 780
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  494 vqkqmklgLVSPESMDNYSHFHELRVTEEEINVLKQDLQNALEESERnKEKVRELEEKLVEREKGTvIKPPVEEYEEMKS 573
Cdd:TIGR02169  781 --------LNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQ-KLNRLTLEKEYLEKEIQE-LQEQRIDLKEQIK 850
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370488827  574 SYCSVIENMNKEKAFLFEKYQEAQEEIMKLKDTLKSqmTQEASDEAEDMKEAMNRMIDELNKQVSELSQLYKEAQAELE 652
Cdd:TIGR02169  851 SIEKEIENLNGKKEELEEELEELEAALRDLESRLGD--LKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLE 927
Ank_2 pfam12796
Ankyrin repeats (3 copies);
181-243 3.30e-08

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 52.04  E-value: 3.30e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370488827 181 LMLACEIGSSNAVEALIKKGADLNLVDSLGYNALHYSKLSENAGIQSLLLSKISQDADLKTPT 243
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNGRT 63
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
417-884 3.76e-08

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: 57.44  E-value: 3.76e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  417 TDNDVRIQQLQEILQDLQKRLESSEAERKQLQVELQSRRAELVClNNTEISENSSDLSQKLKETQSKYEEAMKEVlsvqk 496
Cdd:pfam15921  274 SEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMR-QLSDLESTVSQLRSELREAKRMYEDKIEEL----- 347
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  497 QMKLGLVSPESMDNYSHFHELRVTEEEINVLKQDLQNALEESERNKEKVRELEEKLVEREKGTVIkppveeyeemkssyc 576
Cdd:pfam15921  348 EKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSI--------------- 412
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  577 sVIENMNKEkaflfekYQEAQEEIMKLKDTLKSqMTQEASDEAEDMKEAMNRMIDELNKqVSELSqlykeAQAELEDYRK 656
Cdd:pfam15921  413 -TIDHLRRE-------LDDRNMEVQRLEALLKA-MKSECQGQMERQMAAIQGKNESLEK-VSSLT-----AQLESTKEML 477
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  657 RKSLEDVTAEYIHKAEHEKLMQLTNVSRAKAEDALSEMKSQYSKV-------LNELTQLK----QLVDAQKENS---VSI 722
Cdd:pfam15921  478 RKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLrsrvdlkLQELQHLKnegdHLRNVQTECEalkLQM 557
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  723 TEHLQVITTLRTAAKEMEEKISNLKEHLASKEVEVAKLEKQLLEEKAAMTDAMVPRSSYEKLQSSLESEVSVLA------ 796
Cdd:pfam15921  558 AEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLElekvkl 637
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  797 --------SKLKESVKEKEKVHSEVVQIRSEVSQVKREKENIQTLLKSKEQEV----NELLQKFQQAQEELAEMKRYAES 864
Cdd:pfam15921  638 vnagserlRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMetttNKLKMQLKSAQSELEQTRNTLKS 717
                          490       500
                   ....*....|....*....|
gi 1370488827  865 SSKLEEDKDKKINEMSKEVT 884
Cdd:pfam15921  718 MEGSDGHAMKVAMGMQKQIT 737
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
531-889 7.73e-08

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 56.61  E-value: 7.73e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  531 LQNALEESERNKEKVRELEekLVEREKGTVIKPPVEEyeemkssycsvienmnKEKAflfEKYQEAQEEIMKLKDTLKSQ 610
Cdd:TIGR02169  172 KEKALEELEEVEENIERLD--LIIDEKRQQLERLRRE----------------REKA---ERYQALLKEKREYEGYELLK 230
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  611 MtqeasdeaedmKEAMNRMIDELNKQVSELSQLYKEAQAELEDYRKRksledvtaeyIHKAEhEKLMQLTNVSRAKAEDA 690
Cdd:TIGR02169  231 E-----------KEALERQKEAIERQLASLEEELEKLTEEISELEKR----------LEEIE-QLLEELNKKIKDLGEEE 288
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  691 LSEMKSQYSKVLNELTQLKQLVDAQKENsvsitehlqvittlrtaAKEMEEKISNLKEHLASKEVEVAKLEKQLLEEKaa 770
Cdd:TIGR02169  289 QLRVKEKIGELEAEIASLERSIAEKERE-----------------LEDAEERLAKLEAEIDKLLAEIEELEREIEEER-- 349
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  771 mtdamvprssyeKLQSSLESEVSVLASKLKESVKEKEKVHSEVVQIRSEVSQVKREKENIQtllkskeQEVNELLQKFQQ 850
Cdd:TIGR02169  350 ------------KRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLK-------REINELKRELDR 410
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|
gi 1370488827  851 AQEEL-----------AEMKRYAESSSKLEEDKDKKINEMSKEVTKLKEA 889
Cdd:TIGR02169  411 LQEELqrlseeladlnAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQL 460
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
94-166 1.21e-07

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 55.67  E-value: 1.21e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370488827  94 IRKLLQSKCPAESVDSSGKTALHYAAAQGCLQAVQILCEHKSPINLKDLDGNIPLLLAVQNGHSEICHFLLDH 166
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
PHA02878 PHA02878
ankyrin repeat protein; Provisional
49-217 1.41e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 55.27  E-value: 1.41e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  49 FHLAAAKGHVECLRVMITHGVDVTAQDTTGHSALHLAAKNSHHECIRKLLQS--KCPAESVDSSGKTALHY--------- 117
Cdd:PHA02878   41 LHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSinKCSVFYTLVAIKDAFNNrnveifkii 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 118 ------------------AAAQGCLQA--VQILCEHKSPINLKDLD-GNIPLLLAVQNGHSEICHFLLDHGADVNSRNKS 176
Cdd:PHA02878  121 ltnrykniqtidlvyidkKSKDDIIEAeiTKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKT 200
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1370488827 177 GRTALMLACEIGSSNAVEALIKKGADLNLVDSLGYNALHYS 217
Cdd:PHA02878  201 NNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHIS 241
PHA03100 PHA03100
ankyrin repeat protein; Provisional
35-171 3.51e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 53.90  E-value: 3.51e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  35 NTTVRARPRKLKHCFHLAAAK--GHVECLRVMITHGVDVTAQDTTGHSALHLAAKNSHHEC-IRKLLQSK---------- 101
Cdd:PHA03100   96 GANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDLkILKLLIDKgvdinaknrv 175
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370488827 102 -------CPAESVDSSGKTALHYAAAQGCLQAVQILCEHKSPINLKDLDGNIPLLLAVQNGHSEICHFLLDHGADVN 171
Cdd:PHA03100  176 nyllsygVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIK 252
PHA02798 PHA02798
ankyrin-like protein; Provisional
124-232 3.84e-07

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 53.69  E-value: 3.84e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 124 LQAVQILCEHKSPINLKDLDGNIPLLLAVQN-----GHSEICHFLLDHGADVNSRNKSGRTALMLACEIGSSNAVEAL-- 196
Cdd:PHA02798   51 TDIVKLFINLGANVNGLDNEYSTPLCTILSNikdykHMLDIVKILIENGADINKKNSDGETPLYCLLSNGYINNLEILlf 130
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1370488827 197 -IKKGADLNLVDSLGYNALH-YSKLSENAGIQ--SLLLSK 232
Cdd:PHA02798  131 mIENGADTTLLDKDGFTMLQvYLQSNHHIDIEiiKLLLEK 170
PHA02878 PHA02878
ankyrin repeat protein; Provisional
44-184 4.12e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 53.73  E-value: 4.12e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  44 KLKHCFHLAAAKGHVECLRVMITHGVDVTAQDTTGHSALHLAAKNSHHECIRKLLQSKCPAESVDSSGKTALHYAAAQgC 123
Cdd:PHA02878  167 KGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGY-C 245
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370488827 124 L--QAVQILCEHKSPINLKD-LDGNIPLLLAVqngHSE-ICHFLLDHGADVNSRNKSGRTALMLA 184
Cdd:PHA02878  246 KdyDILKLLLEHGVDVNAKSyILGLTALHSSI---KSErKLKLLLEYGADINSLNSYKLTPLSSA 307
PHA02878 PHA02878
ankyrin repeat protein; Provisional
110-221 4.12e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 53.73  E-value: 4.12e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 110 SGKTALHYAAAQGCLQAVQILCEHKSPINLKDLDGNIPLLLAVQNGHSEICHFLLDHGADVNSRNKSGRTALMLAC-EIG 188
Cdd:PHA02878  167 KGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVgYCK 246
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1370488827 189 SSNAVEALIKKGADLNLVDS-LGYNALHYSKLSE 221
Cdd:PHA02878  247 DYDILKLLLEHGVDVNAKSYiLGLTALHSSIKSE 280
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
422-909 4.52e-07

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 54.03  E-value: 4.52e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  422 RIQQLQEILQDLQKRLESSEAERKQLQVElqsrraelvclnNTEISENSSDLSQKLKEtqskyEEAMKEVLSVQKqmklg 501
Cdd:pfam01576   69 RKQELEEILHELESRLEEEEERSQQLQNE------------KKKMQQHIQDLEEQLDE-----EEAARQKLQLEK----- 126
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  502 lVSPESmdnyshfhELRVTEEEINVLKQDLQNALEESERNKEKVRELEEKLVEREKgtvikpPVEEYEEMKSSYCSVIEN 581
Cdd:pfam01576  127 -VTTEA--------KIKKLEEDILLLEDQNSKLSKERKLLEERISEFTSNLAEEEE------KAKSLSKLKNKHEAMISD 191
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  582 MN--------------KEKAFLFEKYQEAQEEIMKLKDTLKSQMTQEASDEAEdMKEAMNRMIDELNKQVSELSQLyKEA 647
Cdd:pfam01576  192 LEerlkkeekgrqeleKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEE-LQAALARLEEETAQKNNALKKI-REL 269
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  648 QAELEDYRkrkslEDVTAEYIHKAEHEK----LMQLTNVSRAKAEDALSEMKSQY---SKVLNELTQLKQLVDAQKENsv 720
Cdd:pfam01576  270 EAQISELQ-----EDLESERAARNKAEKqrrdLGEELEALKTELEDTLDTTAAQQelrSKREQEVTELKKALEEETRS-- 342
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  721 siteHLQVITTLR----TAAKEMEEKISNLKEHLASKEVEVAKLEKQLLEEKAAMTDAMVPRSSYEKLQSSLESEVSVLA 796
Cdd:pfam01576  343 ----HEAQLQEMRqkhtQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQ 418
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  797 SKLKESVKEKEKVHSEVVQIRSEVSQVKREKENIQTLLKSKEQEVNELLQKFQQAQEELAEMKRYAESSS----KLEEDK 872
Cdd:pfam01576  419 ARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLStrlrQLEDER 498
                          490       500       510
                   ....*....|....*....|....*....|....*..
gi 1370488827  873 DKKINEMSKEVTKLKEALNSLSQLSYSTSSSKRQSQQ 909
Cdd:pfam01576  499 NSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEE 535
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
591-891 4.76e-07

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 53.91  E-value: 4.76e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 591 EKYQEAQEEIMKLKDTLKSQMTQ-----EASDEAEDMKEAMNRMIDELNKQVSELSQLYKEAQAELEDYRKRKSLEDVTA 665
Cdd:PRK03918  158 DDYENAYKNLGEVIKEIKRRIERlekfiKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELK 237
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 666 EYIHKAEHEKLMQLTNVsrAKAEDALSEMKSQYSKVLNELTQLKQLVDAQKENSVSITEHLqvitTLRTAAKEMEEKISN 745
Cdd:PRK03918  238 EEIEELEKELESLEGSK--RKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYI----KLSEFYEEYLDELRE 311
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 746 LKEHLASKEVEVAKLEKQLLEekaamtdamvprssyeklQSSLESEVSVLASKLKESVKEKEKVhSEVVQIRSEVSQVKR 825
Cdd:PRK03918  312 IEKRLSRLEEEINGIEERIKE------------------LEEKEERLEELKKKLKELEKRLEEL-EERHELYEEAKAKKE 372
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370488827 826 EKENIQTLLKSKE-QEVNELLQKFQQAQEELAEmkryaesssKLEEDKDkKINEMSKEVTKLKEALN 891
Cdd:PRK03918  373 ELERLKKRLTGLTpEKLEKELEELEKAKEEIEE---------EISKITA-RIGELKKEIKELKKAIE 429
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
516-888 5.74e-07

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 53.51  E-value: 5.74e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 516 ELRVTEEEINVLKQDLQNALEESERNKEKVRELEEKLVEREkgtvikppvEEYEEMKSSyCSV----IENMNKEKAFLFE 591
Cdd:PRK02224  252 ELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELE---------EERDDLLAE-AGLddadAEAVEARREELED 321
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 592 KYQEAQEEIMKlkdtlKSQMTQEASDEAEDMKEAMNRMIDELNKQVSELSQLYKEAQAELEDYRKRKS-LEDVTAEYihk 670
Cdd:PRK02224  322 RDEELRDRLEE-----CRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREeIEELEEEI--- 393
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 671 AEHEKLMQLTNVSRAKAEDALSEMKSQYSKVLNELTQL--------------KQLVDAQK----ENSVSITEHLQVITtl 732
Cdd:PRK02224  394 EELRERFGDAPVDLGNAEDFLEELREERDELREREAELeatlrtarerveeaEALLEAGKcpecGQPVEGSPHVETIE-- 471
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 733 rtaakEMEEKISNLKEHLASKEVEVAKLEKQLLEEKAAmtdamvprssyeklqSSLESEVSVLASKLKESVKEKEKVHSE 812
Cdd:PRK02224  472 -----EDRERVEELEAELEDLEEEVEEVEERLERAEDL---------------VEAEDRIERLEERREDLEELIAERRET 531
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 813 VVQIRSEVSQVKREKENIQTLLKSKEQEVNELLQKFQQAQEELAEM-KRYAESSSKLE-----EDKDKKINEMSKEVTKL 886
Cdd:PRK02224  532 IEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELnSKLAELKERIEsleriRTLLAAIADAEDEIERL 611

                  ..
gi 1370488827 887 KE 888
Cdd:PRK02224  612 RE 613
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
51-181 6.17e-07

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 53.48  E-value: 6.17e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  51 LAAAKGHVECLRVMIT-HGVDVTAQDTTGHSALHLAAKNSHHECIRKLLQS-----KCPAESVDSSGKTALHYAAAQGCL 124
Cdd:cd22192    23 LAAKENDVQAIKKLLKcPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAapelvNEPMTSDLYQGETALHIAVVNQNL 102
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370488827 125 QAVQIL---------------CEHKSPINLKDLdGNIPLLLAVQNGHSEICHFLLDHGADVNSRNKSGRTAL 181
Cdd:cd22192   103 NLVRELiargadvvspratgtFFRPGPKNLIYY-GEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVL 173
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
75-219 6.90e-07

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 53.16  E-value: 6.90e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  75 DTTGHSALHLAAKNSHHECIRKLLQSKCPAESVdssGKTALHyAAAQGCLQAVQILCEHKSPINLKDLD----------- 143
Cdd:TIGR00870  49 DRLGRSALFVAAIENENLELTELLLNLSCRGAV---GDTLLH-AISLEYVDAVEAILLHLLAAFRKSGPlelandqytse 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 144 ---GNIPLLLAVQNGHSEICHFLLDHGADVNSRNKS--------------GRTALMLACEIGSSNAVEALIKKGADLNLV 206
Cdd:TIGR00870 125 ftpGITALHLAAHRQNYEIVKLLLERGASVPARACGdffvksqgvdsfyhGESPLNAAACLGSPSIVALLSEDPADILTA 204
                         170
                  ....*....|...
gi 1370488827 207 DSLGYNALHYSKL 219
Cdd:TIGR00870 205 DSLGNTLLHLLVM 217
PTZ00121 PTZ00121
MAEBL; Provisional
434-885 8.20e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 53.22  E-value: 8.20e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  434 QKRLESSEAERKQLQVELQSRRAELVclNNTEISENSSDLSQKLKETQSKYEEAMKEVLSVQKQMKLglvspESMDNYSH 513
Cdd:PTZ00121  1451 KKAEEAKKAEEAKKKAEEAKKADEAK--KKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEA-----KKAEEAKK 1523
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  514 FHELRVTEEEINVlkQDLQNAleESERNKEKVRELEEKLVEREKGTVIKPPVEEYEEmkssycsvieNMNKEKAFLFEKY 593
Cdd:PTZ00121  1524 ADEAKKAEEAKKA--DEAKKA--EEKKKADELKKAEELKKAEEKKKAEEAKKAEEDK----------NMALRKAEEAKKA 1589
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  594 QEAQ-EEIMKLKDTLKSQMTQEASDEAEDMKEAMN-RMIDELNKQVSELSQLYKEAQAELEDYRKRKSLEDVTAEYIHKA 671
Cdd:PTZ00121  1590 EEARiEEVMKLYEEEKKMKAEEAKKAEEAKIKAEElKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKK 1669
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  672 EHEKlmqltnvsRAKAEDALSEMKSQYSKvlneltqlkqlvdaqKENSVSITEHLQVITTLRTAAKEMEEKISNLKEHLA 751
Cdd:PTZ00121  1670 AEED--------KKKAEEAKKAEEDEKKA---------------AEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEE 1726
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  752 SKEVEVAKLEKQLLEEKAAMTDAMVPRSSYEKLQ--SSLESEVSVLASKLKESVKE---KEKVHSEVVQIRSEVSQVKRE 826
Cdd:PTZ00121  1727 ENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAhlKKEEEKKAEEIRKEKEAVIEeelDEEDEKRRMEVDKKIKDIFDN 1806
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  827 KENIQTLLKSKEQEVNELLQKFQQAQEELAEMKRYA-ESSSKLEEDKDKKINEMSKEVTK 885
Cdd:PTZ00121  1807 FANIIEGGKEGNLVINDSKEMEDSAIKEVADSKNMQlEEADAFEKHKFNKNNENGEDGNK 1866
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
515-870 8.44e-07

