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Conserved domains on  [gi|2528974265|sp|Q8N283|]
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RecName: Full=Ankyrin repeat domain-containing protein 35

Protein Classification

ankyrin repeat domain-containing protein( domain architecture ID 12790726)

ankyrin (ANK) repeat domain-containing protein may be involved in mediating protein-protein interactions; ankyrin repeat (ANK) domain-containing protein may be involved in mediating protein-protein interactions; ankyrin repeat (ANK) domain-containing protein may be involved in mediating protein-protein interactions; ankyrin repeat (ANK) domain-containing protein may be involved in mediating protein-protein interactions; ankyrin repeat domain-containing protein similar to human prostaglandin E receptor 4-associated protein (fem-1 homolog A), which interacts directly with NF-kappaB1 and attenuates macrophage activation; ankyrin repeat (ANK) domain-containing protein may be involved in mediating protein-protein interactions; ankyrin repeat domain-containing protein similar to human prostaglandin E receptor 4-associated protein (fem-1 homolog A), which interacts directly with NF-kappaB1 and attenuates macrophage activation; ankyrin repeat (ANK) domain-containing protein may be involved in mediating protein-protein interactions; ankyrin repeat (ANK) domain-containing protein may be involved in mediating protein-protein interactions; ankyrin repeat domain-containing protein similar to human prostaglandin E receptor 4-associated protein (fem-1 homolog A), which interacts directly with NF-kappaB1 and attenuates macrophage activation; ankyrin repeat (ANK) domain-containing protein may be involved in mediating protein-protein interactions; ankyrin repeat (ANK) domain-containing protein may be involved in mediating protein-protein interactions; ankyrin repeat domain-containing protein similar to human prostaglandin E receptor 4-associated protein (fem-1 homolog A), which interacts directly with NF-kappaB1 and attenuates macrophage activation; ankyrin repeat (ANK) domain-containing protein may be involved in mediating protein-protein interactions; ankyrin repeat domain-containing protein similar to human prostaglandin E receptor 4-associated protein (fem-1 homolog A), which interacts directly with NF-kappaB1 and attenuates macrophage activation

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
24-242 4.08e-48

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 173.22  E-value: 4.08e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265   24 LLEAVHRGDVGRVAALASRKSARPTKLDSNGQSPFHLAASKGLTECLTILLANGADINSKNEDGSTALHLATISCQPQCV 103
Cdd:COG0666     57 LLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIV 136
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  104 KVLLQHGANEDAVDAENRSPLHWAASSGCASSVLLLCDHEAFLDVLDNDGRTPLMIASLGGHAAICSQLLQRGARVNVTD 183
Cdd:COG0666    137 KLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKD 216
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2528974265  184 KNDKSALILACEKGSAEVAELLLSHGADAGAVDSTGHDALHYALHTQDKALWRHLQQAL 242
Cdd:COG0666    217 NDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLAL 275
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
301-960 1.76e-13

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


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 75.09  E-value: 1.76e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  301 KYEEERRKVVRLEQELVQKTEECKTQAAAYLDLENQIREQAQELGVLLSWEPRASGKQGSSLRpggdgmeqgcPKDLLAE 380
Cdd:TIGR02168  268 KLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELES----------KLDELAE 337
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  381 STQELKKQQQAAATVnpVLAPKKAEDSAPGKIQYEVHGRSQPEEQgppqspaSETIRKA---TGQQLTTNGAQTfgpdha 457
Cdd:TIGR02168  338 ELAELEEKLEELKEE--LESLEAELEELEAELEELESRLEELEEQ-------LETLRSKvaqLELQIASLNNEI------ 402
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  458 dQLPAGQKESSQVlGVEPGGTVAEPVGPAAMNQLLLQLREELAAVWREKDAARGALSRPVMEGALGTPRAEAAAAAWEKM 537
Cdd:TIGR02168  403 -ERLEARLERLED-RRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAA 480
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  538 EARLERVLARLEWAKAGLQ--------VKPEVPSQESREGALKAAPGSIKQDEEKEKRVPGAQGEPLGALGGE------K 603
Cdd:TIGR02168  481 ERELAQLQARLDSLERLQEnlegfsegVKALLKNQSGLSGILGVLSELISVDEGYEAAIEAALGGRLQAVVVEnlnaakK 560
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  604 ALGGLAKGQLEK-EMSVLRLSNSNLLEelgelGRERQRLQRELQSLSQRLQREFVPkPQAQVQLQQLRQSVgLLTNELAm 682
Cdd:TIGR02168  561 AIAFLKQNELGRvTFLPLDSIKGTEIQ-----GNDREILKNIEGFLGVAKDLVKFD-PKLRKALSYLLGGV-LVVDDLD- 632
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  683 ekEATEKLRKLlasqssGLRGLWDCLPADLVGERSAQSKAAES-----------LEELRACISTLVDRHREAQQVLARLQ 751
Cdd:TIGR02168  633 --NALELAKKL------RPGYRIVTLDGDLVRPGGVITGGSAKtnssilerrreIEELEEKIEELEEKIAELEKALAELR 704
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  752 EENQQLRGSLSPCREPGTSLkapaSPQVAALEQDLGKLEEELRAVQATMSGKSQEIGKLKQLLYQATEEVAELRAREAAs 831
Cdd:TIGR02168  705 KELEELEEELEQLRKELEEL----SRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAE- 779
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  832 lrqHEKTRGSLVAQAQAWGQELKALLEKYNTACREVGRLREAVAEERRRSGDLAAQAAEQERQASEMRGRSEQFEKTAEL 911
Cdd:TIGR02168  780 ---AEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIES 856
                          650       660       670       680
                   ....*....|....*....|....*....|....*....|....*....
gi 2528974265  912 LKEKMEHLIGACRDKEAKIKELLKKLEQLSEEVLAIRGENARLALQLQD 960
Cdd:TIGR02168  857 LAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRE 905
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
24-242 4.08e-48

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 173.22  E-value: 4.08e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265   24 LLEAVHRGDVGRVAALASRKSARPTKLDSNGQSPFHLAASKGLTECLTILLANGADINSKNEDGSTALHLATISCQPQCV 103
Cdd:COG0666     57 LLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIV 136
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  104 KVLLQHGANEDAVDAENRSPLHWAASSGCASSVLLLCDHEAFLDVLDNDGRTPLMIASLGGHAAICSQLLQRGARVNVTD 183
Cdd:COG0666    137 KLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKD 216
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2528974265  184 KNDKSALILACEKGSAEVAELLLSHGADAGAVDSTGHDALHYALHTQDKALWRHLQQAL 242
Cdd:COG0666    217 NDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLAL 275
PHA02875 PHA02875
ankyrin repeat protein; Provisional
55-215 1.32e-21

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 98.52  E-value: 1.32e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265   55 QSPFHLAASKGLTECLTILLANGADINSK-NEDGSTALHLATISCQPQCVKVLLQHGANEDAVDAENRSPLHWAASSGCA 133
Cdd:PHA02875    69 ESELHDAVEEGDVKAVEELLDLGKFADDVfYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDI 148
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  134 SSVLLLCDHEAFLDVLDNDGRTPLMIASLGGHAAICSQLLQRGARVNVTDKN-DKSALILACEKGSAEVAELLLSHGADA 212
Cdd:PHA02875   149 KGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNgCVAALCYAIENNKIDIVRLFIKRGADC 228

                   ...
gi 2528974265  213 GAV 215
Cdd:PHA02875   229 NIM 231
Ank_2 pfam12796
Ankyrin repeats (3 copies);
58-150 1.61e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 87.09  E-value: 1.61e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265   58 FHLAASKGLTECLTILLANGADINSKNEDGSTALHLATISCQPQCVKVLLQHGANEDavDAENRSPLHWAASSGCASSVL 137
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL--KDNGRTALHYAARSGHLEIVK 78
                           90
                   ....*....|...
gi 2528974265  138 LLCDHEAFLDVLD 150
Cdd:pfam12796   79 LLLEKGADINVKD 91
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
301-960 1.76e-13

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 75.09  E-value: 1.76e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  301 KYEEERRKVVRLEQELVQKTEECKTQAAAYLDLENQIREQAQELGVLLSWEPRASGKQGSSLRpggdgmeqgcPKDLLAE 380
Cdd:TIGR02168  268 KLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELES----------KLDELAE 337
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  381 STQELKKQQQAAATVnpVLAPKKAEDSAPGKIQYEVHGRSQPEEQgppqspaSETIRKA---TGQQLTTNGAQTfgpdha 457
Cdd:TIGR02168  338 ELAELEEKLEELKEE--LESLEAELEELEAELEELESRLEELEEQ-------LETLRSKvaqLELQIASLNNEI------ 402
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  458 dQLPAGQKESSQVlGVEPGGTVAEPVGPAAMNQLLLQLREELAAVWREKDAARGALSRPVMEGALGTPRAEAAAAAWEKM 537
Cdd:TIGR02168  403 -ERLEARLERLED-RRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAA 480
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  538 EARLERVLARLEWAKAGLQ--------VKPEVPSQESREGALKAAPGSIKQDEEKEKRVPGAQGEPLGALGGE------K 603
Cdd:TIGR02168  481 ERELAQLQARLDSLERLQEnlegfsegVKALLKNQSGLSGILGVLSELISVDEGYEAAIEAALGGRLQAVVVEnlnaakK 560
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  604 ALGGLAKGQLEK-EMSVLRLSNSNLLEelgelGRERQRLQRELQSLSQRLQREFVPkPQAQVQLQQLRQSVgLLTNELAm 682
Cdd:TIGR02168  561 AIAFLKQNELGRvTFLPLDSIKGTEIQ-----GNDREILKNIEGFLGVAKDLVKFD-PKLRKALSYLLGGV-LVVDDLD- 632
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  683 ekEATEKLRKLlasqssGLRGLWDCLPADLVGERSAQSKAAES-----------LEELRACISTLVDRHREAQQVLARLQ 751
Cdd:TIGR02168  633 --NALELAKKL------RPGYRIVTLDGDLVRPGGVITGGSAKtnssilerrreIEELEEKIEELEEKIAELEKALAELR 704
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  752 EENQQLRGSLSPCREPGTSLkapaSPQVAALEQDLGKLEEELRAVQATMSGKSQEIGKLKQLLYQATEEVAELRAREAAs 831
Cdd:TIGR02168  705 KELEELEEELEQLRKELEEL----SRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAE- 779
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  832 lrqHEKTRGSLVAQAQAWGQELKALLEKYNTACREVGRLREAVAEERRRSGDLAAQAAEQERQASEMRGRSEQFEKTAEL 911
Cdd:TIGR02168  780 ---AEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIES 856
                          650       660       670       680
                   ....*....|....*....|....*....|....*....|....*....
gi 2528974265  912 LKEKMEHLIGACRDKEAKIKELLKKLEQLSEEVLAIRGENARLALQLQD 960
Cdd:TIGR02168  857 LAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRE 905
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
631-975 2.42e-13

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 74.59  E-value: 2.42e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  631 LGELGRERQRLQRE------LQSLSQRLQREfvpkpQAQVQLQQLRQsvglLTNELAMEKEATEKLRKLLASQssglrgl 704
Cdd:COG1196    195 LGELERQLEPLERQaekaerYRELKEELKEL-----EAELLLLKLRE----LEAELEELEAELEELEAELEEL------- 258
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  705 wdclpadlvgeRSAQSKAAESLEELRACISTLVDRHREAQQVLARLQEENQQLRGSLSPCREpgtslkapaspQVAALEQ 784
Cdd:COG1196    259 -----------EAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEE-----------RRRELEE 316
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  785 DLGKLEEELRAVQATMSGKSQEIGKLKQLLYQATEEVAELRAREAaslrQHEKTRGSLVAQAQAWGQELKALLEKYNTAC 864
Cdd:COG1196    317 RLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELA----EAEEALLEAEAELAEAEEELEELAEELLEAL 392
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  865 REVGRLREAVAEERRRSGDLAAQAAEQERQASEMRGRSEQFEKTAELLKEKMEHLIGACRDKEAKIKELLKKLEQLSEEV 944
Cdd:COG1196    393 RAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEA 472
                          330       340       350
                   ....*....|....*....|....*....|.
gi 2528974265  945 LAIRGENARLALQLQDSQKNHEEIISTYRNH 975
Cdd:COG1196    473 ALLEAALAELLEELAEAAARLLLLLEAEADY 503
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
613-955 4.00e-09

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 60.82  E-value: 4.00e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  613 LEKEMSVLRLSNSNLLEELGELGRERQRLQRELQSLSQRLQREFVPKPQAQVQLQQLRQSVGLLTNELAMEKEATEKLRk 692
Cdd:PRK02224   277 LAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLE- 355
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  693 llaSQSSGLRGLWDCLPADLVGERSAQSKAAESLEELRACISTLVDRHREAQQVLARLQEENQQLRGSLSPCREpgtslk 772
Cdd:PRK02224   356 ---ERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELRE------ 426
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  773 apaspQVAALEQDLGKLEEELRAVQA---------------------TMSGKSQEIGKLKQLLYQATEEVAELRAR--EA 829
Cdd:PRK02224   427 -----REAELEATLRTARERVEEAEAlleagkcpecgqpvegsphveTIEEDRERVEELEAELEDLEEEVEEVEERleRA 501
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  830 ASLRQHEKTRGSLVAQAQAWGQELKallEKYNTACREvgrlREAVAEERRRSGDLAAQAAEQERQASEMRGRSEQ-FEKT 908
Cdd:PRK02224   502 EDLVEAEDRIERLEERREDLEELIA---ERRETIEEK----RERAEELRERAAELEAEAEEKREAAAEAEEEAEEaREEV 574
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*..
gi 2528974265  909 AELLKEKMEhlIGACRDKEAKIKELLKKLEQLSEEVLAIRGENARLA 955
Cdd:PRK02224   575 AELNSKLAE--LKERIESLERIRTLLAAIADAEDEIERLREKREALA 619
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
612-983 7.70e-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: 56.67  E-value: 7.70e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  612 QLEKEmsvLRLSNSnlleELGELGRERQRLQRELQSLSQrlqrefvpkpqaqvQLQQLRQSVGLLTNELAMEKEATEKlr 691
Cdd:pfam15921  346 ELEKQ---LVLANS----ELTEARTERDQFSQESGNLDD--------------QLQKLLADLHKREKELSLEKEQNKR-- 402
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  692 kllasqssglrgLWDclpadlvgersAQSKAAESLEELRaciSTLVDRHREAQQVLARLQ----EENQQLRGSLSPCREP 767
Cdd:pfam15921  403 ------------LWD-----------RDTGNSITIDHLR---RELDDRNMEVQRLEALLKamksECQGQMERQMAAIQGK 456
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  768 GTSLKAPAS--PQVAALEQDLGKLEEELRAVQATMSGKSQEIGKL------KQLLYQATE-EVAELRAREAASLR--QHE 836
Cdd:pfam15921  457 NESLEKVSSltAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLtaslqeKERAIEATNaEITKLRSRVDLKLQelQHL 536
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  837 KTRGSLVAQAQAWGQELKALLEKYNTAC----REVGRLREAVAEERRRSGDLAAQAAEQERQASEMRGRSEQFektaELL 912
Cdd:pfam15921  537 KNEGDHLRNVQTECEALKLQMAEKDKVIeilrQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEF----KIL 612
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2528974265  913 KEKmehligacrdKEAKIKELLKKLEQLSEEVLAIRGENARLALQLQDSQKNHEEI---ISTYRNHLLNAARGY 983
Cdd:pfam15921  613 KDK----------KDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLlneVKTSRNELNSLSEDY 676
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
24-175 1.64e-06

