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Conserved domains on  [gi|2462602002|ref|XP_054208313|]
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ankycorbin isoform X8 [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];
59-259 5.28e-46

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 167.05  E-value: 5.28e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  59 FHLAAAKGHVECLRVMITHGVDVTAQDTTGHSALHLAAKNSHHECIRKLLQSKCPAESVDSSGKTALHYAAAQGCLQAVQ 138
Cdd:COG0666    58 LLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVK 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 139 ILCEHKSPINLKDLDGNIPLLLAVQNGHSEICHFLLDHGADVNSRNKSGRTALMLACEIGSSNAVEALIKKGADLNLVDS 218
Cdd:COG0666   138 LLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDN 217

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2462602002 219 LGYNALHYSKLSENAGIQSLLLSKISQDADLKTPTKPKQHD 259
Cdd:COG0666   218 DGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLL 258
PRK03918 super family cl35229
DNA double-strand break repair ATPase Rad50;
432-948 2.52e-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: 83.96  E-value: 2.52e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 432 RIQQLQEILQDLQKRLESSEAERKQLQVELQSRRAELvclnnteisENSSDLSQKLKETQSKYEEAMKEVLSVQKQMKlg 511
Cdd:PRK03918  187 RTENIEELIKEKEKELEEVLREINEISSELPELREEL---------EKLEKEVKELEELKEEIEELEKELESLEGSKR-- 255

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 512 lvspesmdnyshfhelrvteeeinVLKQDLQNALEESERNKEKVRELEEKLVEREKgtvIKPPVEEYEEMK---SSYCSV 588
Cdd:PRK03918  256 ------------------------KLEEKIRELEERIEELKKEIEELEEKVKELKE---LKEKAEEYIKLSefyEEYLDE 308

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 589 IENMNKEKAFLFEKYQEAQEEIMKLKDtlKSQMTQEASDEAEDMKEAMNRMidelnKQVSELSQLYKEAQAELEDYRKRK 668
Cdd:PRK03918  309 LREIEKRLSRLEEEINGIEERIKELEE--KEERLEELKKKLKELEKRLEEL-----EERHELYEEAKAKKEELERLKKRL 381

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 669 sledvTAEYIHKAEHEklmqLTNVSRAKAE--DALSEMKSQYSKVLNELTQLKQLVDAQKENSVS-------ITEH--LQ 737
Cdd:PRK03918  382 -----TGLTPEKLEKE----LEELEKAKEEieEEISKITARIGELKKEIKELKKAIEELKKAKGKcpvcgreLTEEhrKE 452

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 738 VITTLRTAAKEMEEKISNLKEHLASKEVEVAKLEKQLLEEKAAMTDamvpRSSYEKLQSSLESEVSVLASKLKESVKEKE 817
Cdd:PRK03918  453 LLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKL----KELAEQLKELEEKLKKYNLEELEKKAEEYE 528

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 818 KVHSEVVQIRSEVSQVKREKENIQTLLKSKEqevnELLQKFQQAQEELAEM-KRYAESSSKLEEDKDKKINEMSKEVTKL 896
Cdd:PRK03918  529 KLKEKLIKLKGEIKSLKKELEKLEELKKKLA----ELEKKLDELEEELAELlKELEELGFESVEELEERLKELEPFYNEY 604

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2462602002 897 KEALNSLSQLSYSTSSSKRQSQQLEALQQQVKQLQNQLAECKKQHQEVISVY 948
Cdd:PRK03918  605 LELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKY 656
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
59-259 5.28e-46

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 167.05  E-value: 5.28e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  59 FHLAAAKGHVECLRVMITHGVDVTAQDTTGHSALHLAAKNSHHECIRKLLQSKCPAESVDSSGKTALHYAAAQGCLQAVQ 138
Cdd:COG0666    58 LLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVK 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 139 ILCEHKSPINLKDLDGNIPLLLAVQNGHSEICHFLLDHGADVNSRNKSGRTALMLACEIGSSNAVEALIKKGADLNLVDS 218
Cdd:COG0666   138 LLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDN 217

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2462602002 219 LGYNALHYSKLSENAGIQSLLLSKISQDADLKTPTKPKQHD 259
Cdd:COG0666   218 DGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLL 258
Ank_2 pfam12796
Ankyrin repeats (3 copies);
92-184 9.56e-24

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 95.95  E-value: 9.56e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  92 LHLAAKNSHHECIRKLLQSKCPAESVDSSGKTALHYAAAQGCLQAVQILCEHKsPINLKDlDGNIPLLLAVQNGHSEICH 171
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHA-DVNLKD-NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 2462602002 172 FLLDHGADVNSRN 184
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 68-241 2.63e-17

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 85.49  E-value: 2.63e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  68 VECLRVMITHGVDVTAQDTTGHSALHLAAKNS--HHECIRKLLQSKCPAESVDSSGKTALHYAAAQGC--LQAVQILCEH 143
Cdd:PHA03100   86 KEIVKLLLEYGANVNAPDNNGITPLLYAISKKsnSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDK 165

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 144 KSPINLKDldgNIPLLLavqnghseichfllDHGADVNSRNKSGRTALMLACEIGSSNAVEALIKKGADLNLVDSLGYNA 223
Cdd:PHA03100  166 GVDINAKN---RVNYLL--------------SYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTP 228

                         170
                  ....*....|....*...
gi 2462602002 224 LHYSKLSENAGIQSLLLS 241
Cdd:PHA03100  229 LHIAILNNNKEIFKLLLN 246
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
432-948 2.52e-16

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 83.96  E-value: 2.52e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 432 RIQQLQEILQDLQKRLESSEAERKQLQVELQSRRAELvclnnteisENSSDLSQKLKETQSKYEEAMKEVLSVQKQMKlg 511
Cdd:PRK03918  187 RTENIEELIKEKEKELEEVLREINEISSELPELREEL---------EKLEKEVKELEELKEEIEELEKELESLEGSKR-- 255

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 512 lvspesmdnyshfhelrvteeeinVLKQDLQNALEESERNKEKVRELEEKLVEREKgtvIKPPVEEYEEMK---SSYCSV 588
Cdd:PRK03918  256 ------------------------KLEEKIRELEERIEELKKEIEELEEKVKELKE---LKEKAEEYIKLSefyEEYLDE 308

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 589 IENMNKEKAFLFEKYQEAQEEIMKLKDtlKSQMTQEASDEAEDMKEAMNRMidelnKQVSELSQLYKEAQAELEDYRKRK 668
Cdd:PRK03918  309 LREIEKRLSRLEEEINGIEERIKELEE--KEERLEELKKKLKELEKRLEEL-----EERHELYEEAKAKKEELERLKKRL 381

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 669 sledvTAEYIHKAEHEklmqLTNVSRAKAE--DALSEMKSQYSKVLNELTQLKQLVDAQKENSVS-------ITEH--LQ 737
Cdd:PRK03918  382 -----TGLTPEKLEKE----LEELEKAKEEieEEISKITARIGELKKEIKELKKAIEELKKAKGKcpvcgreLTEEhrKE 452

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 738 VITTLRTAAKEMEEKISNLKEHLASKEVEVAKLEKQLLEEKAAMTDamvpRSSYEKLQSSLESEVSVLASKLKESVKEKE 817
Cdd:PRK03918  453 LLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKL----KELAEQLKELEEKLKKYNLEELEKKAEEYE 528

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 818 KVHSEVVQIRSEVSQVKREKENIQTLLKSKEqevnELLQKFQQAQEELAEM-KRYAESSSKLEEDKDKKINEMSKEVTKL 896
Cdd:PRK03918  529 KLKEKLIKLKGEIKSLKKELEKLEELKKKLA----ELEKKLDELEEELAELlKELEELGFESVEELEERLKELEPFYNEY 604

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2462602002 897 KEALNSLSQLSYSTSSSKRQSQQLEALQQQVKQLQNQLAECKKQHQEVISVY 948
Cdd:PRK03918  605 LELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKY 656
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 526-896 1.40e-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: 78.56  E-value: 1.40e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  526 ELRVTEEEINVLKQDLQNALEESERNKEKVRELEEKLVEREKGTVI-KPPVEEYEEMKSSYCSVIENMNKEKAFLFEKYQ 604
Cdd:TIGR02168  692 KIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARlEAEVEQLEERIAQLSKELTELEAEIEELEERLE 771

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  605 EAQEEIMKLKDTLKSQmtQEASDEAEDMKEAMNRMIDELNKQVSELSQLYKEAQAELEDYRKRKSLEDVTAEYIH--KAE 682
Cdd:TIGR02168  772 EAEEELAEAEAEIEEL--EAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEeqIEE 849

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  683 HEKLMQLTNVSRAKAEDALSEMKSQYSKVLNELTQLKQLVDAQKENSVSITEHLQvitTLRTAAKEMEEKISNLKEHLAS 762
Cdd:TIGR02168  850 LSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELR---ELESKRSELRRELEELREKLAQ 926

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  763 KEVEVAKLEKQLLEekaamtdamvprssyekLQSSLESEVSVLaskLKESVKEKEKVHSEVVQIRSEVSQVKREKENIQt 842
Cdd:TIGR02168  927 LELRLEGLEVRIDN-----------------LQERLSEEYSLT---LEEAEALENKIEDDEEEARRRLKRLENKIKELG- 985

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2462602002  843 llkskeqEVNEL-LQKFQQAQEELAEMKRYAESSSKLEEDKDKKINEMSKEVTKL 896
Cdd:TIGR02168  986 -------PVNLAaIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDREARER 1033
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 595-900 7.42e-13

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 73.05  E-value: 7.42e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 595 EKAflfEKYQEAQEEIMKLKDTLKSQMTQEASDEAEDMKEAMNRMIDELNKQVSELSQLYKE-AQAELEDYRKRKSLEDV 673
Cdd:COG1196   210 EKA---ERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAElEELRLELEELELELEEA 286

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 674 TA-EYIHKAEHEKLmqltnvsrAKAEDALSEMKSQYSKVLNELTQLKQLVDAQKEnsvsitEHLQVITTLRTAAKEMEEK 752
Cdd:COG1196   287 QAeEYELLAELARL--------EQDIARLEERRRELEERLEELEEELAELEEELE------ELEEELEELEEELEEAEEE 352

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 753 ISNLKEHLASKEVEVAKLEKQLLEEKAAMTDAMVPRSSYEKLQSSLESEVSVLASKLKESVKEKEKVHSEVVQIRSEVSQ 832
Cdd:COG1196   353 LEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAE 432

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462602002 833 VKREKENIQTLLKSKEQEVNELLQKFQQAQEELAEMKRYAESSSKLEEDKDKKINEMSKEVTKLKEAL 900
Cdd:COG1196   433 LEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAE 500
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 90-225 2.68e-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: 2.68e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  90 SALHLAAKNSHHECIRKLLqsKCPaeSVD-----SSGKTALHYAAAQGCLQAVQILCEH-----KSPINLKDLDGNIPLL 159
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLL--KCP--SCDlfqrgALGETALHVAALYDNLEAAVVLMEAapelvNEPMTSDLYQGETALH 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 160 LAVQNGHSEICHFLLDHGADVNS---------RNKS-----GRTALMLACEIGSSNAVEALIKKGADLNLVDSLGYNALH 225
Cdd:cd22192    95 IAVVNQNLNLVRELIARGADVVSpratgtffrPGPKnliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLH 174
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
 527-901 2.73e-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: 64.10  E-value: 2.73e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 527 LRVTEEEINVLKQDLQNALEESERNKEKVRELEEKlverekgtvikppveeYEEMKSSYcsvienmnKEKAFLFEKYQEA 606
Cdd:pfam06160  95 LDDIEEDIKQILEELDELLESEEKNREEVEELKDK----------------YRELRKTL--------LANRFSYGPAIDE 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 607 QEEIMKLKDTLKSQMTQEASD----EAEDMKEAMNRMIDELNKQVSELSQLYKEAQAELEDyrkrkSLEDVtaeyihKAE 682
Cdd:pfam06160 151 LEKQLAEIEEEFSQFEELTESgdylEAREVLEKLEEETDALEELMEDIPPLYEELKTELPD-----QLEEL------KEG 219

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 683 HEKLM-QLTNVSRAKAEDALSEMKSQYSKVLNELTQLKqlVDAQKENSVSITEHLQ----VITTLRTAAKEMEEKISNLK 757
Cdd:pfam06160 220 YREMEeEGYALEHLNVDKEIQQLEEQLEENLALLENLE--LDEAEEALEEIEERIDqlydLLEKEVDAKKYVEKNLPEIE 297

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 758 EHLAskevEVAKLEKQLLEEKAAMTDAMVPRSSYEKLQSSLESEVSVLASKLKESVK---EKEKVHSEVV----QIRSEV 830
Cdd:pfam06160 298 DYLE----HAEEQNKELKEELERVQQSYTLNENELERVRGLEKQLEELEKRYDEIVErleEKEVAYSELQeeleEILEQL 373

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462602002 831 SQVKREKENIQTLLKS---KEQEVNELLQKFQQaqeELAEMKRYAESS--SKLEEDKDKKINEMSKEVTKLKEALN 901
Cdd:pfam06160 374 EEIEEEQEEFKESLQSlrkDELEAREKLDEFKL---ELREIKRLVEKSnlPGLPESYLDYFFDVSDEIEDLADELN 446
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 85-229 6.87e-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: 6.87e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  85 DTTGHSALHLAAKNSHHECIRKLLQSKCPAESVdssGKTALHyAAAQGCLQAVQILCEHKSPINLKDLD----------- 153
Cdd:TIGR00870  49 DRLGRSALFVAAIENENLELTELLLNLSCRGAV---GDTLLH-AISLEYVDAVEAILLHLLAAFRKSGPlelandqytse 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 154 ---GNIPLLLAVQNGHSEICHFLLDHGADVNSRNKS--------------GRTALMLACEIGSSNAVEALIKKGADLNLV 216
Cdd:TIGR00870 125 ftpGITALHLAAHRQNYEIVKLLLERGASVPARACGdffvksqgvdsfyhGESPLNAAACLGSPSIVALLSEDPADILTA 204

                         170
                  ....*....|...
gi 2462602002 217 DSLGYNALHYSKL 229
Cdd:TIGR00870 205 DSLGNTLLHLLVM 217
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 153-181 1.29e-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: 1.29e-05
                           10        20
                   ....*....|....*....|....*....
gi 2462602002  153 DGNIPLLLAVQNGHSEICHFLLDHGADVN 181
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
 697-869 1.54e-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: 48.13  E-value: 1.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 697 AEDALSEMKSQYSKVLNELTQLKQLVDaQKENSVSITEHLQVITTLRTAAKEMEEKISNLKEHLASKEVEVAKLEKQLLE 776
Cdd:cd22656    82 AQNAGGTIDSYYAEILELIDDLADATD-DEELEEAKKTIKALLDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQTALET 160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 777 EKAAMTD------AMVPRSSYEKLQSSLESEVSVLASKLKESVKEKEKvhsevvQIRSEVSQVKREKeNIQTLLKSKEQE 850
Cdd:cd22656   161 LEKALKDlltdegGAIARKEIKDLQKELEKLNEEYAAKLKAKIDELKA------LIADDEAKLAAAL-RLIADLTAADTD 233

                         170
                  ....*....|....*....
gi 2462602002 851 VNELLQKFQQAQEELAEMK 869
Cdd:cd22656   234 LDNLLALIGPAIPALEKLQ 252
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 755-901 8.66e-03

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 39.23  E-value: 8.66e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  755 NLKEHLAsKEVEVAKLEKQLLEEKAAMTDAMVPRSSyeKLQSSLESEVSVLasklKESVKEKEKVH-SEVVQIRSEVSQV 833
Cdd:smart00787 144 GLKEGLD-ENLEGLKEDYKLLMKELELLNSIKPKLR--DRKDALEEELRQL----KQLEDELEDCDpTELDRAKEKLKKL 216

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462602002  834 KREKENIQTLLKSKEQEVNELLQKFQQAQEELAEMK-RYAESSSKLEEDKDKKInemsKEVTKLKEALN 901
Cdd:smart00787 217 LQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNtEIAEAEKKLEQCRGFTF----KEIEKLKEQLK 281
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
59-259 5.28e-46

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 167.05  E-value: 5.28e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  59 FHLAAAKGHVECLRVMITHGVDVTAQDTTGHSALHLAAKNSHHECIRKLLQSKCPAESVDSSGKTALHYAAAQGCLQAVQ 138
Cdd:COG0666    58 LLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVK 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 139 ILCEHKSPINLKDLDGNIPLLLAVQNGHSEICHFLLDHGADVNSRNKSGRTALMLACEIGSSNAVEALIKKGADLNLVDS 218
Cdd:COG0666   138 LLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDN 217

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2462602002 219 LGYNALHYSKLSENAGIQSLLLSKISQDADLKTPTKPKQHD 259
Cdd:COG0666   218 DGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLL 258
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
59-250 6.53e-46

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 167.05  E-value: 6.53e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  59 FHLAAAKGHVECLRVMITHGVDVTAQDTTGHSALHLAAKNSHHECIRKLLQSKCPAESVDSSGKTALHYAAAQGCLQAVQ 138
Cdd:COG0666    91 LHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVK 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 139 ILCEHKSPINLKDLDGNIPLLLAVQNGHSEICHFLLDHGADVNSRNKSGRTALMLACEIGSSNAVEALIKKGADLNLVDS 218
Cdd:COG0666   171 LLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDK 250

                         170       180       190
                  ....*....|....*....|....*....|..
gi 2462602002 219 LGYNALHYSKLSENAGIQSLLLSKISQDADLK 250
Cdd:COG0666   251 DGLTALLLAAAAGAALIVKLLLLALLLLAAAL 282
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
59-252 1.41e-36

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 140.09  E-value: 1.41e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  59 FHLAAAKGHVECLRVMITHGVDVTAQDTTGHSALHLAAKNSHHECIRKLLQSKCPAESVDSSGKTALHYAAAQGCLQAVQ 138
Cdd:COG0666    25 LLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVK 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 139 ILCEHKSPINLKDLDGNIPLLLAVQNGHSEICHFLLDHGADVNSRNKSGRTALMLACEIGSSNAVEALIKKGADLNLVDS 218
Cdd:COG0666   105 LLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDN 184

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2462602002 219 LGYNALHYSKLSENAGIQSLLLSK----ISQDADLKTP 252
Cdd:COG0666   185 DGETPLHLAAENGHLEIVKLLLEAgadvNAKDNDGKTA 222
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
60-224 1.25e-34

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 134.31  E-value: 1.25e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  60 HLAAAKGHVECLRVMITHGVDVTAQDTTGHSALHLAAKNSHHECIRKLLQSKCPAESVDSSGKTALHYAAAQGCLQAVQI 139
Cdd:COG0666   125 HLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKL 204

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 140 LCEHKSPINLKDLDGNIPLLLAVQNGHSEICHFLLDHGADVNSRNKSGRTALMLACEIGSSNAVEALIKKGADLNLVDSL 219
Cdd:COG0666   205 LLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLD 284


                  ....*
gi 2462602002 220 GYNAL 224
Cdd:COG0666   285 LLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
71-252 6.96e-26

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 108.89  E-value: 6.96e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  71 LRVMITHGVDVTAQDTTGHSALHLAAKNSHHECIRKLLQSKCPAESVDSSGKTALHYAAAQGCLQAVQILCEHKSPINLK 150
Cdd:COG0666     4 LLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAK 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 151 DLDGNIPLLLAVQNGHSEICHFLLDHGADVNSRNKSGRTALMLACEIGSSNAVEALIKKGADLNLVDSLGYNALHYSKLS 230
Cdd:COG0666    84 DDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAAN 163

                         170       180
                  ....*....|....*....|....*.
gi 2462602002 231 ENAGIQSLLLSK----ISQDADLKTP 252
Cdd:COG0666   164 GNLEIVKLLLEAgadvNARDNDGETP 189
Ank_2 pfam12796
Ankyrin repeats (3 copies);
92-184 9.56e-24

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 95.95  E-value: 9.56e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  92 LHLAAKNSHHECIRKLLQSKCPAESVDSSGKTALHYAAAQGCLQAVQILCEHKsPINLKDlDGNIPLLLAVQNGHSEICH 171
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHA-DVNLKD-NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 2462602002 172 FLLDHGADVNSRN 184
Cdd:pfam12796  79 LLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
125-217 1.09e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 93.26  E-value: 1.09e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 125 LHYAAAQGCLQAVQILCEHKSPINLKDLDGNIPLLLAVQNGHSEICHFLLDHgADVNSRNKsGRTALMLACEIGSSNAVE 204
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 2462602002 205 ALIKKGADLNLVD 217
Cdd:pfam12796  79 LLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
59-151 1.59e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 92.49  E-value: 1.59e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  59 FHLAAAKGHVECLRVMITHGVDVTAQDTTGHSALHLAAKNSHHECIRKLLQsKCPAESVDsSGKTALHYAAAQGCLQAVQ 138
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 2462602002 139 ILCEHKSPINLKD 151
Cdd:pfam12796  79 LLLEKGADINVKD 91
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
59-191 2.80e-22

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 98.10  E-value: 2.80e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  59 FHLAAAKGHVECLRVMITHGVDVTAQDTTGHSALHLAAKNSHHECIRKLLQSKCPAESVDSSGKTALHYAAAQGCLQAVQ 138
Cdd:COG0666   157 LHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVK 236

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2462602002 139 ILCEHKSPINLKDLDGNIPLLLAVQNGHSEICHFLLDHGADVNSRNKSGRTAL 191
Cdd:COG0666   237 LLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 68-241 2.63e-17

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 85.49  E-value: 2.63e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  68 VECLRVMITHGVDVTAQDTTGHSALHLAAKNS--HHECIRKLLQSKCPAESVDSSGKTALHYAAAQGC--LQAVQILCEH 143
Cdd:PHA03100   86 KEIVKLLLEYGANVNAPDNNGITPLLYAISKKsnSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDK 165

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 144 KSPINLKDldgNIPLLLavqnghseichfllDHGADVNSRNKSGRTALMLACEIGSSNAVEALIKKGADLNLVDSLGYNA 223
Cdd:PHA03100  166 GVDINAKN---RVNYLL--------------SYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTP 228

                         170
                  ....*....|....*...
gi 2462602002 224 LHYSKLSENAGIQSLLLS 241
Cdd:PHA03100  229 LHIAILNNNKEIFKLLLN 246
Ank_2 pfam12796
Ankyrin repeats (3 copies);
158-242 2.84e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 77.85  E-value: 2.84e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 158 LLLAVQNGHSEICHFLLDHGADVNSRNKSGRTALMLACEIGSSNAVEALIKKgADLNLVDSlGYNALHYSKLSENAGIQS 237
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78


                  ....*
gi 2462602002 238 LLLSK 242
Cdd:pfam12796  79 LLLEK 83
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
432-948 2.52e-16

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 83.96  E-value: 2.52e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 432 RIQQLQEILQDLQKRLESSEAERKQLQVELQSRRAELvclnnteisENSSDLSQKLKETQSKYEEAMKEVLSVQKQMKlg 511
Cdd:PRK03918  187 RTENIEELIKEKEKELEEVLREINEISSELPELREEL---------EKLEKEVKELEELKEEIEELEKELESLEGSKR-- 255

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 512 lvspesmdnyshfhelrvteeeinVLKQDLQNALEESERNKEKVRELEEKLVEREKgtvIKPPVEEYEEMK---SSYCSV 588
Cdd:PRK03918  256 ------------------------KLEEKIRELEERIEELKKEIEELEEKVKELKE---LKEKAEEYIKLSefyEEYLDE 308

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 589 IENMNKEKAFLFEKYQEAQEEIMKLKDtlKSQMTQEASDEAEDMKEAMNRMidelnKQVSELSQLYKEAQAELEDYRKRK 668
Cdd:PRK03918  309 LREIEKRLSRLEEEINGIEERIKELEE--KEERLEELKKKLKELEKRLEEL-----EERHELYEEAKAKKEELERLKKRL 381

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 669 sledvTAEYIHKAEHEklmqLTNVSRAKAE--DALSEMKSQYSKVLNELTQLKQLVDAQKENSVS-------ITEH--LQ 737
Cdd:PRK03918  382 -----TGLTPEKLEKE----LEELEKAKEEieEEISKITARIGELKKEIKELKKAIEELKKAKGKcpvcgreLTEEhrKE 452

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 738 VITTLRTAAKEMEEKISNLKEHLASKEVEVAKLEKQLLEEKAAMTDamvpRSSYEKLQSSLESEVSVLASKLKESVKEKE 817
Cdd:PRK03918  453 LLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKL----KELAEQLKELEEKLKKYNLEELEKKAEEYE 528

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 818 KVHSEVVQIRSEVSQVKREKENIQTLLKSKEqevnELLQKFQQAQEELAEM-KRYAESSSKLEEDKDKKINEMSKEVTKL 896
Cdd:PRK03918  529 KLKEKLIKLKGEIKSLKKELEKLEELKKKLA----ELEKKLDELEEELAELlKELEELGFESVEELEERLKELEPFYNEY 604

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2462602002 897 KEALNSLSQLSYSTSSSKRQSQQLEALQQQVKQLQNQLAECKKQHQEVISVY 948
Cdd:PRK03918  605 LELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKY 656
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 59-216 9.26e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 80.81  E-value: 9.26e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  59 FHLAAAKGHVECLRVMITHGV---DVTAQDttGHSALHLAAKNSHHECIRKLLQSKCPAESVDSSGKTALHYAAAQGCLQ 135
Cdd:PHA02875   72 LHDAVEEGDVKAVEELLDLGKfadDVFYKD--GMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIK 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 136 AVQILCEHKSPINLKDLDGNIPLLLAVQNGHSEICHFLLDHGADVNSRNKSGRTALM-LACEIGSSNAVEALIKKGADLN 214
Cdd:PHA02875  150 GIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALcYAIENNKIDIVRLFIKRGADCN 229


                  ..
gi 2462602002 215 LV 216
Cdd:PHA02875  230 IM 231
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 526-896 1.40e-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: 78.56  E-value: 1.40e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  526 ELRVTEEEINVLKQDLQNALEESERNKEKVRELEEKLVEREKGTVI-KPPVEEYEEMKSSYCSVIENMNKEKAFLFEKYQ 604
Cdd:TIGR02168  692 KIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARlEAEVEQLEERIAQLSKELTELEAEIEELEERLE 771

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  605 EAQEEIMKLKDTLKSQmtQEASDEAEDMKEAMNRMIDELNKQVSELSQLYKEAQAELEDYRKRKSLEDVTAEYIH--KAE 682
Cdd:TIGR02168  772 EAEEELAEAEAEIEEL--EAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEeqIEE 849

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  683 HEKLMQLTNVSRAKAEDALSEMKSQYSKVLNELTQLKQLVDAQKENSVSITEHLQvitTLRTAAKEMEEKISNLKEHLAS 762
Cdd:TIGR02168  850 LSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELR---ELESKRSELRRELEELREKLAQ 926

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  763 KEVEVAKLEKQLLEekaamtdamvprssyekLQSSLESEVSVLaskLKESVKEKEKVHSEVVQIRSEVSQVKREKENIQt 842
Cdd:TIGR02168  927 LELRLEGLEVRIDN-----------------LQERLSEEYSLT---LEEAEALENKIEDDEEEARRRLKRLENKIKELG- 985

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2462602002  843 llkskeqEVNEL-LQKFQQAQEELAEMKRYAESSSKLEEDKDKKINEMSKEVTKL 896
Cdd:TIGR02168  986 -------PVNLAaIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDREARER 1033
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 48-224 1.90e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 76.93  E-value: 1.90e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  48 VRARPRKLKHCFHLAAAKGHVECLRVMITHGVDVTAQDTTGHSALHLAAKNSHHECIRKLLQSKCPAESVDSSGKTALHY 127
Cdd:PHA02874  117 VNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHN 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 128 AAAQGCLQAVQILCEHKSPINLKDLDGNIPLLLAVQNGHSEIChfLLDHGADVNSRNKSGRTALMLA----CEIgssNAV 203
Cdd:PHA02874  197 AAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRSAIE--LLINNASINDQDIDGSTPLHHAinppCDI---DII 271

                         170       180
                  ....*....|....*....|.
gi 2462602002 204 EALIKKGADLNLVDSLGYNAL 224
Cdd:PHA02874  272 DILLYHKADISIKDNKGENPI 292
PHA03095 PHA03095
ankyrin-like protein; Provisional
 68-226 2.17e-14

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 76.99  E-value: 2.17e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  68 VECLRVMITHGVDVTAQDTTGHSALHLAAKNSH--HECIRKLLQSKCPAESVDSSGKTALHYAAAQGCLQAVQI--LCEH 143
Cdd:PHA03095  167 VELLRLLIDAGADVYAVDDRFRSLLHHHLQSFKprARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVlpLLIA 246

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 144 KSPINLKDLDGNIPLLLAVQNGHSEICHFLLDHGADVNSRNKSGRTALMLACEIGSSNAVEALIKKGADLNLVDslgyNA 223
Cdd:PHA03095  247 GISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETVA----AT 322