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 52.85  E-value: 8.44e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 515 HELRVTEEEINVLKQDLQNALEESERNKEKVRELEEKLVEREKGTVIKPPVEEYEEMKSSYCSVIENMNKEKA------F 588
Cdd:COG4717    81 KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEErleelrE 160
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 589 LFEKYQEAQEEIMKLKDTLKSQMTQEASDEAEDMKEAMNRmIDELNKQVSELSQLYKEAQAELEDYRKRKSLEDVTAEYI 668
Cdd:COG4717   161 LEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEE-LEELQQRLAELEEELEEAQEELEELEEELEQLENELEAA 239
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 669 HKAEHEKLMQLTNVSRAKAEDALSEMKSQYSKVLNELTQLKqlvdaqkensVSITEHLQVITTLRTAAKEMEEKISNLKE 748
Cdd:COG4717   240 ALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLF----------LVLGLLALLFLLLAREKASLGKEAEELQA 309
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 749 HLASKEVEVAKLEKQLleekaamtdamvprssyEKLQSSLESEVSvLASKLKESVKEKEKVHSEVVQIRSEVSQVKREKE 828
Cdd:COG4717   310 LPALEELEEEELEELL-----------------AALGLPPDLSPE-ELLELLDRIEELQELLREAEELEEELQLEELEQE 371
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 1370488827 829 NIQTLLKSKEQEVNELLQKFQQAQEELAEMKRYAESSSKLEE 870
Cdd:COG4717   372 IAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEE 413
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
143-175 8.85e-07

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 46.13  E-value: 8.85e-07
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1370488827 143 DGNIPLLLAV-QNGHSEICHFLLDHGADVNSRNK 175
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
46 PHA02562
endonuclease subunit; Provisional
546-766 9.36e-07

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 52.71  E-value: 9.36e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 546 RELEEKLVE----REKGTVIKPPVEE-YEEMKSsyCSVIENMNKEKAFLFEKYQEAQEEIMKLKDTLKSQMTQEASDEAE 620
Cdd:PHA02562  153 RKLVEDLLDisvlSEMDKLNKDKIRElNQQIQT--LDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAK 230
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 621 DMKEAMNRMIDELNKQVSELSQlYKEAQAELEDYRKRKSLEDVTAEYIHK---------------AEHEKLMQltnvsra 685
Cdd:PHA02562  231 TIKAEIEELTDELLNLVMDIED-PSAALNKLNTAAAKIKSKIEQFQKVIKmyekggvcptctqqiSEGPDRIT------- 302
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 686 KAEDALSEMKSQYSKVLNELTQLKQLVDAQKENSVSITE-------HLQVITTLRTAAKEMEEKISNLKEHLASKEVEVA 758
Cdd:PHA02562  303 KIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSKKLLElknkistNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELA 382

                  ....*...
gi 1370488827 759 KLEKQLLE 766
Cdd:PHA02562  383 KLQDELDK 390
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
425-859 1.06e-06

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 52.81  E-value: 1.06e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  425 QLQEILQDLQKRLESSEAERKQ-----------------LQVELQSRRAE---LVCLNNTEISENSSDLSQKLKETQSKy 484
Cdd:pfam15921  378 QLQKLLADLHKREKELSLEKEQnkrlwdrdtgnsitidhLRRELDDRNMEvqrLEALLKAMKSECQGQMERQMAAIQGK- 456
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  485 EEAMKEVLSVQKQMKlglvSPESMdnyshfheLRVTEEEINVLKQdlqnALEESERNkekVRELEEKLVEREKGtvIKPP 564
Cdd:pfam15921  457 NESLEKVSSLTAQLE----STKEM--------LRKVVEELTAKKM----TLESSERT---VSDLTASLQEKERA--IEAT 515
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  565 VEEYEEMKSSY---CSVIENMNKEKAFLfeKYQEAQEEIMKLKDTLKSQMTQEASDEAEDMKEAMNRMIDELNKQVSELS 641
Cdd:pfam15921  516 NAEITKLRSRVdlkLQELQHLKNEGDHL--RNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKA 593
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  642 QLYKEA---QAELEDYRKRKSLEDVTAEYIHKAEHEKLMQLTNVSRAKAED--ALSEMKSQYSKVLNE-------LTQLK 709
Cdd:pfam15921  594 QLEKEIndrRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERlrAVKDIKQERDQLLNEvktsrneLNSLS 673
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  710 QLVDAQKENSVSITEHLQVITT-----LRTAAKEMEEKISNLK-----------------EHLASKEVEVAKLEK--QLL 765
Cdd:pfam15921  674 EDYEVLKRNFRNKSEEMETTTNklkmqLKSAQSELEQTRNTLKsmegsdghamkvamgmqKQITAKRGQIDALQSkiQFL 753
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  766 EEkaAMTDAMVPRSSYEKLQSSLESEVSVLASklkesvkEKEKVHSEVVQIRSEVSQVKREKENIQTLLKSKEQEVNELL 845
Cdd:pfam15921  754 EE--AMTNANKEKHFLKEEKNKLSQELSTVAT-------EKNKMAGELEVLRSQERRLKEKVANMEVALDKASLQFAECQ 824
                          490
                   ....*....|....
gi 1370488827  846 QKFQQAQEELAEMK 859
Cdd:pfam15921  825 DIIQRQEQESVRLK 838
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
422-933 1.50e-06

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: 52.28  E-value: 1.50e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  422 RIQQLQEILQDLQKRLESSEAERKQLQVE-------LQSRRAE---LVCLNNTEISENSSDLSQKLKETQSKYEEAMKEV 491
Cdd:TIGR00618  380 HIHTLQQQKTTLTQKLQSLCKELDILQREqatidtrTSAFRDLqgqLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKI 459
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  492 LSVQKQMKLglvsPESMDNYSHFHELRVTEEEINVLKQDLQNALEESERN-KEKVRELEEKLVEREKGTVIKPPVEEYEE 570
Cdd:TIGR00618  460 HLQESAQSL----KEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPlCGSCIHPNPARQDIDNPGPLTRRMQRGEQ 535
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  571 MKSSYCSVIENMNKEKAFLFEKYQEAQEEIMKLKDTLK--SQMTQEASDEAEDMKEAMNRMIDELNKQVSELSQLYKEAQ 648
Cdd:TIGR00618  536 TYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSilTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQH 615
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  649 AELEDYRKRKSLEDVTAEYIHKAEHEKLMQLtnvsrAKAEDALSEMKSQYSKVLNELTQLKQLVDAQKENSVSITEHLQv 728
Cdd:TIGR00618  616 ALLRKLQPEQDLQDVRLHLQQCSQELALKLT-----ALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEK- 689
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  729 itTLRTAAKEMEEKISNLKEHLASKEVEVAKLEKQLleekaamtdamvprssyEKLQSSLESEVSVLASKLKESVKEKEK 808
Cdd:TIGR00618  690 --EQLTYWKEMLAQCQTLLRELETHIEEYDREFNEI-----------------ENASSSLGSDLAAREDALNQSLKELMH 750
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  809 VHSEVVQIRSEVSQVKREKENIQTLLKSKEQEVNELLQKFQQAQEE----LAEMKryAESSSKLEEDKDKKINEMSKEVT 884
Cdd:TIGR00618  751 QARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEdthlLKTLE--AEIGQEIPSDEDILNLQCETLVQ 828
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*....
gi 1370488827  885 KLKEALNSLSQLSYSTSSSKRQSQQLEalqqqvkqlqnqlaECKKQHQE 933
Cdd:TIGR00618  829 EEEQFLSRLEEKSATLGEITHQLLKYE--------------ECSKQLAQ 863
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
420-600 2.05e-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: 49.92  E-value: 2.05e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 420 DVRIQQLQEILQDLQKRLESSEAERKQLQVELQSRRAELVCLNnTEISENSSDLSQkLKETQSKYEEAMKEVLSvQKQMK 499
Cdd:COG1579    16 DSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLE-KEIKRLELEIEE-VEARIKKYEEQLGNVRN-NKEYE 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 500 LGLvspesmdnyshfHELRVTEEEINVLKQDLQNALEESERNKEKVRELEEKLVEREkgtvikppvEEYEEMKSSYCSVI 579
Cdd:COG1579    93 ALQ------------KEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELE---------AELEEKKAELDEEL 151
                         170       180
                  ....*....|....*....|.
gi 1370488827 580 ENMNKEKAFLFEKYQEAQEEI 600
Cdd:COG1579   152 AELEAELEELEAEREELAAKI 172
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
741-934 2.08e-06

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 51.98  E-value: 2.08e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  741 EKISNLKEHLASKEVEVAKLEKQLLEEKaamtdamvprssyeklQSSLESEVSVLASKLKESVKEKEKVHSEVVQIRSEV 820
Cdd:TIGR02168  213 ERYKELKAELRELELALLVLRLEELREE----------------LEELQEELKEAEEELEELTAELQELEEKLEELRLEV 276
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  821 SQVKREKENIQTLLKSKEQEVNELLQKFQQAQEELAEMKRYAESSSKLEEDKDKKINEMSKEVTKLKEALNslsqlsYST 900
Cdd:TIGR02168  277 SELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLE------ELK 350
                          170       180       190
                   ....*....|....*....|....*....|....
gi 1370488827  901 SSSKRQSQQLEALQQQVKQLQNQLAECKKQHQEV 934
Cdd:TIGR02168  351 EELESLEAELEELEAELEELESRLEELEEQLETL 384
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
119-198 3.16e-06

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 51.05  E-value: 3.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 119 AAQGCLQAVQILCEHKSPINLKDLDGNIPLLLAVQNGHSEICHFLLDHGADVNSRNKSGRTALMLACEIGSSNAVEALIK 198
Cdd:PTZ00322   90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
579-812 3.67e-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: 3.67e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 579 IENMNKEKAFLFEKYQEAQEEIMKLKDTLKSqmTQEASDEAEDMKEAMNRMIDELNKQVSELSQLYKEAQAELEDYrkrk 658
Cdd:COG3883    18 IQAKQKELSELQAELEAAQAELDALQAELEE--LNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER---- 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 659 sledVTAEYIHKAEHEKLMQLTN-------VSRAkaeDALSEMKSQYSKVLNELTQLKQLVDAQKENSVsitehlQVITT 731
Cdd:COG3883    92 ----ARALYRSGGSVSYLDVLLGsesfsdfLDRL---SALSKIADADADLLEELKADKAELEAKKAELE------AKLAE 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 732 LRTAAKEMEEKISNLKEHLASKEVEVAKLEKQLLEEKAAMTDAMVPRSSYEKLQSSLESEVSVLASKLKESVKEKEKVHS 811
Cdd:COG3883   159 LEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 238

                  .
gi 1370488827 812 E 812
Cdd:COG3883   239 A 239
Ank_5 pfam13857
Ankyrin repeats (many copies);
137-184 3.70e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 45.03  E-value: 3.70e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1370488827 137 INLKDLDGNIPLLLAVQNGHSEICHFLLDHGADVNSRNKSGRTALMLA 184
Cdd:pfam13857   9 LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_5 pfam13857
Ankyrin repeats (many copies);
108-151 3.93e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 45.03  E-value: 3.93e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1370488827 108 DSSGKTALHYAAAQGCLQAVQILCEHKSPINLKDLDGNIPLLLA 151
Cdd:pfam13857  13 DGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTZ00121 PTZ00121
MAEBL; Provisional
516-971 3.95e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 51.30  E-value: 3.95e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  516 ELRVTEEeinVLKQDLQNALEESERNKEKVRELEEKLVEREKGTVIKPPVEEYEEMKSSYCSVIENMNKEKAFLFEKYQE 595
Cdd:PTZ00121  1186 EVRKAEE---LRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARM 1262
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  596 AQEEIMKLKDTLKSQMTQEASDEAEDMKEAMNRMIDELNKQVSELSQLYKEAQAELEDYRKRKSLEDVTAEYIHKAEHEK 675
Cdd:PTZ00121  1263 AHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAK 1342
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  676 lmQLTNVSRAKAEDALSEMKSQYSKvlNELTQLKQLVDAQK-ENSVSITEHLQVITTLRTAAKEMEEKISNLKEHLASKE 754
Cdd:PTZ00121  1343 --KAAEAAKAEAEAAADEAEAAEEK--AEAAEKKKEEAKKKaDAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKK 1418
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  755 vEVAKLEKQLLEEKAAmtdamvprssyEKLQSSLESEVSvlASKLKESVKEKEKvhsevvqirSEVSQVKREKENIQTLL 834
Cdd:PTZ00121  1419 -KADEAKKKAEEKKKA-----------DEAKKKAEEAKK--ADEAKKKAEEAKK---------AEEAKKKAEEAKKADEA 1475
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  835 KSKEQE---VNELLQKFQQAQEELAEMKRYAESSSKLEEDKDKkinEMSKEVTKLKEALNSLSQLSYSTSSSKRQSQQLE 911
Cdd:PTZ00121  1476 KKKAEEakkADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKA---EEAKKADEAKKAEEAKKADEAKKAEEKKKADELK 1552
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370488827  912 ALQQQVKQLQNQLAECKKQHQE--VISVYRMHLLYAVQGQMDEDVQKVLKQILTMCKNQSQK 971
Cdd:PTZ00121  1553 KAEELKKAEEKKKAEEAKKAEEdkNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKK 1614
Ank_5 pfam13857
Ankyrin repeats (many copies);
64-118 5.02e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 44.64  E-value: 5.02e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1370488827  64 MITHG-VDVTAQDTTGHSALHLAAKNSHHECIRKLLQSKCPAESVDSSGKTALHYA 118
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02798 PHA02798
ankyrin-like protein; Provisional
59-232 5.52e-06

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 50.22  E-value: 5.52e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  59 ECLRVMITHGVDVTAQDTTGHSALHLAAKNSHH---ECIRKLLQSKCPAESVDSS-GKTALHyaaaqgclqavqilCEHK 134
Cdd:PHA02798  126 EILLFMIENGADTTLLDKDGFTMLQVYLQSNHHidiEIIKLLLEKGVDINTHNNKeKYDTLH--------------CYFK 191
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 135 SPINLKDLDgniplllavqnghseICHFLLDHGADVNSRNKSGRTALM--LACEIGSSNAVEA----LIKKGADLNLVDS 208
Cdd:PHA02798  192 YNIDRIDAD---------------ILKLFVDNGFIINKENKSHKKKFMeyLNSLLYDNKRFKKnildFIFSYIDINQVDE 256
                         170       180
                  ....*....|....*....|....
gi 1370488827 209 LGYNALHYSKLSENAGIQSLLLSK 232
Cdd:PHA02798  257 LGFNPLYYSVSHNNRKIFEYLLQL 280
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
141-251 6.42e-06

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 50.28  E-value: 6.42e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 141 DLDGNIPLLLAVqnghsEICHF-----------LLDHGADVNSRNKSGRTALMLACEIGSSNAVEALIKKGADLNLVDSL 209
Cdd:PTZ00322   73 VIDPVVAHMLTV-----ELCQLaasgdavgariLLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKD 147
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1370488827 210 GYNALHYSKLSENAGIQSLLLSKISQDADLKTPTKPKQHDQV 251
Cdd:PTZ00322  148 GKTPLELAEENGFREVVQLLSRHSQCHFELGANAKPDSFTGK 189
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
335-659 7.55e-06

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 50.06  E-value: 7.55e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  335 ADQQDLLSLLQAKVASLtlhNKELQDKLQAKSPKEAEADLSFDSYHSTQTDLGpslgkpgetSPPDSKSSPSVLIHSLGK 414
Cdd:TIGR02168  687 EELEEKIAELEKALAEL---RKELEELEEELEQLRKELEELSRQISALRKDLA---------RLEAEVEQLEERIAQLSK 754
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  415 STTDNDVRIQQLQEILQDLQKRLESSEAERKQLQVELQSRRAELvclnnTEISENSSDLSQKLKETQSKYEEAMKEVLSV 494
Cdd:TIGR02168  755 ELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEEL-----KALREALDELRAELTLLNEEAANLRERLESL 829
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  495 QKQMKLGLVSPESMDNyshfhELRVTEEEInvlkQDLQNALEESERNKEKV-RELEEKLVEREKGTV-IKPPVEEYEEMK 572
Cdd:TIGR02168  830 ERRIAATERRLEDLEE-----QIEELSEDI----ESLAAEIEELEELIEELeSELEALLNERASLEEaLALLRSELEELS 900
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  573 SSycsvIENMNKEKAFLFEKYQEAQEEIMKLK----------DTLKSQMTQEASDEAEDMKEAMN----------RMIDE 632
Cdd:TIGR02168  901 EE----LRELESKRSELRRELEELREKLAQLElrleglevriDNLQERLSEEYSLTLEEAEALENkieddeeearRRLKR 976
                          330       340
                   ....*....|....*....|....*..
gi 1370488827  633 LNKQVSELSQLYKEAQAELEDYRKRKS 659
Cdd:TIGR02168  977 LENKIKELGPVNLAAIEEYEELKERYD 1003
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
614-883 7.94e-06

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 48.75  E-value: 7.94e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 614 EASDEAEDMKEAMNRMIDELNKQVSELSQLYKEAQAELEDYR-KRKSLEDVTAEYIHKA-EHEKLMQLTNVSRAKAEDAL 691
Cdd:COG1340     1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAeKRDELNAQVKELREEAqELREKRDELNEKVKELKEER 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 692 SEMKSQYSKVLNELTQLKQLVDAQKENSVSITEHLQVI--------TTLRTAAKEME--EKISNLKEHLASKEvEVAKLE 761
Cdd:COG1340    81 DELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIerlewrqqTEVLSPEEEKElvEKIKELEKELEKAK-KALEKN 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 762 KQLLEEKAAMTDamvprssyeklqssLESEVSVLASKLKESVKEKEKVHSEVVQIRSEVSQVKREKENIQTLLKSKEQEV 841
Cdd:COG1340   160 EKLKELRAELKE--------------LRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKA 225
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1370488827 842 NELLQKFQQAQEELAEM----KRYAESSSKLEEDKDKKINEMSKEV 883
Cdd:COG1340   226 DELHEEIIELQKELRELrkelKKLRKKQRALKREKEKEELEEKAEE 271
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
422-665 8.95e-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: 48.99  E-value: 8.95e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 422 RIQQLQEILQDLQKRLESSEAERKQLQVELQSRRAELVCLNNT--EISENSSDLSQKLKETQSKYEEAMKEVLSVQKQMK 499
Cdd:COG4942    28 ELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRirALEQELAALEAELAELEKEIAELRAELEAQKEELA 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 500 LGLVSPESMDNYSHFhELRVTEEEINVLKQDLQNALEESERNKEKVRELEEKLverekgtvikppvEEYEEMKSSycsvI 579
Cdd:COG4942   108 ELLRALYRLGRQPPL-ALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADL-------------AELAALRAE----L 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 580 ENMNKEKAFLFEKYQEAQEEIMKLKDTLKSQMTQEASDEAEDMKEamnrmIDELNKQVSELSQLYKEAQAELEDYRKRKS 659
Cdd:COG4942   170 EAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAE-----LAELQQEAEELEALIARLEAEAAAAAERTP 244

                  ....*.
gi 1370488827 660 LEDVTA 665
Cdd:COG4942   245 AAGFAA 250
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
542-790 1.07e-05