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: 52.01  E-value: 1.64e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265   24 LLEAVHRGDVGRVAALASRKSaRPTKldsnGQSPFHLAASKGLTECLTILLANGADIN----------SKNED----GST 89
Cdd:TIGR00870  103 HLLAAFRKSGPLELANDQYTS-EFTP----GITALHLAAHRQNYEIVKLLLERGASVParacgdffvkSQGVDsfyhGES 177
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265   90 ALHLATISCQPQCVKVLLQHGANEDAVDAENRSPLHWAA------------SSGCASSVL----LLCDHEAFLDVLDNDG 153
Cdd:TIGR00870  178 PLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLVmenefkaeyeelSCQMYNFALslldKLRDSKELEVILNHQG 257
                          170       180
                   ....*....|....*....|..
gi 2528974265  154 RTPLMIASLGGHAAICSQLLQR 175
Cdd:TIGR00870  258 LTPLKLAAKEGRIVLFRLKLAI 279
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
56-224 4.10e-05

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: 47.31  E-value: 4.10e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265   56 SPFHLAASKGLTECLTILL-ANGADINSKNEDGSTALHLATISCQPQCVKVLLQhgANEDAVDAENRSPLHwaassgcas 134
Cdd:cd22192     19 SPLLLAAKENDVQAIKKLLkCPSCDLFQRGALGETALHVAALYDNLEAAVVLME--AAPELVNEPMTSDLY--------- 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  135 svlllcdheafldvldnDGRTPLMIASLGGHAAICSQLLQRGARVN---VTD----KNDKSAL-----IL---ACEkGSA 199
Cdd:cd22192     88 -----------------QGETALHIAVVNQNLNLVRELIARGADVVsprATGtffrPGPKNLIyygehPLsfaACV-GNE 149
                          170       180
                   ....*....|....*....|....*
gi 2528974265  200 EVAELLLSHGADAGAVDSTGHDALH 224
Cdd:cd22192    150 EIVRLLIEHGADIRAQDSLGNTVLH 174
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
53-81 2.59e-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: 39.11  E-value: 2.59e-04
                            10        20
                    ....*....|....*....|....*....
gi 2528974265    53 NGQSPFHLAASKGLTECLTILLANGADIN 81
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
24-242 4.08e-48

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 173.22  E-value: 4.08e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265   24 LLEAVHRGDVGRVAALASRKSARPTKLDSNGQSPFHLAASKGLTECLTILLANGADINSKNEDGSTALHLATISCQPQCV 103
Cdd:COG0666     57 LLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIV 136
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  104 KVLLQHGANEDAVDAENRSPLHWAASSGCASSVLLLCDHEAFLDVLDNDGRTPLMIASLGGHAAICSQLLQRGARVNVTD 183
Cdd:COG0666    137 KLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKD 216
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2528974265  184 KNDKSALILACEKGSAEVAELLLSHGADAGAVDSTGHDALHYALHTQDKALWRHLQQAL 242
Cdd:COG0666    217 NDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLAL 275
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
18-262 5.15e-43

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 158.58  E-value: 5.15e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265   18 NRHDQKLLEAVHRGDVGRVAALASRKSARPTKLDSNGQSPFHLAASKGLTECLTILLANGADINSKNEDGSTALHLATIS 97
Cdd:COG0666     18 LLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARN 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265   98 CQPQCVKVLLQHGANEDAVDAENRSPLHWAASSGCASSVLLLCDHEAFLDVLDNDGRTPLMIASLGGHAAICSQLLQRGA 177
Cdd:COG0666     98 GDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGA 177
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  178 RVNVTDKNDKSALILACEKGSAEVAELLLSHGADAGAVDSTGHDALHYALHTQDKALWRHLQQALSRRRRGGQRLVQHPD 257
Cdd:COG0666    178 DVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALL 257

                   ....*
gi 2528974265  258 LASQA 262
Cdd:COG0666    258 LAAAA 262
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
24-223 4.76e-40

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 150.10  E-value: 4.76e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265   24 LLEAVHRGDVGRVAALASRKsARPTKLDSNGQSPFHLAASKGLTECLTILLANGADINSKNEDGSTALHLATISCQPQCV 103
Cdd:COG0666     91 LHAAARNGDLEIVKLLLEAG-ADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIV 169
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  104 KVLLQHGANEDAVDAENRSPLHWAASSGCASSVLLLCDHEAFLDVLDNDGRTPLMIASLGGHAAICSQLLQRGARVNVTD 183
Cdd:COG0666    170 KLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKD 249
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 2528974265  184 KNDKSALILACEKGSAEVAELLLSHGADAGAVDSTGHDAL 223
Cdd:COG0666    250 KDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
36-238 2.56e-31

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 124.68  E-value: 2.56e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265   36 VAALASRKSARPTKLDSNGQSPFHLAASKGLTECLTILLANGADINSKNEDGSTALHLATISCQPQCVKVLLQHGANEDA 115
Cdd:COG0666      3 LLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINA 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  116 VDAENRSPLHWAASSGCASSVLLLCDHEAFLDVLDNDGRTPLMIASLGGHAAICSQLLQRGARVNVTDKNDKSALILACE 195
Cdd:COG0666     83 KDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAA 162
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 2528974265  196 KGSAEVAELLLSHGADAGAVDSTGHDALHYALHTQDKALWRHL 238
Cdd:COG0666    163 NGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLL 205
PHA02875 PHA02875
ankyrin repeat protein; Provisional
55-215 1.32e-21

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 98.52  E-value: 1.32e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265   55 QSPFHLAASKGLTECLTILLANGADINSK-NEDGSTALHLATISCQPQCVKVLLQHGANEDAVDAENRSPLHWAASSGCA 133
Cdd:PHA02875    69 ESELHDAVEEGDVKAVEELLDLGKFADDVfYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDI 148
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  134 SSVLLLCDHEAFLDVLDNDGRTPLMIASLGGHAAICSQLLQRGARVNVTDKN-DKSALILACEKGSAEVAELLLSHGADA 212
Cdd:PHA02875   149 KGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNgCVAALCYAIENNKIDIVRLFIKRGADC 228

                   ...
gi 2528974265  213 GAV 215
Cdd:PHA02875   229 NIM 231
Ank_2 pfam12796
Ankyrin repeats (3 copies);
58-150 1.61e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 87.09  E-value: 1.61e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265   58 FHLAASKGLTECLTILLANGADINSKNEDGSTALHLATISCQPQCVKVLLQHGANEDavDAENRSPLHWAASSGCASSVL 137
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL--KDNGRTALHYAARSGHLEIVK 78
                           90
                   ....*....|...
gi 2528974265  138 LLCDHEAFLDVLD 150
Cdd:pfam12796   79 LLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
124-216 1.68e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 84.01  E-value: 1.68e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  124 LHWAASSGCASSVLLLCDHEAFLDVLDNDGRTPLMIASLGGHAAICSQLLQRgARVNVTDkNDKSALILACEKGSAEVAE 203
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78
                           90
                   ....*....|...
gi 2528974265  204 LLLSHGADAGAVD 216
Cdd:pfam12796   79 LLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
32-218 1.47e-18

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 89.34  E-value: 1.47e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265   32 DVGRVAALASRKSARPTKLDSNGQSPFHLAASK--GLTECLTILLANGADINSKNEDGSTALHLATISCQP--QCVKVLL 107
Cdd:PHA03100    84 DVKEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLI 163
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  108 QHGANedaVDAENRsplhwaassgcassVLLLCDHEAFLDVLDNDGRTPLMIASLGGHAAICSQLLQRGARVNVTDKNDK 187
Cdd:PHA03100   164 DKGVD---INAKNR--------------VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGD 226
                          170       180       190
                   ....*....|....*....|....*....|.
gi 2528974265  188 SALILACEKGSAEVAELLLSHGADAGAVDST 218
Cdd:PHA03100   227 TPLHIAILNNNKEIFKLLLNNGPSIKTIIET 257
PHA02874 PHA02874
ankyrin repeat protein; Provisional
51-227 2.71e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 82.70  E-value: 2.71e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265   51 DSNGQSPFHLAASKGLTECLTILLANGADINSKNEDGSTALHLATISCQPQCVKVLLQHGANEDAVDAENRSPLHWAASS 130
Cdd:PHA02874   121 DAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEY 200
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  131 GCASSVLLLCDHEAFLDVLDNDGRTPLMIASLGGHAAIcsQLLQRGARVNVTDKNDKSALILA----CEKgsaEVAELLL 206
Cdd:PHA02874   201 GDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRSAI--ELLINNASINDQDIDGSTPLHHAinppCDI---DIIDILL 275
                          170       180
                   ....*....|....*....|.
gi 2528974265  207 SHGADAGAVDSTGHDALHYAL 227
Cdd:PHA02874   276 YHKADISIKDNKGENPIDTAF 296
PHA03100 PHA03100
ankyrin repeat protein; Provisional
57-234 8.65e-16

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 80.86  E-value: 8.65e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265   57 PFHLAASKGLTECLTILLANGADINSKNEDGSTALHLAT-----ISCQPQCVKVLLQHGANEDAVDAENRSPLHWAAS-- 129
Cdd:PHA03100    38 PLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSnikynLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISkk 117
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  130 SGCASSVLLLCDHEAFLDVLDNDGRTPLMIASLGGHA--AICSQLLQRGARVNV----------------TDKNDKSALI 191
Cdd:PHA03100   118 SNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKGVDINAknrvnyllsygvpiniKDVYGFTPLH 197
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 2528974265  192 LACEKGSAEVAELLLSHGADAGAVDSTGHDALHYALHTQDKAL 234
Cdd:PHA03100   198 YAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEI 240
PHA03095 PHA03095
ankyrin-like protein; Provisional
51-238 2.07e-15

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 80.07  E-value: 2.07e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265   51 DSNGQSPFHLAASKGLTE-CLTILLANGADINSKNEDGSTALH--LATISCQPQCVKVLLQHGANEDAVDAENRSPLH-W 126
Cdd:PHA03095    80 ERCGFTPLHLYLYNATTLdVIKLLIKAGADVNAKDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAvL 159
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  127 AASSGCASSVL-LLCDHEAFLDVLDNDGRTPL--MIASLGGHAAICSQLLQRGARVNVTDKNDKSALILACEKGS--AEV 201
Cdd:PHA03095   160 LKSRNANVELLrLLIDAGADVYAVDDRFRSLLhhHLQSFKPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSckRSL 239
                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 2528974265  202 AELLLSHGADAGAVDSTGHDALHYALHTQDKALWRHL 238
Cdd:PHA03095   240 VLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRL 276
PHA02876 PHA02876
ankyrin repeat protein; Provisional
54-227 1.03e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 78.57  E-value: 1.03e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265   54 GQSPFHLAASKGL-TECLTILLANGADINSKNEDGSTALHLA-TISCQPQCVKVLLQHGANEDAVDAENRSPLHWAASSG 131
Cdd:PHA02876   307 GETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQAsTLDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRN 386
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  132 CASSVLLLCDHEAFLDVLDNDGRTPLMIASLGGHAAICSQ-LLQRGARVNVTDKNDKSALILACEKG-SAEVAELLLSHG 209
Cdd:PHA02876   387 NVVIINTLLDYGADIEALSQKIGTALHFALCGTNPYMSVKtLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNG 466
                          170
                   ....*....|....*...
gi 2528974265  210 ADAGAVDSTGHDALHYAL 227
Cdd:PHA02876   467 ADVNAINIQNQYPLLIAL 484
PHA03095 PHA03095
ankyrin-like protein; Provisional
35-230 1.19e-14

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 77.76  E-value: 1.19e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265   35 RVAALASRKSARPTKLDSNGQSPFHLAASkGL---TECLTILLANGADINSKNEDGSTALHLATIS--CQPQCVKVLLQH 109
Cdd:PHA03095    98 DVIKLLIKAGADVNAKDKVGRTPLHVYLS-GFninPKVIRLLLRKGADVNALDLYGMTPLAVLLKSrnANVELLRLLIDA 176
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  110 GANEDAVDAENRSPLHWAASSGCASS------VLLLCDHEAfldvLDNDGRTPLMIASLGG--HAAICSQLLQRGARVNV 181
Cdd:PHA03095   177 GADVYAVDDRFRSLLHHHLQSFKPRArivrelIRAGCDPAA----TDMLGNTPLHSMATGSscKRSLVLPLLIAGISINA 252
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2528974265  182 TDKNDKSALILACEKGSAEVAELLLSHGADAGAVDSTG------------HDALHYALHTQ 230
Cdd:PHA03095   253 RNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGntplslmvrnnnGRAVRAALAKN 313
Ank_2 pfam12796
Ankyrin repeats (3 copies);
24-117 2.24e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 69.37  E-value: 2.24e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265   24 LLEAVHRGDVGRVAALASRKsARPTKLDSNGQSPFHLAASKGLTECLTILLANgADINSKNeDGSTALHLATISCQPQCV 103
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENG-ADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIV 77
                           90
                   ....*....|....
gi 2528974265  104 KVLLQHGANEDAVD 117
Cdd:pfam12796   78 KLLLEKGADINVKD 91
PHA02878 PHA02878
ankyrin repeat protein; Provisional
67-217 5.21e-14

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 75.69  E-value: 5.21e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265   67 TECLTILLANGADINSKNED-GSTALHLATISCQPQCVKVLLQHGANEDAVDAENRSPLHWAASSGCASSVLLLCDHEAF 145
Cdd:PHA02878   147 AEITKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGAS 226
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2528974265  146 LDVLDNDGRTPLMIASlgGHA---AICSQLLQRGARVNVTDK-NDKSALILACEkgSAEVAELLLSHGADAGAVDS 217
Cdd:PHA02878   227 TDARDKCGNTPLHISV--GYCkdyDILKLLLEHGVDVNAKSYiLGLTALHSSIK--SERKLKLLLEYGADINSLNS 298
PHA03095 PHA03095
ankyrin-like protein; Provisional
54-234 8.91e-14