                  ...
gi 2462602002 224 LHY 226
Cdd:PHA03095  323 LNT 325
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 62-252 1.59e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 73.84  E-value: 1.59e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  62 AAAKGHVECLRVMITHGVDVTAQDTTGHSALHLAAKNSHH-----------------------ECIRKLLQSKCPAESVD 118
Cdd:PHA02874   42 AIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHdiikllidngvdtsilpipciekDMIKTILDCGIDVNIKD 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 119 SSGKTALHYAAAQGCLQAVQILCEHKSPINLKDLDGNIPLLLAVQNGHSEICHFLLDHGADVNSRNKSGRTALMLACEIG 198
Cdd:PHA02874  122 AELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYG 201

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462602002 199 SSNAVEALIKKGADLNLVDSLGYNALHYSKLSENAGIQsLLLSKIS---QDADLKTP 252
Cdd:PHA02874  202 DYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRSAIE-LLINNASindQDIDGSTP 257
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 60-184 6.13e-13

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 72.98  E-value: 6.13e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  60 HLAAAKGHVECLRVMITHGVDVTAQDTTGHSALHLAAKNSHHECIRKLLQskCPAESVDSSGKTALHYAAAQGCLQAVQI 139
Cdd:PLN03192  563 HIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYH--FASISDPHAAGDLLCTAAKRNDLTAMKE 640

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2462602002 140 LCEHKSPINLKDLDGNIPLLLAVQNGHSEICHFLLDHGADVNSRN 184
Cdd:PLN03192  641 LLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKAN 685
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
432-921 7.07e-13

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 72.79  E-value: 7.07e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 432 RIQQLQEILQDLQKRLESSEAERKQLQVELQSRRAELvclnnteisenssdlsQKLKETQSKYEEAMKEVLSVQKQMKLG 511
Cdd:PRK03918  232 ELEELKEEIEELEKELESLEGSKRKLEEKIRELEERI----------------EELKKEIEELEEKVKELKELKEKAEEY 295

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 512 LVSPESMDNY-SHFHELRVTEEEINVLKQDLQNALEESERNKEKVRELEEKLVE-REKGTVIKPPVEEYEEMKSsycsVI 589
Cdd:PRK03918  296 IKLSEFYEEYlDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKElEKRLEELEERHELYEEAKA----KK 371

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 590 ENMNKEKAFLFEKYQEAQEEIMKLKDTLKSQMTQEASdEAEDMKEAMNRMIDELNKQVSELsqlyKEAQ-------AELE 662
Cdd:PRK03918  372 EELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEIS-KITARIGELKKEIKELKKAIEEL----KKAKgkcpvcgRELT 446

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 663 DYRKRKSLEDVTAEyIHKAEHEKLMQLTNVSRAKAEDALSEMK-SQYSKVLNELTQLKQLVDAQKENSVSITEHLQVIT- 740
Cdd:PRK03918  447 EEHRKELLEEYTAE-LKRIEKELKEIEEKERKLRKELRELEKVlKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAe 525

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 741 ---TLRTAAKEMEEKISNLKEHLASKEV---EVAKLEKQL--LEEKAAMTDAMVPRSSYEKLQSsLESEVSVLAS----- 807
Cdd:PRK03918  526 eyeKLKEKLIKLKGEIKSLKKELEKLEElkkKLAELEKKLdeLEEELAELLKELEELGFESVEE-LEERLKELEPfyney 604

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 808 -KLKESVKEKEKVHSEVVQIRSEVSQVKREKENIQTLLKSKEQEVNELLQKFqqAQEELAEMKRYAESSSKLEEDKDKKI 886
Cdd:PRK03918  605 lELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKY--SEEEYEELREEYLELSRELAGLRAEL 682

                         490       500       510
                  ....*....|....*....|....*....|....*
gi 2462602002 887 NEMSKEVTKLKEALNSLSQLSYSTSSSKRQSQQLE 921
Cdd:PRK03918  683 EELEKRREEIKKTLEKLKEELEEREKAKKELEKLE 717
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 595-900 7.42e-13

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 73.05  E-value: 7.42e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 595 EKAflfEKYQEAQEEIMKLKDTLKSQMTQEASDEAEDMKEAMNRMIDELNKQVSELSQLYKE-AQAELEDYRKRKSLEDV 673
Cdd:COG1196   210 EKA---ERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAElEELRLELEELELELEEA 286

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 674 TA-EYIHKAEHEKLmqltnvsrAKAEDALSEMKSQYSKVLNELTQLKQLVDAQKEnsvsitEHLQVITTLRTAAKEMEEK 752
Cdd:COG1196   287 QAeEYELLAELARL--------EQDIARLEERRRELEERLEELEEELAELEEELE------ELEEELEELEEELEEAEEE 352

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 753 ISNLKEHLASKEVEVAKLEKQLLEEKAAMTDAMVPRSSYEKLQSSLESEVSVLASKLKESVKEKEKVHSEVVQIRSEVSQ 832
Cdd:COG1196   353 LEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAE 432

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462602002 833 VKREKENIQTLLKSKEQEVNELLQKFQQAQEELAEMKRYAESSSKLEEDKDKKINEMSKEVTKLKEAL 900
Cdd:COG1196   433 LEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAE 500
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 432-936 7.55e-13

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 73.05  E-value: 7.55e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 432 RIQQLQEILQDLQKRLESSEAERKQLQVELQSRRAELvclnnTEISENSSDLSQKLKETQSKYEEAMKEVLSVQKQMKLG 511
Cdd:COG1196   233 KLRELEAELEELEAELEELEAELEELEAELAELEAEL-----EELRLELEELELELEEAQAEEYELLAELARLEQDIARL 307

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 512 LvspESMDNYShfHELRVTEEEINVLKQDLQNALEESERNKEKVRELEEKLVEREKGtvikppVEEYEEMKSSYCSVIEN 591
Cdd:COG1196   308 E---ERRRELE--ERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAE------LAEAEEALLEAEAELAE 376

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 592 MNKEKAFLFEKYQEAQEEIMKLKDTLKSQMTQEASDEAEDmkEAMNRMIDELNKQVSELSQLYKEAQAELEDYRKR--KS 669
Cdd:COG1196   377 AEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERL--ERLEEELEELEEALAELEEEEEEEEEALEEAAEEeaEL 454

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 670 LEDVTAEYIHKAEHEKLMQLTNVSRAKAEDALSEMKSQYSKVLNELTQ---------LKQLVDAQKENSVSITEHLQVIT 740
Cdd:COG1196   455 EEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADyegflegvkAALLLAGLRGLAGAVAVLIGVEA 534

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 741 TLRTAAkemEEKISNLKEHLASKEVEVAKLEKQLLEEKAA-------MTDAMVPRSSYEKLQSSLESEVSVLASKLKESV 813
Cdd:COG1196   535 AYEAAL---EAALAAALQNIVVEDDEVAAAAIEYLKAAKAgratflpLDKIRARAALAAALARGAIGAAVDLVASDLREA 611

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 814 KEKEKVHSEVVQIRSEVSQVKREKENIQTLLKSKEQEVNELLQKFQQAQEELAEMKRYAESSSKLEEDKDKKINEMSKEV 893
Cdd:COG1196   612 DARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEE 691

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|...
gi 2462602002 894 TKLKEALNSLSQLSYSTSSSKRQSQQLEALQQQVKQLQNQLAE 936
Cdd:COG1196   692 ELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAER 734
PHA03095 PHA03095
ankyrin-like protein; Provisional
 104-248 1.11e-12

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 71.59  E-value: 1.11e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 104 IRKLLQSKCPAESVDSSGKTALHY---AAAQGCLQAVQILCEHKSPINLKDLDGNIPLLLAVQNGHSE-ICHFLLDHGAD 179
Cdd:PHA03095   30 VRRLLAAGADVNFRGEYGKTPLHLylhYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLdVIKLLIKAGAD 109

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462602002 180 VNSRNKSGRTALMLACEIGSSNA--VEALIKKGADLNLVDSLGYNALHYSKLSENAGIQ--SLLLSKISQDAD 248
Cdd:PHA03095  110 VNAKDKVGRTPLHVYLSGFNINPkvIRLLLRKGADVNALDLYGMTPLAVLLKSRNANVEllRLLIDAGADVYA 182
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 62-213 1.18e-12

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 72.21  E-value: 1.18e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  62 AAAKGHVECLRVMITHGVDVTAQDTTGHSALHLAAKNSHHECIRKLLQSKCPAESVDSSGKTALHYAAAQGCLQAVQILc 141
Cdd:PLN03192  532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRIL- 610

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462602002 142 EHKSPINLKDLDGNIpLLLAVQNGHSEICHFLLDHGADVNSRNKSGRTALMLACEIGSSNAVEALIKKGADL 213
Cdd:PLN03192  611 YHFASISDPHAAGDL-LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADV 681
PHA03095 PHA03095
ankyrin-like protein; Provisional
 57-232 1.23e-12

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 71.21  E-value: 1.23e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  57 HCFHLAAAKghVECLRVMITHGVDVTAQDTTGHSALH--LAAKNSHHECIRKLLQSKCPAESVDSSGKTALH-YAAAQGC 133
Cdd:PHA03095   88 HLYLYNATT--LDVIKLLIKAGADVNAKDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAvLLKSRNA 165

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 134 -LQAVQILCEHKSPINLKDLDGNIPLLLAVQNGHS--EICHFLLDHGADVNSRNKSGRTALMLACEIGSSNA--VEALIK 208
Cdd:PHA03095  166 nVELLRLLIDAGADVYAVDDRFRSLLHHHLQSFKPraRIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRslVLPLLI 245

                         170       180
                  ....*....|....*....|....
gi 2462602002 209 KGADLNLVDSLGYNALHYSKLSEN 232
Cdd:PHA03095  246 AGISINARNRYGQTPLHYAAVFNN 269
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 69-227 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 2462602002  69 ECLRVMITHGVDVTAQDTTGHSALHLAAKNSHHECIRKLLQSKCPAESVDSSGKTALHYAAAQGCLQAVQILCEHKSPIN 148
Cdd:PHA02874  105 DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYAN 184

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462602002 149 LKDLDGNIPLLLAVQNGHSEICHFLLDHGADVNSRNKSGRTALMLACeIGSSNAVEALIKKgADLNLVDSLGYNALHYS 227
Cdd:PHA02874  185 VKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAI-IHNRSAIELLINN-ASINDQDIDGSTPLHHA 261
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 430-901 1.41e-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: 72.02  E-value: 1.41e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  430 DVRIQQLQEILQDLQKRLESSEAERKQLQVELQSRRAELvclnnteisensSDLSQKLKETQSKYEEAMKEVLSVQKqmk 509
Cdd:TIGR02169  328 EAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEEL------------EDLRAELEEVDKEFAETRDELKDYRE--- 392

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  510 lglvspesmdnyshfhELRVTEEEINVLKQDLQNALEESERNKEKVRELEEKLverekgTVIKPPVEEYEEMKssycsvi 589
Cdd:TIGR02169  393 ----------------KLEKLKREINELKRELDRLQEELQRLSEELADLNAAI------AGIEAKINELEEEK------- 443

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  590 enmnKEKAflfEKYQEAQEEIMKLKDTLKSqmtqeASDEAEDMKEAMNRMIDELNKQVSELSQLYKEAQAELEDYRKRKS 669
Cdd:TIGR02169  444 ----EDKA---LEIKKQEWKLEQLAADLSK-----YEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRA 511

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  670 LEDVTAEYIhKAEHEKLMQLTNVSRAKA-----------------EDALSEMKSQYSKV----------LNELTQLKQLV 722
Cdd:TIGR02169  512 VEEVLKASI-QGVHGTVAQLGSVGERYAtaievaagnrlnnvvveDDAVAKEAIELLKRrkagratflpLNKMRDERRDL 590

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  723 DAQKENSVsITEHLQVIttlrtaakEMEEKISN-----LKEHLASKEVEVAK----------LEKQLLEEKAAMTDAMVP 787
Cdd:TIGR02169  591 SILSEDGV-IGFAVDLV--------EFDPKYEPafkyvFGDTLVVEDIEAARrlmgkyrmvtLEGELFEKSGAMTGGSRA 661

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  788 RSSYEKLQSSLESEVSVLASKLKESVKEKEKVHSEVVQIRSEVSQVKREKENIQTLLKSKEQEVNELLQKFQQAQEELAE 867
Cdd:TIGR02169  662 PRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEE 741

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|.
gi 2462602002  868 MKRYAES-SSKLEEDK------DKKINEMSKEVTKLKEALN 901
Cdd:TIGR02169  742 LEEDLSSlEQEIENVKselkelEARIEELEEDLHKLEEALN 782
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 69-218 3.29e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 69.91  E-value: 3.29e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  69 ECLRVMITHGVDVTAQDT-TGHSALHLAAKNSHHECIRKLLQSKCPAESVDSSGKTALHYAAAQGCLQAVQILCEHKSPI 147
Cdd:PHA02878  148 EITKLLLSYGADINMKDRhKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGAST 227

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462602002 148 NLKDLDGNIPLLLAVQNGHS-EICHFLLDHGADVNSRNK-SGRTALMLAceIGSSNAVEALIKKGADLNLVDS 218
Cdd:PHA02878  228 DARDKCGNTPLHISVGYCKDyDILKLLLEHGVDVNAKSYiLGLTALHSS--IKSERKLKLLLEYGADINSLNS 298
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 589-901 1.23e-11

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 68.93  E-value: 1.23e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  589 IENMNKEKAFLFEKYQEAQEEIMKLKDTLksqmtqeasDEAEDMKEAMNRMIDELNKQVSELSQLYKEAQAELEDYRKRK 668
Cdd:TIGR02168  679 IEELEEKIEELEEKIAELEKALAELRKEL---------EELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERI 749

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  669 SLEDVTAEyihkaEHEKLMQLTNVSRAKAEDALSEMKSqyskvlnELTQLKQLVDAQKENSVSITEHLQ----VITTLRT 744
Cdd:TIGR02168  750 AQLSKELT-----ELEAEIEELEERLEEAEEELAEAEA-------EIEELEAQIEQLKEELKALREALDelraELTLLNE 817

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  745 AAKEMEEKISNLKEHLASKEVEVAKLEKQLLEEKAAMtdamvprSSYEKLQSSLESEVSVLASKLKESVKEKEKVHSEVV 824
Cdd:TIGR02168  818 EAANLRERLESLERRIAATERRLEDLEEQIEELSEDI-------ESLAAEIEELEELIEELESELEALLNERASLEEALA 890

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  825 QIRS--------------EVSQVKREKENIQTLLKSKEQEVNELLQKFQQAQEELAEM-KRYAESSSKLEEDKDKKINEM 889
Cdd:TIGR02168  891 LLRSeleelseelrelesKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEySLTLEEAEALENKIEDDEEEA 970

                          330
                   ....*....|..
gi 2462602002  890 SKEVTKLKEALN 901
Cdd:TIGR02168  971 RRRLKRLENKIK 982
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 432-784 2.09e-11

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 68.04  E-value: 2.09e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 432 RIQQLQEILQDLQKRLESSEAERKQ------LQVELQSRRAELVCLNNTEISENSSDLSQKLKETQSKYEEAMKevlsvq 505
Cdd:COG1196   187 NLERLEDILGELERQLEPLERQAEKaeryreLKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEA------ 260

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 506 kqmklglvspesmdnyshfhELRVTEEEINVLKQDLQNALEESERNKEKVRELEEKLVEREKGtvikppVEEYEEMKSSY 585
Cdd:COG1196   261 --------------------ELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQD------IARLEERRREL 314

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 586 CSVIENMNKEKAFLFEKYQEAQEEIMKLkdtlksqmtQEASDEAEDMKEAMNRMIDELNKQVSELSQLYKEAQAELEDyR 665
Cdd:COG1196   315 EERLEELEEELAELEEELEELEEELEEL---------EEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEE-L 384

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 666 KRKSLEDVTAEYIHKAEHEKLMQLTNVSRAKAEDALSEMKSQYSKVLNELTQLKQLVDAQKENSVSITEHLQVITTLRTA 745
Cdd:COG1196   385 AEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLEL 464

                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 2462602002 746 AKEMEEKISNLKEHLASKEVEVAKLEKQLLEEKAAMTDA 784
Cdd:COG1196   465 LAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADY 503
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 430-901 2.58e-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: 68.16  E-value: 2.58e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  430 DVRIQQLQEILQDLQKRLESSEAERKQLQVELQSRRAELvclnnTEISENSSDLSQKLKETQSKYEEAMKEVLSVQKQMK 509
Cdd:TIGR02168  322 EAQLEELESKLDELAEELAELEEKLEELKEELESLEAEL-----EELEAELEELESRLEELEEQLETLRSKVAQLELQIA 396

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  510 LglvspesmdnyshfhelrvTEEEINVLKQDLQNALEESERNKEKVRELEEKLVEREKGTViKPPVEEYEEMKSSYCSVI 589
Cdd:TIGR02168  397 S-------------------LNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKEL-QAELEELEEELEELQEEL 456

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  590 ENMNKEKAFLFEKYQEAQEEIMKLKDTLKS---------QMTQEASDEAEDMKEAMNRMID------------------- 641
Cdd:TIGR02168  457 ERLEEALEELREELEEAEQALDAAERELAQlqarldsleRLQENLEGFSEGVKALLKNQSGlsgilgvlselisvdegye 536

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  642 ---------ELNKQVSELSQLYKEAQAELEDYRKRKS----LEDVTAEYIHKAEHEKLMQLTNVSRAKAEdaLSEMKSQY 708
Cdd:TIGR02168  537 aaieaalggRLQAVVVENLNAAKKAIAFLKQNELGRVtflpLDSIKGTEIQGNDREILKNIEGFLGVAKD--LVKFDPKL 614

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  709 SKVLN----------------------------------------------------------ELTQLKQLVDAQKEnsv 730
Cdd:TIGR02168  615 RKALSyllggvlvvddldnalelakklrpgyrivtldgdlvrpggvitggsaktnssilerrrEIEELEEKIEELEE--- 691

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  731 SITEHLQVITTLRTAAKEMEEKISNLKEHLASKEVEVAKLEKQLLEEKAAMTDAMVPRSSYEKLQSSLESEVSVLASKLK 810
Cdd:TIGR02168  692 KIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLE 771

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  811 ESVKEKEKVHSEVVQIRSEVSQVKREKENIQTLLKSKEQEVNELLQKFQQAQEELAEMKRYAESSSKLEEDKDKKINEMS 890
Cdd:TIGR02168  772 EAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELS 851

                          570
                   ....*....|.
gi 2462602002  891 KEVTKLKEALN 901
Cdd:TIGR02168  852 EDIESLAAEIE 862
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
630-866 3.47e-11

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 67.35  E-value: 3.47e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 630 EDMKEAMNRMIDELNKQVSELSQLYKEAQAELEDYRKRKSLEDVTAEyihkaeheklMQLTNVSRAKAEDALSEMKSQYS 709
Cdd:COG3206   167 ELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVDLSEE----------AKLLLQQLSELESQLAEARAELA 236

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 710 KVLNELTQLKQLVDAQKENSVSITEHlQVITTLRTAAKEMEEKISNLKEHLASKEVEVAKLEKQLLEEKAAMtdamvpRS 789
Cdd:COG3206   237 EAEARLAALRAQLGSGPDALPELLQS-PVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQL------QQ 309

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 790 SYEKLQSSLESEVSVLASKLKESVKEKEKVHSEVVQI---RSEVSQVKREKENIQTLLkskeqevNELLQKFQQAQEELA 866
Cdd:COG3206   310 EAQRILASLEAELEALQAREASLQAQLAQLEARLAELpelEAELRRLEREVEVARELY-------ESLLQRLEEARLAEA 382
PTZ00121 PTZ00121
MAEBL; Provisional
 441-900 7.21e-11

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 66.70  E-value: 7.21e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  441 QDLQKRLESSEAERKQLQVElQSRRAElvclnntEISENSSDLSQKLKETQSKYEEAMKEVLSVQKQMKLGLVSPESMDN 520
Cdd:PTZ00121  1293 DEAKKAEEKKKADEAKKKAE-EAKKAD-------EAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEE 1364

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  521 YSHFHELRVTEEEINV--------LKQDLQNALEESERNKEKVRELEEKLVEREKGTVIKPPVEEYEEMKSSYCSVIENM 592
Cdd:PTZ00121  1365 KAEAAEKKKEEAKKKAdaakkkaeEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAK 1444

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  593 N----KEKAFLFEKYQEAQ---EEIMKLKDTLKSQMTQEASDEAEDMKEAMNRMIDELNKQVSELSQLYKEAQAE----- 660
Cdd:PTZ00121  1445 KadeaKKKAEEAKKAEEAKkkaEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEeakka 1524

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  661 -----LEDYRK----RKSLEDVTAEYIHKAEH-EKLMQLTNVSRAKAEDALSEMKSQYSKVLN--ELTQLKQLVDAQKEN 728
Cdd:PTZ00121  1525 deakkAEEAKKadeaKKAEEKKKADELKKAEElKKAEEKKKAEEAKKAEEDKNMALRKAEEAKkaEEARIEEVMKLYEEE 1604

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  729 SVSITEHLQVITTLRTAAKEM--EEKISNLKEHLASKEVEVAKLEKQL--LEEKAAMTDAMVPRSSYEKLQSSLESEVSV 804
Cdd:PTZ00121  1605 KKMKAEEAKKAEEAKIKAEELkkAEEEKKKVEQLKKKEAEEKKKAEELkkAEEENKIKAAEEAKKAEEDKKKAEEAKKAE 1684

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  805 LASKLK-ESVKEKEKVHSEVVQIRSEVSQVKREKENIQtllksKEQEVNELlqKFQQAQEELAEMKRYAESSSKLEEDKd 883
Cdd:PTZ00121  1685 EDEKKAaEALKKEAEEAKKAEELKKKEAEEKKKAEELK-----KAEEENKI--KAEEAKKEAEEDKKKAEEAKKDEEEK- 1756

                          490
                   ....*....|....*..
gi 2462602002  884 KKINEMSKEVTKLKEAL 900
Cdd:PTZ00121  1757 KKIAHLKKEEEKKAEEI 1773
Ank_4 pfam13637
Ankyrin repeats (many copies);
123-174 8.06e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 58.05  E-value: 8.06e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2462602002 123 TALHYAAAQGCLQAVQILCEHKSPINLKDLDGNIPLLLAVQNGHSEICHFLL 174
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 426-901 1.01e-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: 65.81  E-value: 1.01e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 426 TTDNDVRIQQLQEILQDLQKRLESSEAERKQLQVELQSRRAELVCLNNT--EISENSSDLSQKLKETQSKYEEAMKEVLS 503
Cdd:TIGR04523  28 ANKQDTEEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKikILEQQIKDLNDKLKKNKDKINKLNSDLSK 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 504 VQKQMK--------------------------LGLVSPESMDNYSHFHELRVTEEEINVLKQDLQNALEESERNKEKVRE 557
Cdd:TIGR04523 108 INSEIKndkeqknklevelnklekqkkenkknIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQK 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 558 LEEKL-VEREKGTVIKPPVEEYEEMKSSYCSVIENMNKEKAFLFEKYQEAQEEIMKLKDTLKSQMTQ--EASDEAEDMKE 634
Cdd:TIGR04523 188 NIDKIkNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQlnQLKDEQNKIKK 267

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 635 AMNRMIDEL---NKQVSELSQLYKEAQAELEDYRKRKSLEDVTAEYIHKAEHEKLMQLTNVSRAKAEDALSEMKSQYSKV 711
Cdd:TIGR04523 268 QLSEKQKELeqnNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQL 347

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 712 LNELTQL---------------KQLVDAQKENSvsitEHLQVITTLRTAAKEMEEKISNLKEHLASKEVEVAKLEKQLLE 776
Cdd:TIGR04523 348 KKELTNSesensekqreleekqNEIEKLKKENQ----SYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKEL 423

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 777 EKAAMTDAMVPRSSYEKLQSSLESEVSVLASKLKESVKEKEKVHSEVVQIRSEVSQVKREKENIQTLLKSKEQEVNELLQ 856
Cdd:TIGR04523 424 LEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNE 503

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*
gi 2462602002 857 KFQQAQEELAEMKRYAESSSKLEEDKDKKINEMSKEVTKLKEALN 901
Cdd:TIGR04523 504 EKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELN 548
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 90-225 2.68e-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: 2.68e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  90 SALHLAAKNSHHECIRKLLqsKCPaeSVD-----SSGKTALHYAAAQGCLQAVQILCEH-----KSPINLKDLDGNIPLL 159
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLL--KCP--SCDlfqrgALGETALHVAALYDNLEAAVVLMEAapelvNEPMTSDLYQGETALH 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 160 LAVQNGHSEICHFLLDHGADVNS---------RNKS-----GRTALMLACEIGSSNAVEALIKKGADLNLVDSLGYNALH 225
Cdd:cd22192    95 IAVVNQNLNLVRELIARGADVVSpratgtffrPGPKnliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLH 174
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
 527-901 2.73e-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: 64.10  E-value: 2.73e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 527 LRVTEEEINVLKQDLQNALEESERNKEKVRELEEKlverekgtvikppveeYEEMKSSYcsvienmnKEKAFLFEKYQEA 606
Cdd:pfam06160  95 LDDIEEDIKQILEELDELLESEEKNREEVEELKDK----------------YRELRKTL--------LANRFSYGPAIDE 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 607 QEEIMKLKDTLKSQMTQEASD----EAEDMKEAMNRMIDELNKQVSELSQLYKEAQAELEDyrkrkSLEDVtaeyihKAE 682
Cdd:pfam06160 151 LEKQLAEIEEEFSQFEELTESgdylEAREVLEKLEEETDALEELMEDIPPLYEELKTELPD-----QLEEL------KEG 219

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 683 HEKLM-QLTNVSRAKAEDALSEMKSQYSKVLNELTQLKqlVDAQKENSVSITEHLQ----VITTLRTAAKEMEEKISNLK 757
Cdd:pfam06160 220 YREMEeEGYALEHLNVDKEIQQLEEQLEENLALLENLE--LDEAEEALEEIEERIDqlydLLEKEVDAKKYVEKNLPEIE 297

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 758 EHLAskevEVAKLEKQLLEEKAAMTDAMVPRSSYEKLQSSLESEVSVLASKLKESVK---EKEKVHSEVV----QIRSEV 830
Cdd:pfam06160 298 DYLE----HAEEQNKELKEELERVQQSYTLNENELERVRGLEKQLEELEKRYDEIVErleEKEVAYSELQeeleEILEQL 373

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462602002 831 SQVKREKENIQTLLKS---KEQEVNELLQKFQQaqeELAEMKRYAESS--SKLEEDKDKKINEMSKEVTKLKEALN 901
Cdd:pfam06160 374 EEIEEEQEEFKESLQSlrkDELEAREKLDEFKL---ELREIKRLVEKSnlPGLPESYLDYFFDVSDEIEDLADELN 446
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 538-901 3.50e-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: 64.31  E-value: 3.50e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  538 KQDLQNALEESERNKEKV----RELEEKLVEREKGTVIkppVEEYEEMKSsycsviENMNKEKAFLFEKYQEAQEEIMKL 613
Cdd:TIGR02168  174 RKETERKLERTRENLDRLedilNELERQLKSLERQAEK---AERYKELKA------ELRELELALLVLRLEELREELEEL 244

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  614 KDTLKSQMTQEASDEAE-DMKEAMnrmIDELNKQVSELSQLYKEAQAELEDYRKRksledvtaeyIHKAEHEKlmqltnv 692
Cdd:TIGR02168  245 QEELKEAEEELEELTAElQELEEK---LEELRLEVSELEEEIEELQKELYALANE----------ISRLEQQK------- 304

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  693 srakaedalsemksqysKVLNEltQLKQLVDAQKENSVSITEHLQVITTLRTAAKEMEEKISNLKEHLASKEVEVAKLEK 772
Cdd:TIGR02168  305 -----------------QILRE--RLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEA 365

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  773 QLLEEKAAMTDAMVPRSSYEKLQSSLESEVSVLASKLKESVKEKEKVHSEVVQIRSEVSQVKREKEN-----IQTLLKSK 847
Cdd:TIGR02168  366 ELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEaelkeLQAELEEL 445

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2462602002  848 EQEVNELLQKFQQAQEELAEMKRYAESSSKLEEDKDKKINEMSKEVTKLKEALN 901
Cdd:TIGR02168  446 EEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQE 499
PHA03095 PHA03095
ankyrin-like protein; Provisional
 68-241 4.04e-10