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 49.54  E-value: 1.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 542 KEKVRELEEKLVEREKGTVIKPPVEEYEEmksSYCSVIENMNK--EKAFLFEKYQEAQEEIMKLKDTLKSQMTQEASDEA 619
Cdd:PRK05771   15 KSYKDEVLEALHELGVVHIEDLKEELSNE---RLRKLRSLLTKlsEALDKLRSYLPKLNPLREEKKKVSVKSLEELIKDV 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 620 EDMKEAMNRMIDELNKQVSEL----SQLYKEAQA---------ELEDYRKRKSLeDVTAEYIHKAEHEKLMQLTN----- 681
Cdd:PRK05771   92 EEELEKIEKEIKELEEEISELeneiKELEQEIERlepwgnfdlDLSLLLGFKYV-SVFVGTVPEDKLEELKLESDvenve 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 682 -VSRAKAED-----ALSEMKSQYSKVLNELTQLKQLVDAQKENSVSITEHLQVITTLRTAAKEMEEKISNLKEH-----L 750
Cdd:PRK05771  171 yISTDKGYVyvvvvVLKELSDEVEEELKKLGFERLELEEEGTPSELIREIKEELEEIEKERESLLEELKELAKKyleelL 250
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1370488827 751 ASKEVEVAKLEKQLLEEKAAMTD------AMVPRSSYEKLQSSLES 790
Cdd:PRK05771  251 ALYEYLEIELERAEALSKFLKTDktfaieGWVPEDRVKKLKELIDK 296
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
413-862 1.10e-05

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 49.38  E-value: 1.10e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 413 GKSTTDNDVRIQQLQEILqdlqKRLESSEAERKQLQVELQSRRAELvclnnTEISENSSDLSQKLK--ETQSKYEEAMKE 490
Cdd:COG4717    63 GRKPELNLKELKELEEEL----KEAEEKEEEYAELQEELEELEEEL-----EELEAELEELREELEklEKLLQLLPLYQE 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 491 VLSVQKQMKlglvspesmDNYSHFHELRVTEEEINVLKQDLQNALEESERNKEKVRELEEKLVEREKGTvIKPPVEEYEE 570
Cdd:COG4717   134 LEALEAELA---------ELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEE-LQDLAEELEE 203
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 571 MKSSycsvIENMNKEKAFLFEKYQEAQEEIMKLKDTLKSQMTQEASDEAEDMKEAMNRMIDELNKQVSELSQLYKEAQA- 649
Cdd:COG4717   204 LQQR----LAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVl 279
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 650 ----------ELEDYRKRKSLEDVTAEYIHKAEHEKLMQLtNVSRAKAEDALSEM--KSQYSKVLNELTQLKQLVD--AQ 715
Cdd:COG4717   280 flvlgllallFLLLAREKASLGKEAEELQALPALEELEEE-ELEELLAALGLPPDlsPEELLELLDRIEELQELLReaEE 358
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 716 KENSVSITEHLQVITTLRTAAK----EMEEKISNLKEHLASKEVEVAKLEKQLLEEKAAMTDAMVPRSsyeklQSSLESE 791
Cdd:COG4717   359 LEEELQLEELEQEIAALLAEAGvedeEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALD-----EEELEEE 433
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370488827 792 VSVLASKLKESVKEKEKVHSEVVQIRSEVSQVKrekeniqtllksKEQEVNELLQKFQQAQEELAEM-KRYA 862
Cdd:COG4717   434 LEELEEELEELEEELEELREELAELEAELEQLE------------EDGELAELLQELEELKAELRELaEEWA 493
Ank_5 pfam13857
Ankyrin repeats (many copies);
27-85 1.24e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.49  E-value: 1.24e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1370488827  27 ARRGPVPPNTTvrarPRKLKHCFHLAAAKGHVECLRVMITHGVDVTAQDTTGHSALHLA 85
Cdd:pfam13857   2 LEHGPIDLNRL----DGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
426-872 1.41e-05

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 48.95  E-value: 1.41e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 426 LQEILQDLQKRLESSEAERKQLQVELQSRRAELVCLnnTEISENSSDLSQKLKETQSKYEEAMKEVLSVQKQMKlglvsp 505
Cdd:pfam05483 361 LEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEM--TKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAE------ 432
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 506 esmdnyshfhELRVTEEEINVLKQDLQNALEESERNKEKVRELEE---KLVEREKGTVIKPPVEEYEEMKSSYCSVIEN- 581
Cdd:pfam05483 433 ----------ELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEhylKEVEDLKTELEKEKLKNIELTAHCDKLLLENk 502
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 582 -MNKEKAFLFEKYQEAQEEIMKLKDTLKSQMTQeasdeAEDMKEAMNRMIDELNKQVSELSQLYKEAQAELEdyrkrKSL 660
Cdd:pfam05483 503 eLTQEASDMTLELKKHQEDIINCKKQEERMLKQ-----IENLEEKEMNLRDELESVREEFIQKGDEVKCKLD-----KSE 572
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 661 EDVTAEYIHKAEHEKLMQLTnvsrakaEDALSEMKSQYSKVLNELTQLKQLVDAQKENSVSITEHLQVITT--------L 732
Cdd:pfam05483 573 ENARSIEYEVLKKEKQMKIL-------ENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIkvnkleleL 645
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 733 RTAAKEMEEKISNLKEHLASKEVEVAKLEKQLLEEKAAMTDAMVPRSSYEKLQSSLESEVSVLASKLKESV-KEKEKVHS 811
Cdd:pfam05483 646 ASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYdKIIEERDS 725
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370488827 812 EVVQIRSEVSQVKREKENIQTLLKSKEQEVNELLQKFQQAQEELAEMKRYAESSSKLEEDK 872
Cdd:pfam05483 726 ELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTAILKDK 786
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
143-171 1.44e-05

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 42.57  E-value: 1.44e-05
                           10        20
                   ....*....|....*....|....*....
gi 1370488827  143 DGNIPLLLAVQNGHSEICHFLLDHGADVN 171
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
PTZ00121 PTZ00121
MAEBL; Provisional
541-934 1.93e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.98  E-value: 1.93e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  541 NKEKVRELEEK------LVEREkgtVIKPPVEEYEEMKSSYCSVIENMNKEKAFLFEKyqeaqeEIMKLKDTLKSQMTQE 614
Cdd:PTZ00121  1025 NIEKIEELTEYgnnddvLKEKD---IIDEDIDGNHEGKAEAKAHVGQDEGLKPSYKDF------DFDAKEDNRADEATEE 1095
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  615 ASDEAEDMKEAMNRMIDELNKQvselsqlyKEAQAELEDYRK----RKSLEDVTAEYIHKAEHEKLMQLTNvsraKAEDA 690
Cdd:PTZ00121  1096 AFGKAEEAKKTETGKAEEARKA--------EEAKKKAEDARKaeeaRKAEDARKAEEARKAEDAKRVEIAR----KAEDA 1163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  691 LSEMKSQYSKVLNELTQLKQLVDAQKENSVSITEHLQVITTLRTAakEMEEKISNLKEHLASKEVEVAKLEKQLLEEKAA 770
Cdd:PTZ00121  1164 RKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKA--EEERKAEEARKAEDAKKAEAVKKAEEAKKDAEE 1241
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  771 MTDAMVPRSSYEKLQssLESEVSVLASKLKESVKEKEKVHSEVVQIRSEVSqvkrekeniqtllKSKEQEVNELLQKFQQ 850
Cdd:PTZ00121  1242 AKKAEEERNNEEIRK--FEEARMAHFARRQAAIKAEEARKADELKKAEEKK-------------KADEAKKAEEKKKADE 1306
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  851 AQEELAEMKRYAESSSKLEEDKDKKINEMSKEVTKLKEALNSLSQLSYSTSSSKRQSQQLEALQQQVKQLQNQLAECKKQ 930
Cdd:PTZ00121  1307 AKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKK 1386

                   ....
gi 1370488827  931 HQEV 934
Cdd:PTZ00121  1387 AEEK 1390
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
620-926 2.06e-05

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.78  E-value: 2.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 620 EDMKEAMNR---MIDELNKQVSELsqlykEAQAEL-EDYRK-RKSLEDVTAEYIHKAEHEKLMQLtnvsrAKAEDALSEM 694
Cdd:COG1196   182 EATEENLERledILGELERQLEPL-----ERQAEKaERYRElKEELKELEAELLLLKLRELEAEL-----EELEAELEEL 251
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 695 KSQyskvLNELTQLKQLVDAQKEnsvsitehlqvitTLRTAAKEMEEKISNLKEHLASKEVEVAKLEKQlleekaamtda 774
Cdd:COG1196   252 EAE----LEELEAELAELEAELE-------------ELRLELEELELELEEAQAEEYELLAELARLEQD----------- 303
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 775 mvpRSSYEKLQSSLESEVSVLASKLKESVKEKEKVHSEVVQIRSEVSQVKREKENIQTLLKSKEQEVNELLQKFQQAQEE 854
Cdd:COG1196   304 ---IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE 380
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370488827 855 LAEMKR-YAESSSKLEEDKDKKINEMSKEVTKLKEALNSLSQLSYSTSSSKRQSQQLEALQQQVKQLQNQLAE 926
Cdd:COG1196   381 LEELAEeLLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAE 453
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
687-859 2.11e-05

Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.


Pssm-ID: 439154 [Multi-domain]  Cd Length: 309  Bit Score: 47.75  E-value: 2.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 687 AEDALSEMKSQYSKVLNELTQLKQLVDaQKENSVSITEHLQVITTLRTAAKEMEEKISNLKEHLASKEVEVAKLEKQLLE 766
Cdd:cd22656    82 AQNAGGTIDSYYAEILELIDDLADATD-DEELEEAKKTIKALLDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQTALET 160
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 767 EKAAMTD------AMVPRSSYEKLQSSLESEVSVLASKLKESVKEKEKvhsevvQIRSEVSQVKREKeNIQTLLKSKEQE 840
Cdd:cd22656   161 LEKALKDlltdegGAIARKEIKDLQKELEKLNEEYAAKLKAKIDELKA------LIADDEAKLAAAL-RLIADLTAADTD 233
                         170
                  ....*....|....*....
gi 1370488827 841 VNELLQKFQQAQEELAEMK 859
Cdd:cd22656   234 LDNLLALIGPAIPALEKLQ 252
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
423-860 2.17e-05

rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 48.50  E-value: 2.17e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  423 IQQLQEILQDLQKRLESSEAERKQLQVELQSRRAELVCLNNTEISENSS-DLSQKLKETQSKYEEAMKE--VLSVQKQMK 499
Cdd:TIGR00606  586 INQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSqDEESDLERLKEEIEKSSKQraMLAGATAVY 665
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  500 LGLVSPESMDNYS---HFHELRVTEEEINVLKQDLQNALEESERNKEKVRELEEKLVEREKGTVIKPPVEEyeemkssyc 576
Cdd:TIGR00606  666 SQFITQLTDENQSccpVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQ--------- 736
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  577 SVIENMNKEKAFLFEKYQEAQEEIMKLKDTLKSQMTQ----EASDEAEDMKEAMNRMIDELNKQVSELSQLYKEAQAELE 652
Cdd:TIGR00606  737 SIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLlgtiMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQ 816
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  653 DYRKRKSLEDVTAEYIHKAEH-----------EKLMQLTNVSRAKAEDALSEMKSQYSKVLNELTQLKQLVDAQKENSVS 721
Cdd:TIGR00606  817 GSDLDRTVQQVNQEKQEKQHEldtvvskielnRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTE 896
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  722 ITEHLQVI-----------TTLRTAAKEMEEKISNLKEHLASKEVEVAKLEKQLLEEKAAMTDAM-VPRSSYEKLQSSLE 789
Cdd:TIGR00606  897 VQSLIREIkdakeqdspleTFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIEnKIQDGKDDYLKQKE 976
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  790 SEVSVLASKLKESVKEKEKVHSEVVQIRSEV--------------------SQVKREKENIQTLLKS-KEQEVNELLQKF 848
Cdd:TIGR00606  977 TELNTVNAQLEECEKHQEKINEDMRLMRQDIdtqkiqerwlqdnltlrkreNELKEVEEELKQHLKEmGQMQVLQMKQEH 1056
                          490
                   ....*....|..
gi 1370488827  849 QQAQEELAEMKR 860
Cdd:TIGR00606 1057 QKLEENIDLIKR 1068
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
651-891 3.75e-05

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 47.61  E-value: 3.75e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 651 LEDYRKRksledvTAEYIHKaehEKLMQLTNVSRAKAEDALSEMKSQYSKVLNELTQLKQLVDAQK-----ENSVSITEH 725
Cdd:PRK05771   14 LKSYKDE------VLEALHE---LGVVHIEDLKEELSNERLRKLRSLLTKLSEALDKLRSYLPKLNplreeKKKVSVKSL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 726 LQVITTLRTAAKEMEEKISNLKEHLASKEVEVAKLEKQLLEEKaamtdamvprsSYEKLQSSLESE-----VSVLASKLK 800
Cdd:PRK05771   85 EELIKDVEEELEKIEKEIKELEEEISELENEIKELEQEIERLE-----------PWGNFDLDLSLLlgfkyVSVFVGTVP 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 801 ESVKEKEKVHSEVvqirsEVSQVKREKENIQTL----LKSKEQEVNELLQKFQQAQEELAEMKRYAESSSKLEEdkdkKI 876
Cdd:PRK05771  154 EDKLEELKLESDV-----ENVEYISTDKGYVYVvvvvLKELSDEVEEELKKLGFERLELEEEGTPSELIREIKE----EL 224
                         250
                  ....*....|....*
gi 1370488827 877 NEMSKEVTKLKEALN 891
Cdd:PRK05771  225 EEIEKERESLLEELK 239
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
411-890 4.54e-05

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: 47.53  E-value: 4.54e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  411 SLGKSTTDNDVRIQQLQEILQDLQKRLESseaERKQLQVELQSRRAELvclnNTEISENSSDLSQK------LKETQSKY 484
Cdd:pfam12128  262 HLHFGYKSDETLIASRQEERQETSAELNQ---LLRTLDDQWKEKRDEL----NGELSAADAAVAKDrseleaLEDQHGAF 334
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  485 EEAMKEVLSvQKQMKLGLVSPEsMDNYSHFHELRVT-----EEEINVLKQDLqnaleeSERNKEKVRELEEKLVEREKGT 559
Cdd:pfam12128  335 LDADIETAA-ADQEQLPSWQSE-LENLEERLKALTGkhqdvTAKYNRRRSKI------KEQNNRDIAGIKDKLAKIREAR 406
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  560 VIKPPVEE--YEEMKSSYCSVIENMNKEkaflfekYQEAQEEIMKLKDTLKSQMTQEASDEAEDMKEAMNrmIDELNKQV 637
Cdd:pfam12128  407 DRQLAVAEddLQALESELREQLEAGKLE-------FNEEEYRLKSRLGELKLRLNQATATPELLLQLENF--DERIERAR 477
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  638 SELSQLYKE---AQAELEDYRKRKSLEDVTAEYIHKAEHE---KLMQLTNVSRAKAEDALSEMKSQ-------YSKVLN- 703
Cdd:pfam12128  478 EEQEAANAEverLQSELRQARKRRDQASEALRQASRRLEErqsALDELELQLFPQAGTLLHFLRKEapdweqsIGKVISp 557
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  704 EL---TQLKQLVD----AQKENSVSITEHLQVI---------TTLRTAAKEMEEKISNLKEHLASKEVEVAKLEKQLLEE 767
Cdd:pfam12128  558 ELlhrTDLDPEVWdgsvGGELNLYGVKLDLKRIdvpewaaseEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKA 637
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  768 KAAMTDAMVPRSSYEKLQSSLESEVSVLASKLKESVKE-KEKVHSEVVQIRSEVSQVKREkenIQTLLKSKEQEVNELLQ 846
Cdd:pfam12128  638 SREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAErKDSANERLNSLEAQLKQLDKK---HQAWLEEQKEQKREART 714
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....
gi 1370488827  847 KFQQAQEElaemkryaessskLEEDKDKKINEMSKEVTKLKEAL 890
Cdd:pfam12128  715 EKQAYWQV-------------VEGALDAQLALLKAAIAARRSGA 745
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
458-690 5.49e-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: 5.49e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 458 LVCLNNTEISENSSDLSQKLKETQSKYEEAMKEVLSVQKQMKLGLVSPESMDNyshfhELRVTEEEINVLKQDLQNALEE 537
Cdd:COG4942    10 LLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALER-----RIAALARRIRALEQELAALEAE 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 538 SERNKEKVRELEEKLVEReKGTVIKPPVEEYEEMKSSYCSVI---ENMNK--EKAFLFEKYQEA-QEEIMKLKDTLKSQM 611
Cdd:COG4942    85 LAELEKEIAELRAELEAQ-KEELAELLRALYRLGRQPPLALLlspEDFLDavRRLQYLKYLAPArREQAEELRADLAELA 163
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370488827 612 TQEAsdEAEDMKEAMNRMIDELNKQVSELSQLYKEAQAELEDYRKRKSLEDVTAEYIHKAEHEKLMQLTNVSRAKAEDA 690
Cdd:COG4942   164 ALRA--ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
423-696 5.73e-05

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 46.06  E-value: 5.73e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 423 IQQLQEILQDLQKRLESSEAERKQLQVELQSRRAELVCLNN----------------TEISENSSDLSQKLKETQSKYEE 486
Cdd:COG1340    10 LEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAqvkelreeaqelrekrDELNEKVKELKEERDELNEKLNE 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 487 AMKEVLSVQKQMKLGLVSPESMDNyshfhelrvTEEEINVLKQDLQNA---LEESERNKEKVRELEEKLVEREKGTVIKp 563
Cdd:COG1340    90 LREELDELRKELAELNKAGGSIDK---------LRKEIERLEWRQQTEvlsPEEEKELVEKIKELEKELEKAKKALEKN- 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 564 pvEEYEEMKSSYCSVIENMNKekafLFEKYQEAQEEIMKLKDTLksqmtQEASDEAEDMKE---AMNRMIDELNKQVSEL 640
Cdd:COG1340   160 --EKLKELRAELKELRKEAEE----IHKKIKELAEEAQELHEEM-----IELYKEADELRKeadELHKEIVEAQEKADEL 228
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1370488827 641 SQLYKEAQAELEDYRKrksledVTAEYIHKAEHEKLMQLTNVSRAKAEDALSEMKS 696
Cdd:COG1340   229 HEEIIELQKELRELRK------ELKKLRKKQRALKREKEKEELEEKAEEIFEKLKK 278
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
422-717 6.89e-05