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 75.06  E-value: 8.91e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265   54 GQSPFHLAASKGLTECLTI---LLANGADINSKNEDGSTALHL-ATISCQPQCVKVLLQHGANEDAVDAENRSPLHWAAS 129
Cdd:PHA03095    47 GKTPLHLYLHYSSEKVKDIvrlLLEAGADVNAPERCGFTPLHLyLYNATTLDVIKLLIKAGADVNAKDKVGRTPLHVYLS 126
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  130 SGC--ASSVLLLCDHEAFLDVLDNDGRTPL--MIASLGGHAAICSQLLQRGARVNVTDKNDKSALILACE--KGSAEVAE 203
Cdd:PHA03095   127 GFNinPKVIRLLLRKGADVNALDLYGMTPLavLLKSRNANVELLRLLIDAGADVYAVDDRFRSLLHHHLQsfKPRARIVR 206
                          170       180       190
                   ....*....|....*....|....*....|..
gi 2528974265  204 LLLSHGADAGAVDSTGHDALHY-ALHTQDKAL 234
Cdd:PHA03095   207 ELIRAGCDPAATDMLGNTPLHSmATGSSCKRS 238
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
301-960 1.76e-13

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 75.09  E-value: 1.76e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  301 KYEEERRKVVRLEQELVQKTEECKTQAAAYLDLENQIREQAQELGVLLSWEPRASGKQGSSLRpggdgmeqgcPKDLLAE 380
Cdd:TIGR02168  268 KLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELES----------KLDELAE 337
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  381 STQELKKQQQAAATVnpVLAPKKAEDSAPGKIQYEVHGRSQPEEQgppqspaSETIRKA---TGQQLTTNGAQTfgpdha 457
Cdd:TIGR02168  338 ELAELEEKLEELKEE--LESLEAELEELEAELEELESRLEELEEQ-------LETLRSKvaqLELQIASLNNEI------ 402
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  458 dQLPAGQKESSQVlGVEPGGTVAEPVGPAAMNQLLLQLREELAAVWREKDAARGALSRPVMEGALGTPRAEAAAAAWEKM 537
Cdd:TIGR02168  403 -ERLEARLERLED-RRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAA 480
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  538 EARLERVLARLEWAKAGLQ--------VKPEVPSQESREGALKAAPGSIKQDEEKEKRVPGAQGEPLGALGGE------K 603
Cdd:TIGR02168  481 ERELAQLQARLDSLERLQEnlegfsegVKALLKNQSGLSGILGVLSELISVDEGYEAAIEAALGGRLQAVVVEnlnaakK 560
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  604 ALGGLAKGQLEK-EMSVLRLSNSNLLEelgelGRERQRLQRELQSLSQRLQREFVPkPQAQVQLQQLRQSVgLLTNELAm 682
Cdd:TIGR02168  561 AIAFLKQNELGRvTFLPLDSIKGTEIQ-----GNDREILKNIEGFLGVAKDLVKFD-PKLRKALSYLLGGV-LVVDDLD- 632
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  683 ekEATEKLRKLlasqssGLRGLWDCLPADLVGERSAQSKAAES-----------LEELRACISTLVDRHREAQQVLARLQ 751
Cdd:TIGR02168  633 --NALELAKKL------RPGYRIVTLDGDLVRPGGVITGGSAKtnssilerrreIEELEEKIEELEEKIAELEKALAELR 704
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  752 EENQQLRGSLSPCREPGTSLkapaSPQVAALEQDLGKLEEELRAVQATMSGKSQEIGKLKQLLYQATEEVAELRAREAAs 831
Cdd:TIGR02168  705 KELEELEEELEQLRKELEEL----SRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAE- 779
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  832 lrqHEKTRGSLVAQAQAWGQELKALLEKYNTACREVGRLREAVAEERRRSGDLAAQAAEQERQASEMRGRSEQFEKTAEL 911
Cdd:TIGR02168  780 ---AEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIES 856
                          650       660       670       680
                   ....*....|....*....|....*....|....*....|....*....
gi 2528974265  912 LKEKMEHLIGACRDKEAKIKELLKKLEQLSEEVLAIRGENARLALQLQD 960
Cdd:TIGR02168  857 LAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRE 905
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
631-975 2.42e-13

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 74.59  E-value: 2.42e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  631 LGELGRERQRLQRE------LQSLSQRLQREfvpkpQAQVQLQQLRQsvglLTNELAMEKEATEKLRKLLASQssglrgl 704
Cdd:COG1196    195 LGELERQLEPLERQaekaerYRELKEELKEL-----EAELLLLKLRE----LEAELEELEAELEELEAELEEL------- 258
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  705 wdclpadlvgeRSAQSKAAESLEELRACISTLVDRHREAQQVLARLQEENQQLRGSLSPCREpgtslkapaspQVAALEQ 784
Cdd:COG1196    259 -----------EAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEE-----------RRRELEE 316
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  785 DLGKLEEELRAVQATMSGKSQEIGKLKQLLYQATEEVAELRAREAaslrQHEKTRGSLVAQAQAWGQELKALLEKYNTAC 864
Cdd:COG1196    317 RLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELA----EAEEALLEAEAELAEAEEELEELAEELLEAL 392
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  865 REVGRLREAVAEERRRSGDLAAQAAEQERQASEMRGRSEQFEKTAELLKEKMEHLIGACRDKEAKIKELLKKLEQLSEEV 944
Cdd:COG1196    393 RAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEA 472
                          330       340       350
                   ....*....|....*....|....*....|.
gi 2528974265  945 LAIRGENARLALQLQDSQKNHEEIISTYRNH 975
Cdd:COG1196    473 ALLEAALAELLEELAEAAARLLLLLEAEADY 503
Ank_2 pfam12796
Ankyrin repeats (3 copies);
157-226 2.64e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 66.29  E-value: 2.64e-13
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  157 LMIASLGGHAAICSQLLQRGARVNVTDKNDKSALILACEKGSAEVAELLLSHgADAGAVDStGHDALHYA 226
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYA 68
PHA03095 PHA03095
ankyrin-like protein; Provisional
73-225 3.35e-13

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 73.14  E-value: 3.35e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265   73 LLANGADINSKNEDGSTALHLATISCQPQCVKV---LLQHGANEDAVDAENRSPLHWAASSGCASSVL-LLCDHEAFLDV 148
Cdd:PHA03095    33 LLAAGADVNFRGEYGKTPLHLYLHYSSEKVKDIvrlLLEAGADVNAPERCGFTPLHLYLYNATTLDVIkLLIKAGADVNA 112
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  149 LDNDGRTPLMI--ASLGGHAAICSQLLQRGARVNVTDKNDKSAL-ILACEKG-SAEVAELLLSHGADAGAVDSTGHDALH 224
Cdd:PHA03095   113 KDKVGRTPLHVylSGFNINPKVIRLLLRKGADVNALDLYGMTPLaVLLKSRNaNVELLRLLIDAGADVYAVDDRFRSLLH 192

                   .
gi 2528974265  225 Y 225
Cdd:PHA03095   193 H 193
PHA02875 PHA02875
ankyrin repeat protein; Provisional
70-238 2.37e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 70.02  E-value: 2.37e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265   70 LTILLANGADINSKNEDGSTALHLATISCQPQCVKVLLQHGANEDAVDAENRSPLHWAASSGCASSVLLLCDHEAFL-DV 148
Cdd:PHA02875    18 ARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFAdDV 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  149 LDNDGRTPLMIASLGGHAAICSQLLQRGARVNVTDKNDKSALILACEKGSAEVAELLLSHGADAGAVDSTGHDALHYALH 228
Cdd:PHA02875    98 FYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMA 177
                          170
                   ....*....|
gi 2528974265  229 TQDKALWRHL 238
Cdd:PHA02875   178 KGDIAICKML 187
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
628-963 1.09e-11

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 69.33  E-value: 1.09e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  628 LEELGELGRERQRLQRELQSLSQRLQREFVPKPQA------QVQLQQLRQSvglltnELAMEKEATEKLRKLLASQSSGL 701
Cdd:TIGR02169  176 LEELEEVEENIERLDLIIDEKRQQLERLRREREKAeryqalLKEKREYEGY------ELLKEKEALERQKEAIERQLASL 249
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  702 RGLWdclpADLVGERSAQSKAAESLEELRACISTLVDRHREAQQVlaRLQEENQQLRGSLSPCREpgtSLKAPASpQVAA 781
Cdd:TIGR02169  250 EEEL----EKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQL--RVKEKIGELEAEIASLER---SIAEKER-ELED 319
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  782 LEQDLGKLEEELRAVQATMSGKSQEIGKLKQLLYQATEEVAELRAREAASLRQHEktrgSLVAQAQAWGQELKALLEKYN 861
Cdd:TIGR02169  320 AEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELE----EVDKEFAETRDELKDYREKLE 395
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  862 TACREVGRLREavaeERRRSGDLAAQAaeqerqasemRGRSEQFEKTAELLKEKMEHLIGACRDKEAKIKELLKKLEQLS 941
Cdd:TIGR02169  396 KLKREINELKR----ELDRLQEELQRL----------SEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLA 461
                          330       340
                   ....*....|....*....|..
gi 2528974265  942 EEVLAIRGENARLALQLQDSQK 963
Cdd:TIGR02169  462 ADLSKYEQELYDLKEEYDRVEK 483
PHA02874 PHA02874
ankyrin repeat protein; Provisional
24-227 3.96e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 66.53  E-value: 3.96e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265   24 LLEAVHRGDVgRVAALASRKSARPTKLDSNGQSPFHLAASKGLTECLTILLANGADinsknedgSTALHLATIscQPQCV 103
Cdd:PHA02874    39 LIDAIRSGDA-KIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVD--------TSILPIPCI--EKDMI 107
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  104 KVLLQHGANEDAVDAENRSPLHWAASSGCASSVLLLCDHEAFLDVLDNDGRTPLMIASLGGHAAICSQLLQRGARVNVTD 183
Cdd:PHA02874   108 KTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKD 187
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 2528974265  184 KNDKSALILACEKGSAEVAELLLSHGADAGAVDSTGHDALHYAL 227
Cdd:PHA02874   188 NNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAI 231
PHA03100 PHA03100
ankyrin repeat protein; Provisional
120-227 8.30e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 65.46  E-value: 8.30e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  120 NRSPLHWAASSGCASSVLLLCDHEAFLDVLDNDGRTPLMIASLGGHAA-----ICSQLLQRGARVNVTDKNDKSALILA- 193
Cdd:PHA03100    35 PVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNLtdvkeIVKLLLEYGANVNAPDNNGITPLLYAi 114
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 2528974265  194 -CEKGSAEVAELLLSHGADAGAVDSTGHDALHYAL 227
Cdd:PHA03100   115 sKKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYL 149
PHA02876 PHA02876
ankyrin repeat protein; Provisional
23-226 1.36e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 65.47  E-value: 1.36e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265   23 KLLEAVHRGDVGRVAALASRKSARPTKLDSNGQSPFHLAASKGLTECLTILLANGADINSKNEDGSTALHLATISCQPQC 102
Cdd:PHA02876   147 KLIKERIQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDT 226
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  103 VKVLLQHGANedaVDAENRSPLHWAASSGCASSvLLLCDHEAFLDVLDNDGRTPLMIASLGGH-AAICSQLLQRGARVNV 181
Cdd:PHA02876   227 IKAIIDNRSN---INKNDLSLLKAIRNEDLETS-LLLYDAGFSVNSIDDCKNTPLHHASQAPSlSRLVPKLLERGADVNA 302
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 2528974265  182 TDKNDKSALILACEKG-SAEVAELLLSHGADAGAVDSTGHDALHYA 226
Cdd:PHA02876   303 KNIKGETPLYLMAKNGyDTENIRTLIMLGADVNAADRLYITPLHQA 348
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
128-208 1.81e-10

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 64.92  E-value: 1.81e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  128 ASSGCASSVLLLCDHEAFLDVLDNDGRTPLMIASLGGHAAICSQLLQRGARVNVTDKNDKSALILACEKGSAEVAELLLS 207
Cdd:PTZ00322    90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169

                   .
gi 2528974265  208 H 208
Cdd:PTZ00322   170 H 170
PHA02876 PHA02876
ankyrin repeat protein; Provisional
18-228 3.61e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 63.93  E-value: 3.61e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265   18 NRHDQKLLEAVHRGDVgRVAALASRKSARPTKLDSNGQSPFHLAA-SKGLTECLTILLANGADINSKNEDGSTALHL-AT 95
Cdd:PHA02876   238 NKNDLSLLKAIRNEDL-ETSLLLYDAGFSVNSIDDCKNTPLHHASqAPSLSRLVPKLLERGADVNAKNIKGETPLYLmAK 316
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265   96 ISCQPQCVKVLLQHGANEDAVDAENRSPLHWAASsgcassvlllcdheafldvldndgrtplmiasLGGHAAICSQLLQR 175
Cdd:PHA02876   317 NGYDTENIRTLIMLGADVNAADRLYITPLHQAST--------------------------------LDRNKDIVITLLEL 364
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2528974265  176 GARVNVTDKNDKSALILACEKGSAEVAELLLSHGADAGAVDSTGHDALHYALH 228
Cdd:PHA02876   365 GANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALC 417
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
612-892 5.35e-10

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 63.54  E-value: 5.35e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  612 QLEKEMSVLRLSNSNLLEELGELGRERQRLQRELQSLSQRLQREFVPKPQAQVQLQQLRQSVGLLTNELAMEKEATEKLR 691
Cdd:TIGR02168  695 ELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAE 774
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  692 KLLASQSSG---LRGLWDCLPADLVGERSAQSKAAESLEELRACISTLVDRHREAQQVLARLQEENQQLRGSLSPCREPG 768
Cdd:TIGR02168  775 EELAEAEAEieeLEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDI 854
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  769 TSLKApaspQVAALEQDLGKLEEELRAVQATMSGKSQEIGKLKQLLYQATEEVAELRAREAASLRQHEKTRGSLVAQAQA 848
Cdd:TIGR02168  855 ESLAA----EIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELR 930
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 2528974265  849 WgQELKALLEKYNTACREVGRLREAVAEERRRSGDLAAQAAEQE 892
Cdd:TIGR02168  931 L-EGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRR 973
PHA03095 PHA03095
ankyrin-like protein; Provisional
103-224 5.91e-10

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 62.73  E-value: 5.91e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  103 VKVLLQHGANEDAVDAENRSPLHWAASSGCASS---VLLLCDHEAFLDVLDNDGRTPLmiaslggHAAICSQ-------- 171
Cdd:PHA03095    30 VRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVkdiVRLLLEAGADVNAPERCGFTPL-------HLYLYNAttldvikl 102
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2528974265  172 LLQRGARVNVTDKNDKSALiLACEKG---SAEVAELLLSHGADAGAVDSTGHDALH 224
Cdd:PHA03095   103 LIKAGADVNAKDKVGRTPL-HVYLSGfniNPKVIRLLLRKGADVNALDLYGMTPLA 157
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
606-954 6.18e-10