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 63.12  E-value: 4.04e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  68 VECLRVMITHGVDVTAQDTTGHSALHLaaknshhecirkLLQSKCPAESVDssgktalhyaaaqgclqavqILCEHKSPI 147
Cdd:PHA03095   63 KDIVRLLLEAGADVNAPERCGFTPLHL------------YLYNATTLDVIK--------------------LLIKAGADV 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 148 NLKDLDGNIPL--LLAVQNGHSEICHFLLDHGADVNSRNKSGRTAlmLACEIGSSNA----VEALIKKGADLNLVDSLGY 221
Cdd:PHA03095  111 NAKDKVGRTPLhvYLSGFNINPKVIRLLLRKGADVNALDLYGMTP--LAVLLKSRNAnvelLRLLIDAGADVYAVDDRFR 188

                         170       180
                  ....*....|....*....|..
gi 2462602002 222 NALHYSKLS--ENAGIQSLLLS 241
Cdd:PHA03095  189 SLLHHHLQSfkPRARIVRELIR 210
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 62-240 9.64e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 61.93  E-value: 9.64e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  62 AAAKGHVECLRVMITHGVDVTAQDTTGHSALHLAAKNSHHECIrKLLQSKCPAESVDSSG-KTALHYAAAQGCLQAVQIL 140
Cdd:PHA02875    9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAI-KLLMKHGAIPDVKYPDiESELHDAVEEGDVKAVEEL 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 141 CEHKSPINlkDL---DGNIPLLLAVQNGHSEICHFLLDHGADVNSRNKSGRTALMLACEIGSSNAVEALIKKGADLNLVD 217
Cdd:PHA02875   88 LDLGKFAD--DVfykDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIED 165

                         170       180
                  ....*....|....*....|...
gi 2462602002 218 SLGYNALHYSKLSENAGIQSLLL 240
Cdd:PHA02875  166 CCGCTPLIIAMAKGDIAICKMLL 188
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 440-869 2.04e-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: 61.57  E-value: 2.04e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 440 LQDLQKRLESSEAERKQLQVELQSRRAELVCLNNTEISENSSDLSQKLKETQSKYEEAMKEVLSVQK----------QMK 509
Cdd:TIGR04523 269 LSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKiisqlneqisQLK 348

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 510 LGLVSPESmDNYSHFHELRVTEEEINVLKQDLQNALEESERNKEKVRELEEKLverekgtvikppvEEYEEMKSSYCSVI 589
Cdd:TIGR04523 349 KELTNSES-ENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKI-------------QNQEKLNQQKDEQI 414

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 590 ENMNKEKAFLFEKYQEAQEEIMKLKDTLKSQMTQEASDEAEdmKEAMNRMIDELNKQVSELSQLYKEAQAELEDyrKRKS 669
Cdd:TIGR04523 415 KKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELI--IKNLDNTRESLETQLKVLSRSINKIKQNLEQ--KQKE 490

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 670 LEDVTAEyihkaeheklmqltnvsrakaedaLSEMKSQYSKVLNELTQLKQLVDAQKENsvsitehlqvITTLRTAAKEM 749
Cdd:TIGR04523 491 LKSKEKE------------------------LKKLNEEKKELEEKVKDLTKKISSLKEK----------IEKLESEKKEK 536

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 750 EEKISNLKEHLASKEVEVAK--LEKQLLEEKAAMTDAMVPRSSYEKLQSSLESEVSVLASKLKESVKEKEKVHSEVVQIR 827
Cdd:TIGR04523 537 ESKISDLEDELNKDDFELKKenLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLE 616

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|..
gi 2462602002 828 SEVSQVKREKENIQTLLKSKEQEVNELLQKFQQAQEELAEMK 869
Cdd:TIGR04523 617 KELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIR 658
Ank_4 pfam13637
Ankyrin repeats (many copies);
57-108 2.57e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 53.82  E-value: 2.57e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2462602002  57 HCFHLAAAKGHVECLRVMITHGVDVTAQDTTGHSALHLAAKNSHHECIRKLL 108
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 314-901 2.61e-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: 61.61  E-value: 2.61e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  314 FKAEISSIRENKDRLSDSTTGADSLLDISSE--ADQQDLLSLLQAKVASLTLHNKELQDKLQAKSPKEAEADLSFDSYHS 391
Cdd:TIGR02168  307 LRERLANLERQLEELEAQLEELESKLDELAEelAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRS 386

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  392 tqtdlgpslgkpgetsppdsksspsvLIHSLGKSTTDNDVRIQQLQEILQDLQKRLESSEAERKQLQVELQSRRAELVCL 471
Cdd:TIGR02168  387 --------------------------KVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQA 440

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  472 NNTEISENSSDLSQKLKETQSKYEEAMKEVLSVQ----------KQMKLGLVSPESM-DNYSHFHE-------------- 526
Cdd:TIGR02168  441 ELEELEEELEELQEELERLEEALEELREELEEAEqaldaaerelAQLQARLDSLERLqENLEGFSEgvkallknqsglsg 520

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  527 --------LRVTEE-EI---NVLKQDLQNALEEserNKEKVRELEEKLVEREKGTVI----------KPPVEEYEEMKSS 584
Cdd:TIGR02168  521 ilgvlselISVDEGyEAaieAALGGRLQAVVVE---NLNAAKKAIAFLKQNELGRVTflpldsikgtEIQGNDREILKNI 597

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  585 YCSVIENMNKEKA---------------FLFEKYQEAQEEIMKLK----------DTLKSQ--MTQeASDEAEDMKEAMN 637
Cdd:TIGR02168  598 EGFLGVAKDLVKFdpklrkalsyllggvLVVDDLDNALELAKKLRpgyrivtldgDLVRPGgvITG-GSAKTNSSILERR 676

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  638 RMIDELNKQVSELSQLYKEAQAELEDYrkRKSLEDVTAEyIHKAEHEKLMQLTNVSRAKAEDALSEMKSQyskvlNELTQ 717
Cdd:TIGR02168  677 REIEELEEKIEELEEKIAELEKALAEL--RKELEELEEE-LEQLRKELEELSRQISALRKDLARLEAEVE-----QLEER 748

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  718 LKQLVDAQKENSVSITEHLQVITTLRTAAKEMEEKISNLKEHLASKEVEVAKLEKQLLEEKAAMTDamvprssyeklqss 797
Cdd:TIGR02168  749 IAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTL-------------- 814

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  798 LESEVSVLASKLKESVKEKEKVHSEVVQIRSEVSQVKREKENIQTLLKSKEQEVNELLQKFQQAQEELAEMKRYAESSSK 877
Cdd:TIGR02168  815 LNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRS 894

                          650       660
                   ....*....|....*....|....
gi 2462602002  878 LEEDKDKKINEMSKEVTKLKEALN 901
Cdd:TIGR02168  895 ELEELSEELRELESKRSELRRELE 918
Ank_5 pfam13857
Ankyrin repeats (many copies);
173-226 2.70e-09

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 53.89  E-value: 2.70e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2462602002 173 LLDHG-ADVNSRNKSGRTALMLACEIGSSNAVEALIKKGADLNLVDSLGYNALHY 226
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDL 55
Ank_4 pfam13637
Ankyrin repeats (many copies);
157-207 2.95e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 53.82  E-value: 2.95e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2462602002 157 PLLLAVQNGHSEICHFLLDHGADVNSRNKSGRTALMLACEIGSSNAVEALI 207
Cdd:pfam13637   4 ALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 425-707 4.42e-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: 60.84  E-value: 4.42e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  425 STTDNDVRIQQLQEILQDLQKRLESSEAERKQLQVELQSRRAELVCLNNTEIsenssDLSQKLKETQSKYEEAMKEVLSV 504
Cdd:TIGR02168  671 SILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELE-----ELSRQISALRKDLARLEAEVEQL 745

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  505 QKQMKLGLVSPESMDNY---------SHFHELRVTEEEINVLKQDLQNALEESERNKEKVRELEEKLVE--------REK 567
Cdd:TIGR02168  746 EERIAQLSKELTELEAEieeleerleEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLlneeaanlRER 825

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  568 GTVIKPPVEEYEEMKSSYCSVIENMNKEKAFLFEKYQEAQEEIMKLKDTLKS-----QMTQEASDEAEDMKEAMNRMIDE 642
Cdd:TIGR02168  826 LESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEAllnerASLEEALALLRSELEELSEELRE 905

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462602002  643 LNKQVSELSQLYKEAQAELEDYRKRKS---------LEDVTAEYIHKAE-HEKLMQLTNVSRAKAEDALSEMKSQ 707
Cdd:TIGR02168  906 LESKRSELRRELEELREKLAQLELRLEglevridnlQERLSEEYSLTLEeAEALENKIEDDEEEARRRLKRLENK 980
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 60-240 5.49e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 60.08  E-value: 5.49e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  60 HLAAAKGHVECLRVMITHGVDVTAQDTTGHSALHLAAKNSHHECIRKLLQSKCPAESVDSSgktaLHYAAAQGCLQAVQI 139
Cdd:PHA02876  183 HYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINKNDLS----LLKAIRNEDLETSLL 258

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 140 LCEHKSPINLKDLDGNIPLLLAVQNGH-SEICHFLLDHGADVNSRNKSGRTALMLACEIG-SSNAVEALIKKGADLNLVD 217
Cdd:PHA02876  259 LYDAGFSVNSIDDCKNTPLHHASQAPSlSRLVPKLLERGADVNAKNIKGETPLYLMAKNGyDTENIRTLIMLGADVNAAD 338

                         170       180
                  ....*....|....*....|....
gi 2462602002 218 SLGYNALHY-SKLSENAGIQSLLL 240
Cdd:PHA02876  339 RLYITPLHQaSTLDRNKDIVITLL 362
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 74-227 6.35e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 59.69  E-value: 6.35e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  74 MITHGVDVTAQDTTGHSALHLAAKNSHH-ECIRKLLQSKCPAESVDSSGKTALHYAAAQGCLQAVQI-LCEHKSPINLKD 151
Cdd:PHA02876  293 LLERGADVNAKNIKGETPLYLMAKNGYDtENIRTLIMLGADVNAADRLYITPLHQASTLDRNKDIVItLLELGANVNARD 372

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462602002 152 LDGNIPLLLAVQNGHSEICHFLLDHGADVNSRNKSGRTALMLA-CEIGSSNAVEALIKKGADLNLVDSLGYNALHYS 227
Cdd:PHA02876  373 YCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFAlCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYA 449
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
 527-901 6.35e-09

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 59.85  E-value: 6.35e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 527 LRVTEEEINVLKQDLQNALEESERNKEKVRELEEKlverekgtvikppveeYEEMKSSYcsvienmnKEKAFLF-EKYQE 605
Cdd:PRK04778  114 LDLIEEDIEQILEELQELLESEEKNREEVEQLKDL----------------YRELRKSL--------LANRFSFgPALDE 169

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 606 AQEEIMKLKDTLkSQMTQEASD----EAEDMKEAMNRMIDELNKQVSELSQLYKEAQAELEDyrkrkSLEDVtaeyihKA 681
Cdd:PRK04778  170 LEKQLENLEEEF-SQFVELTESgdyvEAREILDQLEEELAALEQIMEEIPELLKELQTELPD-----QLQEL------KA 237

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 682 EHEKLMQ----LTNVsraKAEDALSEMKSQYSKVLNELTQLKqlVDAQKENSVSITEHLQ----VITTLRTAAKEMEEKI 753
Cdd:PRK04778  238 GYRELVEegyhLDHL---DIEKEIQDLKEQIDENLALLEELD--LDEAEEKNEEIQERIDqlydILEREVKARKYVEKNS 312

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 754 SNLKEHL--ASKEVEVAKLEKQLLEEKAAMTDAMVprSSYEKLQSSLESEVSVLaSKLKESVKEKEKVHSEVV----QIR 827
Cdd:PRK04778  313 DTLPDFLehAKEQNKELKEEIDRVKQSYTLNESEL--ESVRQLEKQLESLEKQY-DEITERIAEQEIAYSELQeeleEIL 389

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462602002 828 SEVSQVKREKENIQTLLKSKEQEVNELLQKFQQAQEELAEMKRYAESSS--KLEEDKDKKINEMSKEVTKLKEALN 901
Cdd:PRK04778  390 KQLEEIEKEQEKLSEMLQGLRKDELEAREKLERYRNKLHEIKRYLEKSNlpGLPEDYLEMFFEVSDEIEALAEELE 465
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 48-226 7.10e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 59.69  E-value: 7.10e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  48 VRARPRKLKHCFHLAAAKGH-VECLRVMITHGVDVTAQDTTGHSALHLAAK-NSHHECIRKLLQSKCPAESVDSSGKTAL 125
Cdd:PHA02876  300 VNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQASTlDRNKDIVITLLELGANVNARDYCDKTPI 379

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 126 HYAAAQGCLQAVQILCEHKSPINL--KDLDGNIPLLLAVQNGHSEIcHFLLDHGADVNSRNKSGRTALMLACEIGSS-NA 202
Cdd:PHA02876  380 HYAAVRNNVVIINTLLDYGADIEAlsQKIGTALHFALCGTNPYMSV-KTLIDRGANVNSKNKDLSTPLHYACKKNCKlDV 458

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2462602002 203 VEALIKKGADLNLVD---------SLGYNA-----LHY 226
Cdd:PHA02876  459 IEMLLDNGADVNAINiqnqyplliALEYHGivnilLHY 496
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 432-944 1.01e-08

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 59.69  E-value: 1.01e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  432 RIQQLQEILQDLQKRLESSEAERKQLQVELQSRRAELVCLNnTEISEnssdLSQKLKETQSKYEEAMKEVLSVQKQMKLG 511
Cdd:TIGR02168  233 RLEELREELEELQEELKEAEEELEELTAELQELEEKLEELR-LEVSE----LEEEIEELQKELYALANEISRLEQQKQIL 307

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  512 LVSPESMDNyshfhELRVTEEEINVLKQDLQNALEESERNKEKVRELEEKLVEREKgtVIKPPVEEYEEMKSSYCSVIEN 591
Cdd:TIGR02168  308 RERLANLER-----QLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEA--ELEELEAELEELESRLEELEEQ 380

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  592 MNKEKAFLFEKYQE---AQEEIMKLKDTLKS------QMTQEASDEAEDMKEAMnrmIDELNKQVSELSQLYKEAQAELE 662
Cdd:TIGR02168  381 LETLRSKVAQLELQiasLNNEIERLEARLERledrreRLQQEIEELLKKLEEAE---LKELQAELEELEEELEELQEELE 457

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  663 DYRKRKSLEDVTAEYIHKAEHEKLMQLTNV-SRAKAEDALSEMKSQYSKVLNELTQ-----------LKQL--VDAQKEN 728
Cdd:TIGR02168  458 RLEEALEELREELEEAEQALDAAERELAQLqARLDSLERLQENLEGFSEGVKALLKnqsglsgilgvLSELisVDEGYEA 537

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  729 SVSIT--EHLQ--VITTLRTAAKEmeekISNLKEHLASK-------EVEVAKLEKQLLEEKAAMTDAMVPRSSYEKLQSS 797
Cdd:TIGR02168  538 AIEAAlgGRLQavVVENLNAAKKA----IAFLKQNELGRvtflpldSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPK 613

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  798 LESEVSVL----------------ASKLKE-----------------SVKEKEKVHSEVVQIRSEVSQVKREKENIQTLL 844
Cdd:TIGR02168  614 LRKALSYLlggvlvvddldnalelAKKLRPgyrivtldgdlvrpggvITGGSAKTNSSILERRREIEELEEKIEELEEKI 693

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  845 KSKEQEVNELLQKFQQAQEELAEMKryaesssKLEEDKDKKINEMSKEVTKL-KEALNSLSQLSYSTSSSKRQSQQLEAL 923
Cdd:TIGR02168  694 AELEKALAELRKELEELEEELEQLR-------KELEELSRQISALRKDLARLeAEVEQLEERIAQLSKELTELEAEIEEL 766

                          570       580
                   ....*....|....*....|.
gi 2462602002  924 QQQVKQLQNQLAECKKQHQEV 944
Cdd:TIGR02168  767 EERLEEAEEELAEAEAEIEEL 787
Ank_4 pfam13637
Ankyrin repeats (many copies);
88-140 1.15e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 51.89  E-value: 1.15e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2462602002  88 GHSALHLAAKNSHHECIRKLLQSKCPAESVDSSGKTALHYAAAQGCLQAVQIL 140
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 427-894 1.74e-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: 58.59  E-value: 1.74e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  427 TDNDVRIQQLQEILQDLQKRLESSEAERKQLQVELQSRRAELVClNNTEISENSSDLSQKLKETQSKYEEAMKEVlsvqk 506
Cdd:pfam15921  274 SEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMR-QLSDLESTVSQLRSELREAKRMYEDKIEEL----- 347

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  507 QMKLGLVSPESMDNYSHFHELRVTEEEINVLKQDLQNALEESERNKEKVRELEEKLVEREKGTVIkppveeyeemkssyc 586
Cdd:pfam15921  348 EKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSI--------------- 412

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  587 sVIENMNKEkaflfekYQEAQEEIMKLKDTLKSqMTQEASDEAEDMKEAMNRMIDELNKqVSELSqlykeAQAELEDYRK 666
Cdd:pfam15921  413 -TIDHLRRE-------LDDRNMEVQRLEALLKA-MKSECQGQMERQMAAIQGKNESLEK-VSSLT-----AQLESTKEML 477

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  667 RKSLEDVTAEYIHKAEHEKLMQLTNVSRAKAEDALSEMKSQYSKV-------LNELTQLK----QLVDAQKENS---VSI 732
Cdd:pfam15921  478 RKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLrsrvdlkLQELQHLKnegdHLRNVQTECEalkLQM 557

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  733 TEHLQVITTLRTAAKEMEEKISNLKEHLASKEVEVAKLEKQLLEEKAAMTDAMVPRSSYEKLQSSLESEVSVLA------ 806
Cdd:pfam15921  558 AEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLElekvkl 637

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  807 --------SKLKESVKEKEKVHSEVVQIRSEVSQVKREKENIQTLLKSKEQEV----NELLQKFQQAQEELAEMKRYAES 874
Cdd:pfam15921  638 vnagserlRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMetttNKLKMQLKSAQSELEQTRNTLKS 717

                          490       500
                   ....*....|....*....|
gi 2462602002  875 SSKLEEDKDKKINEMSKEVT 894
Cdd:pfam15921  718 MEGSDGHAMKVAMGMQKQIT 737
PTZ00121 PTZ00121
MAEBL; Provisional
 432-921 1.79e-08

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 59.00  E-value: 1.79e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  432 RIQQLQEILQDLQKRLESSEAERKQLQVELQSRRAELVCLNNTEISENSSDLSQKLKETQSKYEEAMKEVLSVQKQMKLG 511
Cdd:PTZ00121  1225 KAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKA 1304

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  512 LVSPESMDNYSHFHELRVTEEEINVLKQDLQNALEESERNKEKVRELEEKLVEREKGTVIKppvEEYEEMKSSYCSVIEN 591
Cdd:PTZ00121  1305 DEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEK---AEAAEKKKEEAKKKAD 1381

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  592 MNKEKAFLFEKYQEAQ---EEIMKLKDTLKSQMTQEASDEAEDMKEAMNRMIDELNKQVSElSQLYKEAQAELEDYRKRK 668
Cdd:PTZ00121  1382 AAKKKAEEKKKADEAKkkaEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEE-AKKADEAKKKAEEAKKAE 1460

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  669 SLEDvTAEYIHKAEHEKLMQLTNVSRAKAEDALSEMKSQYSKVLNELTQLKQLVDAQKENSVSITEHLQVITTLRTA--A 746
Cdd:PTZ00121  1461 EAKK-KAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKAdeA 1539

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  747 KEMEEKiSNLKEHLASKEVEVAKLEKQLLEEKAAMTDAMVPRSSYEKLQSSLESEVSVLASKLKESVKEKEKVHSEVVQI 826
Cdd:PTZ00121  1540 KKAEEK-KKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEA 1618

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  827 RSEVSQVKREKENIQTLLKSKEQEVNELLQKFQQAQEELAEMKRYAESSSKLEEDKDKkinemSKEVTKLKEALNSLSQL 906
Cdd:PTZ00121  1619 KIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKK-----AEEAKKAEEDEKKAAEA 1693

                          490
                   ....*....|....*
gi 2462602002  907 SYSTSSSKRQSQQLE 921
Cdd:PTZ00121  1694 LKKEAEEAKKAEELK 1708
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
528-898 1.79e-08

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 58.51  E-value: 1.79e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 528 RVTEEEINVLKQ-DLQNALEESERNKEKVRELEEKLVErekgtvIKPPVEEYEEMKSSYCSVIENMNKekafLFEKYQEA 606
Cdd:PRK02224  180 RVLSDQRGSLDQlKAQIEEKEEKDLHERLNGLESELAE------LDEEIERYEEQREQARETRDEADE----VLEEHEER 249

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 607 QEEIMKLKDTLKSqmTQEASDEAEDMKEAMNRMIDELNKQVSELSQLYKEAQAELEdyrkrksLEDVTAEYI--HKAEHE 684
Cdd:PRK02224  250 REELETLEAEIED--LRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAG-------LDDADAEAVeaRREELE 320

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 685 KlmqltnvSRAKAEDALSEMKSQYSKVLNELTQLKQLVDAQKENSvsitehlqviTTLRTAAKEMEEKISNLKEHLASKE 764
Cdd:PRK02224  321 D-------RDEELRDRLEECRVAAQAHNEEAESLREDADDLEERA----------EELREEAAELESELEEAREAVEDRR 383

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 765 VEVAKLEKQLLEEKAAMTDAMVPRSSYEKLQSSLESEVSVLASKLKE---SVKEKEKVHSEVVQIRSE------------ 829
Cdd:PRK02224  384 EEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAEleaTLRTARERVEEAEALLEAgkcpecgqpveg 463

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 830 ------VSQVKREKENIQTLLKSKEQEVNELLQKFQQAqEELAEMKRYAES-------SSKLEEDKDKKINEMSKEVTKL 896
Cdd:PRK02224  464 sphvetIEEDRERVEELEAELEDLEEEVEEVEERLERA-EDLVEAEDRIERleerredLEELIAERRETIEEKRERAEEL 542


                  ..
gi 2462602002 897 KE 898
Cdd:PRK02224  543 RE 544
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 589-900 2.05e-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: 58.54  E-value: 2.05e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  589 IENMNKEKAFLFEKYQEAQEEIMKLKDTLK--SQMTQEASDEAEDMK---EAMNRMIDELNKQVSELSQLYKEAQAELED 663
Cdd:TIGR02169  683 LEGLKRELSSLQSELRRIENRLDELSQELSdaSRKIGEIEKEIEQLEqeeEKLKERLEELEEDLSSLEQEIENVKSELKE 762

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  664 YRKRKS-LEDVTAEYihKAEHEKLmqltnvsrakaEDALSEmkSQYSKVLNELTQLKQLVdaqkensvsitehlqvittl 742
Cdd:TIGR02169  763 LEARIEeLEEDLHKL--EEALNDL-----------EARLSH--SRIPEIQAELSKLEEEV-------------------- 807

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  743 rtaaKEMEEKISNLKEHLASKEVEVAKLEKQLLEEKAAMTDAMVPRSSYEKLQSSLESEVSVLASKLKES-------VKE 815
Cdd:TIGR02169  808 ----SRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELeaalrdlESR 883

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  816 KEKVHSEVVQIRSEVSQVKREKENIQTLLKSKEQEVNELLQKFQQAQEELAEMKR--YAESSSKLEEDKDKKINEMSKEV 893
Cdd:TIGR02169  884 LGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDpkGEDEEIPEEELSLEDVQAELQRV 963


                   ....*..
gi 2462602002  894 TKLKEAL 900
Cdd:TIGR02169  964 EEEIRAL 970
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
533-900 2.18e-08

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 58.15  E-value: 2.18e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 533 EINVLKQDLQNALEESERNKEKVRELEEKLVE-----REKGTVIKPPVEEYEEMKSSYcsvienmnKEKAFLFEKYQEAQ 607
Cdd:PRK03918  173 EIKRRIERLEKFIKRTENIEELIKEKEKELEEvlreiNEISSELPELREELEKLEKEV--------KELEELKEEIEELE 244

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 608 EEIMKLKDTLKSqmTQEASDEAEDMKEAMNRMIDELNKQVSELSQLYKEAqaelEDYRKRKSLEDVTAEYIHKAEHE--K 685
Cdd:PRK03918  245 KELESLEGSKRK--LEEKIRELEERIEELKKEIEELEEKVKELKELKEKA----EEYIKLSEFYEEYLDELREIEKRlsR 318

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 686 LMQLTNVSRAKAEDA------LSEMKSQYSKVLNELTQLKQLVDA---------------QKENSVSITEHLQVITTLRT 744
Cdd:PRK03918  319 LEEEINGIEERIKELeekeerLEELKKKLKELEKRLEELEERHELyeeakakkeelerlkKRLTGLTPEKLEKELEELEK 398

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 745 AAKEMEEKISNLKEHLASKEVEVAKLEKQLLEEKAAMTDAMVPRSSY-----EKLQSSLESEVSVLASKLKESVKEKEKV 819
Cdd:PRK03918  399 AKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELteehrKELLEEYTAELKRIEKELKEIEEKERKL 478

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 820 HSEVVQIRSEVSQVKREKENIQTL--LKSKEQEVNEL-LQKFQQAQEELAEMKRYA---ESSSKLEEDKDKKINEMSKEV 893
Cdd:PRK03918  479 RKELRELEKVLKKESELIKLKELAeqLKELEEKLKKYnLEELEKKAEEYEKLKEKLiklKGEIKSLKKELEKLEELKKKL 558


                  ....*..
gi 2462602002 894 TKLKEAL 900
Cdd:PRK03918  559 AELEKKL 565
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 424-723 2.51e-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: 2.51e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  424 KSTTDNDVRIQQLQEILQDLQKRLESSEAERKQLQVELQSRRAELvclnnteiSENSSDLSQKlKETQSKYEEAmkevls 503
Cdd:TIGR02169  716 RKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSEL--------KELEARIEEL-EEDLHKLEEA------ 780

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  504 vqkqmklgLVSPESMDNYSHFHELRVTEEEINVLKQDLQNALEESERnKEKVRELEEKLVEREKGTvIKPPVEEYEEMKS 583
Cdd:TIGR02169  781 --------LNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQ-KLNRLTLEKEYLEKEIQE-LQEQRIDLKEQIK 850

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  584 SYCSVIENMNKEKAFLFEKYQEAQEEIMKL----------KDTLKSQMT------QEASDEAEDMKEAMNRMIDELNKQV 647
Cdd:TIGR02169  851 SIEKEIENLNGKKEELEEELEELEAALRDLesrlgdlkkeRDELEAQLRelerkiEELEAQIEKKRKRLSELKAKLEALE 930

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  648 SELSQLYKEAQAELEDYRKRKSLEDVTAEYihKAEHEKLMQLTNVSR------AKAEDALSEMKSQYSKVLNELTQLKQL 721
Cdd:TIGR02169  931 EELSEIEDPKGEDEEIPEEELSLEDVQAEL--QRVEEEIRALEPVNMlaiqeyEEVLKRLDELKEKRAKLEEERKAILER 1008


                   ..
gi 2462602002  722 VD 723
Cdd:TIGR02169 1009 IE 1010
Ank_2 pfam12796
Ankyrin repeats (3 copies);
191-253 2.86e-08

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 52.04  E-value: 2.86e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462602002 191 LMLACEIGSSNAVEALIKKGADLNLVDSLGYNALHYSKLSENAGIQSLLLSKISQDADLKTPT 253
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNGRT 63
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 541-899 5.77e-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: 57.00  E-value: 5.77e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  541 LQNALEESERNKEKVRELEekLVEREKGTVIKPPVEEyeemkssycsvienmnKEKAflfEKYQEAQEEIMKLKDTLKSQ 620
Cdd:TIGR02169  172 KEKALEELEEVEENIERLD--LIIDEKRQQLERLRRE----------------REKA---ERYQALLKEKREYEGYELLK 230

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  621 MtqeasdeaedmKEAMNRMIDELNKQVSELSQLYKEAQAELEDYRKRksledvtaeyIHKAEhEKLMQLTNVSRAKAEDA 700
Cdd:TIGR02169  231 E-----------KEALERQKEAIERQLASLEEELEKLTEEISELEKR----------LEEIE-QLLEELNKKIKDLGEEE 288

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  701 LSEMKSQYSKVLNELTQLKQLVDAQKENsvsitehlqvittlrtaAKEMEEKISNLKEHLASKEVEVAKLEKQLLEEKaa 780
Cdd:TIGR02169  289 QLRVKEKIGELEAEIASLERSIAEKERE-----------------LEDAEERLAKLEAEIDKLLAEIEELEREIEEER-- 349

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  781 mtdamvprssyeKLQSSLESEVSVLASKLKESVKEKEKVHSEVVQIRSEVSQVKREKENIQtllkskeQEVNELLQKFQQ 860
Cdd:TIGR02169  350 ------------KRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLK-------REINELKRELDR 410