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 46.87  E-value: 6.89e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  422 RIQQLQEILQDLQKRLESSEAERKQLQVELQSRRAELVclnNTEISENS-----SDLSQKLKETQSK---YEEAMKEVLS 493
Cdd:COG3096    348 KIERYQEDLEELTERLEEQEEVVEEAAEQLAEAEARLE---AAEEEVDSlksqlADYQQALDVQQTRaiqYQQAVQALEK 424
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  494 VQKQMKLGLVSPESMDNYshFHELRVTEEEIN----VLKQDLQNAlEESERNKEKVRELEEKL---VEREK-GTVIKPPV 565
Cdd:COG3096    425 ARALCGLPDLTPENAEDY--LAAFRAKEQQATeevlELEQKLSVA-DAARRQFEKAYELVCKIageVERSQaWQTARELL 501
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  566 EEYeemkSSYCSVIENMNKEKAFLFEKYQ--EAQEEIMKLKDTLKSQMTQE--ASDEAEDMKEAMNRMIDELNKQVSELS 641
Cdd:COG3096    502 RRY----RSQQALAQRLQQLRAQLAELEQrlRQQQNAERLLEEFCQRIGQQldAAEELEELLAELEAQLEELEEQAAEAV 577
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370488827  642 QLYKEAQAELEDYR-KRKSLEDVTAEYIHKAEH-EKLMQLTNVSRAKAEDALSEMKSQYSKvLNELTQLKQLVDAQKE 717
Cdd:COG3096    578 EQRSELRQQLEQLRaRIKELAARAPAWLAAQDAlERLREQSGEALADSQEVTAAMQQLLER-EREATVERDELAARKQ 654
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
605-854 7.42e-05

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 46.36  E-value: 7.42e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 605 DTLKSQMTQEASDEAEDMKEAMNRmIDELNKQVSELSQLYKEAQAELEDyrKRKSLEDVTAEyIHKAEHEklmqltnvsR 684
Cdd:COG3883    15 DPQIQAKQKELSELQAELEAAQAE-LDALQAELEELNEEYNELQAELEA--LQAEIDKLQAE-IAEAEAE---------I 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 685 AKAEDALSEMKSQYSKVLNELTQLKQLVDAQkensvSITEHLQVITTLRTAAKEMEEKISNLKEHLASKEVEVAKLEKQL 764
Cdd:COG3883    82 EERREELGERARALYRSGGSVSYLDVLLGSE-----SFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKL 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 765 LEEKAAMTDAMVPRSSYEKLQSSLESEVSVLASKLKESVKEKEKVHSEVVQIRSEVSQVKREKENIQTLLKSKEQEVNEL 844
Cdd:COG3883   157 AELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAA 236
                         250
                  ....*....|
gi 1370488827 845 LQKFQQAQEE 854
Cdd:COG3883   237 AAAAAAAASA 246
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
512-890 7.54e-05

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: 46.66  E-value: 7.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 512 SHFHELRVTEEEINVLKQDLQnalEESERNKE---KVRELEEKLVEREKGtvikppveeyeemkssycsvienmNKEKAF 588
Cdd:pfam05557  24 EHKRARIELEKKASALKRQLD---RESDRNQElqkRIRLLEKREAEAEEA------------------------LREQAE 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 589 LFEKYQEAQEEIMKLKDTLKSQMTqeasdEAEDMKEAMNRMIDELNKQVSELSQLYKEAQAELEDYRKRKSLEDVTAEYI 668
Cdd:pfam05557  77 LNRLKKKYLEALNKKLNEKESQLA-----DAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEA 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 669 HK--AEHEKLMQLTNVSRAKAEDALSEMKSQyskvlnelTQLKQLVDAQKENSVSITEHLQVITTLRtaakEMEEKISNL 746
Cdd:pfam05557 152 EQlrQNLEKQQSSLAEAEQRIKELEFEIQSQ--------EQDSEIVKNSKSELARIPELEKELERLR----EHNKHLNEN 219
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 747 KEHLASKEVEVAKLEKQLLEEKAAMTDAMVPRSSYEKLQSSLESEVSVLASKLKESVKeKEKVHSEVVQIRSEVSQVKRE 826
Cdd:pfam05557 220 IENKLLLKEEVEDLKRKLEREEKYREEAATLELEKEKLEQELQSWVKLAQDTGLNLRS-PEDLSRRIEQLQQREIVLKEE 298
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370488827 827 KENIQTLLKSKEQEVNELLQKFQQAQEELAEMKRYAESSSKLEEDKDKKINEMSKEVTKLKEAL 890
Cdd:pfam05557 299 NSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERDGYRAIL 362
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
633-891 8.44e-05

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 46.46  E-value: 8.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 633 LNKQVSE-LSQLYKEAQAELEDYRKRKSledvtAEYIHKAEHEklmqltnvsRAKAEDALSEMKSqYSKVLNELTQLKQL 711
Cdd:PRK05771   14 LKSYKDEvLEALHELGVVHIEDLKEELS-----NERLRKLRSL---------LTKLSEALDKLRS-YLPKLNPLREEKKK 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 712 VDAQKENSV--SITEHLQVIttlRTAAKEMEEKISNLKEHLASKEVEVAKLE---------KQLLEEK-AAMTDAMVPRS 779
Cdd:PRK05771   79 VSVKSLEELikDVEEELEKI---EKEIKELEEEISELENEIKELEQEIERLEpwgnfdldlSLLLGFKyVSVFVGTVPED 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 780 SYEKLQSSLESEVSVLASKLKESV-------KEKEKVHSEVV---------------------QIRSEVSQVKREKENIQ 831
Cdd:PRK05771  156 KLEELKLESDVENVEYISTDKGYVyvvvvvlKELSDEVEEELkklgferleleeegtpselirEIKEELEEIEKERESLL 235
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370488827 832 TLLKSKEQEVNELLqkfQQAQEELAEMKRYAESSSKLEEDKDKKINE---MSKEVTKLKEALN 891
Cdd:PRK05771  236 EELKELAKKYLEEL---LALYEYLEIELERAEALSKFLKTDKTFAIEgwvPEDRVKKLKELID 295
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
177-204 8.80e-05

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 40.32  E-value: 8.80e-05
                          10        20
                  ....*....|....*....|....*...
gi 1370488827 177 GRTALMLACEIGSSNAVEALIKKGADLN 204
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGADIN 29
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
53-133 1.05e-04

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 46.04  E-value: 1.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  53 AAKGHVECLRVMITHGVDVTAQDTTGHSALHLAAKNSHHECIRKLLQSKCPAESVDSSGKTALHYAAAQGCLQAVQILCE 132
Cdd:PTZ00322   90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169

                  .
gi 1370488827 133 H 133
Cdd:PTZ00322  170 H 170
PRK01156 PRK01156
chromosome segregation protein; Provisional
468-860 1.07e-04

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 46.43  E-value: 1.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 468 ENSSDLSQKLKETQSKYEEAMKEVLSVQKQMKLGLVSPESMDNYSH-FHELRVTEEEINVLKQDLQNALEESERNKEKVR 546
Cdd:PRK01156  308 ENKKQILSNIDAEINKYHAIIKKLSVLQKDYNDYIKKKSRYDDLNNqILELEGYEMDYNSYLKSIESLKKKIEEYSKNIE 387
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 547 ELEEKLVEREKGTVIKPP--VEEYEEMKSS---YCSVIENMNKEKAFLFEKYQEAQEEIMKLKDTLKSQM------TQEA 615
Cdd:PRK01156  388 RMSAFISEILKIQEIDPDaiKKELNEINVKlqdISSKVSSLNQRIRALRENLDELSRNMEMLNGQSVCPVcgttlgEEKS 467
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 616 SDEAEDMKEAMNRMIDELNKQVSELSQLYKEA--QAELEDYRKRKSLEDVTAEY--IHKAEHEKLMQLTNVSRAK-AEDA 690
Cdd:PRK01156  468 NHIINHYNEKKSRLEEKIREIEIEVKDIDEKIvdLKKRKEYLESEEINKSINEYnkIESARADLEDIKIKINELKdKHDK 547
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 691 LSEMKSQY---------SKVLNELTQLKQLVDAQKENSVSITEhlQVITTLRTAAKEMEEKISNLKEHLASKEVEVAKLE 761
Cdd:PRK01156  548 YEEIKNRYkslkledldSKRTSWLNALAVISLIDIETNRSRSN--EIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIE 625
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 762 KQLLEEKAAMTDAMVPRSSYEKLQSSLESEVSVLAsKLKESVKEKEKVHSEVVQIRSEVSQVKREKENI-------QTLL 834
Cdd:PRK01156  626 NEANNLNNKYNEIQENKILIEKLRGKIDNYKKQIA-EIDSIIPDLKEITSRINDIEDNLKKSRKALDDAkanrarlESTI 704
                         410       420
                  ....*....|....*....|....*.
gi 1370488827 835 KSKEQEVNELLQKFQQAQEELAEMKR 860
Cdd:PRK01156  705 EILRTRINELSDRINDINETLESMKK 730
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
177-207 1.38e-04

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 39.97  E-value: 1.38e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1370488827 177 GRTALMLACEI-GSSNAVEALIKKGADLNLVD 207
Cdd:pfam00023   2 GNTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
46-188 1.67e-04

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 45.46  E-value: 1.67e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  46 KHCFHlAAAKGHV----ECLRVMITHGVD------VTAQDTT----GHSALHLAAKNSHHECIRKLLQSK-------CPA 104
Cdd:TIGR00870  83 DTLLH-AISLEYVdaveAILLHLLAAFRKsgplelANDQYTSeftpGITALHLAAHRQNYEIVKLLLERGasvparaCGD 161
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 105 ESVDSSGKTALHY-------AAAQGCLQAVQILCEHKSPINLKDLDGNIPL-LLAVQNGHSE-----ICH---FLLDHGA 168
Cdd:TIGR00870 162 FFVKSQGVDSFYHgesplnaAACLGSPSIVALLSEDPADILTADSLGNTLLhLLVMENEFKAeyeelSCQmynFALSLLD 241
                         170       180
                  ....*....|....*....|....*..
gi 1370488827 169 DVNS-------RNKSGRTALMLACEIG 188
Cdd:TIGR00870 242 KLRDskeleviLNHQGLTPLKLAAKEG 268
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
471-699 1.68e-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: 1.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 471 SDLSQKLKETQSKYEEAMKEVLSVQKQMKlglvspesmdnyshfhelrVTEEEINVLKQDLQNALEESERNKEKVRELEE 550
Cdd:COG3883    19 QAKQKELSELQAELEAAQAELDALQAELE-------------------ELNEEYNELQAELEALQAEIDKLQAEIAEAEA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 551 KLVEREkgtvikppvEEYEE-MKSSY------------------------CSVIENMNKEKAFLFEKYQEAQEEIMKLKD 605
Cdd:COG3883    80 EIEERR---------EELGErARALYrsggsvsyldvllgsesfsdfldrLSALSKIADADADLLEELKADKAELEAKKA 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 606 TLKSQMtqeasDEAEDMKEAMNRMIDELNKQVSELSQLYKEAQAELEDYRKRKSLEDVTAEYIHKAEHEKLMQLTNVSRA 685
Cdd:COG3883   151 ELEAKL-----AELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAA 225
                         250
                  ....*....|....
gi 1370488827 686 KAEDALSEMKSQYS 699
Cdd:COG3883   226 AAAAAAAAAAAAAA 239
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
613-858 2.08e-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: 44.75  E-value: 2.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 613 QEASDEAEDMKEAMNRMIDELNKQVSELSQLYKEAQAELEDYRKRKSledVTAEYIHKAEH-----EKLMQLTNVSRAKA 687
Cdd:COG4942    19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIA---ALARRIRALEQelaalEAELAELEKEIAEL 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 688 EDALSEMKSQYSKVLNELTQLKQLVDAQ-KENSVSITEHLQVITTLRTAAKEMEEKISNLKEHLAskevEVAKLEKQLLE 766
Cdd:COG4942    96 RAELEAQKEELAELLRALYRLGRQPPLAlLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLA----ELAALRAELEA 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 767 EKaamtdamvprssyeklqsslesevsvlasklkesvKEKEKVHSEVVQIRSEVSQVKREKENIQTLLKSKEQEVNELLQ 846
Cdd:COG4942   172 ER-----------------------------------AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELA 216
                         250
                  ....*....|..
gi 1370488827 847 KFQQAQEELAEM 858
Cdd:COG4942   217 ELQQEAEELEAL 228
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
418-674 2.18e-04

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 45.29  E-value: 2.18e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  418 DNDVRIQQLQEILQDLQKRLESSEAERKQLQVELQSRRAELVCLNNteiSENSSDLSQKLKETQSKYEEAMKEVLSVQKq 497
Cdd:COG4913    607 DNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQR---LAEYSWDEIDVASAEREIAELEAELERLDA- 682
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  498 mklglvspeSMDnyshfhELRVTEEEINVLKQDLQNALEESERNKEKVRELEEKLVEREkgtvikppvEEYEEMKSSYCS 577
Cdd:COG4913    683 ---------SSD------DLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAE---------EELDELQDRLEA 738
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  578 VIENMNKEKAFLFEKYQEAQeeimkLKDTLKSQMTQEASDEAEDMKEAMNRMIDELNKQVSELSQLYKEAQAEL------ 651
Cdd:COG4913    739 AEDLARLELRALLEERFAAA-----LGDAVERELRENLEERIDALRARLNRAEEELERAMRAFNREWPAETADLdadles 813
                          250       260
                   ....*....|....*....|....
gi 1370488827  652 -EDYRKRksLEDVTAEYIHKAEHE 674
Cdd:COG4913    814 lPEYLAL--LDRLEEDGLPEYEER 835
PHA02874 PHA02874
ankyrin repeat protein; Provisional
122-206 2.58e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 44.57  E-value: 2.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 122 GCLQAVQILCEHKSP-INLKDLDGNIPLLLAVQNGHSEICHFLLDHGADVNSRNKSGRTALMLACEIGSSNAVEALIKKG 200
Cdd:PHA02874   12 GDIEAIEKIIKNKGNcINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNG 91

                  ....*.
gi 1370488827 201 ADLNLV 206
Cdd:PHA02874   92 VDTSIL 97
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
422-891 2.84e-04

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.91  E-value: 2.84e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  422 RIQQLQEILQDLQKRLESSEAERKQLQVELQSRRAELVCLNNtEISENSSD----LSQKLKETQSKYEEAMKEVLSVQKQ 497
Cdd:COG4913    289 RLELLEAELEELRAELARLEAELERLEARLDALREELDELEA-QIRGNGGDrleqLEREIERLERELEERERRRARLEAL 367
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  498 MK-LGLVSPESMDNY-SHFHELRVTEEEINVLKQDLQNALEESERNKEKVR-ELEEKLVERE----KGTVIkPPveEYEE 570
Cdd:COG4913    368 LAaLGLPLPASAEEFaALRAEAAALLEALEEELEALEEALAEAEAALRDLRrELRELEAEIAslerRKSNI-PA--RLLA 444
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  571 MKSSYCSVIENMNKEKAFL----------------FEK---------------YQEAQEEI-----------MKLKDTLK 608
Cdd:COG4913    445 LRDALAEALGLDEAELPFVgelievrpeeerwrgaIERvlggfaltllvppehYAAALRWVnrlhlrgrlvyERVRTGLP 524
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  609 SQMTQEASDE--AEDMKEAMNRMIDELNKQVSELSQLYK-EAQAELEDYRKRksledVTAE---YIHKAEHEKLMQLTNV 682
Cdd:COG4913    525 DPERPRLDPDslAGKLDFKPHPFRAWLEAELGRRFDYVCvDSPEELRRHPRA-----ITRAgqvKGNGTRHEKDDRRRIR 599
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  683 SR----AKAEDALSEMKSQYSKVLNELTQLKQLVDAqkensvsITEHLQVITTLRTAAKEMEEKISNLKEhLASKEVEVA 758
Cdd:COG4913    600 SRyvlgFDNRAKLAALEAELAELEEELAEAEERLEA-------LEAELDALQERREALQRLAEYSWDEID-VASAEREIA 671
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  759 KLEKQLleekaamtdamvprssyEKLQSSlESEVSVLASKLKESVKEKEKVHSEVVQIRSEVSQVKREKENIQTLLKSKE 838
Cdd:COG4913    672 ELEAEL-----------------ERLDAS-SDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQ 733
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1370488827  839 QEVNELLQKFQQAQEELAEMKRYAESSSKLEEDKDKKInemSKEVTKLKEALN 891
Cdd:COG4913    734 DRLEAAEDLARLELRALLEERFAAALGDAVERELRENL---EERIDALRARLN 783
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
424-909 3.23e-04

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: 44.71  E-value: 3.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 424 QQLQEILQDLQKRLESSEAERKQLQVELQSRRAELvclnnteisenSSDLSQKLKETQSKYEEAMKEVLSVQKQMKLGLV 503
Cdd:pfam05483 179 EETRQVYMDLNNNIEKMILAFEELRVQAENARLEM-----------HFKLKEDHEKIQHLEEEYKKEINDKEKQVSLLLI 247
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 504 spesmdnyshfhelRVTEEEINVlkQDLQNALEESernKEKVRELEEK--LVEREKGTVIKPPVEEYEEMKSSYCSVIEN 581
Cdd:pfam05483 248 --------------QITEKENKM--KDLTFLLEES---RDKANQLEEKtkLQDENLKELIEKKDHLTKELEDIKMSLQRS 308
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 582 MNKEKAfLFEKYQEAQEEIMKLKDTLKSQMtqeasDEAEDMKEAMNRMIDELNKQVSELSQLYKEAQAELEdyRKRKSLE 661
Cdd:pfam05483 309 MSTQKA-LEEDLQIATKTICQLTEEKEAQM-----EELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLE--KNEDQLK 380
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 662 DVTAEYIHKA-EHEKLMQLTNVSRAKAEDaLSEMKSQYSKVLNELTQLKQLVDAQKENSVSITEHLQV-----------I 729
Cdd:pfam05483 381 IITMELQKKSsELEEMTKFKNNKEVELEE-LKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQArekeihdleiqL 459
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 730 TTLRTAAKEMEEKISNLKEHLASKEVEVAKL----------EKQLLEEKAAMTDAMVPRS----SYEKLQSSLESEVSVL 795
Cdd:pfam05483 460 TAIKTSEEHYLKEVEDLKTELEKEKLKNIELtahcdkllleNKELTQEASDMTLELKKHQediiNCKKQEERMLKQIENL 539
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 796 ASKLKESVKEKEKVHSEVVQIRSEVS-QVKREKENIQTL----------LKSKEQEVNELLQK-------FQQAQEELAE 857
Cdd:pfam05483 540 EEKEMNLRDELESVREEFIQKGDEVKcKLDKSEENARSIeyevlkkekqMKILENKCNNLKKQienknknIEELHQENKA 619
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1370488827 858 MKRYAESSSKLEEDKDKKINEMSKEVTKLKEALNSLSQLSYSTSSSKRQSQQ 909
Cdd:pfam05483 620 LKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISEE 671
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
411-655 3.28e-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: 3.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 411 SLGKSTTDNDVRIQQLQEILQDLQKRLESSEAERKQLQvelqsRRAELVCLNNTE--ISENSSDLSQKLKETQSKYEEAM 488
Cdd:COG3206   165 NLELRREEARKALEFLEEQLPELRKELEEAEAALEEFR-----QKNGLVDLSEEAklLLQQLSELESQLAEARAELAEAE 239
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 489 KEVLSVQKQMKLGLVSPESMDNYSHFHELRvteEEINVLKQDLQNALEESERNKEKVRELEEKLVEREkgtvikppveey 568
Cdd:COG3206   240 ARLAALRAQLGSGPDALPELLQSPVIQQLR---AQLAELEAELAELSARYTPNHPDVIALRAQIAALR------------ 304
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 569 EEMKSSYCSVIENMNKEKAFLfekyQEAQEEIMKLKDTLKSQMTQEASDEAEdmkeamnrmIDELNKQVSELSQLYKEAQ 648
Cdd:COG3206   305 AQLQQEAQRILASLEAELEAL----QAREASLQAQLAQLEARLAELPELEAE---------LRRLEREVEVARELYESLL 371