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 63.54  E-value: 6.18e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  606 GGLAKGQLEKEMSVLRLSNS--NLLEELGELGRERQRLQRELQSLSQRLQREFVPKPQAQVQLQQLRQSVGLLTNELAME 683
Cdd:TIGR02168  659 GVITGGSAKTNSSILERRREieELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARL 738
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  684 KEATEKLRKLLASQSSglrglwdclpadlvgersAQSKAAESLEELRACISTLVDRHREAQQVLARLQEENQQLRGSLSP 763
Cdd:TIGR02168  739 EAEVEQLEERIAQLSK------------------ELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKA 800
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  764 CREPGTSLKApaspQVAALEQDLGKLEEELRAVQATMSGKSQEIGKLKQLLYQATEEVAEL---RAREAASLRQHEKtrg 840
Cdd:TIGR02168  801 LREALDELRA----ELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLaaeIEELEELIEELES--- 873
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  841 slvaqaqawgqELKALLEKYNTACREVGRLREAVAEERRRSGDLAAQAAEQERQASEMRGRSEQFEKTAELLKEKMEHLI 920
Cdd:TIGR02168  874 -----------ELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQ 942
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|..
gi 2528974265  921 GACRDK--------EAKIKELLKKLEQLSEEVLAIRGENARL 954
Cdd:TIGR02168  943 ERLSEEysltleeaEALENKIEDDEEEARRRLKRLENKIKEL 984
PHA02878 PHA02878
ankyrin repeat protein; Provisional
35-160 8.33e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 62.20  E-value: 8.33e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265   35 RVAALASRKSARPTKLDSNGQSPFHLAASKGLTECLTILLANGADINSKNEDGSTALHLATISCQP-QCVKVLLQHGANE 113
Cdd:PHA02878   182 RLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYCKDyDILKLLLEHGVDV 261
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 2528974265  114 DAVDA-ENRSPLHWAASSgcASSVLLLCDHEAFLDVLDNDGRTPLMIA 160
Cdd:PHA02878   262 NAKSYiLGLTALHSSIKS--ERKLKLLLEYGADINSLNSYKLTPLSSA 307
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
722-968 1.25e-09

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 62.38  E-value: 1.25e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  722 AAESLEELRACISTLVDRHREAQQVLARLQEENQQLRGSLSPCREPGTSLKA---PASPQVAALEQDLGKLEEELRAVQA 798
Cdd:TIGR02168  237 LREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKelyALANEISRLEQQKQILRERLANLER 316
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  799 TMSGKSQEIGKLKQLLYQATEEVAELRAREAASLRQHEktrgSLVAQAQAWGQELKALLEKYNTACREVGRLREAVAEER 878
Cdd:TIGR02168  317 QLEELEAQLEELESKLDELAEELAELEEKLEELKEELE----SLEAELEELEAELEELESRLEELEEQLETLRSKVAQLE 392
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  879 RRsgdLAAQAAEQERQASEM--------RGRSEQFEKTAELLKEKMEHLIGACRDKEAKIKELLKKLEQLSEEVLAIRGE 950
Cdd:TIGR02168  393 LQ---IASLNNEIERLEARLerledrreRLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREE 469
                          250
                   ....*....|....*...
gi 2528974265  951 NARLALQLQDSQKNHEEI 968
Cdd:TIGR02168  470 LEEAEQALDAAERELAQL 487
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
614-939 1.33e-09

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: 62.66  E-value: 1.33e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  614 EKEMSVLRLSNSNLLEELGELGRERQRLQRELQSLSQ----RLQREFVPKPQAqvQLQQLRQSVGLLTNELAMEKEATEK 689
Cdd:COG3096    784 EKRLEELRAERDELAEQYAKASFDVQKLQRLHQAFSQfvggHLAVAFAPDPEA--ELAALRQRRSELERELAQHRAQEQQ 861
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  690 LRKLLASQSSGLRGLWDCLP-ADLVGERSaqskAAESLEELRAcistLVDRHREAQQVLARLQEENQQLRGSLSPCREPg 768
Cdd:COG3096    862 LRQQLDQLKEQLQLLNKLLPqANLLADET----LADRLEELRE----ELDAAQEAQAFIQQHGKALAQLEPLVAVLQSD- 932
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  769 tslkaPAspQVAALEQDLGKLEEELRAVQAT---------------------MSGKSQEIG-KLKQLLYQAteEVAELRA 826
Cdd:COG3096    933 -----PE--QFEQLQADYLQAKEQQRRLKQQifalsevvqrrphfsyedavgLLGENSDLNeKLRARLEQA--EEARREA 1003
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  827 REAasLRQHEktrgslvAQAQAWGQELKALLEKYNTACREVGRLREAVAEERRRSGDLAAQAAEQER-----QASEMRGR 901
Cdd:COG3096   1004 REQ--LRQAQ-------AQYSQYNQVLASLKSSRDAKQQTLQELEQELEELGVQADAEAEERARIRRdelheELSQNRSR 1074
                          330       340       350
                   ....*....|....*....|....*....|....*...
gi 2528974265  902 SEQFEKTAELLKEKMEHLIGACRDKEAKIKELLKKLEQ 939
Cdd:COG3096   1075 RSQLEKQLTRCEAEMDSLQKRLRKAERDYKQEREQVVQ 1112
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
19-142 1.62e-09

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 61.84  E-value: 1.62e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265   19 RHDQKL--LEAVHRGDVGRVAALASRKSARPTKLDSNGQSPFHLAASkGLTECLTILLANGADINSKNEDGSTALHLATI 96
Cdd:PTZ00322    46 RIDTHLeaLEATENKDATPDHNLTTEEVIDPVVAHMLTVELCQLAAS-GDAVGARILLTGGADPNCRDYDGRTPLHIACA 124
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 2528974265   97 SCQPQCVKVLLQHGANEDAVDAENRSPLHWAASSGCASSVLLLCDH 142
Cdd:PTZ00322   125 NGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
Ank_5 pfam13857
Ankyrin repeats (many copies);
39-94 1.77e-09

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 54.27  E-value: 1.77e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2528974265   39 LASRKSARPTKLDSNGQSPFHLAASKGLTECLTILLANGADINSKNEDGSTALHLA 94
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
612-900 2.23e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 61.49  E-value: 2.23e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  612 QLEKEMSVLRLSNSNLLEELGELGRERQRLQRELQSLSQRLQREFVPKPQAQVQLQQLRQSVGLLTNELAMEKEATEKLR 691
Cdd:COG1196    264 ELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELE 343
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  692 KLLASQSSGLRglwdclpADLVGERSAQSKAAESLEELRACISTLVDRHREAQQVLARLQEENQQLRGSLSpcrepgtsl 771
Cdd:COG1196    344 EELEEAEEELE-------EAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEE--------- 407
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  772 kapaspQVAALEQDLGKLEEELRAVQATMSGKSQEIGKLKQLLYQATEEVAELRAREAASLRQHEKTRGSLVAQAQAWGQ 851
Cdd:COG1196    408 ------AEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAE 481
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 2528974265  852 ELKALLEKyntacrevgRLREAVAEERRRSGDLAAQAAEQERQASEMRG 900
Cdd:COG1196    482 LLEELAEA---------AARLLLLLEAEADYEGFLEGVKAALLLAGLRG 521
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
613-955 4.00e-09

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 60.82  E-value: 4.00e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  613 LEKEMSVLRLSNSNLLEELGELGRERQRLQRELQSLSQRLQREFVPKPQAQVQLQQLRQSVGLLTNELAMEKEATEKLRk 692
Cdd:PRK02224   277 LAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLE- 355
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  693 llaSQSSGLRGLWDCLPADLVGERSAQSKAAESLEELRACISTLVDRHREAQQVLARLQEENQQLRGSLSPCREpgtslk 772
Cdd:PRK02224   356 ---ERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELRE------ 426
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  773 apaspQVAALEQDLGKLEEELRAVQA---------------------TMSGKSQEIGKLKQLLYQATEEVAELRAR--EA 829
Cdd:PRK02224   427 -----REAELEATLRTARERVEEAEAlleagkcpecgqpvegsphveTIEEDRERVEELEAELEDLEEEVEEVEERleRA 501
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  830 ASLRQHEKTRGSLVAQAQAWGQELKallEKYNTACREvgrlREAVAEERRRSGDLAAQAAEQERQASEMRGRSEQ-FEKT 908
Cdd:PRK02224   502 EDLVEAEDRIERLEERREDLEELIA---ERRETIEEK----RERAEELRERAAELEAEAEEKREAAAEAEEEAEEaREEV 574
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*..
gi 2528974265  909 AELLKEKMEhlIGACRDKEAKIKELLKKLEQLSEEVLAIRGENARLA 955
Cdd:PRK02224   575 AELNSKLAE--LKERIESLERIRTLLAAIADAEDEIERLREKREALA 619
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
609-954 4.18e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 60.72  E-value: 4.18e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  609 AKGQLEKEMSVLRLSNSNLLEELGELGRERQRLQRELQSLSQRLQREFVPKPQAQVQLQQLRQSVGLLTNELAMEKEATE 688
Cdd:COG1196    422 ELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEA 501
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  689 KLR-----KLLASQSSGLRGLWDCLPADLVGERSAQSKAAESLEELRACIstLVDRHREAQQVLARLQEENQQLRGSLSP 763
Cdd:COG1196    502 DYEgflegVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNI--VVEDDEVAAAAIEYLKAAKAGRATFLPL 579
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  764 CREPGTSLKAPASPQ------VAALEQDLGKLEEELRAVQATMSGKSQEIGKLKQLLYQATEEVAELRAREAA---SLRQ 834
Cdd:COG1196    580 DKIRARAALAAALARgaigaaVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEgegGSAG 659
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  835 HEKTRGSLVAQAQAWGQELKALLEKYNTACREVGRLREAVAEERRRSGDLAAQAAEQERQASEMRGRSEQFEKTAELLKE 914
Cdd:COG1196    660 GSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLE 739
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|
gi 2528974265  915 KMEHLIGACRDKEAKIKELLKKLEQLSEEVLAIRGENARL 954
Cdd:COG1196    740 ELLEEEELLEEEALEELPEPPDLEELERELERLEREIEAL 779
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
21-211 5.80e-09

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 60.27  E-value: 5.80e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265   21 DQKLLEAVHRGDVGRVAALAsRKSARPTKLDSNGQSPFHLAASKGLTECLTILLANGADINSKNEDGSTALHLATISCQP 100
Cdd:PLN03192   526 ASNLLTVASTGNAALLEELL-KAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHH 604
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  101 QCVKVLlqhganedavdaenrspLHWAASSGCASSVLLLCdheafldvldndgrtplmIASLGGHAAICSQLLQRGARVN 180
Cdd:PLN03192   605 KIFRIL-----------------YHFASISDPHAAGDLLC------------------TAAKRNDLTAMKELLKQGLNVD 649
                          170       180       190
                   ....*....|....*....|....*....|.
gi 2528974265  181 VTDKNDKSALILACEKGSAEVAELLLSHGAD 211
Cdd:PLN03192   650 SEDHQGATALQVAMAEDHVDMVRLLIMNGAD 680
Ank_4 pfam13637
Ankyrin repeats (many copies);
56-107 7.40e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 52.66  E-value: 7.40e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2528974265   56 SPFHLAASKGLTECLTILLANGADINSKNEDGSTALHLATISCQPQCVKVLL 107
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
mukB PRK04863
chromosome partition protein MukB;
614-939 2.33e-08

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 58.43  E-value: 2.33e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  614 EKEMSVLRLSNSNLLEELGELGRERQRLQRELQSLSQ----RLQREFVPKPQAQvqLQQLRQSVGLLTNELAMEKEATEK 689
Cdd:PRK04863   785 EKRIEQLRAEREELAERYATLSFDVQKLQRLHQAFSRfigsHLAVAFEADPEAE--LRQLNRRRVELERALADHESQEQQ 862
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  690 LRKLLASQSSGLRGLWDCLP-ADLVGERSAQSKAAESLEELracistlvDRHREAQQVLARLQEENQQLRGSLSPCREPg 768
Cdd:PRK04863   863 QRSQLEQAKEGLSALNRLLPrLNLLADETLADRVEEIREQL--------DEAEEAKRFVQQHGNALAQLEPIVSVLQSD- 933
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  769 tslkaPAspQVAALEQDLGKLEEELRAVQ---------------------ATMSGKSQEIG-KLKQLLYQATEEVAELR- 825
Cdd:PRK04863   934 -----PE--QFEQLKQDYQQAQQTQRDAKqqafaltevvqrrahfsyedaAEMLAKNSDLNeKLRQRLEQAEQERTRARe 1006
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  826 -AREAAS-LRQHEKTRGSLVAQAQAWGQELKALLEKYNtacrEVGRLREAVAEERrrsgdLAAQAAEQERQASEMRGRSE 903
Cdd:PRK04863  1007 qLRQAQAqLAQYNQVLASLKSSYDAKRQMLQELKQELQ----DLGVPADSGAEER-----ARARRDELHARLSANRSRRN 1077
                          330       340       350
                   ....*....|....*....|....*....|....*.
gi 2528974265  904 QFEKTAELLKEKMEHLIGACRDKEAKIKELLKKLEQ 939
Cdd:PRK04863  1078 QLEKQLTFCEAEMDNLTKKLRKLERDYHEMREQVVN 1113
PHA02878 PHA02878
ankyrin repeat protein; Provisional
54-208 2.53e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 57.58  E-value: 2.53e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265   54 GQSPFHLAASKGLTECLTILLANGADINSKNEDGSTALHLATISCQPQCVKVLLQHGANEDAVDAENRSPLHWAASSGCA 133
Cdd:PHA02878   168 GNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYCKD 247
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  134 SSVL-LLCDHEAFLDVLDN-DGRTPLmiaslggHAAICSQ-----LLQRGARVNVTDKNDKSALILACEKGSA-EVAELL 205
Cdd:PHA02878   248 YDILkLLLEHGVDVNAKSYiLGLTAL-------HSSIKSErklklLLEYGADINSLNSYKLTPLSSAVKQYLCiNIGRIL 320