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|
gi 2462602002  861 AQEEL-----------AEMKRYAESSSKLEEDKDKKINEMSKEVTKLKEA 899
Cdd:TIGR02169  411 LQEELqrlseeladlnAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQL 460
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 104-176 1.23e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 55.67  E-value: 1.23e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462602002 104 IRKLLQSKCPAESVDSSGKTALHYAAAQGCLQAVQILCEHKSPINLKDLDGNIPLLLAVQNGHSEICHFLLDH 176
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 59-227 1.38e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 55.27  E-value: 1.38e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  59 FHLAAAKGHVECLRVMITHGVDVTAQDTTGHSALHLAAKNSHHECIRKLLQS--KCPAESVDSSGKTALHY--------- 127
Cdd:PHA02878   41 LHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSinKCSVFYTLVAIKDAFNNrnveifkii 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 128 ------------------AAAQGCLQA--VQILCEHKSPINLKDLD-GNIPLLLAVQNGHSEICHFLLDHGADVNSRNKS 186
Cdd:PHA02878  121 ltnrykniqtidlvyidkKSKDDIIEAeiTKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKT 200

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2462602002 187 GRTALMLACEIGSSNAVEALIKKGADLNLVDSLGYNALHYS 227
Cdd:PHA02878  201 NNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHIS 241
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 432-919 3.12e-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: 54.80  E-value: 3.12e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  432 RIQQLQEILQDLQKRLESSEAERKQLQVElqsrraelvclnNTEISENSSDLSQKLKEtqskyEEAMKEVLSVQKqmklg 511
Cdd:pfam01576   69 RKQELEEILHELESRLEEEEERSQQLQNE------------KKKMQQHIQDLEEQLDE-----EEAARQKLQLEK----- 126

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  512 lVSPESmdnyshfhELRVTEEEINVLKQDLQNALEESERNKEKVRELEEKLVEREKgtvikpPVEEYEEMKSSYCSVIEN 591
Cdd:pfam01576  127 -VTTEA--------KIKKLEEDILLLEDQNSKLSKERKLLEERISEFTSNLAEEEE------KAKSLSKLKNKHEAMISD 191

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  592 MN--------------KEKAFLFEKYQEAQEEIMKLKDTLKSQMTQEASDEAEdMKEAMNRMIDELNKQVSELSQLyKEA 657
Cdd:pfam01576  192 LEerlkkeekgrqeleKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEE-LQAALARLEEETAQKNNALKKI-REL 269

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  658 QAELEDYRkrkslEDVTAEYIHKAEHEK----LMQLTNVSRAKAEDALSEMKSQY---SKVLNELTQLKQLVDAQKENsv 730
Cdd:pfam01576  270 EAQISELQ-----EDLESERAARNKAEKqrrdLGEELEALKTELEDTLDTTAAQQelrSKREQEVTELKKALEEETRS-- 342

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  731 siteHLQVITTLR----TAAKEMEEKISNLKEHLASKEVEVAKLEKQLLEEKAAMTDAMVPRSSYEKLQSSLESEVSVLA 806
Cdd:pfam01576  343 ----HEAQLQEMRqkhtQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQ 418

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  807 SKLKESVKEKEKVHSEVVQIRSEVSQVKREKENIQTLLKSKEQEVNELLQKFQQAQEELAEMKRYAESSS----KLEEDK 882
Cdd:pfam01576  419 ARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLStrlrQLEDER 498

                          490       500       510
                   ....*....|....*....|....*....|....*..
gi 2462602002  883 DKKINEMSKEVTKLKEALNSLSQLSYSTSSSKRQSQQ 919
Cdd:pfam01576  499 NSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEE 535
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 45-181 3.23e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 53.90  E-value: 3.23e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  45 NTTVRARPRKLKHCFHLAAAK--GHVECLRVMITHGVDVTAQDTTGHSALHLAAKNSHHEC-IRKLLQSK---------- 111
Cdd:PHA03100   96 GANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDLkILKLLIDKgvdinaknrv 175

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462602002 112 -------CPAESVDSSGKTALHYAAAQGCLQAVQILCEHKSPINLKDLDGNIPLLLAVQNGHSEICHFLLDHGADVN 181
Cdd:PHA03100  176 nyllsygVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIK 252
PHA02798 PHA02798
ankyrin-like protein; Provisional
 134-242 3.48e-07

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 54.07  E-value: 3.48e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 134 LQAVQILCEHKSPINLKDLDGNIPLLLAVQN----GHS-EICHFLLDHGADVNSRNKSGRTALMLACEIGSSNAVEAL-- 206
Cdd:PHA02798   51 TDIVKLFINLGANVNGLDNEYSTPLCTILSNikdyKHMlDIVKILIENGADINKKNSDGETPLYCLLSNGYINNLEILlf 130

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2462602002 207 -IKKGADLNLVDSLGYNALH-YSKLSENAGIQ--SLLLSK 242
Cdd:PHA02798  131 mIENGADTTLLDKDGFTMLQvYLQSNHHIDIEiiKLLLEK 170
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 54-194 3.96e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 53.73  E-value: 3.96e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  54 KLKHCFHLAAAKGHVECLRVMITHGVDVTAQDTTGHSALHLAAKNSHHECIRKLLQSKCPAESVDSSGKTALHYAAAQgC 133
Cdd:PHA02878  167 KGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGY-C 245

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462602002 134 L--QAVQILCEHKSPINLKD-LDGNIPLLLAVqngHSE-ICHFLLDHGADVNSRNKSGRTALMLA 194
Cdd:PHA02878  246 KdyDILKLLLEHGVDVNAKSyILGLTALHSSI---KSErKLKLLLEYGADINSLNSYKLTPLSSA 307
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 120-231 4.14e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 53.73  E-value: 4.14e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 120 SGKTALHYAAAQGCLQAVQILCEHKSPINLKDLDGNIPLLLAVQNGHSEICHFLLDHGADVNSRNKSGRTALMLAC-EIG 198
Cdd:PHA02878  167 KGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVgYCK 246

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2462602002 199 SSNAVEALIKKGADLNLVDS-LGYNALHYSKLSE 231
Cdd:PHA02878  247 DYDILKLLLEHGVDVNAKSYiLGLTALHSSIKSE 280
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
601-901 4.18e-07

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 54.30  E-value: 4.18e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 601 EKYQEAQEEIMKLKDTLKSQMTQ-----EASDEAEDMKEAMNRMIDELNKQVSELSQLYKEAQAELEDYRKRKSLEDVTA 675
Cdd:PRK03918  158 DDYENAYKNLGEVIKEIKRRIERlekfiKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELK 237

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 676 EYIHKAEHEKLMQLTNVsrAKAEDALSEMKSQYSKVLNELTQLKQLVDAQKENSVSITEHLqvitTLRTAAKEMEEKISN 755
Cdd:PRK03918  238 EEIEELEKELESLEGSK--RKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYI----KLSEFYEEYLDELRE 311

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 756 LKEHLASKEVEVAKLEKQLLEekaamtdamvprssyeklQSSLESEVSVLASKLKESVKEKEKVhSEVVQIRSEVSQVKR 835
Cdd:PRK03918  312 IEKRLSRLEEEINGIEERIKE------------------LEEKEERLEELKKKLKELEKRLEEL-EERHELYEEAKAKKE 372

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462602002 836 EKENIQTLLKSKE-QEVNELLQKFQQAQEELAEmkryaesssKLEEDKDkKINEMSKEVTKLKEALN 901
Cdd:PRK03918  373 ELERLKKRLTGLTpEKLEKELEELEKAKEEIEE---------EISKITA-RIGELKKEIKELKKAIE 429
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
526-898 4.28e-07

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 53.89  E-value: 4.28e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 526 ELRVTEEEINVLKQDLQNALEESERNKEKVRELEEKLVEREkgtvikppvEEYEEMKSSyCSV----IENMNKEKAFLFE 601
Cdd:PRK02224  252 ELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELE---------EERDDLLAE-AGLddadAEAVEARREELED 321

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 602 KYQEAQEEIMKlkdtlKSQMTQEASDEAEDMKEAMNRMIDELNKQVSELSQLYKEAQAELEDYRKRKS-LEDVTAEYihk 680
Cdd:PRK02224  322 RDEELRDRLEE-----CRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREeIEELEEEI--- 393

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 681 AEHEKLMQLTNVSRAKAEDALSEMKSQYSKVLNELTQL--------------KQLVDAQK----ENSVSITEHLQVITtl 742
Cdd:PRK02224  394 EELRERFGDAPVDLGNAEDFLEELREERDELREREAELeatlrtarerveeaEALLEAGKcpecGQPVEGSPHVETIE-- 471

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 743 rtaakEMEEKISNLKEHLASKEVEVAKLEKQLLEEKAAmtdamvprssyeklqSSLESEVSVLASKLKESVKEKEKVHSE 822
Cdd:PRK02224  472 -----EDRERVEELEAELEDLEEEVEEVEERLERAEDL---------------VEAEDRIERLEERREDLEELIAERRET 531

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 823 VVQIRSEVSQVKREKENIQTLLKSKEQEVNELLQKFQQAQEELAEM-KRYAESSSKLE-----EDKDKKINEMSKEVTKL 896
Cdd:PRK02224  532 IEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELnSKLAELKERIEsleriRTLLAAIADAEDEIERL 611


                  ..
gi 2462602002 897 KE 898
Cdd:PRK02224  612 RE 613
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 435-869 4.43e-07

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: 53.97  E-value: 4.43e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  435 QLQEILQDLQKRLESSEAERKQ-----------------LQVELQSRRAE---LVCLNNTEISENSSDLSQKLKETQSKy 494
Cdd:pfam15921  378 QLQKLLADLHKREKELSLEKEQnkrlwdrdtgnsitidhLRRELDDRNMEvqrLEALLKAMKSECQGQMERQMAAIQGK- 456

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  495 EEAMKEVLSVQKQMKlglvSPESMdnyshfheLRVTEEEINVLKQdlqnALEESERNkekVRELEEKLVEREKGtvIKPP 574
Cdd:pfam15921  457 NESLEKVSSLTAQLE----STKEM--------LRKVVEELTAKKM----TLESSERT---VSDLTASLQEKERA--IEAT 515

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  575 VEEYEEMKSSY---CSVIENMNKEKAFLfeKYQEAQEEIMKLKDTLKSQMTQEASDEAEDMKEAMNRMIDELNKQVSELS 651
Cdd:pfam15921  516 NAEITKLRSRVdlkLQELQHLKNEGDHL--RNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKA 593

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  652 QLYKEA---QAELEDYRKRKSLEDVTAEYIHKAEHEKLMQLTNVSRAKAED--ALSEMKSQYSKVLNE-------LTQLK 719
Cdd:pfam15921  594 QLEKEIndrRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERlrAVKDIKQERDQLLNEvktsrneLNSLS 673

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  720 QLVDAQKENSVSITEHLQVITT-----LRTAAKEMEEKISNLK-----------------EHLASKEVEVAKLEK--QLL 775
Cdd:pfam15921  674 EDYEVLKRNFRNKSEEMETTTNklkmqLKSAQSELEQTRNTLKsmegsdghamkvamgmqKQITAKRGQIDALQSkiQFL 753

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  776 EEkaAMTDAMVPRSSYEKLQSSLESEVSVLASklkesvkEKEKVHSEVVQIRSEVSQVKREKENIQTLLKSKEQEVNELL 855
Cdd:pfam15921  754 EE--AMTNANKEKHFLKEEKNKLSQELSTVAT-------EKNKMAGELEVLRSQERRLKEKVANMEVALDKASLQFAECQ 824

                          490
                   ....*....|....
gi 2462602002  856 QKFQQAQEELAEMK 869
Cdd:pfam15921  825 DIIQRQEQESVRLK 838
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
525-880 5.53e-07

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 53.62  E-value: 5.53e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 525 HELRVTEEEINVLKQDLQNALEESERNKEKVRELEEKLVEREKGTVIKPPVEEYEEMKSSYCSVIENMNKEKA------F 598
Cdd:COG4717    81 KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEErleelrE 160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 599 LFEKYQEAQEEIMKLKDTLKSQMTQEASDEAEDMKEAMNRmIDELNKQVSELSQLYKEAQAELEDYRKRKSLEDVTAEYI 678
Cdd:COG4717   161 LEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEE-LEELQQRLAELEEELEEAQEELEELEEELEQLENELEAA 239

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 679 HKAEHEKLMQLTNVSRAKAEDALSEMKSQYSKVLNELTQLKqlvdaqkensVSITEHLQVITTLRTAAKEMEEKISNLKE 758
Cdd:COG4717   240 ALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLF----------LVLGLLALLFLLLAREKASLGKEAEELQA 309

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 759 HLASKEVEVAKLEKQLleekaamtdamvprssyEKLQSSLESEVSvLASKLKESVKEKEKVHSEVVQIRSEVSQVKREKE 838
Cdd:COG4717   310 LPALEELEEEELEELL-----------------AALGLPPDLSPE-ELLELLDRIEELQELLREAEELEEELQLEELEQE 371

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 2462602002 839 NIQTLLKSKEQEVNELLQKFQQAQEELAEMKRYAESSSKLEE 880
Cdd:COG4717   372 IAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEE 413
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 61-191 6.25e-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: 6.25e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  61 LAAAKGHVECLRVMIT-HGVDVTAQDTTGHSALHLAAKNSHHECIRKLLQS-----KCPAESVDSSGKTALHYAAAQGCL 134
Cdd:cd22192    23 LAAKENDVQAIKKLLKcPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAapelvNEPMTSDLYQGETALHIAVVNQNL 102

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462602002 135 QAVQIL---------------CEHKSPINLKDLdGNIPLLLAVQNGHSEICHFLLDHGADVNSRNKSGRTAL 191
Cdd:cd22192   103 NLVRELiargadvvspratgtFFRPGPKNLIYY-GEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVL 173
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 85-229 6.87e-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: 6.87e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  85 DTTGHSALHLAAKNSHHECIRKLLQSKCPAESVdssGKTALHyAAAQGCLQAVQILCEHKSPINLKDLD----------- 153
Cdd:TIGR00870  49 DRLGRSALFVAAIENENLELTELLLNLSCRGAV---GDTLLH-AISLEYVDAVEAILLHLLAAFRKSGPlelandqytse 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 154 ---GNIPLLLAVQNGHSEICHFLLDHGADVNSRNKS--------------GRTALMLACEIGSSNAVEALIKKGADLNLV 216
Cdd:TIGR00870 125 ftpGITALHLAAHRQNYEIVKLLLERGASVPARACGdffvksqgvdsfyhGESPLNAAACLGSPSIVALLSEDPADILTA 204

                         170
                  ....*....|...
gi 2462602002 217 DSLGYNALHYSKL 229
Cdd:TIGR00870 205 DSLGNTLLHLLVM 217
46 PHA02562
endonuclease subunit; Provisional
 556-776 8.05e-07

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 53.09  E-value: 8.05e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 556 RELEEKLVE----REKGTVIKPPVEE-YEEMKSsyCSVIENMNKEKAFLFEKYQEAQEEIMKLKDTLKSQMTQEASDEAE 630
Cdd:PHA02562  153 RKLVEDLLDisvlSEMDKLNKDKIRElNQQIQT--LDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAK 230

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 631 DMKEAMNRMIDELNKQVSELSQlYKEAQAELEDYRKRKSLEDVTAEYIHK---------------AEHEKLMQltnvsra 695
Cdd:PHA02562  231 TIKAEIEELTDELLNLVMDIED-PSAALNKLNTAAAKIKSKIEQFQKVIKmyekggvcptctqqiSEGPDRIT------- 302

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 696 KAEDALSEMKSQYSKVLNELTQLKQLVDAQKENSVSITE-------HLQVITTLRTAAKEMEEKISNLKEHLASKEVEVA 768
Cdd:PHA02562  303 KIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSKKLLElknkistNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELA 382


                  ....*...
gi 2462602002 769 KLEKQLLE 776
Cdd:PHA02562  383 KLQDELDK 390
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 153-185 8.10e-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: 8.10e-07
                          10        20        30
                  ....*....|....*....|....*....|....
gi 2462602002 153 DGNIPLLLAV-QNGHSEICHFLLDHGADVNSRNK 185
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
PTZ00121 PTZ00121
MAEBL; Provisional
 444-895 8.24e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 53.22  E-value: 8.24e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  444 QKRLESSEAERKQLQVELQSRRAELVclNNTEISENSSDLSQKLKETQSKYEEAMKEVLSVQKQMKLglvspESMDNYSH 523
Cdd:PTZ00121  1451 KKAEEAKKAEEAKKKAEEAKKADEAK--KKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEA-----KKAEEAKK 1523

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  524 FHELRVTEEEINVlkQDLQNAleESERNKEKVRELEEKLVEREKGTVIKPPVEEYEEmkssycsvieNMNKEKAFLFEKY 603
Cdd:PTZ00121  1524 ADEAKKAEEAKKA--DEAKKA--EEKKKADELKKAEELKKAEEKKKAEEAKKAEEDK----------NMALRKAEEAKKA 1589

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  604 QEAQ-EEIMKLKDTLKSQMTQEASDEAEDMKEAMN-RMIDELNKQVSELSQLYKEAQAELEDYRKRKSLEDVTAEYIHKA 681
Cdd:PTZ00121  1590 EEARiEEVMKLYEEEKKMKAEEAKKAEEAKIKAEElKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKK 1669

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  682 EHEKlmqltnvsRAKAEDALSEMKSQYSKvlneltqlkqlvdaqKENSVSITEHLQVITTLRTAAKEMEEKISNLKEHLA 761
Cdd:PTZ00121  1670 AEED--------KKKAEEAKKAEEDEKKA---------------AEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEE 1726

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  762 SKEVEVAKLEKQLLEEKAAMTDAMVPRSSYEKLQ--SSLESEVSVLASKLKESVKE---KEKVHSEVVQIRSEVSQVKRE 836
Cdd:PTZ00121  1727 ENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAhlKKEEEKKAEEIRKEKEAVIEeelDEEDEKRRMEVDKKIKDIFDN 1806

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  837 KENIQTLLKSKEQEVNELLQKFQQAQEELAEMKRYA-ESSSKLEEDKDKKINEMSKEVTK 895
Cdd:PTZ00121  1807 FANIIEGGKEGNLVINDSKEMEDSAIKEVADSKNMQlEEADAFEKHKFNKNNENGEDGNK 1866
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 432-943 1.05e-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: 53.05  E-value: 1.05e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  432 RIQQLQEILQDLQKRLESSEAERKQLQVE-------LQSRRAE---LVCLNNTEISENSSDLSQKLKETQSKYEEAMKEV 501
Cdd:TIGR00618  380 HIHTLQQQKTTLTQKLQSLCKELDILQREqatidtrTSAFRDLqgqLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKI 459

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  502 LSVQKQMKLglvsPESMDNYSHFHELRVTEEEINVLKQDLQNALEESERN-KEKVRELEEKLVEREKGTVIKPPVEEYEE 580
Cdd:TIGR00618  460 HLQESAQSL----KEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPlCGSCIHPNPARQDIDNPGPLTRRMQRGEQ 535

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  581 MKSSYCSVIENMNKEKAFLFEKYQEAQEEIMKLKDTLK--SQMTQEASDEAEDMKEAMNRMIDELNKQVSELSQLYKEAQ 658
Cdd:TIGR00618  536 TYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSilTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQH 615

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  659 AELEDYRKRKSLEDVTAEYIHKAEHEKLMQLtnvsrAKAEDALSEMKSQYSKVLNELTQLKQLVDAQKENSVSITEHLQv 738
Cdd:TIGR00618  616 ALLRKLQPEQDLQDVRLHLQQCSQELALKLT-----ALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEK- 689

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  739 itTLRTAAKEMEEKISNLKEHLASKEVEVAKLEKQLleekaamtdamvprssyEKLQSSLESEVSVLASKLKESVKEKEK 818
Cdd:TIGR00618  690 --EQLTYWKEMLAQCQTLLRELETHIEEYDREFNEI-----------------ENASSSLGSDLAAREDALNQSLKELMH 750

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  819 VHSEVVQIRSEVSQVKREKENIQTLLKSKEQEVNELLQKFQQAQEE----LAEMKryAESSSKLEEDKDKKINEMSKEVT 894
Cdd:TIGR00618  751 QARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEdthlLKTLE--AEIGQEIPSDEDILNLQCETLVQ 828

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*....
gi 2462602002  895 KLKEALNSLSQLSYSTSSSKRQSQQLEalqqqvkqlqnqlaECKKQHQE 943
Cdd:TIGR00618  829 EEEQFLSRLEEKSATLGEITHQLLKYE--------------ECSKQLAQ 863
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 430-610 1.44e-06

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 50.31  E-value: 1.44e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 430 DVRIQQLQEILQDLQKRLESSEAERKQLQVELQSRRAELVCLNnTEISENSSDLSQkLKETQSKYEEAMKEVLSvQKQMK 509
Cdd:COG1579    16 DSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLE-KEIKRLELEIEE-VEARIKKYEEQLGNVRN-NKEYE 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 510 LGLvspesmdnyshfHELRVTEEEINVLKQDLQNALEESERNKEKVRELEEKLVEREkgtvikppvEEYEEMKSSYCSVI 589
Cdd:COG1579    93 ALQ------------KEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELE---------AELEEKKAELDEEL 151

                         170       180
                  ....*....|....*....|.
gi 2462602002 590 ENMNKEKAFLFEKYQEAQEEI 610
Cdd:COG1579   152 AELEAELEELEAEREELAAKI 172
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 751-944 1.72e-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: 52.37  E-value: 1.72e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  751 EKISNLKEHLASKEVEVAKLEKQLLEEKaamtdamvprssyeklQSSLESEVSVLASKLKESVKEKEKVHSEVVQIRSEV 830
Cdd:TIGR02168  213 ERYKELKAELRELELALLVLRLEELREE----------------LEELQEELKEAEEELEELTAELQELEEKLEELRLEV 276

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  831 SQVKREKENIQTLLKSKEQEVNELLQKFQQAQEELAEMKRYAESSSKLEEDKDKKINEMSKEVTKLKEALNslsqlsYST 910
Cdd:TIGR02168  277 SELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLE------ELK 350

                          170       180       190
                   ....*....|....*....|....*....|....
gi 2462602002  911 SSSKRQSQQLEALQQQVKQLQNQLAECKKQHQEV 944
Cdd:TIGR02168  351 EELESLEAELEELEAELEELESRLEELEEQLETL 384
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 589-822 2.55e-06

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 50.98  E-value: 2.55e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 589 IENMNKEKAFLFEKYQEAQEEIMKLKDTLKSqmTQEASDEAEDMKEAMNRMIDELNKQVSELSQLYKEAQAELEDYrkrk 668
Cdd:COG3883    18 IQAKQKELSELQAELEAAQAELDALQAELEE--LNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER---- 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 669 sledVTAEYIHKAEHEKLMQLTN-------VSRAkaeDALSEMKSQYSKVLNELTQLKQLVDAQKENSVsitehlQVITT 741
Cdd:COG3883    92 ----ARALYRSGGSVSYLDVLLGsesfsdfLDRL---SALSKIADADADLLEELKADKAELEAKKAELE------AKLAE 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 742 LRTAAKEMEEKISNLKEHLASKEVEVAKLEKQLLEEKAAMTDAMVPRSSYEKLQSSLESEVSVLASKLKESVKEKEKVHS 821
Cdd:COG3883   159 LEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 238


                  .
gi 2462602002 822 E 822
Cdd:COG3883   239 A 239
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 129-208 3.23e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 51.05  E-value: 3.23e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 129 AAQGCLQAVQILCEHKSPINLKDLDGNIPLLLAVQNGHSEICHFLLDHGADVNSRNKSGRTALMLACEIGSSNAVEALIK 208
Cdd:PTZ00322   90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169
Ank_5 pfam13857
Ankyrin repeats (many copies);
147-194 3.74e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 45.03  E-value: 3.74e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2462602002 147 INLKDLDGNIPLLLAVQNGHSEICHFLLDHGADVNSRNKSGRTALMLA 194
Cdd:pfam13857   9 LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_5 pfam13857
Ankyrin repeats (many copies);
118-161 3.97e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 45.03  E-value: 3.97e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 2462602002 118 DSSGKTALHYAAAQGCLQAVQILCEHKSPINLKDLDGNIPLLLA 161
Cdd:pfam13857  13 DGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTZ00121 PTZ00121
MAEBL; Provisional
 526-981 4.17e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 50.91  E-value: 4.17e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  526 ELRVTEEeinVLKQDLQNALEESERNKEKVRELEEKLVEREKGTVIKPPVEEYEEMKSSYCSVIENMNKEKAFLFEKYQE 605
Cdd:PTZ00121  1186 EVRKAEE---LRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARM 1262

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  606 AQEEIMKLKDTLKSQMTQEASDEAEDMKEAMNRMIDELNKQVSELSQLYKEAQAELEDYRKRKSLEDVTAEYIHKAEHEK 685
Cdd:PTZ00121  1263 AHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAK 1342

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  686 lmQLTNVSRAKAEDALSEMKSQYSKvlNELTQLKQLVDAQK-ENSVSITEHLQVITTLRTAAKEMEEKISNLKEHLASKE 764
Cdd:PTZ00121  1343 --KAAEAAKAEAEAAADEAEAAEEK--AEAAEKKKEEAKKKaDAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKK 1418

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  765 vEVAKLEKQLLEEKAAmtdamvprssyEKLQSSLESEVSvlASKLKESVKEKEKVHsevvqirsEVSQVKREKENIQTLL 844
Cdd:PTZ00121  1419 -KADEAKKKAEEKKKA-----------DEAKKKAEEAKK--ADEAKKKAEEAKKAE--------EAKKKAEEAKKADEAK 1476

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  845 KSKEQ--EVNELLQKFQQAQEELAEMKRYAESSSKLEEDKDKkinEMSKEVTKLKEALNSLSQLSYSTSSSKRQSQQLEA 922
Cdd:PTZ00121  1477 KKAEEakKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKA---EEAKKADEAKKAEEAKKADEAKKAEEKKKADELKK 1553

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462602002  923 LQQQVKQLQNQLAECKKQHQE--VISVYRMHLLYAVQGQMDEDVQKVLKQILTMCKNQSQK 981
Cdd:PTZ00121  1554 AEELKKAEEKKKAEEAKKAEEdkNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKK 1614
PHA02798 PHA02798
ankyrin-like protein; Provisional
 69-242 4.62e-06

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 50.22  E-value: 4.62e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  69 ECLRVMITHGVDVTAQDTTGHSALHLAAKNSHH---ECIRKLLQSKCPAESVDSS-GKTALHyaaaqgclqavqilCEHK 144
Cdd:PHA02798  126 EILLFMIENGADTTLLDKDGFTMLQVYLQSNHHidiEIIKLLLEKGVDINTHNNKeKYDTLH--------------CYFK 191

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 145 SPINLKDLDgniplllavqnghseICHFLLDHGADVNSRNKSGRTALM--LACEIGSSNAVEA----LIKKGADLNLVDS 218
Cdd:PHA02798  192 YNIDRIDAD---------------ILKLFVDNGFIINKENKSHKKKFMeyLNSLLYDNKRFKKnildFIFSYIDINQVDE 256

                         170       180
                  ....*....|....*....|....
gi 2462602002 219 LGYNALHYSKLSENAGIQSLLLSK 242
Cdd:PHA02798  257 LGFNPLYYSVSHNNRKIFEYLLQL 280
Ank_5 pfam13857
Ankyrin repeats (many copies);
74-128 5.07e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 44.64  E-value: 5.07e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462602002  74 MITHG-VDVTAQDTTGHSALHLAAKNSHHECIRKLLQSKCPAESVDSSGKTALHYA 128
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
423-872 5.15e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 50.54  E-value: 5.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 423 GKSTTDNDVRIQQLQEILqdlqKRLESSEAERKQLQVELQSRRAELvclnnTEISENSSDLSQKLK--ETQSKYEEAMKE 500
Cdd:COG4717    63 GRKPELNLKELKELEEEL----KEAEEKEEEYAELQEELEELEEEL-----EELEAELEELREELEklEKLLQLLPLYQE 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 501 VLSVQKQMKlglvspesmDNYSHFHELRVTEEEINVLKQDLQNALEESERNKEKVRELEEKLVEREKGTvIKPPVEEYEE 580
Cdd:COG4717   134 LEALEAELA---------ELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEE-LQDLAEELEE 203

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 581 MKSSycsvIENMNKEKAFLFEKYQEAQEEIMKLKDTLKSQMTQEASDEAEDMKEAMNRMIDELNKQVSELSQLYKEAQA- 659
Cdd:COG4717   204 LQQR----LAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVl 279

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 660 ----------ELEDYRKRKSLEDVTAEYIHKAEHEKLMQLtNVSRAKAEDALSEM--KSQYSKVLNELTQLKQLVD--AQ 725
Cdd:COG4717   280 flvlgllallFLLLAREKASLGKEAEELQALPALEELEEE-ELEELLAALGLPPDlsPEELLELLDRIEELQELLReaEE 358