                  ....*..
gi 1370488827 649 AELEDYR 655
Cdd:COG3206   372 QRLEEAR 378
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
465-887 3.43e-04

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: 44.72  E-value: 3.43e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  465 EISENSSDLSQKLKETQSKYEEAM----KEVLSVQKQMKLGLVSPESMdnyshfHELRVTEEEInvlKQDLQNALEESER 540
Cdd:pfam15921   82 EYSHQVKDLQRRLNESNELHEKQKfylrQSVIDLQTKLQEMQMERDAM------ADIRRRESQS---QEDLRNQLQNTVH 152
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  541 NKEKVRELEEKLVEREKGTVikppvEEYEEMKSSYCSVIENMNKekafLFEKYQEAQEEIMKLKDTLKSQmtqeasdEAE 620
Cdd:pfam15921  153 ELEAAKCLKEDMLEDSNTQI-----EQLRKMMLSHEGVLQEIRS----ILVDFEEASGKKIYEHDSMSTM-------HFR 216
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  621 DMKEAMNRMIDELNKQVSELSQLYKEAQAELEDYrkrKSLEDVTAEYIHKAEHEKLMQLtnVSRAKAE-DALSEMKSQYS 699
Cdd:pfam15921  217 SLGSAISKILRELDTEISYLKGRIFPVEDQLEAL---KSESQNKIELLLQQHQDRIEQL--ISEHEVEiTGLTEKASSAR 291
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  700 KVLNELTQLKQLVDAQKENSVSIteHLQVITTLRTAAKEMEekiSNLKEHLASKEVEVAKLEKQLLEEKAAMTDAMVPRS 779
Cdd:pfam15921  292 SQANSIQSQLEIIQEQARNQNSM--YMRQLSDLESTVSQLR---SELREAKRMYEDKIEELEKQLVLANSELTEARTERD 366
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  780 SYEKLQSSLESEVSVLASKL----KESVKEKEKVHS----------EVVQIRSEVSQVKREKENIQTLLKSKEQEV---- 841
Cdd:pfam15921  367 QFSQESGNLDDQLQKLLADLhkreKELSLEKEQNKRlwdrdtgnsiTIDHLRRELDDRNMEVQRLEALLKAMKSECqgqm 446
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370488827  842 ----------NELLQK--------------FQQAQEELAEMKRYAESSSKLEED-------KDKKINEMSKEVTKLK 887
Cdd:pfam15921  447 erqmaaiqgkNESLEKvssltaqlestkemLRKVVEELTAKKMTLESSERTVSDltaslqeKERAIEATNAEITKLR 523
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
409-789 3.59e-04

Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.


Pssm-ID: 428797 [Multi-domain]  Cd Length: 542  Bit Score: 44.46  E-value: 3.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 409 IHSLGKSTTDNDVRIQQLQEILQDLQKRL--------ESSEAERKQLQvELQSRRAELVCLNNT-----------EISEN 469
Cdd:pfam06160 109 LDELLESEEKNREEVEELKDKYRELRKTLlanrfsygPAIDELEKQLA-EIEEEFSQFEELTESgdylearevleKLEEE 187
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 470 SSDLSQK-------LKETQSKYEEAMKEVLSVQKQMKlglvspesMDNYsHFHELRVtEEEINVLKQDLQNALEESERNK 542
Cdd:pfam06160 188 TDALEELmedipplYEELKTELPDQLEELKEGYREME--------EEGY-ALEHLNV-DKEIQQLEEQLEENLALLENLE 257
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 543 -EKVRELEEKLVERekgtvIKPPVEEYEEMKSSYCSVIENMNKEKAFLF---EKYQEAQEEIMKLKDT-LKSQMTQEASD 617
Cdd:pfam06160 258 lDEAEEALEEIEER-----IDQLYDLLEKEVDAKKYVEKNLPEIEDYLEhaeEQNKELKEELERVQQSyTLNENELERVR 332
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 618 EAEDMKEAMNRMIDELNKQVSELSQLYKEAQAELEDYRKRksLEDVTAEyiHKAEHEKLMQLTNVSRaKAEDALSEMKsq 697
Cdd:pfam06160 333 GLEKQLEELEKRYDEIVERLEEKEVAYSELQEELEEILEQ--LEEIEEE--QEEFKESLQSLRKDEL-EAREKLDEFK-- 405
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 698 yskvlNELTQLKQLVdaQKEN----SVSITEHL-QVITTLRTAAKEMEEKISNLKE-----HLASKEVEVAKLEKQLLEE 767
Cdd:pfam06160 406 -----LELREIKRLV--EKSNlpglPESYLDYFfDVSDEIEDLADELNEVPLNMDEvnrllDEAQDDVDTLYEKTEELID 478
                         410       420
                  ....*....|....*....|....*..
gi 1370488827 768 KAAMTDAMVP-----RSSYEKLQSSLE 789
Cdd:pfam06160 479 NATLAEQLIQyanryRSSNPEVAEALT 505
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
177-205 3.68e-04

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 38.72  E-value: 3.68e-04
                           10        20
                   ....*....|....*....|....*....
gi 1370488827  177 GRTALMLACEIGSSNAVEALIKKGADLNL 205
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
424-647 4.48e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 44.28  E-value: 4.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 424 QQLQEILQDLQKRLESSEAERKQLQvELQSRRAELvclnNTEISENSSDLSQKLKETQSKYEEAMKEVLSVQKQMK---- 499
Cdd:PRK03918  528 EKLKEKLIKLKGEIKSLKKELEKLE-ELKKKLAEL----EKKLDELEEELAELLKELEELGFESVEELEERLKELEpfyn 602
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 500 --LGLVSPEsmdnyshfHELRVTEEEINVLKQDLQNALEESERNKEKVRELEEKLVEREKgtviKPPVEEYEEMKSSYCS 577
Cdd:PRK03918  603 eyLELKDAE--------KELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEK----KYSEEEYEELREEYLE 670
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370488827 578 VIENMNKEKAFLfEKYQEAQEEIMKLKDTLKSQMT--QEASDEAEDMKEAMNRMiDELNKQVSELSQLYKEA 647
Cdd:PRK03918  671 LSRELAGLRAEL-EELEKRREEIKKTLEKLKEELEerEKAKKELEKLEKALERV-EELREKVKKYKALLKER 740
PHA03100 PHA03100
ankyrin repeat protein; Provisional
132-243 4.59e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 43.89  E-value: 4.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 132 EHKSPINLKDLDGNIPLLLAVQNGHSEICHFLLDHGADVNSRNKSGRTALMLACEIGSS-----NAVEALIKKGADLNLV 206
Cdd:PHA03100   23 MEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAP 102
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1370488827 207 DSLGYNALHY--SKLSENAGIQSLLLSKISqDADLKTPT 243
Cdd:PHA03100  103 DNNGITPLLYaiSKKSNSYSIVEYLLDNGA-NVNIKNSD 140
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
422-864 5.00e-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: 44.01  E-value: 5.00e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  422 RIQQLQEILQDLQKRLESSEAERKQLQVELQSRraelvclnnTEISENSSDLSQKLKETQSKYEEAMKEVlsvqkqmklg 501
Cdd:pfam01576   20 RQQKAESELKELEKKHQQLCEEKNALQEQLQAE---------TELCAEAEEMRARLAARKQELEEILHEL---------- 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  502 lvspesmdnyshfhELRVTEEEINVlkQDLQNaleESERNKEKVRELEEKLVEREKGTvikppveeyeemkssycsviEN 581
Cdd:pfam01576   81 --------------ESRLEEEEERS--QQLQN---EKKKMQQHIQDLEEQLDEEEAAR--------------------QK 121
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  582 MNKEKAFLFEKYQEAQEEIMKLKDTlKSQMTQEASDEAEDMKEAMNRMIDELN--KQVSELSQLYKEAQAELEDYRKRKs 659
Cdd:pfam01576  122 LQLEKVTTEAKIKKLEEDILLLEDQ-NSKLSKERKLLEERISEFTSNLAEEEEkaKSLSKLKNKHEAMISDLEERLKKE- 199
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  660 ledvtaeyihkaehEKLMQLTNVSRAKAEDALSEMKSQYSKVLNELTQLKQLVDAQKENSVSITEHLQVITTLRTAA--- 736
Cdd:pfam01576  200 --------------EKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNAlkk 265
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  737 -KEMEEKISNLKEHLASKEVEVAKLEKQ---LLEE----KAAMTDAMVPRSSYEKLQSSLESEVSVLASKLKESVKEKE- 807
Cdd:pfam01576  266 iRELEAQISELQEDLESERAARNKAEKQrrdLGEElealKTELEDTLDTTAAQQELRSKREQEVTELKKALEEETRSHEa 345
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370488827  808 -------KVHSEVVQIRSEVSQVKREKENIQTLLKSKEQEVNEL---LQKFQQAQEELAEMKRYAES 864
Cdd:pfam01576  346 qlqemrqKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELqaeLRTLQQAKQDSEHKRKKLEG 412
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
535-911 5.15e-04

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 44.19  E-value: 5.15e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  535 LEESERNKEKVRELEEKLVEREKgtvikppVEEYEEMKSSYCSVIENMNKEKaflfEKYQEAQEEIMKLKDTLKSQMTQE 614
Cdd:pfam02463  159 EEEAAGSRLKRKKKEALKKLIEE-------TENLAELIIDLEELKLQELKLK----EQAKKALEYYQLKEKLELEEEYLL 227
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  615 ASDEAEDMKEAMNRMIDELNKQVSELSQLYKEAQAELEdyrkrkSLEDVTAEYIhkaEHEKLMQLTNVSRAKAEDALSEM 694
Cdd:pfam02463  228 YLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEE------KLAQVLKENK---EEEKEKKLQEEELKLLAKEEEEL 298
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  695 KSQYSKvlneLTQLKQLVDAQKENSVSITEHLQVITTLRTAAKEMEEKIsnLKEHLASKEVEVAKLEKQLLEEKAAmtda 774
Cdd:pfam02463  299 KSELLK----LERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKE--LKELEIKREAEEEEEEELEKLQEKL---- 368
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  775 mvprssyEKLQSSLESEVSVLASKLKESVKEKEKVH---SEVVQIRSEVSQVKREKENIQTLLKSKEQEVNELLQKFQQA 851
Cdd:pfam02463  369 -------EQLEEELLAKKKLESERLSSAAKLKEEELelkSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIEL 441
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  852 QEELAEMKRYAESSSKLEEDKDKkinEMSKEVTKLKEALNSLSQLSYSTSSSKRQSQQLE 911
Cdd:pfam02463  442 KQGKLTEEKEELEKQELKLLKDE---LELKKSEDLLKETQLVKLQEQLELLLSRQKLEER 498
COG5022 COG5022
Myosin heavy chain [General function prediction only];
591-865 5.89e-04

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 43.91  E-value: 5.89e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  591 EKYQEAQEEIMKLKDTLKSQMTQEASDEAEDMKEAM---NRMIDELN--KQVSEL--SQLYKEAQAELEDYRKRKSLEDV 663
Cdd:COG5022    810 KEYRSYLACIIKLQKTIKREKKLRETEEVEFSLKAEvliQKFGRSLKakKRFSLLkkETIYLQSAQRVELAERQLQELKI 889
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  664 TAEyihKAEHEKLMQLTNVSRakaedaLSEMKSQYSKVLNELTQLKqlvdaqkensvsiTEHlqvITTLRTAAKEMEEKI 743
Cdd:COG5022    890 DVK---SISSLKLVNLELESE------IIELKKSLSSDLIENLEFK-------------TEL---IARLKKLLNNIDLEE 944
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  744 SnlkehlASKEVEVAKLEKQLLEEKAAMTDAMVPRSSYEKLQSSLESEVSVLASKLK-----------------ESVKEK 806
Cdd:COG5022    945 G------PSIEYVKLPELNKLHEVESKLKETSEEYEDLLKKSTILVREGNKANSELKnfkkelaelskqygalqESTKQL 1018
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1370488827  807 EKVHSEVVQIRSEVSQVKREKENIQTLLKSKEQEvNELLQKFQQAQEELAEMKRYAESS 865
Cdd:COG5022   1019 KELPVEVAELQSASKIISSESTELSILKPLQKLK-GLLLLENNQLQARYKALKLRRENS 1076
CAGE1 pfam15066
Cancer-associated gene protein 1 family; CAGE-1 is a family of proteins overexpressed in ...
418-557 6.61e-04

Cancer-associated gene protein 1 family; CAGE-1 is a family of proteins overexpressed in tumour tissues compared with surrounding tissues. CAGE-1 gene showed testis-specific expression among normal tissues and displayed wide expression in a variety of cancer cell lines and cancer tissues. CAGE-1 is predominantly expressed during post-meiotic stages. It localizes to the acrosomal matrix and acrosomal granule showing it to be a component of the acrosome of mammalian spermatids and spermatozoa.


Pssm-ID: 464481  Cd Length: 528  Bit Score: 43.28  E-value: 6.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 418 DNDVRIQQLQEILQDLQKRLESSEAERKQLQVELQSRRAELVCLNN---TEISENSSDLSQKLK--ETQSKYEEamkEVL 492
Cdd:pfam15066 388 DINKTLQNLQEILANTQKHLQESRKEKETLQLELKKIKVNYVHLQEryiTEMQQKNKSVSQCLEmdKTLSKKEE---EVE 464
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370488827 493 SVQkQMKLGL--VSPESMDNYSHFHELRvtEEEINVLKQDLQNALEESERNKEKVRELEEKLVEREK 557
Cdd:pfam15066 465 RLQ-QLKGELekATTSALDLLKREKETR--EQEFLSLQEEFQKHEKENLEERQKLKSRLEKLVAQVK 528
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
147-171 6.92e-04

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 38.01  E-value: 6.92e-04
                          10        20
                  ....*....|....*....|....*
gi 1370488827 147 PLLLAVQNGHSEICHFLLDHGADVN 171
Cdd:pfam13606   5 PLHLAARNGRLEIVKLLLENGADIN 29
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
459-887 7.30e-04

reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.


Pssm-ID: 130673 [Multi-domain]  Cd Length: 2757  Bit Score: 43.89  E-value: 7.30e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  459 VCLNNTEISENSSDLSQKLKETQSKYEEAMKEVLSVQKQMK--------------------LGLVSPESMDN--YSHFHE 516
Cdd:TIGR01612  925 ICENTKESIEKFHNKQNILKEILNKNIDTIKESNLIEKSYKdkfdntlidkineldkafkdASLNDYEAKNNelIKYFND 1004
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  517 LRVTeeeinvLKQDLQNALEESERNKEK-VRELEEKLVEREKG---------TVIKPPVEEYEE-----MKSSYCSVIEN 581
Cdd:TIGR01612 1005 LKAN------LGKNKENMLYHQFDEKEKaTNDIEQKIEDANKNipnieiaihTSIYNIIDEIEKeigknIELLNKEILEE 1078
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  582 MN---------KEKA-------FLFEKYQEAQEEIMKLKDTLKS--QMTQEASDEAEDMKEAMNRMIDELNKQVSELSQ- 642
Cdd:TIGR01612 1079 AEinitnfneiKEKLkhynfddFGKEENIKYADEINKIKDDIKNldQKIDHHIKALEEIKKKSENYIDEIKAQINDLEDv 1158
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  643 ----LYKEAQAELEDYRKRKSLEDVTAEYIHKAEHEKLMQLTNVSRAKAedALSEMKS---QYSKVLNELtqLKQLVDAQ 715
Cdd:TIGR01612 1159 adkaISNDDPEEIEKKIENIVTKIDKKKNIYDEIKKLLNEIAEIEKDKT--SLEEVKGinlSYGKNLGKL--FLEKIDEE 1234
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  716 KENSvsitEHLqvittlrtaAKEMEEKISNLKEhLASKEVEVAKLEKQLLEEKAAMTDAMVPRSSYEKLQS--------- 786
Cdd:TIGR01612 1235 KKKS----EHM---------IKAMEAYIEDLDE-IKEKSPEIENEMGIEMDIKAEMETFNISHDDDKDHHIiskkhdeni 1300
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  787 --------------SLESEVSVLASKLKESVKEKEKVHSEVVQIRSEVSQVKR--EKENIQTLLKSKEQEVNELLQKFQQ 850
Cdd:TIGR01612 1301 sdirekslkiiedfSEESDINDIKKELQKNLLDAQKHNSDINLYLNEIANIYNilKLNKIKKIIDEVKEYTKEIEENNKN 1380
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*....
gi 1370488827  851 AQEELAE----MKRYAESSSkLEEDK--------DKKINEMSKEVTKLK 887
Cdd:TIGR01612 1381 IKDELDKseklIKKIKDDIN-LEECKskiestldDKDIDECIKKIKELK 1428
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
411-860 9.60e-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: 43.24  E-value: 9.60e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  411 SLGKSTTDNDVRIQQLQEILQDLQKRLESSEAERKQLQVELQSRRAELvclnnteisensSDLSQKLKETQSKYEEAMKE 490
Cdd:pfam01576  395 TLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSEL------------ESVSSLLNEAEGKNIKLSKD 462
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  491 VLSVQKQMK--LGLVSPESMDNYSHFHELRVTEEEINVLKQDLQNAlEESERNKEK-VRELEEKLVE-REKGTVIKPPVE 566
Cdd:pfam01576  463 VSSLESQLQdtQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEE-EEAKRNVERqLSTLQAQLSDmKKKLEEDAGTLE 541
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  567 EYEEMKSSYCSVIENMN---KEKAFLFEKYQEA----QEEIMKLKDTLKSQMT--------------------------Q 613
Cdd:pfam01576  542 ALEEGKKRLQRELEALTqqlEEKAAAYDKLEKTknrlQQELDDLLVDLDHQRQlvsnlekkqkkfdqmlaeekaisaryA 621
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  614 EASDEAE-DMKE------AMNRMIDELNKQVSELSQLYKEAQAELEDYRKRKsleDVTAEYIHKAEHeklmqltnvSRAK 686
Cdd:pfam01576  622 EERDRAEaEAREketralSLARALEEALEAKEELERTNKQLRAEMEDLVSSK---DDVGKNVHELER---------SKRA 689
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  687 AEDALSEMKSQYSKVLNELTQLKqlvDAQkensvsitehLQVITTLRTAAKEMEEKISNLKEHLASKEVEVAK----LEK 762
Cdd:pfam01576  690 LEQQVEEMKTQLEELEDELQATE---DAK----------LRLEVNMQALKAQFERDLQARDEQGEEKRRQLVKqvreLEA 756
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  763 QLLEEKAAMTDAMVPRSSYEKLQSSLESEVSVLASKLKESVKEKEKVHSEVVQIRSEVSQVKREKENIQTLLKSKEQEVN 842
Cdd:pfam01576  757 ELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARASRDEILAQSKESEKKLK 836
                          490
                   ....*....|....*...
gi 1370488827  843 ELLQKFQQAQEELAEMKR 860
Cdd:pfam01576  837 NLEAELLQLQEDLAASER 854
Ank_4 pfam13637
Ankyrin repeats (many copies);
177-230 1.10e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 38.02  E-value: 1.10e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1370488827 177 GRTALMLACEIGSSNAVEALIKKGADLNLVDSLGYNALHYSKLSENAGIQSLLL 230
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
46-73 1.33e-03

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 37.18  E-value: 1.33e-03
                           10        20
                   ....*....|....*....|....*...
gi 1370488827   46 KHCFHLAAAKGHVECLRVMITHGVDVTA 73
Cdd:smart00248   3 RTPLHLAAENGNLEVVKLLLDKGADINA 30
HMMR_N pfam15905
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ...
409-653 1.44e-03

Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.