                   ...
gi 2528974265  206 LSH 208
Cdd:PHA02878   321 ISN 323
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
539-915 3.13e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 58.02  E-value: 3.13e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  539 ARLERVLARLEWAKAGLQVkpEVPSQESREGALKAAPGSIKQDEEKekrvpgaqgepLGALGGEKALGGLAKGQLEKEMS 618
Cdd:COG1196    239 AELEELEAELEELEAELEE--LEAELAELEAELEELRLELEELELE-----------LEEAQAEEYELLAELARLEQDIA 305
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  619 VLRLSNSNLLEELGELGRERQRLQRELQSLSQRLQREfvpKPQAQVQLQQLRQSVGLLTNELAMEKEATEKLRKLLASQS 698
Cdd:COG1196    306 RLEERRRELEERLEELEEELAELEEELEELEEELEEL---EEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELE 382
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  699 SGLRglwdclpaDLVGERSAQSKAAESLEELRACISTLVDRHREAQQVLARLQEENQQLRgslspcrepgtSLKAPASPQ 778
Cdd:COG1196    383 ELAE--------ELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELE-----------EEEEEEEEA 443
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  779 VAALEQDLGKLEEELRAVQATMSGKSQEIGKLKQLLYQATEEVAELRAREAASLRQHEKTRGSLVAQAQAWGQELKALLe 858
Cdd:COG1196    444 LEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGL- 522
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2528974265  859 kyntaCREVGRLREAVAEERRrsgdlAAQAAEQERQASEMRGRSEQFEKTAELLKEK 915
Cdd:COG1196    523 -----AGAVAVLIGVEAAYEA-----ALEAALAAALQNIVVEDDEVAAAAIEYLKAA 569
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
612-983 7.70e-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: 56.67  E-value: 7.70e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  612 QLEKEmsvLRLSNSnlleELGELGRERQRLQRELQSLSQrlqrefvpkpqaqvQLQQLRQSVGLLTNELAMEKEATEKlr 691
Cdd:pfam15921  346 ELEKQ---LVLANS----ELTEARTERDQFSQESGNLDD--------------QLQKLLADLHKREKELSLEKEQNKR-- 402
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  692 kllasqssglrgLWDclpadlvgersAQSKAAESLEELRaciSTLVDRHREAQQVLARLQ----EENQQLRGSLSPCREP 767
Cdd:pfam15921  403 ------------LWD-----------RDTGNSITIDHLR---RELDDRNMEVQRLEALLKamksECQGQMERQMAAIQGK 456
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  768 GTSLKAPAS--PQVAALEQDLGKLEEELRAVQATMSGKSQEIGKL------KQLLYQATE-EVAELRAREAASLR--QHE 836
Cdd:pfam15921  457 NESLEKVSSltAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLtaslqeKERAIEATNaEITKLRSRVDLKLQelQHL 536
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  837 KTRGSLVAQAQAWGQELKALLEKYNTAC----REVGRLREAVAEERRRSGDLAAQAAEQERQASEMRGRSEQFektaELL 912
Cdd:pfam15921  537 KNEGDHLRNVQTECEALKLQMAEKDKVIeilrQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEF----KIL 612
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2528974265  913 KEKmehligacrdKEAKIKELLKKLEQLSEEVLAIRGENARLALQLQDSQKNHEEI---ISTYRNHLLNAARGY 983
Cdd:pfam15921  613 KDK----------KDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLlneVKTSRNELNSLSEDY 676
PTZ00121 PTZ00121
MAEBL; Provisional
549-936 8.40e-08

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 56.69  E-value: 8.40e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  549 EWAKAGLQVKPEVPSQESREGALKAAPGSIKQDEEKEKRVPGAQGEPLGALGGEKALGGLAKGQLEKEmsvlrlSNSNLL 628
Cdd:PTZ00121  1402 EDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEA------KKADEA 1475
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  629 EELGELGRERQRLQRELQSLSQRLQrEFVPKPQAQVQLQQLRQsvglltnelAMEKEATEKLRKLL-ASQSSGLRGLWDC 707
Cdd:PTZ00121  1476 KKKAEEAKKADEAKKKAEEAKKKAD-EAKKAAEAKKKADEAKK---------AEEAKKADEAKKAEeAKKADEAKKAEEK 1545
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  708 LPADLVGERSAQSKAAE--SLEELRACISTLVDRHREAQqVLARLQEENQQLRGSLSPCREPGTSLKAPASPQVAALEQD 785
Cdd:PTZ00121  1546 KKADELKKAEELKKAEEkkKAEEAKKAEEDKNMALRKAE-EAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEE 1624
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  786 LGKLEEELRAVQATMSGKSQEIGKLKQLlyQATEEVAELRAREAASLRQHEKTRGSLVAQAQAWGQELKALLEKYNTACR 865
Cdd:PTZ00121  1625 LKKAEEEKKKVEQLKKKEAEEKKKAEEL--KKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAK 1702
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  866 EVGRLREAVAEERRRSGDLAA--------------QAAEQERQASEMRGRSEQFEKTAELLKEKMEHLIGACRDKEAKIK 931
Cdd:PTZ00121  1703 KAEELKKKEAEEKKKAEELKKaeeenkikaeeakkEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIE 1782

                   ....*
gi 2528974265  932 ELLKK 936
Cdd:PTZ00121  1783 EELDE 1787
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
778-985 1.16e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 56.22  E-value: 1.16e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  778 QVAALEQDLGKLEEELRAVQATMSGKSQEIGKLKQLLYQATEEVAELRAREA---ASLRQHEKTRGSLVAQAQAWGQELK 854
Cdd:TIGR02168  226 ELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSeleEEIEELQKELYALANEISRLEQQKQ 305
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  855 ALLEKYNTACREVGRLREAVAEERRRSGDLAAQAAEQERQASEMRGRSEQFEKTAELLKEKMEHLIGACRDKEAKIKELL 934
Cdd:TIGR02168  306 ILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLR 385
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2528974265  935 KKLEQLSEEVLAIRGENARLALQLQDSQKNHEEIISTYRNHLLNAARGYME 985
Cdd:TIGR02168  386 SKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELK 436
PHA02946 PHA02946
ankyin-like protein; Provisional
64-231 3.17e-07

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 53.90  E-value: 3.17e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265   64 KGLTE-CLTILLANGADINSKNEDGSTALHLATISCQPQCVKVLLQHGANEDAVDAENRSPLHWAASSgcassvlllcDH 142
Cdd:PHA02946    48 KGLDErFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGT----------DD 117
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  143 EAFLDVldndgrtplmiaslgghaaicSQLLQRGARVNVTDKNDKSALILACEKGSAEVAELLLSHGADAGAVDSTGHDA 222
Cdd:PHA02946   118 EVIERI---------------------NLLVQYGAKINNSVDEEGCGPLLACTDPSERVFKKIMSIGFEARIVDKFGKNH 176

                   ....*....
gi 2528974265  223 LHYALHTQD 231
Cdd:PHA02946   177 IHRHLMSDN 185
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
679-976 4.07e-07

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: 54.20  E-value: 4.07e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  679 ELAMEKEATEKLRKLLASQSSGLRGLWDCLPADLVGERSAQSKAAESLEELRACISTLVDR---HREAQQVLARLQE-EN 754
Cdd:TIGR00618  195 KAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQlkkQQLLKQLRARIEElRA 274
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  755 QQLRGSLSPCREPGTSLKAPASPQVAALEQDLGKLEEELRAVQATMSGKSQEIGKLKQLLYQ---------------ATE 819
Cdd:TIGR00618  275 QEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQqssieeqrrllqtlhSQE 354
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  820 EVAELRAREAASLRQHEKTRGSLVAQAQAWGQELKALLEKYNTACREVGRLREAVA-------EERRRSGDLAAQAAEQE 892
Cdd:TIGR00618  355 IHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQAtidtrtsAFRDLQGQLAHAKKQQE 434
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  893 RQASEMRGRSEQFEKTAELLKEKMEHLIGACRDKEAKiKELLKKLEQLSEEVLAIRGENARLALQLQDSQKNHEEIISTY 972
Cdd:TIGR00618  435 LQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKER-EQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHP 513

                   ....
gi 2528974265  973 RNHL 976
Cdd:TIGR00618  514 NPAR 517
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
612-955 4.78e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 53.91  E-value: 4.78e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  612 QLEKEMSVLRLSNsnLLEELGELGRERQRLQRELQSLSQRLQrefvpkpQAQVQLQQLRQSVGlltnelAMEKEATEKLR 691
Cdd:TIGR02168  224 ELELALLVLRLEE--LREELEELQEELKEAEEELEELTAELQ-------ELEEKLEELRLEVS------ELEEEIEELQK 288
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  692 KLLASQSsglrglwdcLPADLVGERSAQSKAAESLEELRACISTLVDRHR----EAQQVLARLQEENQQLRgslspcrep 767
Cdd:TIGR02168  289 ELYALAN---------EISRLEQQKQILRERLANLERQLEELEAQLEELEskldELAEELAELEEKLEELK--------- 350
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  768 gtslkapasPQVAALEQDLGKLEEELRAVQATMSGKSQEIGKLKQLLYQATEEVAELRAReaasLRQHEKTRGSLVAQAQ 847
Cdd:TIGR02168  351 ---------EELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNE----IERLEARLERLEDRRE 417
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  848 AWGQELKALLEKYNTAcrEVGRLREAVAEERRRSGDLAAQAAEQERQASEMRGRSEQFEKTAELLKEKMEHLigacRDKE 927
Cdd:TIGR02168  418 RLQQEIEELLKKLEEA--ELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQL----QARL 491
                          330       340
                   ....*....|....*....|....*...
gi 2528974265  928 AKIKELLKKLEQLSEEVLAIRGENARLA 955
Cdd:TIGR02168  492 DSLERLQENLEGFSEGVKALLKNQSGLS 519
PTZ00121 PTZ00121
MAEBL; Provisional
788-968 8.96e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 53.22  E-value: 8.96e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  788 KLEEELRAVQATmsgKSQEIGKLKQLLYQATEEVAELRAREAASLRQHEKTRGSLVAQAQAWGQELKALLEKYNTACREV 867
Cdd:PTZ00121  1213 KAEEARKAEDAK---KAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEK 1289
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  868 GRLREAVAEERRRSGDLAAQAAEQERQASEMRGRSEQFEKTAELLKEKMEHLIGACRDKEAKIKELLKKLEQLSEEVLAI 947
Cdd:PTZ00121  1290 KKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAA 1369
                          170       180
                   ....*....|....*....|.
gi 2528974265  948 RGENARLALQLQDSQKNHEEI 968
Cdd:PTZ00121  1370 EKKKEEAKKKADAAKKKAEEK 1390
Ank_5 pfam13857
Ankyrin repeats (many copies);
172-226 9.66e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 46.57  E-value: 9.66e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2528974265  172 LLQRG-ARVNVTDKNDKSALILACEKGSAEVAELLLSHGADAGAVDSTGHDALHYA 226
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
721-911 1.04e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 53.00  E-value: 1.04e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  721 KAAESLEELRACISTLvdRHREAQQVLARLQEENQQLRGSLSpcrepgtSLKApaspQVAALEQDLGKLEEELRAVQATM 800
Cdd:COG4913    266 AARERLAELEYLRAAL--RLWFAQRRLELLEAELEELRAELA-------RLEA----ELERLEARLDALREELDELEAQI 332
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  801 SG-KSQEIGKLKQLLYQATEEVAELRAReaaslrqhektRGSLVAQAQAWGQELKALLEKYNTACREVGRLREAVAEERR 879
Cdd:COG4913    333 RGnGGDRLEQLEREIERLERELEERERR-----------RARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELE 401
                          170       180       190
                   ....*....|....*....|....*....|..
gi 2528974265  880 RSGDLAAQAAEQERQAsemrgRSEQFEKTAEL 911
Cdd:COG4913    402 ALEEALAEAEAALRDL-----RRELRELEAEI 428
Ank_4 pfam13637
Ankyrin repeats (many copies);
120-173 1.15e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 46.50  E-value: 1.15e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2528974265  120 NRSPLHWAASSGCASSVLLLCDHEAFLDVLDNDGRTPLMIASLGGHAAICSQLL 173
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
738-982 1.43e-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: 51.69  E-value: 1.43e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  738 DRHREAQQVLARLQEENQQLRGSLspcrepgtslkapaspqvAALEQDLGKLEEELRAVQATMSGKSQEIGKLKQLLYQA 817
Cdd:COG4942     20 DAAAEAEAELEQLQQEIAELEKEL------------------AALKKEEKALLKQLAALERRIAALARRIRALEQELAAL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  818 TEEVAELRAREAASLRQHEKTRGSLVAQAQAWGQ-----ELKALL--EKYNTACREVGRLREAVAEERRRSGDLAAQAAE 890
Cdd:COG4942     82 EAELAELEKEIAELRAELEAQKEELAELLRALYRlgrqpPLALLLspEDFLDAVRRLQYLKYLAPARREQAEELRADLAE 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  891 QERQASEMRGRSEQFEKTAELLKEKMEHLIGACRDKEAKIKELLKKLEQLSEEVLAIRGENARLALQLQDSQKNHEEIIS 970
Cdd:COG4942    162 LAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
                          250
                   ....*....|..
gi 2528974265  971 TYRNHLLNAARG 982
Cdd:COG4942    242 RTPAAGFAALKG 253
Ank_4 pfam13637
Ankyrin repeats (many copies);
87-131 1.50e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 46.11  E-value: 1.50e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 2528974265   87 GSTALHLATISCQPQCVKVLLQHGANEDAVDAENRSPLHWAASSG 131
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNG 45
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
24-175 1.64e-06

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: 52.01  E-value: 1.64e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265   24 LLEAVHRGDVGRVAALASRKSaRPTKldsnGQSPFHLAASKGLTECLTILLANGADIN----------SKNED----GST 89
Cdd:TIGR00870  103 HLLAAFRKSGPLELANDQYTS-EFTP----GITALHLAAHRQNYEIVKLLLERGASVParacgdffvkSQGVDsfyhGES 177
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265   90 ALHLATISCQPQCVKVLLQHGANEDAVDAENRSPLHWAA------------SSGCASSVL----LLCDHEAFLDVLDNDG 153
Cdd:TIGR00870  178 PLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLVmenefkaeyeelSCQMYNFALslldKLRDSKELEVILNHQG 257
                          170       180
                   ....*....|....*....|..
gi 2528974265  154 RTPLMIASLGGHAAICSQLLQR 175
Cdd:TIGR00870  258 LTPLKLAAKEGRIVLFRLKLAI 279
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
611-907 2.31e-06

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 51.99  E-value: 2.31e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  611 GQLEKEMSVLRLSNSNLLEELGELGRERQRLQRELQSLSQRLQREFVPKPQAQVQLQQLRQSVGLLTNELAMEK-----E 685
Cdd:TIGR02169  719 GEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRipeiqA 798
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  686 ATEKLRKLLASQSSGLRGLWDCLPADLVGERSAQSKAAESLEELRACISTLVDRHREAQQVLARLQEENQQLRGSLSPCR 765
Cdd:TIGR02169  799 ELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALR 878
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  766 EPGTSLKAPASpQVAALEQDLGKLEEELRAVQATMSGKSQEIGKLKQLLYQATEEVAELRA--REAASLRQHEKTRGSLV 843
Cdd:TIGR02169  879 DLESRLGDLKK-ERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDpkGEDEEIPEEELSLEDVQ 957
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2528974265  844 AQAQAWGQELKALLEKYNTACREvgrlreaVAEERRRSGDLAAQAAEQERQASEMRGRSEQFEK 907
Cdd:TIGR02169  958 AELQRVEEEIRALEPVNMLAIQE-------YEEVLKRLDELKEKRAKLEEERKAILERIEEYEK 1014
PHA02878 PHA02878
ankyrin repeat protein; Provisional
136-226 4.32e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 50.26  E-value: 4.32e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  136 VLLLCDHEAFLDVLD-NDGRTPLMIASLGGHAAICSQLLQRGARVNVTDKNDKSALILACEKGSAEVAELLLSHGADAGA 214
Cdd:PHA02878   150 TKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDA 229
                           90
                   ....*....|..
gi 2528974265  215 VDSTGHDALHYA 226
Cdd:PHA02878   230 RDKCGNTPLHIS 241
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
776-973 4.90e-06