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 726 KENSVSITEHLQVITTLRTAAK----EMEEKISNLKEHLASKEVEVAKLEKQLLEEKAAMTDAMVPRSsyeklQSSLESE 801
Cdd:COG4717   359 LEEELQLEELEQEIAALLAEAGvedeEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALD-----EEELEEE 433

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462602002 802 VSVLASKLKESVKEKEKVHSEVVQIRSEVSQVKrekeniqtllksKEQEVNELLQKFQQAQEELAEM-KRYA 872
Cdd:COG4717   434 LEELEEELEELEEELEELREELAELEAELEQLE------------EDGELAELLQELEELKAELRELaEEWA 493
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
624-893 5.38e-06

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 49.52  E-value: 5.38e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 624 EASDEAEDMKEAMNRMIDELNKQVSELSQLYKEAQAELEDYR-KRKSLEDVTAEYIHKA-EHEKLMQLTNVSRAKAEDAL 701
Cdd:COG1340     1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAeKRDELNAQVKELREEAqELREKRDELNEKVKELKEER 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 702 SEMKSQYSKVLNELTQLKQLVDAQKENSVSITEHLQVI--------TTLRTAAKEME--EKISNLKEHLASKEvEVAKLE 771
Cdd:COG1340    81 DELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIerlewrqqTEVLSPEEEKElvEKIKELEKELEKAK-KALEKN 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 772 KQLLEEKAAMTDAMVPRSSYEKlqsslesevsvlasKLKESVKEKEKVHSEVVQIRSEVSQVKREKENIQTLLKSKEQEV 851
Cdd:COG1340   160 EKLKELRAELKELRKEAEEIHK--------------KIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKA 225

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 2462602002 852 NELLQKFQQAQEELAEM----KRYAESSSKLEEDKDKKINEMSKEV 893
Cdd:COG1340   226 DELHEEIIELQKELRELrkelKKLRKKQRALKREKEKEELEEKAEE 271
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 345-669 6.35e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 50.44  E-value: 6.35e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  345 ADQQDLLSLLQAKVASLtlhNKELQDKLQAKSPKEAEADLSFDSYHSTQTDLGpslgkpgetSPPDSKSSPSVLIHSLGK 424
Cdd:TIGR02168  687 EELEEKIAELEKALAEL---RKELEELEEELEQLRKELEELSRQISALRKDLA---------RLEAEVEQLEERIAQLSK 754

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  425 STTDNDVRIQQLQEILQDLQKRLESSEAERKQLQVELQSRRAELvclnnTEISENSSDLSQKLKETQSKYEEAMKEVLSV 504
Cdd:TIGR02168  755 ELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEEL-----KALREALDELRAELTLLNEEAANLRERLESL 829

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  505 QKQMKLGLVSPESMDNyshfhELRVTEEEInvlkQDLQNALEESERNKEKV-RELEEKLVEREKGTV-IKPPVEEYEEMK 582
Cdd:TIGR02168  830 ERRIAATERRLEDLEE-----QIEELSEDI----ESLAAEIEELEELIEELeSELEALLNERASLEEaLALLRSELEELS 900

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  583 SSycsvIENMNKEKAFLFEKYQEAQEEIMKLK----------DTLKSQMTQEASDEAEDMKEAMN----------RMIDE 642
Cdd:TIGR02168  901 EE----LRELESKRSELRRELEELREKLAQLElrleglevriDNLQERLSEEYSLTLEEAEALENkieddeeearRRLKR 976

                          330       340
                   ....*....|....*....|....*..
gi 2462602002  643 LNKQVSELSQLYKEAQAELEDYRKRKS 669
Cdd:TIGR02168  977 LENKIKELGPVNLAAIEEYEELKERYD 1003
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 151-261 6.50e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 50.28  E-value: 6.50e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 151 DLDGNIPLLLAVqnghsEICHF-----------LLDHGADVNSRNKSGRTALMLACEIGSSNAVEALIKKGADLNLVDSL 219
Cdd:PTZ00322   73 VIDPVVAHMLTV-----ELCQLaasgdavgariLLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKD 147

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2462602002 220 GYNALHYSKLSENAGIQSLLLSKISQDADLKTPTKPKQHDQV 261
Cdd:PTZ00322  148 GKTPLELAEENGFREVVQLLSRHSQCHFELGANAKPDSFTGK 189
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 432-675 6.98e-06

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 49.38  E-value: 6.98e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 432 RIQQLQEILQDLQKRLESSEAERKQLQVELQSRRAELVCLNNT--EISENSSDLSQKLKETQSKYEEAMKEVLSVQKQMK 509
Cdd:COG4942    28 ELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRirALEQELAALEAELAELEKEIAELRAELEAQKEELA 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 510 LGLVSPESMDNYSHFhELRVTEEEINVLKQDLQNALEESERNKEKVRELEEKLverekgtvikppvEEYEEMKSSycsvI 589
Cdd:COG4942   108 ELLRALYRLGRQPPL-ALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADL-------------AELAALRAE----L 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 590 ENMNKEKAFLFEKYQEAQEEIMKLKDTLKSQMTQEASDEAEDMKEamnrmIDELNKQVSELSQLYKEAQAELEDYRKRKS 669
Cdd:COG4942   170 EAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAE-----LAELQQEAEELEALIARLEAEAAAAAERTP 244


                  ....*.
gi 2462602002 670 LEDVTA 675
Cdd:COG4942   245 AAGFAA 250
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 436-882 7.16e-06

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


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 50.11  E-value: 7.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 436 LQEILQDLQKRLESSEAERKQLQVELQSRRAELVCLnnTEISENSSDLSQKLKETQSKYEEAMKEVLSVQKQMKlglvsp 515
Cdd:pfam05483 361 LEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEM--TKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAE------ 432

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 516 esmdnyshfhELRVTEEEINVLKQDLQNALEESERNKEKVRELEE---KLVEREKGTVIKPPVEEYEEMKSSYCSVIEN- 591
Cdd:pfam05483 433 ----------ELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEhylKEVEDLKTELEKEKLKNIELTAHCDKLLLENk 502

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 592 -MNKEKAFLFEKYQEAQEEIMKLKDTLKSQMTQeasdeAEDMKEAMNRMIDELNKQVSELSQLYKEAQAELEdyrkrKSL 670
Cdd:pfam05483 503 eLTQEASDMTLELKKHQEDIINCKKQEERMLKQ-----IENLEEKEMNLRDELESVREEFIQKGDEVKCKLD-----KSE 572

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 671 EDVTAEYIHKAEHEKLMQLTnvsrakaEDALSEMKSQYSKVLNELTQLKQLVDAQKENSVSITEHLQVITT--------L 742
Cdd:pfam05483 573 ENARSIEYEVLKKEKQMKIL-------ENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIkvnkleleL 645

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 743 RTAAKEMEEKISNLKEHLASKEVEVAKLEKQLLEEKAAMTDAMVPRSSYEKLQSSLESEVSVLASKLKESV-KEKEKVHS 821
Cdd:pfam05483 646 ASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYdKIIEERDS 725

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462602002 822 EVVQIRSEVSQVKREKENIQTLLKSKEQEVNELLQKFQQAQEELAEMKRYAESSSKLEEDK 882
Cdd:pfam05483 726 ELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTAILKDK 786
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
 552-800 1.01e-05

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 49.54  E-value: 1.01e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 552 KEKVRELEEKLVEREKGTVIKPPVEEYEEmksSYCSVIENMNK--EKAFLFEKYQEAQEEIMKLKDTLKSQMTQEASDEA 629
Cdd:PRK05771   15 KSYKDEVLEALHELGVVHIEDLKEELSNE---RLRKLRSLLTKlsEALDKLRSYLPKLNPLREEKKKVSVKSLEELIKDV 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 630 EDMKEAMNRMIDELNKQVSEL----SQLYKEAQA---------ELEDYRKRKSLeDVTAEYIHKAEHEKLMQLTN----- 691
Cdd:PRK05771   92 EEELEKIEKEIKELEEEISELeneiKELEQEIERlepwgnfdlDLSLLLGFKYV-SVFVGTVPEDKLEELKLESDvenve 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 692 -VSRAKAED-----ALSEMKSQYSKVLNELTQLKQLVDAQKENSVSITEHLQVITTLRTAAKEMEEKISNLKEH-----L 760
Cdd:PRK05771  171 yISTDKGYVyvvvvVLKELSDEVEEELKKLGFERLELEEEGTPSELIREIKEELEEIEKERESLLEELKELAKKyleelL 250

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 2462602002 761 ASKEVEVAKLEKQLLEEKAAMTD------AMVPRSSYEKLQSSLES 800
Cdd:PRK05771  251 ALYEYLEIELERAEALSKFLKTDktfaieGWVPEDRVKKLKELIDK 296
Ank_5 pfam13857
Ankyrin repeats (many copies);
37-95 1.25e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.49  E-value: 1.25e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462602002  37 ARRGPVPPNTTvrarPRKLKHCFHLAAAKGHVECLRVMITHGVDVTAQDTTGHSALHLA 95
Cdd:pfam13857   2 LEHGPIDLNRL----DGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 153-181 1.29e-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: 1.29e-05
                           10        20
                   ....*....|....*....|....*....
gi 2462602002  153 DGNIPLLLAVQNGHSEICHFLLDHGADVN 181
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 433-870 1.46e-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: 49.27  E-value: 1.46e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  433 IQQLQEILQDLQKRLESSEAERKQLQVELQSRRAELVCLNNTEISENSS-DLSQKLKETQSKYEEAMKE--VLSVQKQMK 509
Cdd:TIGR00606  586 INQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSqDEESDLERLKEEIEKSSKQraMLAGATAVY 665

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  510 LGLVSPESMDNYSHF---HELRVTEEEINVLKQDLQNALEESERNKEKVRELEEKLVEREKGTVIKPPVEEyeemkssyc 586
Cdd:TIGR00606  666 SQFITQLTDENQSCCpvcQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQ--------- 736

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  587 SVIENMNKEKAFLFEKYQEAQEEIMKLKDTLKSQMTQ----EASDEAEDMKEAMNRMIDELNKQVSELSQLYKEAQAELE 662
Cdd:TIGR00606  737 SIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLlgtiMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQ 816

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  663 DYRKRKSLEDVTAEYIHKAEH-----------EKLMQLTNVSRAKAEDALSEMKSQYSKVLNELTQLKQLVDAQKENSVS 731
Cdd:TIGR00606  817 GSDLDRTVQQVNQEKQEKQHEldtvvskielnRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTE 896

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  732 ITEHLQVI-----------TTLRTAAKEMEEKISNLKEHLASKEVEVAKLEKQLLEEKAAMTDAM-VPRSSYEKLQSSLE 799
Cdd:TIGR00606  897 VQSLIREIkdakeqdspleTFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIEnKIQDGKDDYLKQKE 976

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  800 SEVSVLASKLKESVKEKEKVHSEVVQIRSEV--------------------SQVKREKENIQTLLKS-KEQEVNELLQKF 858
Cdd:TIGR00606  977 TELNTVNAQLEECEKHQEKINEDMRLMRQDIdtqkiqerwlqdnltlrkreNELKEVEEELKQHLKEmGQMQVLQMKQEH 1056

                          490
                   ....*....|..
gi 2462602002  859 QQAQEELAEMKR 870
Cdd:TIGR00606 1057 QKLEENIDLIKR 1068
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
 697-869 1.54e-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: 48.13  E-value: 1.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 697 AEDALSEMKSQYSKVLNELTQLKQLVDaQKENSVSITEHLQVITTLRTAAKEMEEKISNLKEHLASKEVEVAKLEKQLLE 776
Cdd:cd22656    82 AQNAGGTIDSYYAEILELIDDLADATD-DEELEEAKKTIKALLDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQTALET 160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 777 EKAAMTD------AMVPRSSYEKLQSSLESEVSVLASKLKESVKEKEKvhsevvQIRSEVSQVKREKeNIQTLLKSKEQE 850
Cdd:cd22656   161 LEKALKDlltdegGAIARKEIKDLQKELEKLNEEYAAKLKAKIDELKA------LIADDEAKLAAAL-RLIADLTAADTD 233

                         170
                  ....*....|....*....
gi 2462602002 851 VNELLQKFQQAQEELAEMK 869
Cdd:cd22656   234 LDNLLALIGPAIPALEKLQ 252
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 630-936 1.74e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.78  E-value: 1.74e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 630 EDMKEAMNR---MIDELNKQVSELsqlykEAQAEL-EDYRK-RKSLEDVTAEYIHKAEHEKLMQLtnvsrAKAEDALSEM 704
Cdd:COG1196   182 EATEENLERledILGELERQLEPL-----ERQAEKaERYRElKEELKELEAELLLLKLRELEAEL-----EELEAELEEL 251

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 705 KSQyskvLNELTQLKQLVDAQKEnsvsitehlqvitTLRTAAKEMEEKISNLKEHLASKEVEVAKLEKQlleekaamtda 784
Cdd:COG1196   252 EAE----LEELEAELAELEAELE-------------ELRLELEELELELEEAQAEEYELLAELARLEQD----------- 303

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 785 mvpRSSYEKLQSSLESEVSVLASKLKESVKEKEKVHSEVVQIRSEVSQVKREKENIQTLLKSKEQEVNELLQKFQQAQEE 864
Cdd:COG1196   304 ---IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE 380

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462602002 865 LAEMKR-YAESSSKLEEDKDKKINEMSKEVTKLKEALNSLSQLSYSTSSSKRQSQQLEALQQQVKQLQNQLAE 936
Cdd:COG1196   381 LEELAEeLLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAE 453
PTZ00121 PTZ00121
MAEBL; Provisional
 551-944 1.94e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.98  E-value: 1.94e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  551 NKEKVRELEEK------LVEREkgtVIKPPVEEYEEMKSSYCSVIENMNKEKAFLFEKyqeaqeEIMKLKDTLKSQMTQE 624
Cdd:PTZ00121  1025 NIEKIEELTEYgnnddvLKEKD---IIDEDIDGNHEGKAEAKAHVGQDEGLKPSYKDF------DFDAKEDNRADEATEE 1095

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  625 ASDEAEDMKEAMNRMIDELNKQvselsqlyKEAQAELEDYRK----RKSLEDVTAEYIHKAEHEKLMQLTNvsraKAEDA 700
Cdd:PTZ00121  1096 AFGKAEEAKKTETGKAEEARKA--------EEAKKKAEDARKaeeaRKAEDARKAEEARKAEDAKRVEIAR----KAEDA 1163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  701 LSEMKSQYSKVLNELTQLKQLVDAQKENSVSITEHLQVITTLRTAakEMEEKISNLKEHLASKEVEVAKLEKQLLEEKAA 780
Cdd:PTZ00121  1164 RKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKA--EEERKAEEARKAEDAKKAEAVKKAEEAKKDAEE 1241

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  781 MTDAMVPRSSYEKLQssLESEVSVLASKLKESVKEKEKVHSEVVQIRSEVSqvkrekeniqtllKSKEQEVNELLQKFQQ 860
Cdd:PTZ00121  1242 AKKAEEERNNEEIRK--FEEARMAHFARRQAAIKAEEARKADELKKAEEKK-------------KADEAKKAEEKKKADE 1306

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  861 AQEELAEMKRYAESSSKLEEDKDKKINEMSKEVTKLKEALNSLSQLSYSTSSSKRQSQQLEALQQQVKQLQNQLAECKKQ 940
Cdd:PTZ00121  1307 AKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKK 1386


                   ....
gi 2462602002  941 HQEV 944
Cdd:PTZ00121  1387 AEEK 1390
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 421-900 2.91e-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: 48.30  E-value: 2.91e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  421 SLGKSTTDNDVRIQQLQEILQDLQKRLESseaERKQLQVELQSRRAELvclnNTEISENSSDLSQK------LKETQSKY 494
Cdd:pfam12128  262 HLHFGYKSDETLIASRQEERQETSAELNQ---LLRTLDDQWKEKRDEL----NGELSAADAAVAKDrseleaLEDQHGAF 334

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  495 EEAMKEVLSvQKQMKLGLVSPEsMDNYSHFHELRVT-----EEEINVLKQDLqnaleeSERNKEKVRELEEKLVEREKGT 569
Cdd:pfam12128  335 LDADIETAA-ADQEQLPSWQSE-LENLEERLKALTGkhqdvTAKYNRRRSKI------KEQNNRDIAGIKDKLAKIREAR 406

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  570 VIKPPVEE--YEEMKSSYCSVIENMNKEkaflfekYQEAQEEIMKLKDTLKSQMTQEASDEAEDMKEAMNrmIDELNKQV 647
Cdd:pfam12128  407 DRQLAVAEddLQALESELREQLEAGKLE-------FNEEEYRLKSRLGELKLRLNQATATPELLLQLENF--DERIERAR 477

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  648 SELSQLYKE---AQAELEDYRKRKSLEDVTAEYIHKAEHE---KLMQLTNVSRAKAEDALSEMKSQ-------YSKVLN- 713
Cdd:pfam12128  478 EEQEAANAEverLQSELRQARKRRDQASEALRQASRRLEErqsALDELELQLFPQAGTLLHFLRKEapdweqsIGKVISp 557

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  714 EL---TQLKQLVD----AQKENSVSITEHLQVI---------TTLRTAAKEMEEKISNLKEHLASKEVEVAKLEKQLLEE 777
Cdd:pfam12128  558 ELlhrTDLDPEVWdgsvGGELNLYGVKLDLKRIdvpewaaseEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKA 637

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  778 KAAMTDAMVPRSSYEKLQSSLESEVSVLASKLKESVKE-KEKVHSEVVQIRSEVSQVKREkenIQTLLKSKEQEVNELLQ 856
Cdd:pfam12128  638 SREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAErKDSANERLNSLEAQLKQLDKK---HQAWLEEQKEQKREART 714

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....
gi 2462602002  857 KFQQAQEElaemkryaessskLEEDKDKKINEMSKEVTKLKEAL 900
Cdd:pfam12128  715 EKQAYWQV-------------VEGALDAQLALLKAAIAARRSGA 745
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
 661-901 3.57e-05

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 47.61  E-value: 3.57e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 661 LEDYRKRksledvTAEYIHKaehEKLMQLTNVSRAKAEDALSEMKSQYSKVLNELTQLKQLVDAQK-----ENSVSITEH 735
Cdd:PRK05771   14 LKSYKDE------VLEALHE---LGVVHIEDLKEELSNERLRKLRSLLTKLSEALDKLRSYLPKLNplreeKKKVSVKSL 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 736 LQVITTLRTAAKEMEEKISNLKEHLASKEVEVAKLEKQLLEEKaamtdamvprsSYEKLQSSLESE-----VSVLASKLK 810
Cdd:PRK05771   85 EELIKDVEEELEKIEKEIKELEEEISELENEIKELEQEIERLE-----------PWGNFDLDLSLLlgfkyVSVFVGTVP 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 811 ESVKEKEKVHSEVvqirsEVSQVKREKENIQTL----LKSKEQEVNELLQKFQQAQEELAEMKRYAESSSKLEEdkdkKI 886
Cdd:PRK05771  154 EDKLEELKLESDV-----ENVEYISTDKGYVYVvvvvLKELSDEVEEELKKLGFERLELEEEGTPSELIREIKE----EL 224

                         250
                  ....*....|....*
gi 2462602002 887 NEMSKEVTKLKEALN 901
Cdd:PRK05771  225 EEIEKERESLLEELK 239
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
433-706 3.82e-05

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 46.83  E-value: 3.82e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 433 IQQLQEILQDLQKRLESSEAERKQLQVELQSRRAELVCLNN----------------TEISENSSDLSQKLKETQSKYEE 496
Cdd:COG1340    10 LEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAqvkelreeaqelrekrDELNEKVKELKEERDELNEKLNE 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 497 AMKEVLSVQKQMKLGLVSPESMDnyshfhelrVTEEEINVLKQDLQNA---LEESERNKEKVRELEEKLVEREKGTVIKp 573
Cdd:COG1340    90 LREELDELRKELAELNKAGGSID---------KLRKEIERLEWRQQTEvlsPEEEKELVEKIKELEKELEKAKKALEKN- 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 574 pvEEYEEMKSSYCSVIENMNKekafLFEKYQEAQEEIMKLKDTLksqmtQEASDEAEDMKE---AMNRMIDELNKQVSEL 650
Cdd:COG1340   160 --EKLKELRAELKELRKEAEE----IHKKIKELAEEAQELHEEM-----IELYKEADELRKeadELHKEIVEAQEKADEL 228

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462602002 651 SQLYKEAQAELEDYRKrksledVTAEYIHKAEHEKLMQLTNVSRAKAEDALSEMKS 706
Cdd:COG1340   229 HEEIIELQKELRELRK------ELKKLRKKQRALKREKEKEELEEKAEEIFEKLKK 278
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 468-700 4.51e-05

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 47.07  E-value: 4.51e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 468 LVCLNNTEISENSSDLSQKLKETQSKYEEAMKEVLSVQKQMKLGLVSPESMDNyshfhELRVTEEEINVLKQDLQNALEE 547
Cdd:COG4942    10 LLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALER-----RIAALARRIRALEQELAALEAE 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 548 SERNKEKVRELEEKLVEReKGTVIKPPVEEYEEMKSSYCSVI---ENMNK--EKAFLFEKYQEA-QEEIMKLKDTLKSQM 621
Cdd:COG4942    85 LAELEKEIAELRAELEAQ-KEELAELLRALYRLGRQPPLALLlspEDFLDavRRLQYLKYLAPArREQAEELRADLAELA 163

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462602002 622 TQEAsdEAEDMKEAMNRMIDELNKQVSELSQLYKEAQAELEDYRKRKSLEDVTAEYIHKAEHEKLMQLTNVSRAKAEDA 700
Cdd:COG4942   164 ALRA--ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 615-864 5.16e-05

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 46.75  E-value: 5.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 615 DTLKSQMTQEASDEAEDMKEAMNRmIDELNKQVSELSQLYKEAQAELEDyrKRKSLEDVTAEyIHKAEHEklmqltnvsR 694
Cdd:COG3883    15 DPQIQAKQKELSELQAELEAAQAE-LDALQAELEELNEEYNELQAELEA--LQAEIDKLQAE-IAEAEAE---------I 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 695 AKAEDALSEMKSQYSKVLNELTQLKQLVDAQkensvSITEHLQVITTLRTAAKEMEEKISNLKEHLASKEVEVAKLEKQL 774
Cdd:COG3883    82 EERREELGERARALYRSGGSVSYLDVLLGSE-----SFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKL 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 775 LEEKAAMTDAMVPRSSYEKLQSSLESEVSVLASKLKESVKEKEKVHSEVVQIRSEVSQVKREKENIQTLLKSKEQEVNEL 854
Cdd:COG3883   157 AELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAA 236

                         250
                  ....*....|
gi 2462602002 855 LQKFQQAQEE 864
Cdd:COG3883   237 AAAAAAAASA 246
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 432-727 5.36e-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: 47.25  E-value: 5.36e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  432 RIQQLQEILQDLQKRLESSEAERKQLQVELQSRRAELVclnNTEISENS-----SDLSQKLKETQSK---YEEAMKEVLS 503
Cdd:COG3096    348 KIERYQEDLEELTERLEEQEEVVEEAAEQLAEAEARLE---AAEEEVDSlksqlADYQQALDVQQTRaiqYQQAVQALEK 424

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  504 VQKQMKLGLVSPESMDNYshFHELRVTEEEIN----VLKQDLQNAlEESERNKEKVRELEEKL---VEREK-GTVIKPPV 575
Cdd:COG3096    425 ARALCGLPDLTPENAEDY--LAAFRAKEQQATeevlELEQKLSVA-DAARRQFEKAYELVCKIageVERSQaWQTARELL 501

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  576 EEYeemkSSYCSVIENMNKEKAFLFEKYQ--EAQEEIMKLKDTLKSQMTQE--ASDEAEDMKEAMNRMIDELNKQVSELS 651
Cdd:COG3096    502 RRY----RSQQALAQRLQQLRAQLAELEQrlRQQQNAERLLEEFCQRIGQQldAAEELEELLAELEAQLEELEEQAAEAV 577

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462602002  652 QLYKEAQAELEDYR-KRKSLEDVTAEYIHKAEH-EKLMQLTNVSRAKAEDALSEMKSQYSKvLNELTQLKQLVDAQKE 727
Cdd:COG3096    578 EQRSELRQQLEQLRaRIKELAARAPAWLAAQDAlERLREQSGEALADSQEVTAAMQQLLER-EREATVERDELAARKQ 654
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 522-900 6.27e-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: 47.04  E-value: 6.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 522 SHFHELRVTEEEINVLKQDLQnalEESERNKE---KVRELEEKLVEREKGtvikppveeyeemkssycsvienmNKEKAF 598
Cdd:pfam05557  24 EHKRARIELEKKASALKRQLD---RESDRNQElqkRIRLLEKREAEAEEA------------------------LREQAE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 599 LFEKYQEAQEEIMKLKDTLKSQMTqeasdEAEDMKEAMNRMIDELNKQVSELSQLYKEAQAELEDYRKRKSLEDVTAEYI 678
Cdd:pfam05557  77 LNRLKKKYLEALNKKLNEKESQLA-----DAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEA 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 679 HK--AEHEKLMQLTNVSRAKAEDALSEMKSQyskvlnelTQLKQLVDAQKENSVSITEHLQVITTLRtaakEMEEKISNL 756
Cdd:pfam05557 152 EQlrQNLEKQQSSLAEAEQRIKELEFEIQSQ--------EQDSEIVKNSKSELARIPELEKELERLR----EHNKHLNEN 219

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 757 KEHLASKEVEVAKLEKQLLEEKAAMTDAMVPRSSYEKLQSSLESEVSVLASKLKESVKeKEKVHSEVVQIRSEVSQVKRE 836
Cdd:pfam05557 220 IENKLLLKEEVEDLKRKLEREEKYREEAATLELEKEKLEQELQSWVKLAQDTGLNLRS-PEDLSRRIEQLQQREIVLKEE 298

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462602002 837 KENIQTLLKSKEQEVNELLQKFQQAQEELAEMKRYAESSSKLEEDKDKKINEMSKEVTKLKEAL 900
Cdd:pfam05557 299 NSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERDGYRAIL 362
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
 643-901 7.84e-05

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 46.46  E-value: 7.84e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 643 LNKQVSE-LSQLYKEAQAELEDYRKRKSledvtAEYIHKAEHEklmqltnvsRAKAEDALSEMKSqYSKVLNELTQLKQL 721
Cdd:PRK05771   14 LKSYKDEvLEALHELGVVHIEDLKEELS-----NERLRKLRSL---------LTKLSEALDKLRS-YLPKLNPLREEKKK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 722 VDAQKENSV--SITEHLQVIttlRTAAKEMEEKISNLKEHLASKEVEVAKLE---------KQLLEEK-AAMTDAMVPRS 789
Cdd:PRK05771   79 VSVKSLEELikDVEEELEKI---EKEIKELEEEISELENEIKELEQEIERLEpwgnfdldlSLLLGFKyVSVFVGTVPED 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 790 SYEKLQSSLESEVSVLASKLKESV-------KEKEKVHSEVV---------------------QIRSEVSQVKREKENIQ 841
Cdd:PRK05771  156 KLEELKLESDVENVEYISTDKGYVyvvvvvlKELSDEVEEELkklgferleleeegtpselirEIKEELEEIEKERESLL 235

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462602002 842 TLLKSKEQEVNELLqkfQQAQEELAEMKRYAESSSKLEEDKDKKINE---MSKEVTKLKEALN 901
Cdd:PRK05771  236 EELKELAKKYLEEL---LALYEYLEIELERAEALSKFLKTDKTFAIEgwvPEDRVKKLKELID 295
PRK01156 PRK01156
chromosome segregation protein; Provisional
 478-870 8.37e-05

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 46.43  E-value: 8.37e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 478 ENSSDLSQKLKETQSKYEEAMKEVLSVQKQMKLGLVSPESMDNYSH-FHELRVTEEEINVLKQDLQNALEESERNKEKVR 556
Cdd:PRK01156  308 ENKKQILSNIDAEINKYHAIIKKLSVLQKDYNDYIKKKSRYDDLNNqILELEGYEMDYNSYLKSIESLKKKIEEYSKNIE 387

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 557 ELEEKLVEREKGTVIKPP--VEEYEEMKSS---YCSVIENMNKEKAFLFEKYQEAQEEIMKLKDTLKSQM------TQEA 625
Cdd:PRK01156  388 RMSAFISEILKIQEIDPDaiKKELNEINVKlqdISSKVSSLNQRIRALRENLDELSRNMEMLNGQSVCPVcgttlgEEKS 467

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 626 SDEAEDMKEAMNRMIDELNKQVSELSQLYKEA--QAELEDYRKRKSLEDVTAEY--IHKAEHEKLMQLTNVSRAK-AEDA 700
Cdd:PRK01156  468 NHIINHYNEKKSRLEEKIREIEIEVKDIDEKIvdLKKRKEYLESEEINKSINEYnkIESARADLEDIKIKINELKdKHDK 547