Pssm-ID: 464932 [Multi-domain]  Cd Length: 329  Bit Score: 42.11  E-value: 1.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 409 IHSLGKSTTDNDVRIQQLQEILQDLQKRLESSEAERKQLQVELQSRRAELV------CLNNTEISENS-----SDLSQKL 477
Cdd:pfam15905  82 IRALVQERGEQDKRLQALEEELEKVEAKLNAAVREKTSLSASVASLEKQLLeltrvnELLKAKFSEDGtqkkmSSLSMEL 161
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 478 KETQSKYEEAMKEVLSVQKQMKLGLvspesmdnyshfhelrvteeeinvlkQDLQNALEESernKEKVRELEEKLVEREK 557
Cdd:pfam15905 162 MKLRNKLEAKMKEVMAKQEGMEGKL--------------------------QVTQKNLEHS---KGKVAQLEEKLVSTEK 212
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 558 GTVikppVEEYEEMKssycsvIENMNKEKAFLFEKYQEAQEEIMKLKDTLKsqmtqEASDEAEDMKEAMNRMIDELNKQV 637
Cdd:pfam15905 213 EKI----EEKSETEK------LLEYITELSCVSEQVEKYKLDIAQLEELLK-----EKNDEIESLKQSLEEKEQELSKQI 277
                         250
                  ....*....|....*.
gi 1370488827 638 SELSQLYKEAQAELED 653
Cdd:pfam15905 278 KDLNEKCKLLESEKEE 293
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
527-891 1.50e-03

reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.


Pssm-ID: 130673 [Multi-domain]  Cd Length: 2757  Bit Score: 42.73  E-value: 1.50e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  527 LKQDLQNALEESERNKEKVRELEEKlverekgtvIKPPVEEYEEmkssycSVIEnMNKEKAFLFEKYQEAQEEIM---KL 603
Cdd:TIGR01612  538 LYKEIEAGLKESYELAKNWKKLIHE---------IKKELEEENE------DSIH-LEKEIKDLFDKYLEIDDEIIyinKL 601
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  604 KDTLKSQMtQEASDEAEDMKEAM---------NRMIDELNK----QVSE----LSQLYKEAQAELEDYRKrkslEDVTAE 666
Cdd:TIGR01612  602 KLELKEKI-KNISDKNEYIKKAIdlkkiiennNAYIDELAKispyQVPEhlknKDKIYSTIKSELSKIYE----DDIDAL 676
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  667 YIHKAEHEKLMQLTNVS-RAKAEDALSEMKSQYSKVLNELTQLKQLVDAQKENSVSitEHLQVITTLRTAA-KEMEEKIS 744
Cdd:TIGR01612  677 YNELSSIVKENAIDNTEdKAKLDDLKSKIDKEYDKIQNMETATVELHLSNIENKKN--ELLDIIVEIKKHIhGEINKDLN 754
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  745 NLKEHLASKEVEVAKLEKQLLEEKAAMTdamVPRSSYEKLQSSLESEVSVLASKLKESVK--EKEKVHSEVVQIRS-EVS 821
Cdd:TIGR01612  755 KILEDFKNKEKELSNKINDYAKEKDELN---KYKSKISEIKNHYNDQINIDNIKDEDAKQnyDKSKEYIKTISIKEdEIF 831
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  822 QVKREKENIQTLLKSKEQEV----NELLQKFQQAQEELAEM--KRYAESSSKLEEDKDKK-------INEMSKEVTKLKE 888
Cdd:TIGR01612  832 KIINEMKFMKDDFLNKVDKFinfeNNCKEKIDSEHEQFAELtnKIKAEISDDKLNDYEKKfndskslINEINKSIEEEYQ 911

                   ...
gi 1370488827  889 ALN 891
Cdd:TIGR01612  912 NIN 914
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
582-860 1.55e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.59  E-value: 1.55e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  582 MNKEKAF-LFEKYQEAQEeIMKLKDTLKSQMTqeasdEAEDMKEAmnrmIDELNKQVSELSQLYKEAqaeLEDYRKRKSL 660
Cdd:COG4913    188 IGSEKALrLLHKTQSFKP-IGDLDDFVREYML-----EEPDTFEA----ADALVEHFDDLERAHEAL---EDAREQIELL 254
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  661 EDVTAEY-------IHKAEHEKLMQLTNVSRAKAEDALSEmksqyskvlNELTQLKQLVDAQKENsvsitehlqvITTLR 733
Cdd:COG4913    255 EPIRELAeryaaarERLAELEYLRAALRLWFAQRRLELLE---------AELEELRAELARLEAE----------LERLE 315
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  734 TAAKEMEEKISNLKEHLASKEVE-VAKLEKQLLEEKAAMTDAMVPRSSYEKLQSSLESEVSVLASKLKEsvkekekvhse 812
Cdd:COG4913    316 ARLDALREELDELEAQIRGNGGDrLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAA----------- 384
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 1370488827  813 vvqirsEVSQVKREKENIQTLLKSKEQEVNELLQKFQQAQEELAEMKR 860
Cdd:COG4913    385 ------LRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEA 426
PHA02876 PHA02876
ankyrin repeat protein; Provisional
152-222 1.60e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 42.36  E-value: 1.60e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370488827 152 VQNGHSEICHFLLDHGADVNSRNKSGRTALMLACEIGSSNAVEALIKKGADLNLVDSLGYNALHYSKLSEN 222
Cdd:PHA02876  153 IQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKN 223
COG5022 COG5022
Myosin heavy chain [General function prediction only];
426-891 1.68e-03

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 42.37  E-value: 1.68e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  426 LQEILQDLQKRLESSEAERKQLQVELQSRRAELVCLN-NTEISENSSDLSQKLKET---QSKYEEAMKEVLSVQKQMKLG 501
Cdd:COG5022    799 LQPLLSLLGSRKEYRSYLACIIKLQKTIKREKKLRETeEVEFSLKAEVLIQKFGRSlkaKKRFSLLKKETIYLQSAQRVE 878
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  502 LVSPESMD------NYSHFHELRVT-EEEINVLKQDLQNAL-EESERNKEKVRELEEKL------VEREKGTVIKPPVEE 567
Cdd:COG5022    879 LAERQLQElkidvkSISSLKLVNLElESEIIELKKSLSSDLiENLEFKTELIARLKKLLnnidleEGPSIEYVKLPELNK 958
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  568 YEEMKSSY---CSVIENMNKEKAFLFEKYQEAQEEIMKLKDTLKSQMTQ-EASDEAEDMKEAMNRMIDELNKqvseLSQL 643
Cdd:COG5022    959 LHEVESKLketSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQyGALQESTKQLKELPVEVAELQS----ASKI 1034
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  644 YKEAQAELedyRKRKSLEDVTAEYIhKAEHEKLMQLTNVS-RAKAEDALSEMKSQYSKVLNELTQLKQL-VDAQKENSVS 721
Cdd:COG5022   1035 ISSESTEL---SILKPLQKLKGLLL-LENNQLQARYKALKlRRENSLLDDKQLYQLESTENLLKTINVKdLEVTNRNLVK 1110
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  722 ITEHLQVITTLRTAAKEMEEKISNLKEHLASKEVEVAKLEK-QLLEEKAAMTDAMVPRSSYEKLQSSLESEvSVLASKLK 800
Cdd:COG5022   1111 PANVLQFIVAQMIKLNLLQEISKFLSQLVNTLEPVFQKLSVlQLELDGLFWEANLEALPSPPPFAALSEKR-LYQSALYD 1189
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  801 ESVKEKekvHSEVVQIRSEVSqvkrekeniqtLLKSKEQEVNELLQKFQQAQEELAEMKRYAESSSKLEEDKDKKINEMS 880
Cdd:COG5022   1190 EKSKLS---SSEVNDLKNELI-----------ALFSKIFSGWPRGDKLKKLISEGWVPTEYSTSLKGFNNLNKKFDTPAS 1255
                          490
                   ....*....|.
gi 1370488827  881 KEVTKLKEALN 891
Cdd:COG5022   1256 MSNEKLLSLLN 1266
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
583-909 1.84e-03

Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 444066 [Multi-domain]  Cd Length: 594  Bit Score: 42.25  E-value: 1.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 583 NKEKAFLFEKYQEAQEEIMKLKDTLKsqmtQEASDEAEDMKEAMNRMIDELNKQVSELSQLYKEAQAELEDYRKRKSLED 662
Cdd:COG5185   241 PESELEDLAQTSDKLEKLVEQNTDLR----LEKLGENAESSKRLNENANNLIKQFENTKEKIAEYTKSIDIKKATESLEE 316
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 663 VTAEYIHKAEHEKLMqltnvsrAKAEDALSEMKSQYSKVLNELTQLKQLVDAQKENSVSITEHLQVITTLRTAAKEMEEK 742
Cdd:COG5185   317 QLAAAEAEQELEESK-------RETETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEVELSKSSEELDSFKDTIEST 389
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 743 ISNLKEHLASkevevAKLEKQLLEEKAAMTDAMVPRSSyEKLQSSLESevsvLASKLKESVKEKEKVHSEVVQIRSEVSQ 822
Cdd:COG5185   390 KESLDEIPQN-----QRGYAQEILATLEDTLKAADRQI-EELQRQIEQ----ATSSNEEVSKLLNELISELNKVMREADE 459
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 823 VKREK--ENIQTLLKSKEQEVNELLQKFQQAQEELAEMKryaESSSKLEEDKDKKINEMSKEVTKLKEALNSLSQLSYST 900
Cdd:COG5185   460 ESQSRleEAYDEINRSVRSKKEDLNEELTQIESRVSTLK---ATLEKLRAKLERQLEGVRSKLDQVAESLKDFMRARGYA 536

                  ....*....
gi 1370488827 901 SSSKRQSQQ 909
Cdd:COG5185   537 HILALENLI 545
PHA02791 PHA02791
ankyrin-like protein; Provisional
94-239 1.88e-03

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 41.18  E-value: 1.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  94 IRKLLQSKcPAESVDSSGKTALHYAAAQGCLQAVQILCEHKSPINLkdLDGNIPLLLAVQNGHSEICHFLLDHGADVNSR 173
Cdd:PHA02791   14 LKSFLSSK-DAFKADVHGHSALYYAIADNNVRLVCTLLNAGALKNL--LENEFPLHQAATLEDTKIVKILLFSGMDDSQF 90
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370488827 174 NKSGRTALMLACEIGSSNAVEALIKKGADLNLVDSLGY-NALHYSKLSENAGIQSLLLSKISQDADL 239
Cdd:PHA02791   91 DDKGNTALYYAVDSGNMQTVKLFVKKNWRLMFYGKTGWkTSFYHAVMLNDVSIVSYFLSEIPSTFDL 157
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
516-657 2.04e-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: 41.06  E-value: 2.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 516 ELRVTEEEINVLKQDLQNALEESERNKEKVRELEEKLVEREK--GTVIKPpvEEYEEMKSSycsvIENMNKEKAFLFEKY 593
Cdd:COG1579    39 ELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEqlGNVRNN--KEYEALQKE----IESLKRRISDLEDEI 112
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370488827 594 QEAQEEIMKLKDTLKsqmtqEASDEAEDMKEAMNRMIDELNKQVSELSQLYKEAQAELEDYRKR 657
Cdd:COG1579   113 LELMERIEELEEELA-----ELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAK 171
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
702-857 2.07e-03

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 41.80  E-value: 2.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 702 LNELTQLKQLVDAQKENSVSitEHLQVITTLRTAAKEMEEKISNLKEHLASKEVEVAKLEKQ----------LLEEKAAM 771
Cdd:pfam07888  43 RAELLQAQEAANRQREKEKE--RYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKykelsasseeLSEEKDAL 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 772 TDAmvpRSSYEKLQSSLESEVSVLASKLKESVKEKEKVHSEVVQIRSEVSQVKREKENIQTLLKSKEQEVNELLQKFQQA 851
Cdd:pfam07888 121 LAQ---RAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQEL 197

                  ....*.
gi 1370488827 852 QEELAE 857
Cdd:pfam07888 198 RNSLAQ 203
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
627-806 2.36e-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: 40.68  E-value: 2.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 627 NRMIDELNKQVSELSQLYKEAQAELEDYRKRksLEDVTAEyihKAEHEKLMQLTNVSRAKAEDALSEMKS--QYSKVLNE 704
Cdd:COG1579    23 EHRLKELPAELAELEDELAALEARLEAAKTE--LEDLEKE---IKRLELEIEEVEARIKKYEEQLGNVRNnkEYEALQKE 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 705 LTQLKQLvdaqkensvsitehlqvITTLRTAAKEMEEKISNLKEHLASKEVEVAKLEKQLLEEKAAMTDAMvprSSYEKL 784
Cdd:COG1579    98 IESLKRR-----------------ISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEEL---AELEAE 157
                         170       180
                  ....*....|....*....|..
gi 1370488827 785 QSSLESEVSVLASKLKESVKEK 806
Cdd:COG1579   158 LEELEAEREELAAKIPPELLAL 179
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
424-912 2.37e-03

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 41.88  E-value: 2.37e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  424 QQLQEILQDLQKRLESSEAERKQLQVELQsrraelvclnNTEISENSSDLSQKLKETQSKYEEAMKEVLSvqkqmklglv 503
Cdd:TIGR00618  208 LCTPCMPDTYHERKQVLEKELKHLREALQ----------QTQQSHAYLTQKREAQEEQLKKQQLLKQLRA---------- 267
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  504 spesmdnyshfhelrvTEEEINVLKQDLQNALEESERNKEKvreleEKLVEREKGtvikppVEEYEEMKSSYCSVIENMN 583
Cdd:TIGR00618  268 ----------------RIEELRAQEAVLEETQERINRARKA-----APLAAHIKA------VTQIEQQAQRIHTELQSKM 320
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  584 KEKAFLFEKYQEAQEEIMKLKDTLKS-QMTQEASDEAEDMKEAMNRMIDELNKQVSELSQLYKEAQAELEDYRKRKSL-- 660
Cdd:TIGR00618  321 RSRAKLLMKRAAHVKQQSSIEEQRRLlQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLck 400
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  661 -------EDVTAEYIHKAEHEKLMQLTnVSRAKAEDALSEMKSQYSKVLNELTQLKQLVDAQKENSVSITEHLQVITTLR 733
Cdd:TIGR00618  401 eldilqrEQATIDTRTSAFRDLQGQLA-HAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKE 479
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  734 TAAKEMEEKISNLKEHLASKEVEVAKLEKQLLEEKAAMTDAMVPRSSYEKLQsSLESEVSVLAsklkesvKEKEKVHSEV 813
Cdd:TIGR00618  480 QIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQ-RGEQTYAQLE-------TSEEDVYHQL 551
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  814 VQIRSEVSQVKREKENIQTLLKSKEQEVNELLQKFQQAQEELAEMKRYAESSSKLEedkDKKINEMSKEVTKLKEALNSL 893
Cdd:TIGR00618  552 TSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAE---DMLACEQHALLRKLQPEQDLQ 628
                          490
                   ....*....|....*....
gi 1370488827  894 SQLSYSTSSSKRQSQQLEA 912
Cdd:TIGR00618  629 DVRLHLQQCSQELALKLTA 647
PTZ00108 PTZ00108
DNA topoisomerase 2-like protein; Provisional
418-840 2.44e-03