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 49.52  E-value: 4.90e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  776 SPQVAALEQDLGKLEEELRAVQATMSGKSQEIGKLKQLLYQATEEVAELRAReaasLRQHEKTRGSLVAQAQAWGQELKA 855
Cdd:COG1340      7 SSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREE----AQELREKRDELNEKVKELKEERDE 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  856 LLEKYNTACREVGRLREAVAEERRRSGDLAA-----QAAEQERQASEMRGRSEQ--FEKTAEL--LKEKMEHLIgacrDK 926
Cdd:COG1340     83 LNEKLNELREELDELRKELAELNKAGGSIDKlrkeiERLEWRQQTEVLSPEEEKelVEKIKELekELEKAKKAL----EK 158
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 2528974265  927 EAKIKELLKKLEQLSEEVLAIRGENARLAlqlQDSQKNHEEIISTYR 973
Cdd:COG1340    159 NEKLKELRAELKELRKEAEEIHKKIKELA---EEAQELHEEMIELYK 202
PHA02876 PHA02876
ankyrin repeat protein; Provisional
104-244 9.19e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 49.68  E-value: 9.19e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  104 KVLLQHGANEDAVDAENRSPLHWAASSGCASSVLLLCDHEAFLDVLDNDGRTPLMIASLGGHAAICSQLLQRGARVNvtd 183
Cdd:PHA02876   162 EMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNIN--- 238
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2528974265  184 KNDKSaLILACEKGSAEVAELLLSHGADAGAVDSTGHDALHYAlhTQDKALWRHLQQALSR 244
Cdd:PHA02876   239 KNDLS-LLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHA--SQAPSLSRLVPKLLER 296
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
609-972 1.09e-05

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 49.79  E-value: 1.09e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  609 AKGQLEKEMSVLRLSNSNLLEELGELGRERQRLQRELQSLSQRLQREFVPKPQAQVQLQQLRQSVGLLTNELAMEKEA-- 686
Cdd:pfam01576  209 AKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAArn 288
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  687 -TEKLRKLLASQSSGLRG-LWDCLPADLVgERSAQSKAAESLEELRACISTLVDRHReaQQVLARLQEENQQLRgSLSPC 764
Cdd:pfam01576  289 kAEKQRRDLGEELEALKTeLEDTLDTTAA-QQELRSKREQEVTELKKALEEETRSHE--AQLQEMRQKHTQALE-ELTEQ 364
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  765 REPGTSLKAPASPQVAALEQDLGKLEEELRAVQatmSGKSQEIGKLKQLLYQateeVAELRAReaasLRQHEKTRGSLVA 844
Cdd:pfam01576  365 LEQAKRNKANLEKAKQALESENAELQAELRTLQ---QAKQDSEHKRKKLEGQ----LQELQAR----LSESERQRAELAE 433
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  845 QAQAWGQELKALLEKYNTACREVGRLREAVAEERRRSGDLAAQAAEQERQASEMRGRSEQFEKTAELLKEKMEHLIGACR 924
Cdd:pfam01576  434 KLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKR 513
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2528974265  925 DKE-------AKIKELLKKLEQLSEEVLAIRGENARLALQLQDSQKNHEEIISTY 972
Cdd:pfam01576  514 NVErqlstlqAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAY 568
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
627-827 1.28e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 49.53  E-value: 1.28e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  627 LLEELGELGRERQRLQRELQSLSQRLQRefVPKPQAQVQLQQLRQSVGLLTNELAMEKEATEKLRKLLASQSSGLRGLwd 706
Cdd:COG4913    253 LLEPIRELAERYAAARERLAELEYLRAA--LRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDEL-- 328
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  707 clpadlvgERSAQSKAAESLEELRACISTLVDRHREAQQVLARLQEENQQLRGSLSPCREPGTSLKAPASPQVAALEQDL 786
Cdd:COG4913    329 --------EAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEEL 400
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 2528974265  787 GKLEEELRAVQAtmsgksqEIGKLKQLLYQATEEVAELRAR 827
Cdd:COG4913    401 EALEEALAEAEA-------ALRDLRRELRELEAEIASLERR 434
PTZ00121 PTZ00121
MAEBL; Provisional
715-967 2.11e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.98  E-value: 2.11e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  715 ERSAQSKAAESLEELRAcistlVDRHREAQQVLARLQEE--NQQLRGSLSPCREPGTSLKAPASPQVAALEQDLGKLEEE 792
Cdd:PTZ00121  1215 EEARKAEDAKKAEAVKK-----AEEAKKDAEEAKKAEEErnNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEK 1289
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  793 LRAVQATmsgKSQEIGKLKQLLYQATE----EVAELRAREA------ASLRQHEKTRGSLVA--QAQAWGQELKALLEKY 860
Cdd:PTZ00121  1290 KKADEAK---KAEEKKKADEAKKKAEEakkaDEAKKKAEEAkkkadaAKKKAEEAKKAAEAAkaEAEAAADEAEAAEEKA 1366
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  861 NTAcrevgrlrEAVAEERRRSGDLAAQAAEQERQASEMRGRSEQFEKTAELLKEKMEhligacrdKEAKIKELLKKLEQL 940
Cdd:PTZ00121  1367 EAA--------EKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAA--------AKKKADEAKKKAEEK 1430
                          250       260
                   ....*....|....*....|....*...
gi 2528974265  941 SE-EVLAIRGENARLAlqlQDSQKNHEE 967
Cdd:PTZ00121  1431 KKaDEAKKKAEEAKKA---DEAKKKAEE 1455
PTZ00121 PTZ00121
MAEBL; Provisional
784-953 3.47e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.21  E-value: 3.47e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  784 QDLGKLEEELRAVQA-------TMSGKSQEIgkLKQLLYQATEEVAELRARE----AASLRQHE--KTRGSLVAQAQAWG 850
Cdd:PTZ00121  1555 EELKKAEEKKKAEEAkkaeedkNMALRKAEE--AKKAEEARIEEVMKLYEEEkkmkAEEAKKAEeaKIKAEELKKAEEEK 1632
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  851 QELKALLEKYNTACREVGRLREAVAEERRRSGDLAAQAAEQERQASEMRGRSEQFEKTAELLKEKMEHLIGACRDKEaKI 930
Cdd:PTZ00121  1633 KKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKK-KE 1711
                          170       180
                   ....*....|....*....|....*
gi 2528974265  931 KELLKKLEQL--SEEVLAIRGENAR 953
Cdd:PTZ00121  1712 AEEKKKAEELkkAEEENKIKAEEAK 1736
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
56-224 4.10e-05

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: 47.31  E-value: 4.10e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265   56 SPFHLAASKGLTECLTILL-ANGADINSKNEDGSTALHLATISCQPQCVKVLLQhgANEDAVDAENRSPLHwaassgcas 134
Cdd:cd22192     19 SPLLLAAKENDVQAIKKLLkCPSCDLFQRGALGETALHVAALYDNLEAAVVLME--AAPELVNEPMTSDLY--------- 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  135 svlllcdheafldvldnDGRTPLMIASLGGHAAICSQLLQRGARVN---VTD----KNDKSAL-----IL---ACEkGSA 199
Cdd:cd22192     88 -----------------QGETALHIAVVNQNLNLVRELIARGADVVsprATGtffrPGPKNLIyygehPLsfaACV-GNE 149
                          170       180
                   ....*....|....*....|....*
gi 2528974265  200 EVAELLLSHGADAGAVDSTGHDALH 224
Cdd:cd22192    150 EIVRLLIEHGADIRAQDSLGNTVLH 174
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
629-983 4.28e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 47.45  E-value: 4.28e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  629 EELGELGRERQRLQRELQSLSQRLQREFVPKP--QAQVQLQQLRQSVGLLTNELAMEKEATEKLRKLLASQSSGLRGLWD 706
Cdd:COG4717    102 EELEELEAELEELREELEKLEKLLQLLPLYQEleALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEE 181
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  707 CLPADLVGERSAQSKAAESLEELRACISTLVDRHREAQQVLARLQEENQQLRGSLSPCREPGTSLKAPASPQVAAL---- 782
Cdd:COG4717    182 LLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAAllal 261
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  783 -----------------------------------EQDLGKLEEELRAVQATMSGKSQEIGKLKQL-------------- 813
Cdd:COG4717    262 lglggsllsliltiagvlflvlgllallflllareKASLGKEAEELQALPALEELEEEELEELLAAlglppdlspeelle 341
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  814 LYQATEEVAELR-----AREAASLRQHEKTRGSLVAQAQAWG-QELKALLEKYNTACREVGRLREavAEERRRSGDLAAQ 887
Cdd:COG4717    342 LLDRIEELQELLreaeeLEEELQLEELEQEIAALLAEAGVEDeEELRAALEQAEEYQELKEELEE--LEEQLEELLGELE 419
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  888 AAEQERQASEMRGRSEQFEKTAELLKEKMEHLIGACRDKEAKIK---------ELLKKLEQLSEEVLAIRGENARLALQL 958
Cdd:COG4717    420 ELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEqleedgelaELLQELEELKAELRELAEEWAALKLAL 499
                          410       420
                   ....*....|....*....|....*
gi 2528974265  959 QDSQKNHEEIISTYRNHLLNAARGY 983
Cdd:COG4717    500 ELLEEAREEYREERLPPVLERASEY 524
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
152-184 4.43e-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. 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: 41.51  E-value: 4.43e-05
                           10        20        30
                   ....*....|....*....|....*....|....
gi 2528974265  152 DGRTPLMIASL-GGHAAICSQLLQRGARVNVTDK 184
Cdd:pfam00023    1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
Ank_5 pfam13857
Ankyrin repeats (many copies);
137-193 5.74e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.56  E-value: 5.74e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2528974265  137 LLLCDHEAfLDVLDNDGRTPLMIASLGGHAAICSQLLQRGARVNVTDKNDKSALILA 193
Cdd:pfam13857    1 LLEHGPID-LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
721-968 5.78e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 46.98  E-value: 5.78e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  721 KAAESLEELracISTLVDRHREAQQVLARLQEENQQLRGSLSPCREPGTSLKAPASpQVAALEQDLGKLEEELRAVQATM 800
Cdd:PRK03918   186 KRTENIEEL---IKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKE-EIEELEKELESLEGSKRKLEEKI 261
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  801 SGKSQEIGKLKqllyqatEEVAEL--RAREAASLRQHEKTRgslvaqaqawgQELKALLEKYNTACREV----GRLREAV 874
Cdd:PRK03918   262 RELEERIEELK-------KEIEELeeKVKELKELKEKAEEY-----------IKLSEFYEEYLDELREIekrlSRLEEEI 323
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  875 AEERRRSGDLA---AQAAEQERQASEMRGRSEQFEKTAELL---KEKMEHLIG-----ACRDKE---AKIKELLKKLEQL 940
Cdd:PRK03918   324 NGIEERIKELEekeERLEELKKKLKELEKRLEELEERHELYeeaKAKKEELERlkkrlTGLTPEkleKELEELEKAKEEI 403
                          250       260
                   ....*....|....*....|....*...
gi 2528974265  941 SEEVLAIRGENARLALQLQDSQKNHEEI 968
Cdd:PRK03918   404 EEEISKITARIGELKKEIKELKKAIEEL 431
Ank_5 pfam13857
Ankyrin repeats (many copies);
106-160 6.33e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.56  E-value: 6.33e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2528974265  106 LLQHG-ANEDAVDAENRSPLHWAASSGCASSVLLLCDHEAFLDVLDNDGRTPLMIA 160
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
17-224 6.39e-05

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: 47.00  E-value: 6.39e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265   17 WNRHDQKLLEAVHRGDVGRVA-ALASRKSARPTKLDSNGQSPFHLAASKGLTECLTILLANgadINSKNEDGSTALHLAT 95
Cdd:TIGR00870   14 LSDEEKAFLPAAERGDLASVYrDLEEPKKLNINCPDRLGRSALFVAAIENENLELTELLLN---LSCRGAVGDTLLHAIS 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265   96 ISCQpQCVKVLLQHganEDAVDAENRSPLHWAASSGCASSVlllcdheafldvldndGRTPLMIASLGGHAAICSQLLQR 175
Cdd:TIGR00870   91 LEYV-DAVEAILLH---LLAAFRKSGPLELANDQYTSEFTP----------------GITALHLAAHRQNYEIVKLLLER 150
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2528974265  176 GARVNVTDKND--------------KSALILACEKGSAEVAELLLSHGADAGAVDSTGHDALH 224
Cdd:TIGR00870  151 GASVPARACGDffvksqgvdsfyhgESPLNAAACLGSPSIVALLSEDPADILTADSLGNTLLH 213
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
629-881 6.42e-05

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 46.30  E-value: 6.42e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  629 EELGELGRERQRLQRELQSLSQRLQREFVPKPQAQVQLQQLRQSVGLLTNELamekeateklrkllasqssglrglwdcl 708
Cdd:COG4942     20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRI---------------------------- 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  709 padlvgersaqSKAAESLEELRACISTLVDRHREAQQVLARLQEE-NQQLRGSLSPCREPGTS-LKAPASPQ-------- 778
Cdd:COG4942     72 -----------RALEQELAALEAELAELEKEIAELRAELEAQKEElAELLRALYRLGRQPPLAlLLSPEDFLdavrrlqy 140
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  779 VAALEQDLGKLEEELRAVQATMSGKSQEIGKLKQLLYQATEEVAELRAREAASLRQHEKTRGSLVAQAQAWGQELKALLE 858
Cdd:COG4942    141 LKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQ 220
                          250       260
                   ....*....|....*....|...
gi 2528974265  859 KYNTACREVGRLREAVAEERRRS 881
Cdd:COG4942    221 EAEELEALIARLEAEAAAAAERT 243
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
86-117 6.63e-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. 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: 40.74  E-value: 6.63e-05
                           10        20        30
                   ....*....|....*....|....*....|...
gi 2528974265   86 DGSTALHLATISC-QPQCVKVLLQHGANEDAVD 117
Cdd:pfam00023    1 DGNTPLHLAAGRRgNLEIVKLLLSKGADVNARD 33
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
629-976 6.88e-05