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 701 LSEMKSQY---------SKVLNELTQLKQLVDAQKENSVSITEhlQVITTLRTAAKEMEEKISNLKEHLASKEVEVAKLE 771
Cdd:PRK01156  548 YEEIKNRYkslkledldSKRTSWLNALAVISLIDIETNRSRSN--EIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIE 625

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 772 KQLLEEKAAMTDAMVPRSSYEKLQSSLESEVSVLAsKLKESVKEKEKVHSEVVQIRSEVSQVKREKENI-------QTLL 844
Cdd:PRK01156  626 NEANNLNNKYNEIQENKILIEKLRGKIDNYKKQIA-EIDSIIPDLKEITSRINDIEDNLKKSRKALDDAkanrarlESTI 704

                         410       420
                  ....*....|....*....|....*.
gi 2462602002 845 KSKEQEVNELLQKFQQAQEELAEMKR 870
Cdd:PRK01156  705 EILRTRINELSDRINDINETLESMKK 730
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 187-214 8.89e-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: 8.89e-05
                          10        20
                  ....*....|....*....|....*...
gi 2462602002 187 GRTALMLACEIGSSNAVEALIKKGADLN 214
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGADIN 29
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 63-143 1.07e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 46.04  E-value: 1.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  63 AAKGHVECLRVMITHGVDVTAQDTTGHSALHLAAKNSHHECIRKLLQSKCPAESVDSSGKTALHYAAAQGCLQAVQILCE 142
Cdd:PTZ00322   90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169


                  .
gi 2462602002 143 H 143
Cdd:PTZ00322  170 H 170
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 481-709 1.10e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 45.59  E-value: 1.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 481 SDLSQKLKETQSKYEEAMKEVLSVQKQMKlglvspesmdnyshfhelrVTEEEINVLKQDLQNALEESERNKEKVRELEE 560
Cdd:COG3883    19 QAKQKELSELQAELEAAQAELDALQAELE-------------------ELNEEYNELQAELEALQAEIDKLQAEIAEAEA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 561 KLVEREkgtvikppvEEYEE-MKSSY------------------------CSVIENMNKEKAFLFEKYQEAQEEIMKLKD 615
Cdd:COG3883    80 EIEERR---------EELGErARALYrsggsvsyldvllgsesfsdfldrLSALSKIADADADLLEELKADKAELEAKKA 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 616 TLKSQMtqeasDEAEDMKEAMNRMIDELNKQVSELSQLYKEAQAELEDYRKRKSLEDVTAEYIHKAEHEKLMQLTNVSRA 695
Cdd:COG3883   151 ELEAKL-----AELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAA 225

                         250
                  ....*....|....
gi 2462602002 696 KAEDALSEMKSQYS 709
Cdd:COG3883   226 AAAAAAAAAAAAAA 239
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 434-919 1.19e-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: 46.25  E-value: 1.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 434 QQLQEILQDLQKRLESSEAERKQLQVELQSRRAELvclnnteisenSSDLSQKLKETQSKYEEAMKEVLSVQKQMKLGLV 513
Cdd:pfam05483 179 EETRQVYMDLNNNIEKMILAFEELRVQAENARLEM-----------HFKLKEDHEKIQHLEEEYKKEINDKEKQVSLLLI 247

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 514 spesmdnyshfhelRVTEEEINVlkQDLQNALEESernKEKVRELEEK--LVEREKGTVIKPPVEEYEEMKSSYCSVIEN 591
Cdd:pfam05483 248 --------------QITEKENKM--KDLTFLLEES---RDKANQLEEKtkLQDENLKELIEKKDHLTKELEDIKMSLQRS 308

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 592 MNKEKAfLFEKYQEAQEEIMKLKDTLKSQMtqeasDEAEDMKEAMNRMIDELNKQVSELSQLYKEAQAELEdyRKRKSLE 671
Cdd:pfam05483 309 MSTQKA-LEEDLQIATKTICQLTEEKEAQM-----EELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLE--KNEDQLK 380

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 672 DVTAEYIHKA-EHEKLMQLTNVSRAKAEDaLSEMKSQYSKVLNELTQLKQLVDAQKENSVSITEHLQV-----------I 739
Cdd:pfam05483 381 IITMELQKKSsELEEMTKFKNNKEVELEE-LKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQArekeihdleiqL 459

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 740 TTLRTAAKEMEEKISNLKEHLASKEVEVAKL----------EKQLLEEKAAMTDAMVPRS----SYEKLQSSLESEVSVL 805
Cdd:pfam05483 460 TAIKTSEEHYLKEVEDLKTELEKEKLKNIELtahcdkllleNKELTQEASDMTLELKKHQediiNCKKQEERMLKQIENL 539

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 806 ASKLKESVKEKEKVHSEVVQIRSEVS-QVKREKENIQTL----------LKSKEQEVNELLQK-------FQQAQEELAE 867
Cdd:pfam05483 540 EEKEMNLRDELESVREEFIQKGDEVKcKLDKSEENARSIeyevlkkekqMKILENKCNNLKKQienknknIEELHQENKA 619

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2462602002 868 MKRYAESSSKLEEDKDKKINEMSKEVTKLKEALNSLSQLSYSTSSSKRQSQQ 919
Cdd:pfam05483 620 LKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISEE 671
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 187-217 1.31e-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: 1.31e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 2462602002 187 GRTALMLACEI-GSSNAVEALIKKGADLNLVD 217
Cdd:pfam00023   2 GNTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 623-868 1.59e-04

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 45.14  E-value: 1.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 623 QEASDEAEDMKEAMNRMIDELNKQVSELSQLYKEAQAELEDYRKRKSledVTAEYIHKAEH-----EKLMQLTNVSRAKA 697
Cdd:COG4942    19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIA---ALARRIRALEQelaalEAELAELEKEIAEL 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 698 EDALSEMKSQYSKVLNELTQLKQLVDAQ-KENSVSITEHLQVITTLRTAAKEMEEKISNLKEHLAskevEVAKLEKQLLE 776
Cdd:COG4942    96 RAELEAQKEELAELLRALYRLGRQPPLAlLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLA----ELAALRAELEA 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 777 EKaamtdamvprssyeklqsslesevsvlasklkesvKEKEKVHSEVVQIRSEVSQVKREKENIQTLLKSKEQEVNELLQ 856
Cdd:COG4942   172 ER-----------------------------------AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELA 216

                         250
                  ....*....|..
gi 2462602002 857 KFQQAQEELAEM 868
Cdd:COG4942   217 ELQQEAEELEAL 228
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 475-897 1.59e-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: 45.88  E-value: 1.59e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  475 EISENSSDLSQKLKETQSKYEEAM----KEVLSVQKQMKLGLVSPESMdnyshfHELRVTEEEInvlKQDLQNALEESER 550
Cdd:pfam15921   82 EYSHQVKDLQRRLNESNELHEKQKfylrQSVIDLQTKLQEMQMERDAM------ADIRRRESQS---QEDLRNQLQNTVH 152

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  551 NKEKVRELEEKLVEREKGTVikppvEEYEEMKSSYCSVIENMNKekafLFEKYQEAQEEIMKLKDTLKSQmtqeasdEAE 630
Cdd:pfam15921  153 ELEAAKCLKEDMLEDSNTQI-----EQLRKMMLSHEGVLQEIRS----ILVDFEEASGKKIYEHDSMSTM-------HFR 216

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  631 DMKEAMNRMIDELNKQVSELSQLYKEAQAELEDYrkrKSLEDVTAEYIHKAEHEKLMQLtnVSRAKAE-DALSEMKSQYS 709
Cdd:pfam15921  217 SLGSAISKILRELDTEISYLKGRIFPVEDQLEAL---KSESQNKIELLLQQHQDRIEQL--ISEHEVEiTGLTEKASSAR 291

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  710 KVLNELTQLKQLVDAQKENSVSIteHLQVITTLRTAAKEMEekiSNLKEHLASKEVEVAKLEKQLLEEKAAMTDAMVPRS 789
Cdd:pfam15921  292 SQANSIQSQLEIIQEQARNQNSM--YMRQLSDLESTVSQLR---SELREAKRMYEDKIEELEKQLVLANSELTEARTERD 366

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  790 SYEKLQSSLESEVSVLASKL----KESVKEKEKVHS----------EVVQIRSEVSQVKREKENIQTLLKSKEQEV---- 851
Cdd:pfam15921  367 QFSQESGNLDDQLQKLLADLhkreKELSLEKEQNKRlwdrdtgnsiTIDHLRRELDDRNMEVQRLEALLKAMKSECqgqm 446

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462602002  852 ----------NELLQK--------------FQQAQEELAEMKRYAESSSKLEED-------KDKKINEMSKEVTKLK 897
Cdd:pfam15921  447 erqmaaiqgkNESLEKvssltaqlestkemLRKVVEELTAKKMTLESSERTVSDltaslqeKERAIEATNAEITKLR 523
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 56-198 1.61e-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: 1.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  56 KHCFHlAAAKGHV----ECLRVMITHGVD------VTAQDTT----GHSALHLAAKNSHHECIRKLLQSK-------CPA 114
Cdd:TIGR00870  83 DTLLH-AISLEYVdaveAILLHLLAAFRKsgplelANDQYTSeftpGITALHLAAHRQNYEIVKLLLERGasvparaCGD 161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 115 ESVDSSGKTALHY-------AAAQGCLQAVQILCEHKSPINLKDLDGNIPL-LLAVQNGHSE-----ICH---FLLDHGA 178
Cdd:TIGR00870 162 FFVKSQGVDSFYHgesplnaAACLGSPSIVALLSEDPADILTADSLGNTLLhLLVMENEFKAeyeelSCQmynFALSLLD 241

                         170       180
                  ....*....|....*....|....*..
gi 2462602002 179 DVNS-------RNKSGRTALMLACEIG 198
Cdd:TIGR00870 242 KLRDskeleviLNHQGLTPLKLAAKEG 268
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
428-684 1.88e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 45.68  E-value: 1.88e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  428 DNDVRIQQLQEILQDLQKRLESSEAERKQLQVELQSRRAELVCLNNteiSENSSDLSQKLKETQSKYEEAMKEVLSVQKq 507
Cdd:COG4913    607 DNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQR---LAEYSWDEIDVASAEREIAELEAELERLDA- 682

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  508 mklglvspeSMDnyshfhELRVTEEEINVLKQDLQNALEESERNKEKVRELEEKLVEREkgtvikppvEEYEEMKSSYCS 587
Cdd:COG4913    683 ---------SSD------DLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAE---------EELDELQDRLEA 738

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  588 VIENMNKEKAFLFEKYQEAQeeimkLKDTLKSQMTQEASDEAEDMKEAMNRMIDELNKQVSELSQLYKEAQAEL------ 661
Cdd:COG4913    739 AEDLARLELRALLEERFAAA-----LGDAVERELRENLEERIDALRARLNRAEEELERAMRAFNREWPAETADLdadles 813

                          250       260
                   ....*....|....*....|....
gi 2462602002  662 -EDYRKRksLEDVTAEYIHKAEHE 684
Cdd:COG4913    814 lPEYLAL--LDRLEEDGLPEYEER 835
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
432-901 1.93e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 45.68  E-value: 1.93e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  432 RIQQLQEILQDLQKRLESSEAERKQLQVELQSRRAELVCLNNtEISENSSD----LSQKLKETQSKYEEAMKEVLSVQKQ 507
Cdd:COG4913    289 RLELLEAELEELRAELARLEAELERLEARLDALREELDELEA-QIRGNGGDrleqLEREIERLERELEERERRRARLEAL 367

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  508 MK-LGLVSPESMDNY-SHFHELRVTEEEINVLKQDLQNALEESERNKEKVR-ELEEKLVERE----KGTVIkPPveEYEE 580
Cdd:COG4913    368 LAaLGLPLPASAEEFaALRAEAAALLEALEEELEALEEALAEAEAALRDLRrELRELEAEIAslerRKSNI-PA--RLLA 444

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  581 MKSSYCSVIENMNKEKAFL----------------FEK---------------YQEAQEEI-----------MKLKDTLK 618
Cdd:COG4913    445 LRDALAEALGLDEAELPFVgelievrpeeerwrgaIERvlggfaltllvppehYAAALRWVnrlhlrgrlvyERVRTGLP 524

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  619 SQMTQEASDE--AEDMKEAMNRMIDELNKQVSELSQLYK-EAQAELEDYRKRksledVTAE---YIHKAEHEKLMQLTNV 692
Cdd:COG4913    525 DPERPRLDPDslAGKLDFKPHPFRAWLEAELGRRFDYVCvDSPEELRRHPRA-----ITRAgqvKGNGTRHEKDDRRRIR 599

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  693 SR----AKAEDALSEMKSQYSKVLNELTQLKQLVDAqkensvsITEHLQVITTLRTAAKEMEEKISNLKEhLASKEVEVA 768
Cdd:COG4913    600 SRyvlgFDNRAKLAALEAELAELEEELAEAEERLEA-------LEAELDALQERREALQRLAEYSWDEID-VASAEREIA 671

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  769 KLEKQLleekaamtdamvprssyEKLQSSlESEVSVLASKLKESVKEKEKVHSEVVQIRSEVSQVKREKENIQTLLKSKE 848
Cdd:COG4913    672 ELEAEL-----------------ERLDAS-SDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQ 733

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2462602002  849 QEVNELLQKFQQAQEELAEMKRYAESSSKLEEDKDKKInemSKEVTKLKEALN 901
Cdd:COG4913    734 DRLEAAEDLARLELRALLEERFAAALGDAVERELRENL---EERIDALRARLN 783
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
 419-799 2.10e-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: 45.23  E-value: 2.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 419 IHSLGKSTTDNDVRIQQLQEILQDLQKRL--------ESSEAERKQLQvELQSRRAELVCLNNT-----------EISEN 479
Cdd:pfam06160 109 LDELLESEEKNREEVEELKDKYRELRKTLlanrfsygPAIDELEKQLA-EIEEEFSQFEELTESgdylearevleKLEEE 187

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 480 SSDLSQK-------LKETQSKYEEAMKEVLSVQKQMKlglvspesMDNYsHFHELRVtEEEINVLKQDLQNALEESERNK 552
Cdd:pfam06160 188 TDALEELmedipplYEELKTELPDQLEELKEGYREME--------EEGY-ALEHLNV-DKEIQQLEEQLEENLALLENLE 257

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 553 -EKVRELEEKLVERekgtvIKPPVEEYEEMKSSYCSVIENMNKEKAFLF---EKYQEAQEEIMKLKDT-LKSQMTQEASD 627
Cdd:pfam06160 258 lDEAEEALEEIEER-----IDQLYDLLEKEVDAKKYVEKNLPEIEDYLEhaeEQNKELKEELERVQQSyTLNENELERVR 332

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 628 EAEDMKEAMNRMIDELNKQVSELSQLYKEAQAELEDYRKRksLEDVTAEyiHKAEHEKLMQLTNVSRaKAEDALSEMKsq 707
Cdd:pfam06160 333 GLEKQLEELEKRYDEIVERLEEKEVAYSELQEELEEILEQ--LEEIEEE--QEEFKESLQSLRKDEL-EAREKLDEFK-- 405

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 708 yskvlNELTQLKQLVdaQKEN----SVSITEHL-QVITTLRTAAKEMEEKISNLKE-----HLASKEVEVAKLEKQLLEE 777
Cdd:pfam06160 406 -----LELREIKRLV--EKSNlpglPESYLDYFfDVSDEIEDLADELNEVPLNMDEvnrllDEAQDDVDTLYEKTEELID 478

                         410       420
                  ....*....|....*....|....*..
gi 2462602002 778 KAAMTDAMVP-----RSSYEKLQSSLE 799
Cdd:pfam06160 479 NATLAEQLIQyanryRSSNPEVAEALT 505
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
421-665 2.57e-04

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 45.01  E-value: 2.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 421 SLGKSTTDNDVRIQQLQEILQDLQKRLESSEAERKQLQvelqsRRAELVCLNNTE--ISENSSDLSQKLKETQSKYEEAM 498
Cdd:COG3206   165 NLELRREEARKALEFLEEQLPELRKELEEAEAALEEFR-----QKNGLVDLSEEAklLLQQLSELESQLAEARAELAEAE 239

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 499 KEVLSVQKQMKLGLVSPESMDNYSHFHELRvteEEINVLKQDLQNALEESERNKEKVRELEEKLVEREkgtvikppveey 578
Cdd:COG3206   240 ARLAALRAQLGSGPDALPELLQSPVIQQLR---AQLAELEAELAELSARYTPNHPDVIALRAQIAALR------------ 304

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 579 EEMKSSYCSVIENMNKEKAFLfekyQEAQEEIMKLKDTLKSQMTQEASDEAEdmkeamnrmIDELNKQVSELSQLYKEAQ 658
Cdd:COG3206   305 AQLQQEAQRILASLEAELEAL----QAREASLQAQLAQLEARLAELPELEAE---------LRRLEREVEVARELYESLL 371


                  ....*..
gi 2462602002 659 AELEDYR 665
Cdd:COG3206   372 QRLEEAR 378
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 132-216 2.61e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 44.57  E-value: 2.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 132 GCLQAVQILCEHKSP-INLKDLDGNIPLLLAVQNGHSEICHFLLDHGADVNSRNKSGRTALMLACEIGSSNAVEALIKKG 210
Cdd:PHA02874   12 GDIEAIEKIIKNKGNcINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNG 91


                  ....*.
gi 2462602002 211 ADLNLV 216
Cdd:PHA02874   92 VDTSIL 97
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 432-874 2.94e-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: 44.78  E-value: 2.94e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  432 RIQQLQEILQDLQKRLESSEAERKQLQVELQSRraelvclnnTEISENSSDLSQKLKETQSKYEEAMKEVlsvqkqmklg 511
Cdd:pfam01576   20 RQQKAESELKELEKKHQQLCEEKNALQEQLQAE---------TELCAEAEEMRARLAARKQELEEILHEL---------- 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  512 lvspesmdnyshfhELRVTEEEINVlkQDLQNaleESERNKEKVRELEEKLVEREKGTvikppveeyeemkssycsviEN 591
Cdd:pfam01576   81 --------------ESRLEEEEERS--QQLQN---EKKKMQQHIQDLEEQLDEEEAAR--------------------QK 121

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  592 MNKEKAFLFEKYQEAQEEIMKLKDTlKSQMTQEASDEAEDMKEAMNRMIDELN--KQVSELSQLYKEAQAELEDYRKRKs 669
Cdd:pfam01576  122 LQLEKVTTEAKIKKLEEDILLLEDQ-NSKLSKERKLLEERISEFTSNLAEEEEkaKSLSKLKNKHEAMISDLEERLKKE- 199

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  670 ledvtaeyihkaehEKLMQLTNVSRAKAEDALSEMKSQYSKVLNELTQLKQLVDAQKENSVSITEHLQVITTLRTAA--- 746
Cdd:pfam01576  200 --------------EKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNAlkk 265

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  747 -KEMEEKISNLKEHLASKEVEVAKLEKQ---LLEE----KAAMTDAMVPRSSYEKLQSSLESEVSVLASKLKESVKEKE- 817
Cdd:pfam01576  266 iRELEAQISELQEDLESERAARNKAEKQrrdLGEElealKTELEDTLDTTAAQQELRSKREQEVTELKKALEEETRSHEa 345

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462602002  818 -------KVHSEVVQIRSEVSQVKREKENIQTLLKSKEQEVNEL---LQKFQQAQEELAEMKRYAES 874
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 ...
 545-921 3.30e-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: 44.58  E-value: 3.30e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  545 LEESERNKEKVRELEEKLVEREKgtvikppVEEYEEMKSSYCSVIENMNKEKaflfEKYQEAQEEIMKLKDTLKSQMTQE 624
Cdd:pfam02463  159 EEEAAGSRLKRKKKEALKKLIEE-------TENLAELIIDLEELKLQELKLK----EQAKKALEYYQLKEKLELEEEYLL 227

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  625 ASDEAEDMKEAMNRMIDELNKQVSELSQLYKEAQAELEdyrkrkSLEDVTAEYIhkaEHEKLMQLTNVSRAKAEDALSEM 704
Cdd:pfam02463  228 YLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEE------KLAQVLKENK---EEEKEKKLQEEELKLLAKEEEEL 298

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  705 KSQYSKvlneLTQLKQLVDAQKENSVSITEHLQVITTLRTAAKEMEEKIsnLKEHLASKEVEVAKLEKQLLEEKAAmtda 784
Cdd:pfam02463  299 KSELLK----LERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKE--LKELEIKREAEEEEEEELEKLQEKL---- 368

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  785 mvprssyEKLQSSLESEVSVLASKLKESVKEKEKVH---SEVVQIRSEVSQVKREKENIQTLLKSKEQEVNELLQKFQQA 861
Cdd:pfam02463  369 -------EQLEEELLAKKKLESERLSSAAKLKEEELelkSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIEL 441

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  862 QEELAEMKRYAESSSKLEEDKDKkinEMSKEVTKLKEALNSLSQLSYSTSSSKRQSQQLE 921
Cdd:pfam02463  442 KQGKLTEEKEELEKQELKLLKDE---LELKKSEDLLKETQLVKLQEQLELLLSRQKLEER 498
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 187-215 3.37e-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: 3.37e-04
                           10        20
                   ....*....|....*....|....*....
gi 2462602002  187 GRTALMLACEIGSSNAVEALIKKGADLNL 215
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
434-657 3.82e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 44.28  E-value: 3.82e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 434 QQLQEILQDLQKRLESSEAERKQLQvELQSRRAELvclnNTEISENSSDLSQKLKETQSKYEEAMKEVLSVQKQMK---- 509
Cdd:PRK03918  528 EKLKEKLIKLKGEIKSLKKELEKLE-ELKKKLAEL----EKKLDELEEELAELLKELEELGFESVEELEERLKELEpfyn 602

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 510 --LGLVSPEsmdnyshfHELRVTEEEINVLKQDLQNALEESERNKEKVRELEEKLVEREKgtviKPPVEEYEEMKSSYCS 587
Cdd:PRK03918  603 eyLELKDAE--------KELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEK----KYSEEEYEELREEYLE 670

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462602002 588 VIENMNKEKAFLfEKYQEAQEEIMKLKDTLKSQMT--QEASDEAEDMKEAMNRMiDELNKQVSELSQLYKEA 657
Cdd:PRK03918  671 LSRELAGLRAEL-EELEKRREEIKKTLEKLKEELEerEKAKKELEKLEKALERV-EELREKVKKYKALLKER 740
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 142-253 4.08e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 43.89  E-value: 4.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 142 EHKSPINLKDLDGNIPLLLAVQNGHSEICHFLLDHGADVNSRNKSGRTALMLACEIGSS-----NAVEALIKKGADLNLV 216
Cdd:PHA03100   23 MEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAP 102

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2462602002 217 DSLGYNALHY--SKLSENAGIQSLLLSKISqDADLKTPT 253
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 ...
 421-870 5.60e-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: 44.01  E-value: 5.60e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  421 SLGKSTTDNDVRIQQLQEILQDLQKRLESSEAERKQLQVELQSRRAELvclnnteisensSDLSQKLKETQSKYEEAMKE 500
Cdd:pfam01576  395 TLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSEL------------ESVSSLLNEAEGKNIKLSKD 462

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  501 VLSVQKQMK--LGLVSPESMDNYSHFHELRVTEEEINVLKQDLQNAlEESERNKEK-VRELEEKLVE-REKGTVIKPPVE 576
Cdd:pfam01576  463 VSSLESQLQdtQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEE-EEAKRNVERqLSTLQAQLSDmKKKLEEDAGTLE 541

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  577 EYEEMKSSYCSVIENMN---KEKAFLFEKYQEA----QEEIMKLKDTLKSQMT--------------------------Q 623
Cdd:pfam01576  542 ALEEGKKRLQRELEALTqqlEEKAAAYDKLEKTknrlQQELDDLLVDLDHQRQlvsnlekkqkkfdqmlaeekaisaryA 621

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  624 EASDEAE-DMKE------AMNRMIDELNKQVSELSQLYKEAQAELEDYRKRKsleDVTAEYIHKAEHeklmqltnvSRAK 696
Cdd:pfam01576  622 EERDRAEaEAREketralSLARALEEALEAKEELERTNKQLRAEMEDLVSSK---DDVGKNVHELER---------SKRA 689

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  697 AEDALSEMKSQYSKVLNELTQLKqlvDAQkensvsitehLQVITTLRTAAKEMEEKISNLKEHLASKEVEVAK----LEK 772
Cdd:pfam01576  690 LEQQVEEMKTQLEELEDELQATE---DAK----------LRLEVNMQALKAQFERDLQARDEQGEEKRRQLVKqvreLEA 756

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  773 QLLEEKAAMTDAMVPRSSYEKLQSSLESEVSVLASKLKESVKEKEKVHSEVVQIRSEVSQVKREKENIQTLLKSKEQEVN 852
Cdd:pfam01576  757 ELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARASRDEILAQSKESEKKLK 836

                          490
                   ....*....|....*...
gi 2462602002  853 ELLQKFQQAQEELAEMKR 870
Cdd:pfam01576  837 NLEAELLQLQEDLAASER 854
COG5022 COG5022
Myosin heavy chain [General function prediction only];
601-875 5.62e-04

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 43.91  E-value: 5.62e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  601 EKYQEAQEEIMKLKDTLKSQMTQEASDEAEDMKEAM---NRMIDELN--KQVSEL--SQLYKEAQAELEDYRKRKSLEDV 673
Cdd:COG5022    810 KEYRSYLACIIKLQKTIKREKKLRETEEVEFSLKAEvliQKFGRSLKakKRFSLLkkETIYLQSAQRVELAERQLQELKI 889

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  674 TAEyihKAEHEKLMQLTNVSRakaedaLSEMKSQYSKVLNELTQLKqlvdaqkensvsiTEHlqvITTLRTAAKEMEEKI 753
Cdd:COG5022    890 DVK---SISSLKLVNLELESE------IIELKKSLSSDLIENLEFK-------------TEL---IARLKKLLNNIDLEE 944

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  754 SnlkehlASKEVEVAKLEKQLLEEKAAMTDAMVPRSSYEKLQSSLESEVSVLASKLK-----------------ESVKEK 816
Cdd:COG5022    945 G------PSIEYVKLPELNKLHEVESKLKETSEEYEDLLKKSTILVREGNKANSELKnfkkelaelskqygalqESTKQL 1018

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462602002  817 EKVHSEVVQIRSEVSQVKREKENIQTLLKSKEQEvNELLQKFQQAQEELAEMKRYAESS 875
Cdd:COG5022   1019 KELPVEVAELQSASKIISSESTELSILKPLQKLK-GLLLLENNQLQARYKALKLRRENS 1076
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
 469-897 6.09e-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: 6.09e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  469 VCLNNTEISENSSDLSQKLKETQSKYEEAMKEVLSVQKQMK--------------------LGLVSPESMDN--YSHFHE 526
Cdd:TIGR01612  925 ICENTKESIEKFHNKQNILKEILNKNIDTIKESNLIEKSYKdkfdntlidkineldkafkdASLNDYEAKNNelIKYFND 1004

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  527 LRVTeeeinvLKQDLQNALEESERNKEK-VRELEEKLVEREKG---------TVIKPPVEEYEE-----MKSSYCSVIEN 591
Cdd:TIGR01612 1005 LKAN------LGKNKENMLYHQFDEKEKaTNDIEQKIEDANKNipnieiaihTSIYNIIDEIEKeigknIELLNKEILEE 1078

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  592 MN---------KEKA-------FLFEKYQEAQEEIMKLKDTLKS--QMTQEASDEAEDMKEAMNRMIDELNKQVSELSQ- 652
Cdd:TIGR01612 1079 AEinitnfneiKEKLkhynfddFGKEENIKYADEINKIKDDIKNldQKIDHHIKALEEIKKKSENYIDEIKAQINDLEDv 1158

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  653 ----LYKEAQAELEDYRKRKSLEDVTAEYIHKAEHEKLMQLTNVSRAKAedALSEMKS---QYSKVLNELtqLKQLVDAQ 725
Cdd:TIGR01612 1159 adkaISNDDPEEIEKKIENIVTKIDKKKNIYDEIKKLLNEIAEIEKDKT--SLEEVKGinlSYGKNLGKL--FLEKIDEE 1234

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  726 KENSvsitEHLqvittlrtaAKEMEEKISNLKEhLASKEVEVAKLEKQLLEEKAAMTDAMVPRSSYEKLQS--------- 796
Cdd:TIGR01612 1235 KKKS----EHM---------IKAMEAYIEDLDE-IKEKSPEIENEMGIEMDIKAEMETFNISHDDDKDHHIiskkhdeni 1300

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  797 --------------SLESEVSVLASKLKESVKEKEKVHSEVVQIRSEVSQVKR--EKENIQTLLKSKEQEVNELLQKFQQ 860
Cdd:TIGR01612 1301 sdirekslkiiedfSEESDINDIKKELQKNLLDAQKHNSDINLYLNEIANIYNilKLNKIKKIIDEVKEYTKEIEENNKN 1380