DNA topoisomerase 2-like protein; Provisional


Pssm-ID: 240271 [Multi-domain]  Cd Length: 1388  Bit Score: 41.96  E-value: 2.44e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  418 DNDVRIQQ---LQEILQDL-QKRLESSEaERKQLQVELQSRRAELvcLNNT-----EISENSSDLSQKLKetqskyeeam 488
Cdd:PTZ00108   967 DENGKIKKysdALDILKEFyLVRLDLYK-KRKEYLLGKLERELAR--LSNKvrfikHVINGELVITNAKK---------- 1033
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  489 KEVLSVQKQMKLGLVSP-ESMDNYSHFHELRVTEEEINVLKQDLQNALEESERN-------------KEKVRELEEKLVE 554
Cdd:PTZ00108  1034 KDLVKELKKLGYVRFKDiIKKKSEKITAEEEEGAEEDDEADDEDDEEELGAAVSydyllsmpiwsltKEKVEKLNAELEK 1113
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  555 REKgtvikppveEYEEMKSsycSVIENMNKekaflfekyqeaqEEIMKLKDTLKSQMTQEASDEAEDMKEAMNRMIDELN 634
Cdd:PTZ00108  1114 KEK---------ELEKLKN---TTPKDMWL-------------EDLDKFEEALEEQEEVEEKEIAKEQRLKSKTKGKASK 1168
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  635 KQVSELSQLyKEAQAELEDYRKRKSLEDVTAEYIHKAEHEKLMQLTNVSRAKAEDalsemKSQYSKVLNELTQLKQLVDA 714
Cdd:PTZ00108  1169 LRKPKLKKK-EKKKKKSSADKSKKASVVGNSKRVDSDEKRKLDDKPDNKKSNSSG-----SDQEDDEEQKTKPKKSSVKR 1242
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  715 QKENSVSITEHLQVITTLRTAAKEMEEKISNLKEHLASKEVEVAKLEKQLLEEKAamTDAMVPRSSYEKLQSSLESEVSV 794
Cdd:PTZ00108  1243 LKSKKNNSSKSSEDNDEFSSDDLSKEGKPKNAPKRVSAVQYSPPPPSKRPDGESN--GGSKPSSPTKKKVKKRLEGSLAA 1320
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*.
gi 1370488827  795 LASKLKESVKEKEKVHSEVVQIRSEVSQVKREKENIQTLLKSKEQE 840
Cdd:PTZ00108  1321 LKKKKKSEKKTARKKKSKTRVKQASASQSSRLLRRPRKKKSDSSSE 1366
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
409-769 2.59e-03

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 41.36  E-value: 2.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 409 IHSLGKSTTDNDVRIQQLQEILQDLQKRL--------ESSEAERKQLQvELQSRRAELVCLNNT-----------EISEN 469
Cdd:PRK04778  128 LQELLESEEKNREEVEQLKDLYRELRKSLlanrfsfgPALDELEKQLE-NLEEEFSQFVELTESgdyveareildQLEEE 206
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 470 SSDLSQK-------LKETQSKYEEAMKEVLSVQKQMKlglvspesMDNYsHFHELRVtEEEINVLKQDLQNALE-----E 537
Cdd:PRK04778  207 LAALEQImeeipelLKELQTELPDQLQELKAGYRELV--------EEGY-HLDHLDI-EKEIQDLKEQIDENLAlleelD 276
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 538 SERNKEKVRELEEK------LVEREKGTviKPPVEEYEEMKSSYCSVIENMNK----EKAFLFEKYQEAQEEIMKLKdTL 607
Cdd:PRK04778  277 LDEAEEKNEEIQERidqlydILEREVKA--RKYVEKNSDTLPDFLEHAKEQNKelkeEIDRVKQSYTLNESELESVR-QL 353
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 608 KSQMtqeasdeaedmkEAMNRMIDELNKQVSELSQLYKEAQAELEDYRKRksLEDVTAEYIHKAEHekLMQLTNvSRAKA 687
Cdd:PRK04778  354 EKQL------------ESLEKQYDEITERIAEQEIAYSELQEELEEILKQ--LEEIEKEQEKLSEM--LQGLRK-DELEA 416
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 688 EDALSEMKsqyskvlNELTQLKQLVdaQKEN----SVSITEHLQVITT-LRTAAKEMEEKISNLKEhlASKEVEVAKLEK 762
Cdd:PRK04778  417 REKLERYR-------NKLHEIKRYL--EKSNlpglPEDYLEMFFEVSDeIEALAEELEEKPINMEA--VNRLLEEATEDV 485

                  ....*..
gi 1370488827 763 QLLEEKA 769
Cdd:PRK04778  486 ETLEEET 492
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
517-874 2.63e-03

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 41.42  E-value: 2.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 517 LRVTEEEINVLKQDLQNALEESERNKEKVRELEEKLVEREkgTVIKPPVEEYEEMKSSYCSVI---ENMNKEKAFLFEKY 593
Cdd:pfam07888  47 LQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELK--EELRQSREKHEELEEKYKELSassEELSEEKDALLAQR 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 594 QEAQEEIMKLKDTLK--SQMTQEASDEAEDMKEAMNRMIDELNKQVSELSQL-YKEAQAELEDYRKRKSLEdvtaeyihk 670
Cdd:pfam07888 125 AAHEARIRELEEDIKtlTQRVLERETELERMKERAKKAGAQRKEEEAERKQLqAKLQQTEEELRSLSKEFQ--------- 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 671 aeheklmqltnvsraKAEDALSEMKSQYSKVLNELTQLKQLVDAQKENSVSITEHLQVITTLRTAAKEMEEKISNLKEHL 750
Cdd:pfam07888 196 ---------------ELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEEL 260
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 751 AS--------------KEVEVAKLEKQLLEEKAAMTDAmvpRSSY----EKLQSSLESEVSVLASKLKESVKEKEKVHSE 812
Cdd:pfam07888 261 SSmaaqrdrtqaelhqARLQAAQLTLQLADASLALREG---RARWaqerETLQQSAEADKDRIEKLSAELQRLEERLQEE 337
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370488827 813 VVQIRSEVSQVKREKENIQTLLKSKEQEVNEL---LQKFQQAQEEL-AEMKRYAESSSKLEEDKDK 874
Cdd:pfam07888 338 RMEREKLEVELGREKDCNRVQLSESRRELQELkasLRVAQKEKEQLqAEKQELLEYIRQLEQRLET 403
Mitofilin pfam09731
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ...
529-807 2.70e-03

Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.


Pssm-ID: 430783 [Multi-domain]  Cd Length: 618  Bit Score: 41.67  E-value: 2.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 529 QDLQNALEESERNKEKVRELEEKLVEREKGTVIKPPVEEYEEMKSSYCSVIENMNKEKAFLFEKYQEAQEEIMKLKDTLK 608
Cdd:pfam09731 124 QEKEKALEEVLKEAISKAESATAVAKEAKDDAIQAVKAHTDSLKEASDTAEISREKATDSALQKAEALAEKLKEVINLAK 203
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 609 SQMTQEASDEAEDMKEAMNRMIDELNKQVSELSQLYKEAqAELEDYRKRKSLEDVtaeyIHKAEHEKLMqlTNVSRAKAE 688
Cdd:pfam09731 204 QSEEEAAPPLLDAAPETPPKLPEHLDNVEEKVEKAQSLA-KLVDQYKELVASERI----VFQQELVSIF--PDIIPVLKE 276
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 689 DALSEMKSQYSKVLNELTQLKQLVDAQKENSVSITEHLQVIttLRTAAKEMEEKISNLKEHLaskEVEVAKLEKQLLEEK 768
Cdd:pfam09731 277 DNLLSNDDLNSLIAHAHREIDQLSKKLAELKKREEKHIERA--LEKQKEELDKLAEELSARL---EEVRAADEAQLRLEF 351
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1370488827 769 AAMTDAMvpRSSYE-KLQSSLESEVSVLASKLKESVKEKE 807
Cdd:pfam09731 352 EREREEI--RESYEeKLRTELERQAEAHEEHLKDVLVEQE 389
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
566-887 2.88e-03

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 41.36  E-value: 2.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 566 EEYEEMKSSYCSVIENmnkekafLFEKYQEAQEEIMKLKDTLKSQMTQEASDEAEDMKEAMNRMIDELNKQVSELSQLYK 645
Cdd:PRK04778   64 EKFEEWRQKWDEIVTN-------SLPDIEEQLFEAEELNDKFRFRKAKHEINEIESLLDLIEEDIEQILEELQELLESEE 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 646 EAQAE----LEDYRK-RKSLED------VTAEYIHK------AEHEKLMQLTN----------VSRAKAE-DALSEMKSQ 697
Cdd:PRK04778  137 KNREEveqlKDLYRElRKSLLAnrfsfgPALDELEKqlenleEEFSQFVELTEsgdyveareiLDQLEEElAALEQIMEE 216
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 698 YSKVLNELT-----QLKQLVDAQKENSVS--ITEHLQVITTLrtaaKEMEEKISNLKEHLASKEVEVAKLEKQLLEEK-- 768
Cdd:PRK04778  217 IPELLKELQtelpdQLQELKAGYRELVEEgyHLDHLDIEKEI----QDLKEQIDENLALLEELDLDEAEEKNEEIQERid 292
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 769 ---AAMTDAMVPRSSYEKLQSSLESEVSVLASKLKESVKEKEKV-------HSEVVQIRS---EVSQVKREKENIQTLLK 835
Cdd:PRK04778  293 qlyDILEREVKARKYVEKNSDTLPDFLEHAKEQNKELKEEIDRVkqsytlnESELESVRQlekQLESLEKQYDEITERIA 372
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1370488827 836 SKEQEVNELLQKFQQAQEELAEMK----RYAESSSKLEEDKDK---KINEMSKEVTKLK 887
Cdd:PRK04778  373 EQEIAYSELQEELEEILKQLEEIEkeqeKLSEMLQGLRKDELEareKLERYRNKLHEIK 431
46 PHA02562
endonuclease subunit; Provisional
706-885 3.05e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 41.15  E-value: 3.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 706 TQLKQLVDAQKENSVSITEHLQVITTLRTAAKEMEEKISNLKEHLASKEVEVAKLEKQLLEEKAAMTDA----------- 774
Cdd:PHA02562  199 TYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIkskieqfqkvi 278
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 775 ------------MVPRSSYEKLQSSLESEVSVLA---SKLKESVKEKEKVHSEVVQIRSEVSQVKREKENIQTLLKSKEQ 839
Cdd:PHA02562  279 kmyekggvcptcTQQISEGPDRITKIKDKLKELQhslEKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVD 358
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1370488827 840 EVNELLQKFQQAQeelAEMKRYAESSSKLEEDKDKKINEMSKEVTK 885
Cdd:PHA02562  359 KAKKVKAAIEELQ---AEFVDNAEELAKLQDELDKIVKTKSELVKE 401
PRK01156 PRK01156
chromosome segregation protein; Provisional
517-887 3.06e-03

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 41.43  E-value: 3.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 517 LRVTEEEINVLKQDLQNALEESERNKEKVRELEEKLVEREKGtvIKPPVEEYEEMKSSYCSVIENMNKEKAFLFEKyQEA 596
Cdd:PRK01156  178 LRAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKE--IERLSIEYNNAMDDYNNLKSALNELSSLEDMK-NRY 254
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 597 QEEIMKLKDTLksQMTQEASDEAEDMKEAMNRMIDE--------------LNKQVSELSQLYKEAQAELEDYRK-RKSLE 661
Cdd:PRK01156  255 ESEIKTAESDL--SMELEKNNYYKELEERHMKIINDpvyknrnyindyfkYKNDIENKKQILSNIDAEINKYHAiIKKLS 332
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 662 DVTAEYIHKAEHEKLMQLTNvsraKAEDALSEMKSQYSKVLNELTQLKQLVDAQKENS------VSITEHLQVIT--TLR 733
Cdd:PRK01156  333 VLQKDYNDYIKKKSRYDDLN----NQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIermsafISEILKIQEIDpdAIK 408
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 734 TAAKEMEEKISNLKEHLASKEVEVAKLEKQL--LEEKAAMTDAmvpRSSYEKLQSSLESEVSvlASKLKESVKEKEKVHS 811
Cdd:PRK01156  409 KELNEINVKLQDISSKVSSLNQRIRALRENLdeLSRNMEMLNG---QSVCPVCGTTLGEEKS--NHIINHYNEKKSRLEE 483
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370488827 812 EVVQIRSEVSQVKREKENIQTLLKSKE-QEVNELLQKFQQAQEELAEMKRYAESSSKLeEDKDKKINEMSKEVTKLK 887
Cdd:PRK01156  484 KIREIEIEVKDIDEKIVDLKKRKEYLEsEEINKSINEYNKIESARADLEDIKIKINEL-KDKHDKYEEIKNRYKSLK 559
PHA02946 PHA02946
ankyin-like protein; Provisional
94-242 3.21e-03

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 41.19  E-value: 3.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  94 IRKLLQSKCPAESVDSSGKTALHYAAAQGCLQAVQILCEHKSPINLKDLDGNIPL--LLAVQNGHSEICHFLLDHGADVN 171
Cdd:PHA02946   55 VEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLyyLSGTDDEVIERINLLVQYGAKIN 134
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370488827 172 SRNKSGRTALMLACEIGSSNAVEALIKKGADLNLVDSLGYNALHYSKLSEN------AGIQSLLLSKISQDADLKTP 242
Cdd:PHA02946  135 NSVDEEGCGPLLACTDPSERVFKKIMSIGFEARIVDKFGKNHIHRHLMSDNpkastiSWMMKLGISPSKPDHDGNTP 211
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
599-824 3.38e-03

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 41.48  E-value: 3.38e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  599 EIMKLKDTLKSQMTQEASDEAEDMKEAMN------RMIDELNKQVS----------ELSQLYKEAQAELEDYRKRK-SLE 661
Cdd:COG3096    882 QANLLADETLADRLEELREELDAAQEAQAfiqqhgKALAQLEPLVAvlqsdpeqfeQLQADYLQAKEQQRRLKQQIfALS 961
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  662 DVTAEYIHKAEHEKLMQLTNVS----------------RAKAEDALSEMKSQYSKVLNELTQLKQLVDAQKEnsvsiteh 725
Cdd:COG3096    962 EVVQRRPHFSYEDAVGLLGENSdlneklrarleqaeeaRREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQ-------- 1033
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  726 lqvitTLRTAAKEMEEkisnLKEHLASKEVEVAKLEKQLLEEKAAMTDAMvpRSSYEKLQSSLESEVSVLASKLKesvKE 805
Cdd:COG3096   1034 -----TLQELEQELEE----LGVQADAEAEERARIRRDELHEELSQNRSR--RSQLEKQLTRCEAEMDSLQKRLR---KA 1099
                          250
                   ....*....|....*....
gi 1370488827  806 KEKVHsevvQIRSEVSQVK 824
Cdd:COG3096   1100 ERDYK----QEREQVVQAK 1114
MPS2 pfam17060
Monopolar spindle protein 2; Is a fungal transmembrane protein which is part of the component ...
542-754 3.57e-03

Monopolar spindle protein 2; Is a fungal transmembrane protein which is part of the component of the spindle pole body (SPB) required for the insertion of the nascent SPB into the nuclear envelope and for the proper execution of spindle pole body (SPB) duplication. It seems that Mps2-Spc24 interaction may contribute to the localization of Spc24 and other kinetochore components to the inner plaque of the SPB.


Pssm-ID: 407228 [Multi-domain]  Cd Length: 340  Bit Score: 40.73  E-value: 3.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 542 KEKVRELEEKLVEREKGTVIKPPVEEYEEMKSSYCSVIEnmnkekaflfekyqeaqeeimkLKDTLKSQMTQEASDEAED 621
Cdd:pfam17060  67 KESFSEMFNGLVGNNFKTVINKIFEDCDGIPASFISALE----------------------LKEDVKSSPRSEADSLGTP 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 622 MKEAMNRMI--DELNKQVSELSQLYKEAQAELEDYRKRKSLEDvtaEYIHKAEHEkLMQLTNvsrakaedALSEMKSQYS 699
Cdd:pfam17060 125 IKVDLLRNLkpQESPETPRRINRKYKSLELRVESMKDELEFKD---ETIMEKDRE-LTELTS--------TISKLKDKYD 192
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1370488827 700 KVLNELTQLKQLVDAQKENSV-SITEHLQVITTLRTAAKEMEEKISNLKEHLASKE 754
Cdd:pfam17060 193 FLSREFEFYKQHHEHGGNNSIkTATKHEFIISELKRKLQEQNRLIRILQEQIQFDP 248
Macoilin pfam09726
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 ...
632-866 3.80e-03

Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 trasnmembrane helices, followed by a C-terminal coiled-coil region. Macoilin is a highly conserved protein present in eukaryotes. Macoilin appears to be found in the ER and be involved in the function of neurons.


Pssm-ID: 462859 [Multi-domain]  Cd Length: 670  Bit Score: 40.99  E-value: 3.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 632 ELNKQVSELSQLYKEAQAELEDYRKRKsleDVTAEYIHKAEHEKLMQLTNVS----RAKAEdalSEMKSQYSKVLNELTQ 707
Cdd:pfam09726 420 ELRSQISSLTSLERSLKSELGQLRQEN---DLLQTKLHNAVSAKQKDKQTVQqlekRLKAE---QEARASAEKQLAEEKK 493
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 708 LKQLVDAQKENSVS--ITEHLQVITTLRTAAKEMEEKISNLKEHLASKEVEVAKLEKQLLEekaamtdamvpRSSYEKLQ 785
Cdd:pfam09726 494 RKKEEEATAARAVAlaAASRGECTESLKQRKRELESEIKKLTHDIKLKEEQIRELEIKVQE-----------LRKYKESE 562
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 786 SSLESEVSVLaSKLKESVKEKEKVHSEVVQIR----SEVSQVKREKENIQTLLKSKEQEVNELLQKFQQAQEELAEMKRY 861
Cdd:pfam09726 563 KDTEVLMSAL-SAMQDKNQHLENSLSAETRIKldlfSALGDAKRQLEIAQGQIYQKDQEIKDLKQKIAEVMAVMPSTSRI 641

                  ....*
gi 1370488827 862 AESSS 866
Cdd:pfam09726 642 TPVTP 646
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
685-915 3.91e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 40.52  E-value: 3.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 685 AKAEDALSEMKSQYSKVLNELTQLKQLVDAQKENSVSITEHLQV----ITTLRTAAKEMEEKISNLKEHLASKEVEVAKL 760
Cdd:COG4942    16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAAlerrIAALARRIRALEQELAALEAELAELEKEIAEL 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 761 EKQLLEEKAAMTDAMvpRSSYeklQSSLESEVSVL--ASKLKESVKEKEKVHSEVVQIRSEVSQVKREKENIQTLLKSKE 838
Cdd:COG4942    96 RAELEAQKEELAELL--RALY---RLGRQPPLALLlsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELE 170
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370488827 839 QEVNELLQKFQQAQEELAEMkryaessSKLEEDKDKKINEMSKEvtklkealnslsqlsystssSKRQSQQLEALQQ 915
Cdd:COG4942   171 AERAELEALLAELEEERAAL-------EALKAERQKLLARLEKE--------------------LAELAAELAELQQ 220
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
409-676 5.09e-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: 40.77  E-value: 5.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 409 IHSLGKSTTDNDVRIQQLQEILQDLQKRLESSEAERKQLQVELQSRRAELVcLNNTEISEnssdlsqkLKETQSKYEEAM 488
Cdd:TIGR04523 386 IKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETII-KNNSEIKD--------LTNQDSVKELII 456
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 489 KEVLSVQKQMKlglvspesmdnyshfHELRVTEEEINVLKQDLQNALEESERNKEKVRELEEKLVEREKgtvikpPVEEY 568
Cdd:TIGR04523 457 KNLDNTRESLE---------------TQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEE------KVKDL 515
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 569 EEMKSSYCSVIENMNKEKAFLFEKYQEAQEEIMKLKDTLKSQMTQEASDEAEDMKEAMNRMIDELNKQVSELSQLYKEAQ 648
Cdd:TIGR04523 516 TKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKE 595
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1370488827 649 AELEDYRKRKSLEDVTAEYIH------KAEHEKL 676
Cdd:TIGR04523 596 KEKKDLIKEIEEKEKKISSLEkelekaKKENEKL 629
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
50-112 5.30e-03