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


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 47.02  E-value: 6.88e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  629 EELGELGRERQRLQRELQSLSQRLQREFVPKPQAQVQLQQLRQSVGLLTNELAMEKEATEK------------------L 690
Cdd:pfam05483  282 ENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKakaahsfvvtefeattcsL 361
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  691 RKLLASQSSGLRGLWDCLPADLVGERSAQSKAAE----------SLEELRACIS---TLVDRHREAQQVLARLQEENQQL 757
Cdd:pfam05483  362 EELLRTEQQRLEKNEDQLKIITMELQKKSSELEEmtkfknnkevELEELKKILAedeKLLDEKKQFEKIAEELKGKEQEL 441
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  758 RGSLSpcrepgtslkapaspqvaALEQDLGKLEEELRAVQATMSGKSQEIGKLKQLLYQATEEVAELRAREAASLRQHEK 837
Cdd:pfam05483  442 IFLLQ------------------AREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKE 503
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  838 trgsLVAQAQAWGQELKALLEKYNTACREVGRLREAV----AEERRRSGDLAAQAAEQERQASEMRGRSEQFEKTAE--- 910
Cdd:pfam05483  504 ----LTQEASDMTLELKKHQEDIINCKKQEERMLKQIenleEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARsie 579
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  911 ---LLKEK-MEHLIGACRDKEAKIKELLKKLEQLSEEVLAIRGENA--------------RLALQLQDSQKNHEEIISTY 972
Cdd:pfam05483  580 yevLKKEKqMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSaenkqlnayeikvnKLELELASAKQKFEEIIDNY 659

                   ....
gi 2528974265  973 RNHL 976
Cdd:pfam05483  660 QKEI 663
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
784-966 6.97e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 46.68  E-value: 6.97e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  784 QDLGKLEEELRAVQATMSGKSQEIGKLKQLlyqaTEEVAELRAREAAslRQHEKTRGSLVAQAQAWGQELKALLEKYNTA 863
Cdd:COG4717     71 KELKELEEELKEAEEKEEEYAELQEELEEL----EEELEELEAELEE--LREELEKLEKLLQLLPLYQELEALEAELAEL 144
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  864 CREVGRLREAVAEERRRSGDLAAQAAEQERQASEMRgrsEQFEKTAELLKEKMEHLIGACRDKEAKIKELLKKLEQLSEE 943
Cdd:COG4717    145 PERLEELEERLEELRELEEELEELEAELAELQEELE---ELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEE 221
                          170       180
                   ....*....|....*....|...
gi 2528974265  944 VLAIRGENARLALQLQDSQKNHE 966
Cdd:COG4717    222 LEELEEELEQLENELEAAALEER 244
Ank_5 pfam13857
Ankyrin repeats (many copies);
73-127 8.42e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.18  E-value: 8.42e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2528974265   73 LLANG-ADINSKNEDGSTALHLAtISCQ-PQCVKVLLQHGANEDAVDAENRSPLHWA 127
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVA-AKYGaLEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
53-85 9.25e-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. 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: 40.35  E-value: 9.25e-05
                           10        20        30
                   ....*....|....*....|....*....|....
gi 2528974265   53 NGQSPFHLAASK-GLTECLTILLANGADINSKNE 85
Cdd:pfam00023    1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
Ank_4 pfam13637
Ankyrin repeats (many copies);
153-206 9.46e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 41.11  E-value: 9.46e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2528974265  153 GRTPLMIASLGGHAAICSQLLQRGARVNVTDKNDKSALILACEKGSAEVAELLL 206
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02878 PHA02878
ankyrin repeat protein; Provisional
57-234 1.34e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 45.64  E-value: 1.34e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265   57 PFHLAASKGLTECLTILLANGADINSKNEDGSTALHLATISCQPQCVKVLLQHgANEDAVDAENRsplhwAASSGCAS-- 134
Cdd:PHA02878    40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRS-INKCSVFYTLV-----AIKDAFNNrn 113
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  135 ----SVLLLCDHEAFLDVLDNDGRTPLMIASLggHAAICSQLLQRGARVNVTDKN-DKSALILACEKGSAEVAELLLSHG 209
Cdd:PHA02878   114 veifKIILTNRYKNIQTIDLVYIDKKSKDDII--EAEITKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYG 191
                          170       180
                   ....*....|....*....|....*.
gi 2528974265  210 ADAGAVDSTGHDALHYAL-HTQDKAL 234
Cdd:PHA02878   192 ANVNIPDKTNNSPLHHAVkHYNKPIV 217
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
724-949 1.35e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.06  E-value: 1.35e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  724 ESLEELRACISTLvDRHREAQQVLARLQEENQQLRgslspcrepgtSLKAPASPQVAALEQDLgkLEEELRAVQATMSGK 803
Cdd:COG4913    242 EALEDAREQIELL-EPIRELAERYAAARERLAELE-----------YLRAALRLWFAQRRLEL--LEAELEELRAELARL 307
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  804 SQEIGKLKQLLYQATEEVAELRAreaaslrqhektrgslvAQAQAWGQELKALLekyntacREVGRLREAVAEERRRSGD 883
Cdd:COG4913    308 EAELERLEARLDALREELDELEA-----------------QIRGNGGDRLEQLE-------REIERLERELEERERRRAR 363
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  884 LAAQAAEQERQASEMRGRSEQFEKTAELLKEKMEHLIGACRDK----EAKIKELLKKLEQLSEEVLAIRG 949
Cdd:COG4913    364 LEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEAlaeaEAALRDLRRELRELEAEIASLER 433
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
609-834 1.51e-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: 1.51e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  609 AKGQLEKEMSVLRLSNSNLLEELGELGRERQRLQRELQSLSQRLQREFVPKPQAQVQLQQLRQSVGLLTNELAMEKEATE 688
Cdd:COG4942     21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  689 KLRKLLASQSSGL--RGLWDCLPADLVGERSAQS-KAAESLEELRACISTLVDRHREAQQVLARLQEENQQLRGSLSpcr 765
Cdd:COG4942    101 AQKEELAELLRALyrLGRQPPLALLLSPEDFLDAvRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE--- 177
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2528974265  766 epgtSLKAPASPQVAALEQDLGKLEEELRAVQATMSGKSQEIGKLKQLLYQATEEVAELRAREAASLRQ 834
Cdd:COG4942    178 ----ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
541-974 1.75e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 45.44  E-value: 1.75e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  541 LERVLARLEWAKAGLQVKpeVPSQESREGALKAapgSIKQDEEKEKRVPGAQGEPLG--ALGGEKALGGLAKGQLEKEMS 618
Cdd:PRK03918   243 LEKELESLEGSKRKLEEK--IRELEERIEELKK---EIEELEEKVKELKELKEKAEEyiKLSEFYEEYLDELREIEKRLS 317
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  619 VL---------RLSN-SNLLEELGELGRERQRLQRELQSLSQRLqREFVPKPQAQVQLQQLRQSVGLLTNELAMEK---- 684
Cdd:PRK03918   318 RLeeeingieeRIKElEEKEERLEELKKKLKELEKRLEELEERH-ELYEEAKAKKEELERLKKRLTGLTPEKLEKEleel 396
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  685 -----EATEKLRKLLASQSSgLRGLWDCLPADLVGERSAQSKA------------AESLEELRACISTLVDRHREAQQVL 747
Cdd:PRK03918   397 ekakeEIEEEISKITARIGE-LKKEIKELKKAIEELKKAKGKCpvcgrelteehrKELLEEYTAELKRIEKELKEIEEKE 475
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  748 ARLQEENQQLRGSLSPCREPgTSLKAPASpQVAALEQDLGKL--------EEELRAVQATMSGKSQEIGKLKQLLYQATE 819
Cdd:PRK03918   476 RKLRKELRELEKVLKKESEL-IKLKELAE-QLKELEEKLKKYnleelekkAEEYEKLKEKLIKLKGEIKSLKKELEKLEE 553
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  820 EVAELRAREAAsLRQHEKTRGSLVAQAQAWGQELKALLEkyntacREVGRLREAVAEErrrsgdLAAQAAEQERQASEmr 899
Cdd:PRK03918   554 LKKKLAELEKK-LDELEEELAELLKELEELGFESVEELE------ERLKELEPFYNEY------LELKDAEKELEREE-- 618
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  900 grsEQFEKTAELLKEKMEHLigacRDKEAKIKELLKKLEQL------------SEEVLAIRGENARLALQLQDSQKNHEE 967
Cdd:PRK03918   619 ---KELKKLEEELDKAFEEL----AETEKRLEELRKELEELekkyseeeyeelREEYLELSRELAGLRAELEELEKRREE 691

                   ....*..
gi 2528974265  968 IISTYRN 974
Cdd:PRK03918   692 IKKTLEK 698
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
721-973 1.75e-04

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: 45.71  E-value: 1.75e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  721 KAAESLEELRACISTLVDRHREAQQVLARLQEENQQLRGSLSPCREPGTSLKAPASPQVAALE-------------QDLG 787
Cdd:COG3096    344 RQQEKIERYQEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDvqqtraiqyqqavQALE 423
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  788 KLEEELRAVQATMSGKSQEIGKLKQLLYQATEEVAELRAR---EAASLRQHEKTRGSL------VAQAQAWgQELKALLE 858
Cdd:COG3096    424 KARALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQKlsvADAARRQFEKAYELVckiageVERSQAW-QTARELLR 502
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  859 KYntacrevgrlREAVAeerrrsgdLAAQAAEQERQASEMRGRSEQFEKTAELLKEKMEHlIGACRDKEAKIKELLKKLE 938
Cdd:COG3096    503 RY----------RSQQA--------LAQRLQQLRAQLAELEQRLRQQQNAERLLEEFCQR-IGQQLDAAEELEELLAELE 563
                          250       260       270
                   ....*....|....*....|....*....|....*
gi 2528974265  939 QLSEEVLAIRGENARLALQLQDSQKNHEEIISTYR 973
Cdd:COG3096    564 AQLEELEEQAAEAVEQRSELRQQLEQLRARIKELA 598
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
627-988 1.96e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.14  E-value: 1.96e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  627 LLEELGEL----GRERQRLQRELQSLSQRLQrefvpkpQAQVQLQQLRQSVGLLtNELAMEKEATEKLRKLLASQSSGLR 702
Cdd:COG4717     51 LEKEADELfkpqGRKPELNLKELKELEEELK-------EAEEKEEEYAELQEEL-EELEEELEELEAELEELREELEKLE 122
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  703 GLWDCLPADLVGERSAQSKAA--ESLEELRACISTLVDRHREAQQVLARLQEENQQLRGSLSPCREPGTSLKAPASPQVA 780
Cdd:COG4717    123 KLLQLLPLYQELEALEAELAElpERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELE 202
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  781 ALEQDLGKLEEELRAVQATMSGKSQEIGKL--KQLLYQATEEVAELR--AREAASLRQHEKTRGSLVAQAQAWGQELKAL 856
Cdd:COG4717    203 ELQQRLAELEEELEEAQEELEELEEELEQLenELEAAALEERLKEARllLLIAAALLALLGLGGSLLSLILTIAGVLFLV 282
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  857 LEKYNTACREVGRLREAVAEERRRSGDLAA----QAAEQERQASEMRGRSEQFEKTAELLKEKMEHLIGACR-----DKE 927
Cdd:COG4717    283 LGLLALLFLLLAREKASLGKEAEELQALPAleelEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLReaeelEEE 362
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2528974265  928 AKIKELLKKLEQL-------SEEVLAIRGENARLALQLQDSQKNHEEIISTYRNHLLNAARGYMEHEV 988
Cdd:COG4717    363 LQLEELEQEIAALlaeagveDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEEL 430
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
713-971 2.16e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 45.42  E-value: 2.16e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  713 VGERSAQSKAAESLEELRACISTLVDRhrEAQQVLARLQEENQQLRGSLSPC---REPGTSLKAPASPQVAALE---QDL 786
Cdd:PRK02224   176 LGVERVLSDQRGSLDQLKAQIEEKEEK--DLHERLNGLESELAELDEEIERYeeqREQARETRDEADEVLEEHEerrEEL 253
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  787 GKLEEELRAVQATMSGKSQEIGKLKQLLYQATEEVAELRAReaaslrqhektRGSLVAQAQAWGQELKALLEKYNTACRE 866
Cdd:PRK02224   254 ETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEE-----------RDDLLAEAGLDDADAEAVEARREELEDR 322
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  867 VGRLREAVAEERrrsgdLAAQAAEQerQASEMRGRSEQFEKTAELLKEKMEHLIGACRDKEAKIKELLKKLEQLSEEVLA 946
Cdd:PRK02224   323 DEELRDRLEECR-----VAAQAHNE--EAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEE 395
                          250       260
                   ....*....|....*....|....*
gi 2528974265  947 IRGENARLALQLQDSQKNHEEIIST 971
Cdd:PRK02224   396 LRERFGDAPVDLGNAEDFLEELREE 420
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
53-81 2.59e-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: 39.11  E-value: 2.59e-04
                            10        20
                    ....*....|....*....|....*....
gi 2528974265    53 NGQSPFHLAASKGLTECLTILLANGADIN 81
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
634-967 2.72e-04

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 45.17  E-value: 2.72e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  634 LGRERQRLQRELQSLSQRLQREFVPKPQAQVQLQQLRQSVGLLTNELAMEKEATEKLR-----------------KLLAS 696
Cdd:pfam01576   66 LAARKQELEEILHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQlekvtteakikkleediLLLED 145
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  697 QSSGL---RGLWDCLPADLVGERSAQSKAAESLEELR----ACISTLVDRHREAQQVLARLQEENQQLRGSLSPCREPGT 769
Cdd:pfam01576  146 QNSKLskeRKLLEERISEFTSNLAEEEEKAKSLSKLKnkheAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIA 225
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  770 SLKApaspQVAALEQDLGKLEEELRAVQA----TMSGKSQEIGKLKQLLYQATEEVAELrAREAASLRQHEKTRGSLVAQ 845
Cdd:pfam01576  226 ELQA----QIAELRAQLAKKEEELQAALArleeETAQKNNALKKIRELEAQISELQEDL-ESERAARNKAEKQRRDLGEE 300
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  846 AQAWGQELKALLEKYNTAC-------REVGRLREAVAEERRRsgdlaaqaaeQERQASEMRGR-SEQFEKTAELLKEKME 917
Cdd:pfam01576  301 LEALKTELEDTLDTTAAQQelrskreQEVTELKKALEEETRS----------HEAQLQEMRQKhTQALEELTEQLEQAKR 370
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2528974265  918 HLIGACRDK---EAKIKELLKKLEQLSEEVLAIRGENARLALQLQDSQKNHEE 967
Cdd:pfam01576  371 NKANLEKAKqalESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSE 423
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
625-944 2.86e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 45.05  E-value: 2.86e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  625 SNLLEELGELGRERQRLQRELQSLSQRL--QREFVPKPQAQVQLQQLRQSV-GLLTNELAMEKEATEKLRKLLASQSSGL 701
Cdd:PRK03918   462 KRIEKELKEIEEKERKLRKELRELEKVLkkESELIKLKELAEQLKELEEKLkKYNLEELEKKAEEYEKLKEKLIKLKGEI 541
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  702 RGLWDclpaDLVGERSAQSKAAESLEELRACISTLVDRHREAQQVLARLQEENQQLRGSLSPCREPGTSLKApaspqvaa 781
Cdd:PRK03918   542 KSLKK----ELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKD-------- 609
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  782 LEQDLGKLEEELRAVQATMSGKSQEIGKLKQLLYQATEEVAELRAReaASLRQHEKTRgslvaqaqawgqelkallEKYN 861
Cdd:PRK03918   610 AEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKK--YSEEEYEELR------------------EEYL 669
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  862 TACREVGRLREAVAEERRRSGDLAAQAAEQERQASEMRGRSEQFEKTaELLKEKMEHLIGACRDKEAKIKE-LLKKLEQL 940
Cdd:PRK03918   670 ELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKL-EKALERVEELREKVKKYKALLKErALSKVGEI 748