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*....
gi 2462602002  861 AQEELAE----MKRYAESSSkLEEDK--------DKKINEMSKEVTKLK 897
Cdd:TIGR01612 1381 IKDELDKseklIKKIKDDIN-LEECKskiestldDKDIDECIKKIKELK 1428
CAGE1 pfam15066
Cancer-associated gene protein 1 family; CAGE-1 is a family of proteins overexpressed in ...
 428-567 6.19e-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: 43.67  E-value: 6.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 428 DNDVRIQQLQEILQDLQKRLESSEAERKQLQVELQSRRAELVCLNN---TEISENSSDLSQKLK--ETQSKYEEamkEVL 502
Cdd:pfam15066 388 DINKTLQNLQEILANTQKHLQESRKEKETLQLELKKIKVNYVHLQEryiTEMQQKNKSVSQCLEmdKTLSKKEE---EVE 464

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462602002 503 SVQkQMKLGL--VSPESMDNYSHFHELRvtEEEINVLKQDLQNALEESERNKEKVRELEEKLVEREK 567
Cdd:pfam15066 465 RLQ-QLKGELekATTSALDLLKREKETR--EQEFLSLQEEFQKHEKENLEERQKLKSRLEKLVAQVK 528
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 157-181 6.99e-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: 6.99e-04
                          10        20
                  ....*....|....*....|....*
gi 2462602002 157 PLLLAVQNGHSEICHFLLDHGADVN 181
Cdd:pfam13606   5 PLHLAARNGRLEIVKLLLENGADIN 29
Ank_4 pfam13637
Ankyrin repeats (many copies);
187-240 1.11e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 38.02  E-value: 1.11e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2462602002 187 GRTALMLACEIGSSNAVEALIKKGADLNLVDSLGYNALHYSKLSENAGIQSLLL 240
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
 537-901 1.15e-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: 43.12  E-value: 1.15e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  537 LKQDLQNALEESERNKEKVRELEEKlverekgtvIKPPVEEYEEmkssycSVIEnMNKEKAFLFEKYQEAQEEIM---KL 613
Cdd:TIGR01612  538 LYKEIEAGLKESYELAKNWKKLIHE---------IKKELEEENE------DSIH-LEKEIKDLFDKYLEIDDEIIyinKL 601

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  614 KDTLKSQMtQEASDEAEDMKEAM---------NRMIDELNK----QVSE----LSQLYKEAQAELEDYRKrkslEDVTAE 676
Cdd:TIGR01612  602 KLELKEKI-KNISDKNEYIKKAIdlkkiiennNAYIDELAKispyQVPEhlknKDKIYSTIKSELSKIYE----DDIDAL 676

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  677 YIHKAEHEKLMQLTNVS-RAKAEDALSEMKSQYSKVLNELTQLKQLVDAQKENSVSitEHLQVITTLRTAA-KEMEEKIS 754
Cdd:TIGR01612  677 YNELSSIVKENAIDNTEdKAKLDDLKSKIDKEYDKIQNMETATVELHLSNIENKKN--ELLDIIVEIKKHIhGEINKDLN 754

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  755 NLKEHLASKEVEVAKLEKQLLEEKAAMTdamVPRSSYEKLQSSLESEVSVLASKLKESVK--EKEKVHSEVVQIRS-EVS 831
Cdd:TIGR01612  755 KILEDFKNKEKELSNKINDYAKEKDELN---KYKSKISEIKNHYNDQINIDNIKDEDAKQnyDKSKEYIKTISIKEdEIF 831

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  832 QVKREKENIQTLLKSKEQEV----NELLQKFQQAQEELAEM--KRYAESSSKLEEDKDKK-------INEMSKEVTKLKE 898
Cdd:TIGR01612  832 KIINEMKFMKDDFLNKVDKFinfeNNCKEKIDSEHEQFAELtnKIKAEISDDKLNDYEKKfndskslINEINKSIEEEYQ 911


                   ...
gi 2462602002  899 ALN 901
Cdd:TIGR01612  912 NIN 914
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
592-870 1.16e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.98  E-value: 1.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  592 MNKEKAF-LFEKYQEAQEeIMKLKDTLKSQMTqeasdEAEDMKEAmnrmIDELNKQVSELSQLYKEAqaeLEDYRKRKSL 670
Cdd:COG4913    188 IGSEKALrLLHKTQSFKP-IGDLDDFVREYML-----EEPDTFEA----ADALVEHFDDLERAHEAL---EDAREQIELL 254

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  671 EDVTAEY-------IHKAEHEKLMQLTNVSRAKAEDALSEmksqyskvlNELTQLKQLVDAQKENsvsitehlqvITTLR 743
Cdd:COG4913    255 EPIRELAeryaaarERLAELEYLRAALRLWFAQRRLELLE---------AELEELRAELARLEAE----------LERLE 315

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  744 TAAKEMEEKISNLKEHLASKEVE-VAKLEKQLLEEKAAMTDAMVPRSSYEKLQSSLESEVSVLASKLKEsvkekekvhse 822
Cdd:COG4913    316 ARLDALREELDELEAQIRGNGGDrLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAA----------- 384

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 2462602002  823 vvqirsEVSQVKREKENIQTLLKSKEQEVNELLQKFQQAQEELAEMKR 870
Cdd:COG4913    385 ------LRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEA 426
HMMR_N pfam15905
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ...
 419-663 1.17e-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: 1.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 419 IHSLGKSTTDNDVRIQQLQEILQDLQKRLESSEAERKQLQVELQSRRAELV------CLNNTEISENS-----SDLSQKL 487
Cdd:pfam15905  82 IRALVQERGEQDKRLQALEEELEKVEAKLNAAVREKTSLSASVASLEKQLLeltrvnELLKAKFSEDGtqkkmSSLSMEL 161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 488 KETQSKYEEAMKEVLSVQKQMKLGLvspesmdnyshfhelrvteeeinvlkQDLQNALEESernKEKVRELEEKLVEREK 567
Cdd:pfam15905 162 MKLRNKLEAKMKEVMAKQEGMEGKL--------------------------QVTQKNLEHS---KGKVAQLEEKLVSTEK 212

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 568 GTVikppVEEYEEMKssycsvIENMNKEKAFLFEKYQEAQEEIMKLKDTLKsqmtqEASDEAEDMKEAMNRMIDELNKQV 647
Cdd:pfam15905 213 EKI----EEKSETEK------LLEYITELSCVSEQVEKYKLDIAQLEELLK-----EKNDEIESLKQSLEEKEQELSKQI 277

                         250
                  ....*....|....*.
gi 2462602002 648 SELSQLYKEAQAELED 663
Cdd:pfam15905 278 KDLNEKCKLLESEKEE 293
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 56-83 1.23e-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: 1.23e-03
                           10        20
                   ....*....|....*....|....*...
gi 2462602002   56 KHCFHLAAAKGHVECLRVMITHGVDVTA 83
Cdd:smart00248   3 RTPLHLAAENGNLEVVKLLLDKGADINA 30
COG5022 COG5022
Myosin heavy chain [General function prediction only];
436-901 1.45e-03

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 42.76  E-value: 1.45e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  436 LQEILQDLQKRLESSEAERKQLQVELQSRRAELVCLN-NTEISENSSDLSQKLKET---QSKYEEAMKEVLSVQKQMKLG 511
Cdd:COG5022    799 LQPLLSLLGSRKEYRSYLACIIKLQKTIKREKKLRETeEVEFSLKAEVLIQKFGRSlkaKKRFSLLKKETIYLQSAQRVE 878

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  512 LVSPESMD------NYSHFHELRVT-EEEINVLKQDLQNAL-EESERNKEKVRELEEKL------VEREKGTVIKPPVEE 577
Cdd:COG5022    879 LAERQLQElkidvkSISSLKLVNLElESEIIELKKSLSSDLiENLEFKTELIARLKKLLnnidleEGPSIEYVKLPELNK 958

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  578 YEEMKSSY---CSVIENMNKEKAFLFEKYQEAQEEIMKLKDTLKSQMTQ-EASDEAEDMKEAMNRMIDELNKqvseLSQL 653
Cdd:COG5022    959 LHEVESKLketSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQyGALQESTKQLKELPVEVAELQS----ASKI 1034

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  654 YKEAQAELedyRKRKSLEDVTAEYIhKAEHEKLMQLTNVS-RAKAEDALSEMKSQYSKVLNELTQLKQL-VDAQKENSVS 731
Cdd:COG5022   1035 ISSESTEL---SILKPLQKLKGLLL-LENNQLQARYKALKlRRENSLLDDKQLYQLESTENLLKTINVKdLEVTNRNLVK 1110

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  732 ITEHLQVITTLRTAAKEMEEKISNLKEHLASKEVEVAKLEK-QLLEEKAAMTDAMVPRSSYEKLQSSLESEvSVLASKLK 810
Cdd:COG5022   1111 PANVLQFIVAQMIKLNLLQEISKFLSQLVNTLEPVFQKLSVlQLELDGLFWEANLEALPSPPPFAALSEKR-LYQSALYD 1189

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  811 ESVKEKekvHSEVVQIRSEVSqvkrekeniqtLLKSKEQEVNELLQKFQQAQEELAEMKRYAESSSKLEEDKDKKINEMS 890
Cdd:COG5022   1190 EKSKLS---SSEVNDLKNELI-----------ALFSKIFSGWPRGDKLKKLISEGWVPTEYSTSLKGFNNLNKKFDTPAS 1255

                          490
                   ....*....|.
gi 2462602002  891 KEVTKLKEALN 901
Cdd:COG5022   1256 MSNEKLLSLLN 1266
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
 593-919 1.48e-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: 1.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 593 NKEKAFLFEKYQEAQEEIMKLKDTLKsqmtQEASDEAEDMKEAMNRMIDELNKQVSELSQLYKEAQAELEDYRKRKSLED 672
Cdd:COG5185   241 PESELEDLAQTSDKLEKLVEQNTDLR----LEKLGENAESSKRLNENANNLIKQFENTKEKIAEYTKSIDIKKATESLEE 316

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 673 VTAEYIHKAEHEKLMqltnvsrAKAEDALSEMKSQYSKVLNELTQLKQLVDAQKENSVSITEHLQVITTLRTAAKEMEEK 752
Cdd:COG5185   317 QLAAAEAEQELEESK-------RETETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEVELSKSSEELDSFKDTIEST 389

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 753 ISNLKEHLASkevevAKLEKQLLEEKAAMTDAMVPRSSyEKLQSSLESevsvLASKLKESVKEKEKVHSEVVQIRSEVSQ 832
Cdd:COG5185   390 KESLDEIPQN-----QRGYAQEILATLEDTLKAADRQI-EELQRQIEQ----ATSSNEEVSKLLNELISELNKVMREADE 459

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 833 VKREK--ENIQTLLKSKEQEVNELLQKFQQAQEELAEMKryaESSSKLEEDKDKKINEMSKEVTKLKEALNSLSQLSYST 910
Cdd:COG5185   460 ESQSRleEAYDEINRSVRSKKEDLNEELTQIESRVSTLK---ATLEKLRAKLERQLEGVRSKLDQVAESLKDFMRARGYA 536


                  ....*....
gi 2462602002 911 SSSKRQSQQ 919
Cdd:COG5185   537 HILALENLI 545
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 434-922 1.48e-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: 42.65  E-value: 1.48e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  434 QQLQEILQDLQKRLESSEAERKQLQVELQsrraelvclnNTEISENSSDLSQKLKETQSKYEEAMKEVLSvqkqmklglv 513
Cdd:TIGR00618  208 LCTPCMPDTYHERKQVLEKELKHLREALQ----------QTQQSHAYLTQKREAQEEQLKKQQLLKQLRA---------- 267

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  514 spesmdnyshfhelrvTEEEINVLKQDLQNALEESERNKEKvreleEKLVEREKGtvikppVEEYEEMKSSYCSVIENMN 593
Cdd:TIGR00618  268 ----------------RIEELRAQEAVLEETQERINRARKA-----APLAAHIKA------VTQIEQQAQRIHTELQSKM 320

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  594 KEKAFLFEKYQEAQEEIMKLKDTLKS-QMTQEASDEAEDMKEAMNRMIDELNKQVSELSQLYKEAQAELEDYRKRKSL-- 670
Cdd:TIGR00618  321 RSRAKLLMKRAAHVKQQSSIEEQRRLlQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLck 400

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  671 -------EDVTAEYIHKAEHEKLMQLTnVSRAKAEDALSEMKSQYSKVLNELTQLKQLVDAQKENSVSITEHLQVITTLR 743
Cdd:TIGR00618  401 eldilqrEQATIDTRTSAFRDLQGQLA-HAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKE 479

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  744 TAAKEMEEKISNLKEHLASKEVEVAKLEKQLLEEKAAMTDAMVPRSSYEKLQsSLESEVSVLAsklkesvKEKEKVHSEV 823
Cdd:TIGR00618  480 QIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQ-RGEQTYAQLE-------TSEEDVYHQL 551

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  824 VQIRSEVSQVKREKENIQTLLKSKEQEVNELLQKFQQAQEELAEMKRYAESSSKLEedkDKKINEMSKEVTKLKEALNSL 903
Cdd:TIGR00618  552 TSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAE---DMLACEQHALLRKLQPEQDLQ 628

                          490
                   ....*....|....*....
gi 2462602002  904 SQLSYSTSSSKRQSQQLEA 922
Cdd:TIGR00618  629 DVRLHLQQCSQELALKLTA 647
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 162-232 1.51e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 42.36  E-value: 1.51e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462602002 162 VQNGHSEICHFLLDHGADVNSRNKSGRTALMLACEIGSSNAVEALIKKGADLNLVDSLGYNALHYSKLSEN 232
Cdd:PHA02876  153 IQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKN 223
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 526-667 1.58e-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: 1.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 526 ELRVTEEEINVLKQDLQNALEESERNKEKVRELEEKLVEREK--GTVIKPpvEEYEEMKSSycsvIENMNKEKAFLFEKY 603
Cdd:COG1579    39 ELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEqlGNVRNN--KEYEALQKE----IESLKRRISDLEDEI 112

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462602002 604 QEAQEEIMKLKDTLKsqmtqEASDEAEDMKEAMNRMIDELNKQVSELSQLYKEAQAELEDYRKR 667
Cdd:COG1579   113 LELMERIEELEEELA-----ELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAK 171
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
 419-779 1.64e-03

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 42.13  E-value: 1.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 419 IHSLGKSTTDNDVRIQQLQEILQDLQKRL--------ESSEAERKQLQvELQSRRAELVCLNNT-----------EISEN 479
Cdd:PRK04778  128 LQELLESEEKNREEVEQLKDLYRELRKSLlanrfsfgPALDELEKQLE-NLEEEFSQFVELTESgdyveareildQLEEE 206

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 480 SSDLSQK-------LKETQSKYEEAMKEVLSVQKQMKlglvspesMDNYsHFHELRVtEEEINVLKQDLQNALE-----E 547
Cdd:PRK04778  207 LAALEQImeeipelLKELQTELPDQLQELKAGYRELV--------EEGY-HLDHLDI-EKEIQDLKEQIDENLAlleelD 276

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 548 SERNKEKVRELEEK------LVEREKGTviKPPVEEYEEMKSSYCSVIENMNK----EKAFLFEKYQEAQEEIMKLKdTL 617
Cdd:PRK04778  277 LDEAEEKNEEIQERidqlydILEREVKA--RKYVEKNSDTLPDFLEHAKEQNKelkeEIDRVKQSYTLNESELESVR-QL 353

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 618 KSQMtqeasdeaedmkEAMNRMIDELNKQVSELSQLYKEAQAELEDYRKRksLEDVTAEYIHKAEHekLMQLTNvSRAKA 697
Cdd:PRK04778  354 EKQL------------ESLEKQYDEITERIAEQEIAYSELQEELEEILKQ--LEEIEKEQEKLSEM--LQGLRK-DELEA 416

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 698 EDALSEMKsqyskvlNELTQLKQLVdaQKEN----SVSITEHLQVITT-LRTAAKEMEEKISNLKEhlASKEVEVAKLEK 772
Cdd:PRK04778  417 REKLERYR-------NKLHEIKRYL--EKSNlpglPEDYLEMFFEVSDeIEALAEELEEKPINMEA--VNRLLEEATEDV 485


                  ....*..
gi 2462602002 773 QLLEEKA 779
Cdd:PRK04778  486 ETLEEET 492
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 637-816 1.77e-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: 1.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 637 NRMIDELNKQVSELSQLYKEAQAELEDYRKRksLEDVTAEyihKAEHEKLMQLTNVSRAKAEDALSEMKS--QYSKVLNE 714
Cdd:COG1579    23 EHRLKELPAELAELEDELAALEARLEAAKTE--LEDLEKE---IKRLELEIEEVEARIKKYEEQLGNVRNnkEYEALQKE 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 715 LTQLKQLvdaqkensvsitehlqvITTLRTAAKEMEEKISNLKEHLASKEVEVAKLEKQLLEEKAAMTDAMvprSSYEKL 794
Cdd:COG1579    98 IESLKRR-----------------ISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEEL---AELEAE 157

                         170       180
                  ....*....|....*....|..
gi 2462602002 795 QSSLESEVSVLASKLKESVKEK 816
Cdd:COG1579   158 LEELEAEREELAAKIPPELLAL 179
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 712-867 1.87e-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: 1.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 712 LNELTQLKQLVDAQKENSVSitEHLQVITTLRTAAKEMEEKISNLKEHLASKEVEVAKLEKQ----------LLEEKAAM 781
Cdd:pfam07888  43 RAELLQAQEAANRQREKEKE--RYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKykelsasseeLSEEKDAL 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 782 TDAmvpRSSYEKLQSSLESEVSVLASKLKESVKEKEKVHSEVVQIRSEVSQVKREKENIQTLLKSKEQEVNELLQKFQQA 861
Cdd:pfam07888 121 LAQ---RAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQEL 197


                  ....*.
gi 2462602002 862 QEELAE 867
Cdd:pfam07888 198 RNSLAQ 203
PHA02791 PHA02791
ankyrin-like protein; Provisional
 104-249 1.87e-03

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 41.57  E-value: 1.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 104 IRKLLQSKcPAESVDSSGKTALHYAAAQGCLQAVQILCEHKSPINLkdLDGNIPLLLAVQNGHSEICHFLLDHGADVNSR 183
Cdd:PHA02791   14 LKSFLSSK-DAFKADVHGHSALYYAIADNNVRLVCTLLNAGALKNL--LENEFPLHQAATLEDTKIVKILLFSGMDDSQF 90

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462602002 184 NKSGRTALMLACEIGSSNAVEALIKKGADLNLVDSLGY-NALHYSKLSENAGIQSLLLSKISQDADL 249
Cdd:PHA02791   91 DDKGNTALYYAVDSGNMQTVKLFVKKNWRLMFYGKTGWkTSFYHAVMLNDVSIVSYFLSEIPSTFDL 157
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
 576-897 1.93e-03

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 42.13  E-value: 1.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 576 EEYEEMKSSYCSVIENmnkekafLFEKYQEAQEEIMKLKDTLKSQMTQEASDEAEDMKEAMNRMIDELNKQVSELSQLYK 655
Cdd:PRK04778   64 EKFEEWRQKWDEIVTN-------SLPDIEEQLFEAEELNDKFRFRKAKHEINEIESLLDLIEEDIEQILEELQELLESEE 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 656 EAQAE----LEDYRK-RKSLED------VTAEYIHK------AEHEKLMQLTN----------VSRAKAE-DALSEMKSQ 707
Cdd:PRK04778  137 KNREEveqlKDLYRElRKSLLAnrfsfgPALDELEKqlenleEEFSQFVELTEsgdyveareiLDQLEEElAALEQIMEE 216

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 708 YSKVLNELT-----QLKQLVDAQKENSVS--ITEHLQVITTLrtaaKEMEEKISNLKEHLASKEVEVAKLEKQLLEEK-- 778
Cdd:PRK04778  217 IPELLKELQtelpdQLQELKAGYRELVEEgyHLDHLDIEKEI----QDLKEQIDENLALLEELDLDEAEEKNEEIQERid 292

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 779 ---AAMTDAMVPRSSYEKLQSSLESEVSVLASKLKESVKEKEKV-------HSEVVQIRS---EVSQVKREKENIQTLLK 845
Cdd:PRK04778  293 qlyDILEREVKARKYVEKNSDTLPDFLEHAKEQNKELKEEIDRVkqsytlnESELESVRQlekQLESLEKQYDEITERIA 372

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462602002 846 SKEQEVNELLQKFQQAQEELAEMK----RYAESSSKLEEDKDK---KINEMSKEVTKLK 897
Cdd:PRK04778  373 EQEIAYSELQEELEEILKQLEEIEkeqeKLSEMLQGLRKDELEareKLERYRNKLHEIK 431
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 527-884 2.04e-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: 2.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 527 LRVTEEEINVLKQDLQNALEESERNKEKVRELEEKLVEREkgTVIKPPVEEYEEMKSSYCSVI---ENMNKEKAFLFEKY 603
Cdd:pfam07888  47 LQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELK--EELRQSREKHEELEEKYKELSassEELSEEKDALLAQR 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 604 QEAQEEIMKLKDTLK--SQMTQEASDEAEDMKEAMNRMIDELNKQVSELSQL-YKEAQAELEDYRKRKSLEdvtaeyihk 680
Cdd:pfam07888 125 AAHEARIRELEEDIKtlTQRVLERETELERMKERAKKAGAQRKEEEAERKQLqAKLQQTEEELRSLSKEFQ--------- 195

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 681 aeheklmqltnvsraKAEDALSEMKSQYSKVLNELTQLKQLVDAQKENSVSITEHLQVITTLRTAAKEMEEKISNLKEHL 760
Cdd:pfam07888 196 ---------------ELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEEL 260

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 761 AS--------------KEVEVAKLEKQLLEEKAAMTDAmvpRSSYEK----LQSSLESEVSVLASKLKESVKEKEKVHSE 822
Cdd:pfam07888 261 SSmaaqrdrtqaelhqARLQAAQLTLQLADASLALREG---RARWAQeretLQQSAEADKDRIEKLSAELQRLEERLQEE 337

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462602002 823 VVQIRSEVSQVKREKENIQTLLKSKEQEVNEL---LQKFQQAQEEL-AEMKRYAESSSKLEEDKDK 884
Cdd:pfam07888 338 RMEREKLEVELGREKDCNRVQLSESRRELQELkasLRVAQKEKEQLqAEKQELLEYIRQLEQRLET 403
Mitofilin pfam09731
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ...
 539-817 2.23e-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: 2.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 539 QDLQNALEESERNKEKVRELEEKLVEREKGTVIKPPVEEYEEMKSSYCSVIENMNKEKAFLFEKYQEAQEEIMKLKDTLK 618
Cdd:pfam09731 124 QEKEKALEEVLKEAISKAESATAVAKEAKDDAIQAVKAHTDSLKEASDTAEISREKATDSALQKAEALAEKLKEVINLAK 203

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 619 SQMTQEASDEAEDMKEAMNRMIDELNKQVSELSQLYKEAqAELEDYRKRKSLEDVtaeyIHKAEHEKLMqlTNVSRAKAE 698
Cdd:pfam09731 204 QSEEEAAPPLLDAAPETPPKLPEHLDNVEEKVEKAQSLA-KLVDQYKELVASERI----VFQQELVSIF--PDIIPVLKE 276

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 699 DALSEMKSQYSKVLNELTQLKQLVDAQKENSVSITEHLQVIttLRTAAKEMEEKISNLKEHLaskEVEVAKLEKQLLEEK 778
Cdd:pfam09731 277 DNLLSNDDLNSLIAHAHREIDQLSKKLAELKKREEKHIERA--LEKQKEELDKLAEELSARL---EEVRAADEAQLRLEF 351

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 2462602002 779 AAMTDAMvpRSSYE-KLQSSLESEVSVLASKLKESVKEKE 817
Cdd:pfam09731 352 EREREEI--RESYEeKLRTELERQAEAHEEHLKDVLVEQE 389
PTZ00108 PTZ00108
DNA topoisomerase 2-like protein; Provisional
 428-850 2.36e-03

DNA topoisomerase 2-like protein; Provisional


Pssm-ID: 240271 [Multi-domain]  Cd Length: 1388  Bit Score: 41.96  E-value: 2.36e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  428 DNDVRIQQ---LQEILQDL-QKRLESSEaERKQLQVELQSRRAELvcLNNT-----EISENSSDLSQKLKetqskyeeam 498
Cdd:PTZ00108   967 DENGKIKKysdALDILKEFyLVRLDLYK-KRKEYLLGKLERELAR--LSNKvrfikHVINGELVITNAKK---------- 1033

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  499 KEVLSVQKQMKLGLVSP-ESMDNYSHFHELRVTEEEINVLKQDLQNALEESERN-------------KEKVRELEEKLVE 564
Cdd:PTZ00108  1034 KDLVKELKKLGYVRFKDiIKKKSEKITAEEEEGAEEDDEADDEDDEEELGAAVSydyllsmpiwsltKEKVEKLNAELEK 1113

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  565 REKgtvikppveEYEEMKSsycSVIENMNKekaflfekyqeaqEEIMKLKDTLKSQMTQEASDEAEDMKEAMNRMIDELN 644
Cdd:PTZ00108  1114 KEK---------ELEKLKN---TTPKDMWL-------------EDLDKFEEALEEQEEVEEKEIAKEQRLKSKTKGKASK 1168

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  645 KQVSELSQLyKEAQAELEDYRKRKSLEDVTAEYIHKAEHEKLMQLTNVSRAKAEDalsemKSQYSKVLNELTQLKQLVDA 724
Cdd:PTZ00108  1169 LRKPKLKKK-EKKKKKSSADKSKKASVVGNSKRVDSDEKRKLDDKPDNKKSNSSG-----SDQEDDEEQKTKPKKSSVKR 1242

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  725 QKENSVSITEHLQVITTLRTAAKEMEEKISNLKEHLASKEVEVAKLEKQLLEEKAamTDAMVPRSSYEKLQSSLESEVSV 804
Cdd:PTZ00108  1243 LKSKKNNSSKSSEDNDEFSSDDLSKEGKPKNAPKRVSAVQYSPPPPSKRPDGESN--GGSKPSSPTKKKVKKRLEGSLAA 1320

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*.
gi 2462602002  805 LASKLKESVKEKEKVHSEVVQIRSEVSQVKREKENIQTLLKSKEQE 850
Cdd:PTZ00108  1321 LKKKKKSEKKTARKKKSKTRVKQASASQSSRLLRRPRKKKSDSSSE 1366
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 609-834 2.74e-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: 41.86  E-value: 2.74e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  609 EIMKLKDTLKSQMTQEASDEAEDMKEAMN------RMIDELNKQVS----------ELSQLYKEAQAELEDYRKRK-SLE 671
Cdd:COG3096    882 QANLLADETLADRLEELREELDAAQEAQAfiqqhgKALAQLEPLVAvlqsdpeqfeQLQADYLQAKEQQRRLKQQIfALS 961

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  672 DVTAEYIHKAEHEKLMQLTNVS----------------RAKAEDALSEMKSQYSKVLNELTQLKQLVDAQKEnsvsiteh 735
Cdd:COG3096    962 EVVQRRPHFSYEDAVGLLGENSdlneklrarleqaeeaRREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQ-------- 1033

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  736 lqvitTLRTAAKEMEEkisnLKEHLASKEVEVAKLEKQLLEEKAAMTDAMvpRSSYEKLQSSLESEVSVLASKLKesvKE 815
Cdd:COG3096   1034 -----TLQELEQELEE----LGVQADAEAEERARIRRDELHEELSQNRSR--RSQLEKQLTRCEAEMDSLQKRLR---KA 1099

                          250
                   ....*....|....*....
gi 2462602002  816 KEKVHsevvQIRSEVSQVK 834
Cdd:COG3096   1100 ERDYK----QEREQVVQAK 1114
PRK01156 PRK01156
chromosome segregation protein; Provisional
 527-897 2.80e-03

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 41.81  E-value: 2.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 527 LRVTEEEINVLKQDLQNALEESERNKEKVRELEEKLVEREKGtvIKPPVEEYEEMKSSYCSVIENMNKEKAFLFEKyQEA 606
Cdd:PRK01156  178 LRAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKE--IERLSIEYNNAMDDYNNLKSALNELSSLEDMK-NRY 254

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 607 QEEIMKLKDTLksQMTQEASDEAEDMKEAMNRMIDE--------------LNKQVSELSQLYKEAQAELEDYRK-RKSLE 671
Cdd:PRK01156  255 ESEIKTAESDL--SMELEKNNYYKELEERHMKIINDpvyknrnyindyfkYKNDIENKKQILSNIDAEINKYHAiIKKLS 332

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 672 DVTAEYIHKAEHEKLMQLTNvsraKAEDALSEMKSQYSKVLNELTQLKQLVDAQKENS------VSITEHLQVIT--TLR 743
Cdd:PRK01156  333 VLQKDYNDYIKKKSRYDDLN----NQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIermsafISEILKIQEIDpdAIK 408