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 40.65  E-value: 5.30e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370488827  50 HLAAAKGHVECLRVMITHGVDVTAQDTTGHSALHLAAKNSHHECIRKLLQSKCPAESVDSSGK 112
Cdd:PTZ00322  120 HIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFELGANAK 182
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
506-757 5.39e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.67  E-value: 5.39e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  506 ESMDNYSHFHE-LRVTEEEINVLKQ--DLQNALEESERNKEKVRELEEKLverekgtvikpPVEEYEEMKSSYCSVIENM 582
Cdd:COG4913    232 EHFDDLERAHEaLEDAREQIELLEPirELAERYAAARERLAELEYLRAAL-----------RLWFAQRRLELLEAELEEL 300
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  583 NKEKAFLFEKYQEAQEEIMKLK---DTLKSQMTQEASDEAEDMKEAMNRMIDELNKQVSELSQLYKEAQA-ELEDYRKRK 658
Cdd:COG4913    301 RAELARLEAELERLEARLDALReelDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAAlGLPLPASAE 380
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  659 SLEDVTAEYI-HKAEHEKLMQLTNVSRAKAEDALSEMKSQYSKVLNELTQLKQlvdaqkeNSVSITEHLQvitTLRTAak 737
Cdd:COG4913    381 EFAALRAEAAaLLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLER-------RKSNIPARLL---ALRDA-- 448
                          250       260
                   ....*....|....*....|
gi 1370488827  738 emeekisnLKEHLASKEVEV 757
Cdd:COG4913    449 --------LAEALGLDEAEL 460
PTZ00440 PTZ00440
reticulocyte binding protein 2-like protein; Provisional
418-890 5.92e-03

reticulocyte binding protein 2-like protein; Provisional


Pssm-ID: 240419 [Multi-domain]  Cd Length: 2722  Bit Score: 40.59  E-value: 5.92e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  418 DNDVRIQQLQEILQDLQKRLESSEAERKQLQVELQSRRAELvclNNTEISENSSDLSQKLKETQSKYEEA-----MKEVL 492
Cdd:PTZ00440   592 EIDNIIQQIEELINEALFNKEKFINEKNDLQEKVKYILNKF---YKGDLQELLDELSHFLDDHKYLYHEAkskedLQTLL 668
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  493 --SVQKQMKLGLVSPESMDN--------YSHFHELR--VTEEEINVLKQDLQNALEESernkekvreleeklveREKGTV 560
Cdd:PTZ00440   669 ntSKNEYEKLEFMKSDNIDNiiknlkkeLQNLLSLKenIIKKQLNNIEQDISNSLNQY----------------TIKYND 732
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  561 IKPPVEEYEEMKSSYCSVIENMNKEKAFLFEKYQEAQEEIMKLKDTlksqmtqeaSDEAEDMKEAMNRMIDELNKQVSEL 640
Cdd:PTZ00440   733 LKSSIEEYKEEEEKLEVYKHQIINRKNEFILHLYENDKDLPDGKNT---------YEEFLQYKDTILNKENKISNDINIL 803
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  641 SQLYKEAQAELEDYR-KRKSLEDVTAEyiHKAEHEKLMQ-----LTNVSRAKAEDALSEMKSQYSKVLNELTQLKQLVDA 714
Cdd:PTZ00440   804 KENKKNNQDLLNSYNiLIQKLEAHTEK--NDEELKQLLQkfpteDENLNLKELEKEFNENNQIVDNIIKDIENMNKNINI 881
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  715 QKENSVSITE---HLQVITTLRTAAKEMEEKISNLKEHLASKEV----EVAKLEKQLLEEKAAM-------------TDA 774
Cdd:PTZ00440   882 IKTLNIAINRsnsNKQLVEHLLNNKIDLKNKLEQHMKIINTDNIiqknEKLNLLNNLNKEKEKIekqlsdtkinnlkMQI 961
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  775 MVPRSSYEKLQSSLESEVSVLASKLKESVKEKEKVHSEVVQIRSEV--------SQVKREKENIQTL----LKSKEQEVN 842
Cdd:PTZ00440   962 EKTLEYYDKSKENINGNDGTHLEKLDKEKDEWEHFKSEIDKLNVNYnilnkkidDLIKKQHDDIIELidklIKEKGKEIE 1041
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*...
gi 1370488827  843 ELLQKFQQAQEELAEMKRYAESSSKLEEDKDKKINEMSKEVTKLKEAL 890
Cdd:PTZ00440  1042 EKVDQYISLLEKMKTKLSSFHFNIDIKKYKNPKIKEEIKLLEEKVEAL 1089
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
124-242 6.19e-03

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 39.94  E-value: 6.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 124 LQAVQILCEHKSPINLKDLDGNIPLLLAVQNGHSEICHFLLDHGADVNSRNKSGRTALMLACEIGSSNAVEALIKKGADL 203
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1370488827 204 NLVDSLGYNALHYSKLSENAGIQSLLLSK----ISQDADLKTP 242
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAgadvNARDKDGETP 123
COG5022 COG5022
Myosin heavy chain [General function prediction only];
756-910 6.40e-03

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 40.45  E-value: 6.40e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  756 EVAKLEKQLLEEKAAmtdamVPRSSYEKLQSS-LESEVSVLASKLKESVKEKEKVHSEvvqirsEVSQVKREKENIQT-L 833
Cdd:COG5022    876 RVELAERQLQELKID-----VKSISSLKLVNLeLESEIIELKKSLSSDLIENLEFKTE------LIARLKKLLNNIDLeE 944
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  834 LKSKEQEVNELLQKFQQA----QEELAEMKRYAESSSKLEEDKDKKINEMSKEVTKLKEALNSLSQLSYSTSSSKRQSQQ 909
Cdd:COG5022    945 GPSIEYVKLPELNKLHEVesklKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQYGALQESTKQLKELPVE 1024

                   .
gi 1370488827  910 L 910
Cdd:COG5022   1025 V 1025
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
424-870 6.88e-03

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: 40.42  E-value: 6.88e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  424 QQLQEILQDLQKRLESSEAERKQLQVELQSRRAELVCLNN--TEISENSSDLSQKLKETQSKYEEAMKEVLSVQKQMKLG 501
Cdd:TIGR00606  301 EQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQekTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELD 380
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  502 LVS--PESMDNYSHFHELRVTEEE-----INVLKQDLQNALEESERNKEKVRELEEKLVE--REKGTVIKPPVEEYEEMK 572
Cdd:TIGR00606  381 GFErgPFSERQIKNFHTLVIERQEdeaktAAQLCADLQSKERLKQEQADEIRDEKKGLGRtiELKKEILEKKQEELKFVI 460
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  573 SSycsvIENMNKEKAFLFEKYQEAQEEIMKLKDTLKSQMTQEASDEAEDMKEAMNRMIDELNKQVSELSQL--YKEAQAE 650
Cdd:TIGR00606  461 KE----LQQLEGSSDRILELDQELRKAERELSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLnhHTTTRTQ 536
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  651 LEDYRKRKSLEDvtaEYIHKAEHEKLMQLTNVS-----RAKAEDALSEMKSQYSKVLNELTQLKQLVDAQKENSVSITEH 725
Cdd:TIGR00606  537 MEMLTKDKMDKD---EQIRKIKSRHSDELTSLLgyfpnKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNE 613
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  726 LQVITTLRTAAKE----------MEEKISNLKEhlaskEVEVAKLEKQLLEEKAAMTDAMVPRSSYE------------K 783
Cdd:TIGR00606  614 LESKEEQLSSYEDklfdvcgsqdEESDLERLKE-----EIEKSSKQRAMLAGATAVYSQFITQLTDEnqsccpvcqrvfQ 688
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  784 LQSSLESEVSVLASKLKESVKEKEKVHSEVVQIRSEVSQVKREKENIQTLLKSKEQEVNELLQKFQQAQEELAEMKRYAE 863
Cdd:TIGR00606  689 TEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIE 768

                   ....*..
gi 1370488827  864 SSSKLEE 870
Cdd:TIGR00606  769 EQETLLG 775
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
468-876 7.04e-03

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: 40.48  E-value: 7.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 468 ENSSDLSQKLKETQSKyeeAMKEVLSVQKQMKLGLvSPESMDNYSHFHELRVTEEEINVLKQDLQNALEESERNKEKVRE 547
Cdd:pfam05483 105 ENKLQENRKIIEAQRK---AIQELQFENEKVSLKL-EEEIQENKDLIKENNATRHLCNLLKETCARSAEKTKKYEYEREE 180
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 548 LEEKLVEREKGtvIKPPVEEYEEMKSSYCSVIENMNKEKAFLFEKYQEAQEEIMKLKDTLKSQMT------QEASDEAED 621
Cdd:pfam05483 181 TRQVYMDLNNN--IEKMILAFEELRVQAENARLEMHFKLKEDHEKIQHLEEEYKKEINDKEKQVSllliqiTEKENKMKD 258
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 622 MKEAMNRMIDELNkQVSELSQLYKEAQAELEDYRKR--KSLEDVTAEyihkaehekLMQLTNVSRAKAEDALSEMKSQYS 699
Cdd:pfam05483 259 LTFLLEESRDKAN-QLEEKTKLQDENLKELIEKKDHltKELEDIKMS---------LQRSMSTQKALEEDLQIATKTICQ 328
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 700 KVLNELTQLKQLVDAQKENSVSITEHLQVITTLRTAAKEMEEKISNLKEHLASKEVEVAKLEKQLLEekaaMTdamvprs 779
Cdd:pfam05483 329 LTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEE----MT------- 397
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 780 syeKLQSSLESEVsvlaSKLKESVKEKEKVHSEVVQIRSEVSQVKREKENIQTLLKSKEQEVNEL-LQKFQQAQEELAEM 858
Cdd:pfam05483 398 ---KFKNNKEVEL----EELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLeIQLTAIKTSEEHYL 470
                         410
                  ....*....|....*...
gi 1370488827 859 KRYAESSSKLEEDKDKKI 876
Cdd:pfam05483 471 KEVEDLKTELEKEKLKNI 488
RecN COG0497
DNA repair ATPase RecN [Replication, recombination and repair];
512-774 7.67e-03

DNA repair ATPase RecN [Replication, recombination and repair];


Pssm-ID: 440263 [Multi-domain]  Cd Length: 555  Bit Score: 40.06  E-value: 7.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 512 SHFHELRVTEEEINVLKQDLQNALEESERNKEKVRELEEklverekgtvIKPPVEEYEEMKSSYcSVIENMNKekafLFE 591
Cdd:COG0497   162 EAYRAWRALKKELEELRADEAERARELDLLRFQLEELEA----------AALQPGEEEELEEER-RRLSNAEK----LRE 226
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 592 KYQEAQEEImklkdtlksqmtQEASDEAEDM-KEAMNRM--IDELNKQVSELSQLYKEAQAELEDyrkrksLEDVTAEYI 668
Cdd:COG0497   227 ALQEALEAL------------SGGEGGALDLlGQALRALerLAEYDPSLAELAERLESALIELEE------AASELRRYL 288
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 669 HKAEHEklmqltnvsrakaEDALSEMKSQyskvLNELTQLKqlvdaQKENsVSITEhlqVITTLRTAAKEMEEkISNLKE 748
Cdd:COG0497   289 DSLEFD-------------PERLEEVEER----LALLRRLA-----RKYG-VTVEE---LLAYAEELRAELAE-LENSDE 341
                         250       260
                  ....*....|....*....|....*.
gi 1370488827 749 HLASKEVEVAKLEKQLLEEKAAMTDA 774
Cdd:COG0497   342 RLEELEAELAEAEAELLEAAEKLSAA 367
46 PHA02562
endonuclease subunit; Provisional
420-646 7.76e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 40.00  E-value: 7.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 420 DVRIQQLQEILQDLQKRLESSEAERKQLQVELQSRRAELVCL---NNTEISENSSDLSqKLKETQSKYEEAMKEVLSVQK 496
Cdd:PHA02562  187 DMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEaktIKAEIEELTDELL-NLVMDIEDPSAALNKLNTAAA 265
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 497 QMKlglvspESMDNYSHFHELRVTEEEINVLKQDLQNALEESERNKEKVRELEEKLverekgTVIKPPVEEYEEMKSSYC 576
Cdd:PHA02562  266 KIK------SKIEQFQKVIKMYEKGGVCPTCTQQISEGPDRITKIKDKLKELQHSL------EKLDTAIDELEEIMDEFN 333
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 577 SVIENMNKEKAFLFEKYQEAQEEIMKLKDtLKSQMtQEASDEAEDMKEAMNRMIDELNKQVSELSQLYKE 646
Cdd:PHA02562  334 EQSKKLLELKNKISTNKQSLITLVDKAKK-VKAAI-EELQAEFVDNAEELAKLQDELDKIVKTKSELVKE 401
PLN03229 PLN03229
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
581-874 8.98e-03

acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional


Pssm-ID: 178768 [Multi-domain]  Cd Length: 762  Bit Score: 39.84  E-value: 8.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 581 NMNKEKAfLFEKYQEAQEEIMKLKDtlksQMTQEASDEAEDMKEAMNRMIDELNKqvsELSQLYKEA------QAELEDY 654
Cdd:PLN03229  420 NMKKREA-VKTPVRELEGEVEKLKE----QILKAKESSSKPSELALNEMIEKLKK---EIDLEYTEAviamglQERLENL 491
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 655 RKRKS--------LEDVTAEYIHKAEHE----------------KLMQLTNVSRAKaedALSEMKSQYSKVLNELTQ-LK 709
Cdd:PLN03229  492 REEFSkansqdqlMHPVLMEKIEKLKDEfnkrlsrapnylslkyKLDMLNEFSRAK---ALSEKKSKAEKLKAEINKkFK 568
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 710 QLVDA----QKENSVSITEHLQVITTLRTAAKEMEEKISNLKEHLaskEVEVAKLEKQLLEEKAAMTDAMVPRSSY---E 782
Cdd:PLN03229  569 EVMDRpeikEKMEALKAEVASSGASSGDELDDDLKEKVEKMKKEI---ELELAGVLKSMGLEVIGVTKKNKDTAEQtppP 645
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 783 KLQSSLESEVSVLASKLKESVKEKEkVHSEVVQIRSEVSQVKR-----EKENIQTLLKSKEQEV------NELLQKFQQA 851
Cdd:PLN03229  646 NLQEKIESLNEEINKKIERVIRSSD-LKSKIELLKLEVAKASKtpdvtEKEKIEALEQQIKQKIaealnsSELKEKFEEL 724
                         330       340
                  ....*....|....*....|....
gi 1370488827 852 QEELAEMKR-YAESSSKLEEDKDK 874
Cdd:PLN03229  725 EAELAAAREtAAESNGSLKNDDDK 748
HAMP COG2770
HAMP domain [Signal transduction mechanisms];
607-857 8.99e-03

HAMP domain [Signal transduction mechanisms];


Pssm-ID: 442051 [Multi-domain]  Cd Length: 631  Bit Score: 39.71  E-value: 8.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 607 LKSQMTQEASDEAEDMKEAMNRMIDELNKQVSELSQLYKEAQAELEDYRKRKSLEDVTAEYIHKAEHEKLMQLTNVSRAK 686
Cdd:COG2770   255 LDVRIPVSRKDEIGELARAFNRMADSLRESIEEAEEEEELAEAELARLLEALLELLLALLLLLLALLLLAAAALLLELLL 334
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 687 AEDALSEMKSQYSKVLNELTQLKQLVDAQKENSVSITEHLQVITTLRTAAKEMEEKISNLKEHLASKEVEVAKLEKQLLE 766
Cdd:COG2770   335 LLLLALLLLLLLAADLLLALALAALLLLLALELLLEAELLVLLALEALALEAELAAVLALLAALAAALLLLELALEELVL 414
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 767 EKAAMTDAMVPRSSYEKLQSSLESEVSVLASKLKESVKEKEKVHSEVVQIRSEVSQVKREKENIQTLLKSKEQEVNELLQ 846
Cdd:COG2770   415 ALLALALLALAAAAAAAEAAAAALELAAAAIAAAAAAEAEGGLAELEAEELVAAAEALLLLAALLLLAALGALELLLLEE 494
                         250
                  ....*....|.
gi 1370488827 847 KFQQAQEELAE 857
Cdd:COG2770   495 EEEAGAAAEEL 505
mukB PRK04863
chromosome partition protein MukB;
623-891 9.14e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 39.94  E-value: 9.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  623 KEAMNRMIDELNKQVSELSQLYKEAQAELEDY-RKRKSLEDVTAEYIHKA---EHEKLMQLTNVSRAKAEDALSEMKSQY 698
Cdd:PRK04863   781 RAAREKRIEQLRAEREELAERYATLSFDVQKLqRLHQAFSRFIGSHLAVAfeaDPEAELRQLNRRRVELERALADHESQE 860
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  699 SKVLNELTQLKQLVDA--QKENSVSI--TEHLQ-VITTLRTAAKEMEEKISNLKEH-------------LASKEVEVAKL 760
Cdd:PRK04863   861 QQQRSQLEQAKEGLSAlnRLLPRLNLlaDETLAdRVEEIREQLDEAEEAKRFVQQHgnalaqlepivsvLQSDPEQFEQL 940
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827  761 EKQLLEEKA----------AMTDAMVPRS--SYEKLQSSLESEvSVLASKLKESVKEKEKVHSEV-VQIRSEVSQVkREK 827
Cdd:PRK04863   941 KQDYQQAQQtqrdakqqafALTEVVQRRAhfSYEDAAEMLAKN-SDLNEKLRQRLEQAEQERTRArEQLRQAQAQL-AQY 1018
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370488827  828 ENIQTLLKS----KEQEVNELLQKFQ----QAQEELAEmkRYAESSSKLEE---DKDKKINEMSKEVTKLKEALN 891
Cdd:PRK04863  1019 NQVLASLKSsydaKRQMLQELKQELQdlgvPADSGAEE--RARARRDELHArlsANRSRRNQLEKQLTFCEAEMD 1091
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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