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 744 TAAKEMEEKISNLKEHLASKEVEVAKLEKQL--LEEKAAMTDAmvpRSSYEKLQSSLESEVSvlASKLKESVKEKEKVHS 821
Cdd:PRK01156  409 KELNEINVKLQDISSKVSSLNQRIRALRENLdeLSRNMEMLNG---QSVCPVCGTTLGEEKS--NHIINHYNEKKSRLEE 483

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462602002 822 EVVQIRSEVSQVKREKENIQTLLKSKE-QEVNELLQKFQQAQEELAEMKRYAESSSKLeEDKDKKINEMSKEVTKLK 897
Cdd:PRK01156  484 KIREIEIEVKDIDEKIVDLKKRKEYLEsEEINKSINEYNKIESARADLEDIKIKINEL-KDKHDKYEEIKNRYKSLK 559
46 PHA02562
endonuclease subunit; Provisional
 716-895 2.84e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 41.54  E-value: 2.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 716 TQLKQLVDAQKENSVSITEHLQVITTLRTAAKEMEEKISNLKEHLASKEVEVAKLEKQLLEEKAAMTDA----------- 784
Cdd:PHA02562  199 TYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIkskieqfqkvi 278

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 785 ------------MVPRSSYEKLQSSLESEVSVLA---SKLKESVKEKEKVHSEVVQIRSEVSQVKREKENIQTLLKSKEQ 849
Cdd:PHA02562  279 kmyekggvcptcTQQISEGPDRITKIKDKLKELQhslEKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVD 358

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2462602002 850 EVNELLQKFQQAQeelAEMKRYAESSSKLEEDKDKKINEMSKEVTK 895
Cdd:PHA02562  359 KAKKVKAAIEELQ---AEFVDNAEELAKLQDELDKIVKTKSELVKE 401
MPS2 pfam17060
Monopolar spindle protein 2; Is a fungal transmembrane protein which is part of the component ...
 552-764 3.22e-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: 3.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 552 KEKVRELEEKLVEREKGTVIKPPVEEYEEMKSSYCSVIEnmnkekaflfekyqeaqeeimkLKDTLKSQMTQEASDEAED 631
Cdd:pfam17060  67 KESFSEMFNGLVGNNFKTVINKIFEDCDGIPASFISALE----------------------LKEDVKSSPRSEADSLGTP 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 632 MKEAMNRMI--DELNKQVSELSQLYKEAQAELEDYRKRKSLEDvtaEYIHKAEHEkLMQLTNvsrakaedALSEMKSQYS 709
Cdd:pfam17060 125 IKVDLLRNLkpQESPETPRRINRKYKSLELRVESMKDELEFKD---ETIMEKDRE-LTELTS--------TISKLKDKYD 192

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462602002 710 KVLNELTQLKQLVDAQKENSV-SITEHLQVITTLRTAAKEMEEKISNLKEHLASKE 764
Cdd:pfam17060 193 FLSREFEFYKQHHEHGGNNSIkTATKHEFIISELKRKLQEQNRLIRILQEQIQFDP 248
PHA02946 PHA02946
ankyin-like protein; Provisional
 104-252 3.25e-03

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 41.19  E-value: 3.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 104 IRKLLQSKCPAESVDSSGKTALHYAAAQGCLQAVQILCEHKSPINLKDLDGNIPL--LLAVQNGHSEICHFLLDHGADVN 181
Cdd:PHA02946   55 VEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLyyLSGTDDEVIERINLLVQYGAKIN 134

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462602002 182 SRNKSGRTALMLACEIGSSNAVEALIKKGADLNLVDSLGYNALHYSKLSEN------AGIQSLLLSKISQDADLKTP 252
Cdd:PHA02946  135 NSVDEEGCGPLLACTDPSERVFKKIMSIGFEARIVDKFGKNHIHRHLMSDNpkastiSWMMKLGISPSKPDHDGNTP 211
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 695-925 3.36e-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: 40.90  E-value: 3.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 695 AKAEDALSEMKSQYSKVLNELTQLKQLVDAQKENSVSITEHLQV----ITTLRTAAKEMEEKISNLKEHLASKEVEVAKL 770
Cdd:COG4942    16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAAlerrIAALARRIRALEQELAALEAELAELEKEIAEL 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 771 EKQLLEEKAAMTDAMvpRSSYeklQSSLESEVSVL--ASKLKESVKEKEKVHSEVVQIRSEVSQVKREKENIQTLLKSKE 848
Cdd:COG4942    96 RAELEAQKEELAELL--RALY---RLGRQPPLALLlsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELE 170

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462602002 849 QEVNELLQKFQQAQEELAEMkryaessSKLEEDKDKKINEMSKEvtklkealnslsqlsystssSKRQSQQLEALQQ 925
Cdd:COG4942   171 AERAELEALLAELEEERAAL-------EALKAERQKLLARLEKE--------------------LAELAAELAELQQ 220
Macoilin pfam09726
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 ...
 642-876 3.63e-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: 3.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 642 ELNKQVSELSQLYKEAQAELEDYRKRKsleDVTAEYIHKAEHEKLMQLTNVS----RAKAEdalSEMKSQYSKVLNELTQ 717
Cdd:pfam09726 420 ELRSQISSLTSLERSLKSELGQLRQEN---DLLQTKLHNAVSAKQKDKQTVQqlekRLKAE---QEARASAEKQLAEEKK 493

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 718 LKQLVDAQKENSVS--ITEHLQVITTLRTAAKEMEEKISNLKEHLASKEVEVAKLEKQLLEekaamtdamvpRSSYEKLQ 795
Cdd:pfam09726 494 RKKEEEATAARAVAlaAASRGECTESLKQRKRELESEIKKLTHDIKLKEEQIRELEIKVQE-----------LRKYKESE 562

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 796 SSLESEVSVLaSKLKESVKEKEKVHSEVVQIR----SEVSQVKREKENIQTLLKSKEQEVNELLQKFQQAQEELAEMKRY 871
Cdd:pfam09726 563 KDTEVLMSAL-SAMQDKNQHLENSLSAETRIKldlfSALGDAKRQLEIAQGQIYQKDQEIKDLKQKIAEVMAVMPSTSRI 641


                  ....*
gi 2462602002 872 AESSS 876
Cdd:pfam09726 642 TPVTP 646
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 478-886 3.89e-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: 41.25  E-value: 3.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 478 ENSSDLSQKLKETQSKyeeAMKEVLSVQKQMKLGLvSPESMDNYSHFHELRVTEEEINVLKQDLQNALEESERNKEKVRE 557
Cdd:pfam05483 105 ENKLQENRKIIEAQRK---AIQELQFENEKVSLKL-EEEIQENKDLIKENNATRHLCNLLKETCARSAEKTKKYEYEREE 180

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 558 LEEKLVEREKGtvIKPPVEEYEEMKSSYCSVIENMNKEKAFLFEKYQEAQEEIMKLKDTLKSQMT------QEASDEAED 631
Cdd:pfam05483 181 TRQVYMDLNNN--IEKMILAFEELRVQAENARLEMHFKLKEDHEKIQHLEEEYKKEINDKEKQVSllliqiTEKENKMKD 258

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 632 MKEAMNRMIDELNkQVSELSQLYKEAQAELEDYRKR--KSLEDVTAEyihkaehekLMQLTNVSRAKAEDALSEMKSQYS 709
Cdd:pfam05483 259 LTFLLEESRDKAN-QLEEKTKLQDENLKELIEKKDHltKELEDIKMS---------LQRSMSTQKALEEDLQIATKTICQ 328

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 710 KVLNELTQLKQLVDAQKENSVSITEHLQVITTLRTAAKEMEEKISNLKEHLASKEVEVAKLEKQLLEekaaMTdamvprs 789
Cdd:pfam05483 329 LTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEE----MT------- 397

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 790 syeKLQSSLESEVsvlaSKLKESVKEKEKVHSEVVQIRSEVSQVKREKENIQTLLKSKEQEVNEL-LQKFQQAQEELAEM 868
Cdd:pfam05483 398 ---KFKNNKEVEL----EELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLeIQLTAIKTSEEHYL 470

                         410
                  ....*....|....*...
gi 2462602002 869 KRYAESSSKLEEDKDKKI 886
Cdd:pfam05483 471 KEVEDLKTELEKEKLKNI 488
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
516-767 4.05e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.05  E-value: 4.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  516 ESMDNYSHFHE-LRVTEEEINVLKQ--DLQNALEESERNKEKVRELEEKLverekgtvikpPVEEYEEMKSSYCSVIENM 592
Cdd:COG4913    232 EHFDDLERAHEaLEDAREQIELLEPirELAERYAAARERLAELEYLRAAL-----------RLWFAQRRLELLEAELEEL 300

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  593 NKEKAFLFEKYQEAQEEIMKLK---DTLKSQMTQEASDEAEDMKEAMNRMIDELNKQVSELSQLYKEAQA-ELEDYRKRK 668
Cdd:COG4913    301 RAELARLEAELERLEARLDALReelDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAAlGLPLPASAE 380

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  669 SLEDVTAEYI-HKAEHEKLMQLTNVSRAKAEDALSEMKSQYSKVLNELTQLKQlvdaqkeNSVSITEHLQvitTLRTAak 747
Cdd:COG4913    381 EFAALRAEAAaLLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLER-------RKSNIPARLL---ALRDA-- 448

                          250       260
                   ....*....|....*....|
gi 2462602002  748 emeekisnLKEHLASKEVEV 767
Cdd:COG4913    449 --------LAEALGLDEAEL 460
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 419-686 4.09e-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: 41.16  E-value: 4.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 419 IHSLGKSTTDNDVRIQQLQEILQDLQKRLESSEAERKQLQVELQSRRAELVcLNNTEISEnssdlsqkLKETQSKYEEAM 498
Cdd:TIGR04523 386 IKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETII-KNNSEIKD--------LTNQDSVKELII 456

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 499 KEVLSVQKQMKlglvspesmdnyshfHELRVTEEEINVLKQDLQNALEESERNKEKVRELEEKLVEREKgtvikpPVEEY 578
Cdd:TIGR04523 457 KNLDNTRESLE---------------TQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEE------KVKDL 515

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 579 EEMKSSYCSVIENMNKEKAFLFEKYQEAQEEIMKLKDTLKSQMTQEASDEAEDMKEAMNRMIDELNKQVSELSQLYKEAQ 658
Cdd:TIGR04523 516 TKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKE 595

                         250       260       270
                  ....*....|....*....|....*....|....
gi 2462602002 659 AELEDYRKRKSLEDVTAEYIH------KAEHEKL 686
Cdd:TIGR04523 596 KEKKDLIKEIEEKEKKISSLEkelekaKKENEKL 629
PTZ00440 PTZ00440
reticulocyte binding protein 2-like protein; Provisional
 428-900 4.28e-03

reticulocyte binding protein 2-like protein; Provisional


Pssm-ID: 240419 [Multi-domain]  Cd Length: 2722  Bit Score: 41.36  E-value: 4.28e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  428 DNDVRIQQLQEILQDLQKRLESSEAERKQLQVELQSRRAELvclNNTEISENSSDLSQKLKETQSKYEEA-----MKEVL 502
Cdd:PTZ00440   592 EIDNIIQQIEELINEALFNKEKFINEKNDLQEKVKYILNKF---YKGDLQELLDELSHFLDDHKYLYHEAkskedLQTLL 668

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  503 --SVQKQMKLGLVSPESMDNY--------SHFHELR--VTEEEINVLKQDLQNALEESernkekvreleeklveREKGTV 570
Cdd:PTZ00440   669 ntSKNEYEKLEFMKSDNIDNIiknlkkelQNLLSLKenIIKKQLNNIEQDISNSLNQY----------------TIKYND 732

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  571 IKPPVEEYEEMKSSYCSVIENMNKEKAFLFEKYQEAQEEIMKLKDTlksqmtqeaSDEAEDMKEAMNRMIDELNKQVSEL 650
Cdd:PTZ00440   733 LKSSIEEYKEEEEKLEVYKHQIINRKNEFILHLYENDKDLPDGKNT---------YEEFLQYKDTILNKENKISNDINIL 803

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  651 SQLYKEAQAELEDYR-KRKSLEDVTAEyiHKAEHEKLMQ-----LTNVSRAKAEDALSEMKSQYSKVLNELTQLKQLVDA 724
Cdd:PTZ00440   804 KENKKNNQDLLNSYNiLIQKLEAHTEK--NDEELKQLLQkfpteDENLNLKELEKEFNENNQIVDNIIKDIENMNKNINI 881

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  725 QKENSVSITE---HLQVITTLRTAAKEMEEKISNLKEHLASKEV----EVAKLEKQLLEEKAAM-------------TDA 784
Cdd:PTZ00440   882 IKTLNIAINRsnsNKQLVEHLLNNKIDLKNKLEQHMKIINTDNIiqknEKLNLLNNLNKEKEKIekqlsdtkinnlkMQI 961

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  785 MVPRSSYEKLQSSLESEVSVLASKLKESVKEKEKVHSEVVQIRSEV--------SQVKREKENIQTL----LKSKEQEVN 852
Cdd:PTZ00440   962 EKTLEYYDKSKENINGNDGTHLEKLDKEKDEWEHFKSEIDKLNVNYnilnkkidDLIKKQHDDIIELidklIKEKGKEIE 1041

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*...
gi 2462602002  853 ELLQKFQQAQEELAEMKRYAESSSKLEEDKDKKINEMSKEVTKLKEAL 900
Cdd:PTZ00440  1042 EKVDQYISLLEKMKTKLSSFHFNIDIKKYKNPKIKEEIKLLEEKVEAL 1089
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 434-880 5.35e-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: 40.80  E-value: 5.35e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  434 QQLQEILQDLQKRLESSEAERKQLQVELQSRRAELVCLNN--TEISENSSDLSQKLKETQSKYEEAMKEVLSVQKQMKLG 511
Cdd:TIGR00606  301 EQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQekTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELD 380

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  512 LVS--PESMDNYSHFHELRVTEEE-----INVLKQDLQNALEESERNKEKVRELEEKLVE--REKGTVIKPPVEEYEEMK 582
Cdd:TIGR00606  381 GFErgPFSERQIKNFHTLVIERQEdeaktAAQLCADLQSKERLKQEQADEIRDEKKGLGRtiELKKEILEKKQEELKFVI 460

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  583 SSycsvIENMNKEKAFLFEKYQEAQEEIMKLKDTLKSQMTQEASDEAEDMKEAMNRMIDELNKQVSELSQL--YKEAQAE 660
Cdd:TIGR00606  461 KE----LQQLEGSSDRILELDQELRKAERELSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLnhHTTTRTQ 536

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  661 LEDYRKRKSLEDvtaEYIHKAEHEKLMQLTNVS-----RAKAEDALSEMKSQYSKVLNELTQLKQLVDAQKENSVSITEH 735
Cdd:TIGR00606  537 MEMLTKDKMDKD---EQIRKIKSRHSDELTSLLgyfpnKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNE 613

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  736 LQVITTLRTAAKE----------MEEKISNLKEhlaskEVEVAKLEKQLLEEKAAMTDAMVPRSSYE------------K 793
Cdd:TIGR00606  614 LESKEEQLSSYEDklfdvcgsqdEESDLERLKE-----EIEKSSKQRAMLAGATAVYSQFITQLTDEnqsccpvcqrvfQ 688

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  794 LQSSLESEVSVLASKLKESVKEKEKVHSEVVQIRSEVSQVKREKENIQTLLKSKEQEVNELLQKFQQAQEELAEMKRYAE 873
Cdd:TIGR00606  689 TEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIE 768


                   ....*..
gi 2462602002  874 SSSKLEE 880
Cdd:TIGR00606  769 EQETLLG 775
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 60-122 5.37e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 40.65  E-value: 5.37e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462602002  60 HLAAAKGHVECLRVMITHGVDVTAQDTTGHSALHLAAKNSHHECIRKLLQSKCPAESVDSSGK 122
Cdd:PTZ00322  120 HIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFELGANAK 182
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
134-252 5.59e-03

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 39.94  E-value: 5.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 134 LQAVQILCEHKSPINLKDLDGNIPLLLAVQNGHSEICHFLLDHGADVNSRNKSGRTALMLACEIGSSNAVEALIKKGADL 213
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2462602002 214 NLVDSLGYNALHYSKLSENAGIQSLLLSK----ISQDADLKTP 252
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAgadvNARDKDGETP 123
HAMP COG2770
HAMP domain [Signal transduction mechanisms];
617-867 5.89e-03

HAMP domain [Signal transduction mechanisms];


Pssm-ID: 442051 [Multi-domain]  Cd Length: 631  Bit Score: 40.48  E-value: 5.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 617 LKSQMTQEASDEAEDMKEAMNRMIDELNKQVSELSQLYKEAQAELEDYRKRKSLEDVTAEYIHKAEHEKLMQLTNVSRAK 696
Cdd:COG2770   255 LDVRIPVSRKDEIGELARAFNRMADSLRESIEEAEEEEELAEAELARLLEALLELLLALLLLLLALLLLAAAALLLELLL 334

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 697 AEDALSEMKSQYSKVLNELTQLKQLVDAQKENSVSITEHLQVITTLRTAAKEMEEKISNLKEHLASKEVEVAKLEKQLLE 776
Cdd:COG2770   335 LLLLALLLLLLLAADLLLALALAALLLLLALELLLEAELLVLLALEALALEAELAAVLALLAALAAALLLLELALEELVL 414

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 777 EKAAMTDAMVPRSSYEKLQSSLESEVSVLASKLKESVKEKEKVHSEVVQIRSEVSQVKREKENIQTLLKSKEQEVNELLQ 856
Cdd:COG2770   415 ALLALALLALAAAAAAAEAAAAALELAAAAIAAAAAAEAEGGLAELEAEELVAAAEALLLLAALLLLAALGALELLLLEE 494

                         250
                  ....*....|.
gi 2462602002 857 KFQQAQEELAE 867
Cdd:COG2770   495 EEEAGAAAEEL 505
RecN COG0497
DNA repair ATPase RecN [Replication, recombination and repair];
522-784 6.01e-03

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


Pssm-ID: 440263 [Multi-domain]  Cd Length: 555  Bit Score: 40.44  E-value: 6.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 522 SHFHELRVTEEEINVLKQDLQNALEESERNKEKVRELEEklverekgtvIKPPVEEYEEMKSSYcSVIENMNKekafLFE 601
Cdd:COG0497   162 EAYRAWRALKKELEELRADEAERARELDLLRFQLEELEA----------AALQPGEEEELEEER-RRLSNAEK----LRE 226

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 602 KYQEAQEEImklkdtlksqmtQEASDEAEDM-KEAMNRM--IDELNKQVSELSQLYKEAQAELEDyrkrksLEDVTAEYI 678
Cdd:COG0497   227 ALQEALEAL------------SGGEGGALDLlGQALRALerLAEYDPSLAELAERLESALIELEE------AASELRRYL 288

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 679 HKAEHEklmqltnvsrakaEDALSEMKSQyskvLNELTQLKqlvdaQKENsVSITEhlqVITTLRTAAKEMEEkISNLKE 758
Cdd:COG0497   289 DSLEFD-------------PERLEEVEER----LALLRRLA-----RKYG-VTVEE---LLAYAEELRAELAE-LENSDE 341

                         250       260
                  ....*....|....*....|....*.
gi 2462602002 759 HLASKEVEVAKLEKQLLEEKAAMTDA 784
Cdd:COG0497   342 RLEELEAELAEAEAELLEAAEKLSAA 367
COG5022 COG5022
Myosin heavy chain [General function prediction only];
766-920 6.11e-03

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 40.83  E-value: 6.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  766 EVAKLEKQLLEEKAAmtdamVPRSSYEKLQSS-LESEVSVLASKLKESVKEKEKVHSEvvqirsEVSQVKREKENIQT-L 843
Cdd:COG5022    876 RVELAERQLQELKID-----VKSISSLKLVNLeLESEIIELKKSLSSDLIENLEFKTE------LIARLKKLLNNIDLeE 944

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  844 LKSKEQEVNELLQKFQQA----QEELAEMKRYAESSSKLEEDKDKKINEMSKEVTKLKEALNSLSQLSYSTSSSKRQSQQ 919
Cdd:COG5022    945 GPSIEYVKLPELNKLHEVesklKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQYGALQESTKQLKELPVE 1024


                   .
gi 2462602002  920 L 920
Cdd:COG5022   1025 V 1025
46 PHA02562
endonuclease subunit; Provisional
 430-656 6.67e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 40.38  E-value: 6.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 430 DVRIQQLQEILQDLQKRLESSEAERKQLQVELQSRRAELVCL---NNTEISENSSDLSqKLKETQSKYEEAMKEVLSVQK 506
Cdd:PHA02562  187 DMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEaktIKAEIEELTDELL-NLVMDIEDPSAALNKLNTAAA 265

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 507 QMKlglvspESMDNYSHFHELRVTEEEINVLKQDLQNALEESERNKEKVRELEEKLverekgTVIKPPVEEYEEMKSSYC 586
Cdd:PHA02562  266 KIK------SKIEQFQKVIKMYEKGGVCPTCTQQISEGPDRITKIKDKLKELQHSL------EKLDTAIDELEEIMDEFN 333

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 587 SVIENMNKEKAFLFEKYQEAQEEIMKLKDtLKSQMtQEASDEAEDMKEAMNRMIDELNKQVSELSQLYKE 656
Cdd:PHA02562  334 EQSKKLLELKNKISTNKQSLITLVDKAKK-VKAAI-EELQAEFVDNAEELAKLQDELDKIVKTKSELVKE 401
mukB PRK04863
chromosome partition protein MukB;
633-901 6.77e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 40.33  E-value: 6.77e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  633 KEAMNRMIDELNKQVSELSQLYKEAQAELEDY-RKRKSLEDVTAEYIHKA---EHEKLMQLTNVSRAKAEDALSEMKSQY 708
Cdd:PRK04863   781 RAAREKRIEQLRAEREELAERYATLSFDVQKLqRLHQAFSRFIGSHLAVAfeaDPEAELRQLNRRRVELERALADHESQE 860

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  709 SKVLNELTQLKQLVDA--QKENSVSI--TEHLQ-VITTLRTAAKEMEEKISNLKEH-------------LASKEVEVAKL 770
Cdd:PRK04863   861 QQQRSQLEQAKEGLSAlnRLLPRLNLlaDETLAdRVEEIREQLDEAEEAKRFVQQHgnalaqlepivsvLQSDPEQFEQL 940

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  771 EKQLLEEKA----------AMTDAMVPRS--SYEKLQSSLESEvSVLASKLKESVKEKEKVHSEV-VQIRSEVSQVkREK 837
Cdd:PRK04863   941 KQDYQQAQQtqrdakqqafALTEVVQRRAhfSYEDAAEMLAKN-SDLNEKLRQRLEQAEQERTRArEQLRQAQAQL-AQY 1018

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462602002  838 ENIQTLLKS----KEQEVNELLQKFQ----QAQEELAEmkRYAESSSKLEE---DKDKKINEMSKEVTKLKEALN 901
Cdd:PRK04863  1019 NQVLASLKSsydaKRQMLQELKQELQdlgvPADSGAEE--RARARRDELHArlsANRSRRNQLEKQLTFCEAEMD 1091
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 755-901 8.66e-03

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 39.23  E-value: 8.66e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  755 NLKEHLAsKEVEVAKLEKQLLEEKAAMTDAMVPRSSyeKLQSSLESEVSVLasklKESVKEKEKVH-SEVVQIRSEVSQV 833
Cdd:smart00787 144 GLKEGLD-ENLEGLKEDYKLLMKELELLNSIKPKLR--DRKDALEEELRQL----KQLEDELEDCDpTELDRAKEKLKKL 216

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462602002  834 KREKENIQTLLKSKEQEVNELLQKFQQAQEELAEMK-RYAESSSKLEEDKDKKInemsKEVTKLKEALN 901
Cdd:smart00787 217 LQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNtEIAEAEKKLEQCRGFTF----KEIEKLKEQLK 281
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 131-234 8.99e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 40.05  E-value: 8.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 131 QGCLQAVQILCEHKSPINLKDLDGNIPLLLAVQNGHSEICHFLLDHGADVNSRNKSGRTALMLACEIGSSNAVEALIKKG 210
Cdd:PHA02876  155 QDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNR 234

                          90       100
                  ....*....|....*....|....*....
gi 2462602002 211 A-----DLNLVDSLGYNALHYSKLSENAG 234
Cdd:PHA02876  235 SninknDLSLLKAIRNEDLETSLLLYDAG 263
PLN03229 PLN03229
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
 591-884 9.40e-03

acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional


Pssm-ID: 178768 [Multi-domain]  Cd Length: 762  Bit Score: 39.84  E-value: 9.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 591 NMNKEKAfLFEKYQEAQEEIMKLKDtlksQMTQEASDEAEDMKEAMNRMIDELNKqvsELSQLYKEA------QAELEDY 664
Cdd:PLN03229  420 NMKKREA-VKTPVRELEGEVEKLKE----QILKAKESSSKPSELALNEMIEKLKK---EIDLEYTEAviamglQERLENL 491

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 665 RKRKS--------LEDVTAEYIHKAEHE----------------KLMQLTNVSRAKaedALSEMKSQYSKVLNELTQ-LK 719
Cdd:PLN03229  492 REEFSkansqdqlMHPVLMEKIEKLKDEfnkrlsrapnylslkyKLDMLNEFSRAK---ALSEKKSKAEKLKAEINKkFK 568

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 720 QLVDA----QKENSVSITEHLQVITTLRTAAKEMEEKISNLKEHLaskEVEVAKLEKQLLEEKAAMTDAMVPRSSY---E 792
Cdd:PLN03229  569 EVMDRpeikEKMEALKAEVASSGASSGDELDDDLKEKVEKMKKEI---ELELAGVLKSMGLEVIGVTKKNKDTAEQtppP 645

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 793 KLQSSLESEVSVLASKLKESVKEKEkVHSEVVQIRSEVSQVKR-----EKENIQTLLKSKEQEV------NELLQKFQQA 861
Cdd:PLN03229  646 NLQEKIESLNEEINKKIERVIRSSD-LKSKIELLKLEVAKASKtpdvtEKEKIEALEQQIKQKIaealnsSELKEKFEEL 724

                         330       340
                  ....*....|....*....|....
gi 2462602002 862 QEELAEMKR-YAESSSKLEEDKDK 884
Cdd:PLN03229  725 EAELAAAREtAAESNGSLKNDDDK 748
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
546-728 9.46e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 40.00  E-value: 9.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 546 EESERNKEKVRELEEKLVE-REKGTVIKPPveeyEEMKSSYcSVIENMNKEKAFLFEKYQEAQEEIMKLKDTLKSQMTQE 624
Cdd:COG3206   182 EQLPELRKELEEAEAALEEfRQKNGLVDLS----EEAKLLL-QQLSELESQLAEARAELAEAEARLAALRAQLGSGPDAL 256

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002 625 ASDEAEDMKEAMNRMIDELNKQVSELSQLY-------KEAQAELEDYRKRksLEDVTAEYIHKAEHEKLMQLTNVSRAKA 697
Cdd:COG3206   257 PELLQSPVIQQLRAQLAELEAELAELSARYtpnhpdvIALRAQIAALRAQ--LQQEAQRILASLEAELEALQAREASLQA 334

                         170       180       190
                  ....*....|....*....|....*....|..
gi 2462602002 698 E-DALSEMKSQYSKVLNELTQLKQLVDAQKEN 728
Cdd:COG3206   335 QlAQLEARLAELPELEAELRRLEREVEVAREL 366
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 432-782 9.70e-03

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


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 39.95  E-value: 9.70e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  432 RIQQLQEILQDLQKRLESSEAERKQLQVELQSRRAELVCLNNTEISENSsdlsQKLKETQSKYEEAMKEVLSVQKQMKLG 511
Cdd:pfam02463  650 KGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQ----LEIKKKEQREKEELKKLKLEAEELLAD 725

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  512 LV------SPESMDNYSHFHELRVTEEEINVLKQDLQNALEESERNKEKVRELEEKLVEREKGTVIKppvEEYEEMKSSY 585
Cdd:pfam02463  726 RVqeaqdkINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEK---EEKLKAQEEE 802

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  586 CSVIENMNKEKAFLFEKYQEAQEEIMKLKDT---LKSQMTQEASDEAEDMKEAMNRMIDELNKQVSELSQLYKEAQAELE 662
Cdd:pfam02463  803 LRALEEELKEEAELLEEEQLLIEQEEKIKEEeleELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQ 882

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602002  663 DYRKRKSLEdVTAEYIHKAEHEKLMQLTNVSRAKAEDALSEMKSQYSKVLNELTQLKQLVDAQKENSVSITEHLQVITTL 742
Cdd:pfam02463  883 KLKDELESK-EEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEER 961

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|
gi 2462602002  743 RTAAKEMEEKISNLKEHLASKEVEVAKLEKQLLEEKAAMT 782
Cdd:pfam02463  962 NKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLE 1001
 
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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