                   ....
gi 2528974265  941 SEEV 944
Cdd:PRK03918   749 ASEI 752
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
721-967 3.65e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 44.65  E-value: 3.65e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  721 KAAESLEELRACIstlvDRHREAQQVLARLQEENQQLRGSLSPC-REpgtslKAPASPQVAALEQDLGKLEEELRAVQAT 799
Cdd:PRK02224   231 QARETRDEADEVL----EEHEERREELETLEAEIEDLRETIAETeRE-----REELAEEVRDLRERLEELEEERDDLLAE 301
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  800 MSGKSQEIGKLKQllyqateEVAELRAREaaslrqhEKTRGSLVAQAQAWGQELKallekyntacrEVGRLREAVAEERR 879
Cdd:PRK02224   302 AGLDDADAEAVEA-------RREELEDRD-------EELRDRLEECRVAAQAHNE-----------EAESLREDADDLEE 356
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  880 RSGDLAAQAAEQERQASEMRGRSEQFEKTAELLKEKMEHLIGACRDKEAKIKELLKKLEQLSEEVLAIRGENARLALQLQ 959
Cdd:PRK02224   357 RAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLR 436

                   ....*...
gi 2528974265  960 DSQKNHEE 967
Cdd:PRK02224   437 TARERVEE 444
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
612-948 4.13e-04

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 44.24  E-value: 4.13e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  612 QLEKEMSVLRLSNSNLLEELGELGRERQRLQRELQSLSQRLQ------REFVPKPQAQVQLQQLRQS--VGLLTNELAME 683
Cdd:TIGR04523  346 QLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKnlesqiNDLESKIQNQEKLNQQKDEqiKKLQQEKELLE 425
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  684 KEaTEKLRKLLASQSSGLRglwdclpaDLVGERSAQSKAAESL----EELRACISTLVDRHREAQQVLARLQEENQQLRG 759
Cdd:TIGR04523  426 KE-IERLKETIIKNNSEIK--------DLTNQDSVKELIIKNLdntrESLETQLKVLSRSINKIKQNLEQKQKELKSKEK 496
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  760 SLSPCREPGTSLKApaspQVAALEQDLGKLEEELRAVQATMSGKSQEIGKLKqllyqatEEVAELrareaaslrQHEKTR 839
Cdd:TIGR04523  497 ELKKLNEEKKELEE----KVKDLTKKISSLKEKIEKLESEKKEKESKISDLE-------DELNKD---------DFELKK 556
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  840 GSLVAQAQAWGQELKALLEKYNTACREVGRLREAVAEERRRSGDLAAQAAEQERQASEMrgrseqfEKTAELLKEKMEHL 919
Cdd:TIGR04523  557 ENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSL-------EKELEKAKKENEKL 629
                          330       340
                   ....*....|....*....|....*....
gi 2528974265  920 igacrdkEAKIKELLKKLEQLSEEVLAIR 948
Cdd:TIGR04523  630 -------SSIIKNIKSKKNKLKQEVKQIK 651
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
662-880 4.61e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.14  E-value: 4.61e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  662 AQVQLQQLRQSVGLLTNELAMEKEATEKLRKLLAsqssglrglwdclpaDLVGERSAQSKAAESLEELRAcISTLVDRHR 741
Cdd:COG4913    608 NRAKLAALEAELAELEEELAEAEERLEALEAELD---------------ALQERREALQRLAEYSWDEID-VASAEREIA 671
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  742 EAQQVLARLQEENQQLRGslspcrepgtsLKApaspQVAALEQDLGKLEEELRAVQATMSGKSQEIGKLKQLLYQATEEV 821
Cdd:COG4913    672 ELEAELERLDASSDDLAA-----------LEE----QLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRL 736
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2528974265  822 AELRAREAASLRQHEKTRGSLVAQAQAWGQELKALLEKYNTACREVGRLREAVAEERRR 880
Cdd:COG4913    737 EAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRA 795
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
612-974 5.07e-04

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 43.86  E-value: 5.07e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  612 QLEKEMSVLRLSNSNLLEELGELGRERQRLQRELQSLSQRLQREFVPKPQAQVQLQ----QLRQSVGLLTN--------- 678
Cdd:TIGR04523  215 SLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSekqkELEQNNKKIKElekqlnqlk 294
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  679 ----ELAMEKEA--TEKLRKLLASQSSGLRGlwdcLPADLVGERSAQSKAAESLEELRACISTL------VDRH-REAQQ 745
Cdd:TIGR04523  295 seisDLNNQKEQdwNKELKSELKNQEKKLEE----IQNQISQNNKIISQLNEQISQLKKELTNSesenseKQRElEEKQN 370
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  746 VLARLQEENQQLRGSLspcrepgTSLKApaspQVAALEQDLGK-------LEEELRAVQATMSGKSQEIGKLKQLLYQAT 818
Cdd:TIGR04523  371 EIEKLKKENQSYKQEI-------KNLES----QINDLESKIQNqeklnqqKDEQIKKLQQEKELLEKEIERLKETIIKNN 439
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  819 EEVAELRAREAA---SLRQHEKTRGSLvaqaqawGQELKALLEKYNtacrevgrlreavaEERRRSGDLAAQAAEQERQA 895
Cdd:TIGR04523  440 SEIKDLTNQDSVkelIIKNLDNTRESL-------ETQLKVLSRSIN--------------KIKQNLEQKQKELKSKEKEL 498
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  896 SEMRGRSEQFEKTAELLKEKMEHLIGACRDKEAKIKELLKKLEQLSEEVLAIRGENARLAL--QLQDSQKNHEEIISTYR 973
Cdd:TIGR04523  499 KKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLekEIDEKNKEIEELKQTQK 578

                   .
gi 2528974265  974 N 974
Cdd:TIGR04523  579 S 579
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
24-162 6.32e-04

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: 43.46  E-value: 6.32e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265   24 LLEAVHRGDVGRVAALASRKSARPTKLDSNGQSPFHLAASKGLTECLTILLANGAD-----INSKNEDGSTALHLATISC 98
Cdd:cd22192     21 LLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElvnepMTSDLYQGETALHIAVVNQ 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265   99 QPQCVKVLLQHGAneDAVDAE----------------NRSPLHWAASSGCASSVLLLCDHEAFLDVLDNDGRTPLMIASL 162
Cdd:cd22192    101 NLNLVRELIARGA--DVVSPRatgtffrpgpknliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHILVL 178
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
45-118 7.21e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 43.35  E-value: 7.21e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2528974265   45 ARPTKLDSNGQSPFHLAASKGLTECLTILLANGADINSKNEDGSTALHLATISCQPQCVKVLLQHGANEDAVDA 118
Cdd:PTZ00322   106 ADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFELGA 179
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
733-872 8.24e-04

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 43.47  E-value: 8.24e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  733 ISTLVDRHREAQQVLARLQEENQQLRGSLSpcREPGTSLKAPASPQVAALEQDLGKLEEELRAVQATMSGKS-------Q 805
Cdd:COG3206    221 LSELESQLAEARAELAEAEARLAALRAQLG--SGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHpdvialrA 298
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2528974265  806 EIGKLKQLLYQATEEVAELRAREAASLRQHEKTRGSLVAQAQAWGQELKALLEKYNTACREVGRLRE 872
Cdd:COG3206    299 QIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARE 365
PHA02859 PHA02859
ankyrin repeat protein; Provisional
49-153 8.43e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 41.73  E-value: 8.43e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265   49 KLDSNGQSPFH--LAASKGLT-ECLTILLANGADINSKNEDGSTALH--LATISCQPQCVKVLLQHGANEDAVDAENRSP 123
Cdd:PHA02859    82 KTRDNNLSALHhyLSFNKNVEpEILKILIDSGSSITEEDEDGKNLLHmyMCNFNVRINVIKLLIDSGVSFLNKDFDNNNI 161
                           90       100       110
                   ....*....|....*....|....*....|
gi 2528974265  124 LHwaassgcasSVLLLCDHEAFLDVLDNDG 153
Cdd:PHA02859   162 LY---------SYILFHSDKKIFDFLTSLG 182
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
54-175 1.23e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily (TRPV), named after the vanilloid receptor 1 (TRPV1), consists of six members: four thermo-sensing channels (TRPV1, TRPV2, TRPV3, and TRPV4) and two Ca2+ selective channels (TRPV5 and TRPV6). The calcium-selective channels TRPV5 and TRPV6 can be heterotetramers and are important for general Ca2+ homeostasis. All four channels within the TRPV1-4 group show temperature-invoked currents when expressed in heterologous cell systems, ranging from activation at ~25C for TRPV4 to ~52C for TRPV2. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. The TRP family consists of membrane proteins that function as ion channels that communicate between the cell and its environment, by a vast array of physical or chemical stimuli, including radiation (in the form of temperature, infrared ,or light) and pressure (osmotic or mechanical). TRP channels are formed by a tetrameric complex of channel subunits. Based on sequence identity, the mammalian TRP channel family is classified into six subfamilies, with significant sequence similarity within the transmembrane domains, but very low similarity in their N- and C-terminal cytoplasmic regions. The six subfamilies are named based on their first member: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPA (ankyrin), TRPML (mucolipin), and TRPP (polycystic).


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 42.56  E-value: 1.23e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265   54 GQSPFHLAASKGLTECLTILLANGADINSKNED-------------GSTALHLATISCQPQCVKVLLQHGANEDAVDAE- 119
Cdd:cd21882     73 GQTALHIAIENRNLNLVRLLVENGADVSARATGrffrkspgnlfyfGELPLSLAACTNQEEIVRLLLENGAQPAALEAQd 152
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2528974265  120 --------------NRSPLHWAASSGCASSVLLL---CDHEAFLDVLDN-DGRTPLMIASLGGHAAICSQLLQR 175
Cdd:cd21882    153 slgntvlhalvlqaDNTPENSAFVCQMYNLLLSYgahLDPTQQLEEIPNhQGLTPLKLAAVEGKIVMFQHILQR 226
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
666-948 1.36e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 42.72  E-value: 1.36e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  666 LQQLRQSVGLLTNELAMEKEATEKLRKLLASQSSGLRG--LWDCLPADLVGERSAQ-SKAAESLEELRACISTL---VDR 739
Cdd:PRK02224   421 RDELREREAELEATLRTARERVEEAEALLEAGKCPECGqpVEGSPHVETIEEDRERvEELEAELEDLEEEVEEVeerLER 500
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  740 HREAQQVLARLQ--EENQQLRGSLSPCREPGTSLKapaSPQVAALEQDLGKLEEELRAVQATMSGKSQEIGKlkqllyqA 817
Cdd:PRK02224   501 AEDLVEAEDRIErlEERREDLEELIAERRETIEEK---RERAEELRERAAELEAEAEEKREAAAEAEEEAEE-------A 570
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  818 TEEVAELRAREAA---SLRQHEKTRGSLVAQAQAwGQELKALLEKYNTACREVGRLREAVAEERRRSGDLAAqaAEQERQ 894
Cdd:PRK02224   571 REEVAELNSKLAElkeRIESLERIRTLLAAIADA-EDEIERLREKREALAELNDERRERLAEKRERKRELEA--EFDEAR 647
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2528974265  895 ASEMRGRSEQFEKTAELLKEKMEHL----------IGACRDKEAKIKELLKKLEQLSEEVLAIR 948
Cdd:PRK02224   648 IEEAREDKERAEEYLEQVEEKLDELreerddlqaeIGAVENELEELEELRERREALENRVEALE 711
Ank_4 pfam13637
Ankyrin repeats (many copies);
188-234 1.46e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 37.64  E-value: 1.46e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 2528974265  188 SALILACEKGSAEVAELLLSHGADAGAVDSTGHDALHYALHTQDKAL 234
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEV 49
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
152-181 1.58e-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: 36.80  E-value: 1.58e-03
                            10        20        30
                    ....*....|....*....|....*....|
gi 2528974265   152 DGRTPLMIASLGGHAAICSQLLQRGARVNV 181
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
629-966 1.68e-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: 42.26  E-value: 1.68e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  629 EELGELGRERQRLQRELQSLSQRLQREFVPKPQAQVQLQQLRQSVGLLTNELAMEKEATEKlrkllASQSSGLRGLWDCL 708
Cdd:TIGR00618  300 KAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDA-----HEVATSIREISCQQ 374
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  709 PADLVGERSAQSKAAESLEELRACISTLVDRHREAQQVLARLQEENQqLRGSLSPCREPGTSLKAPASPQVAALEQDLGK 788
Cdd:TIGR00618  375 HTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRD-LQGQLAHAKKQQELQQRYAELCAAAITCTAQC 453
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  789 LEEELRAVQATMSGKSQEIGKLKQLlYQATEEVAELRAREAASLRQHEKTRGSLVAQAQAWGQELKALLEKYNTACR--- 865
Cdd:TIGR00618  454 EKLEKIHLQESAQSLKEREQQLQTK-EQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRmqr 532
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  866 ---EVGRLREAVAEERRRSGDLAAQAAEQERQASEMRGRSEQFEKTAELLKEKMEHLigacrdkEAKIKELLKKLEQLSE 942
Cdd:TIGR00618  533 geqTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNL-------QNITVRLQDLTEKLSE 605
                          330       340
                   ....*....|....*....|....
gi 2528974265  943 EVLAIRGENARLALQLQDSQKNHE 966
Cdd:TIGR00618  606 AEDMLACEQHALLRKLQPEQDLQD 629
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
53-81 1.69e-03

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: 36.85  E-value: 1.69e-03
                           10        20
                   ....*....|....*....|....*....
gi 2528974265   53 NGQSPFHLAASKGLTECLTILLANGADIN 81
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADIN 29
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
45-175 1.70e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a temperature-sensitive Transient Receptor Potential (TRP) ion channel that is activated by warm temperatures, synthetic small-molecule chemicals, and natural compounds from plants. TRPV3 function is regulated by physiological factors such as extracellular divalent cations and acidic pH, intracellular adenosine triphosphate, membrane voltage, and arachidonic acid. It is expressed in both neuronal and non-neuronal tissues including epidermal keratinocytes, epithelial cells in the gut, endothelial cells in blood vessels, and neurons in dorsal root ganglia and CNS. TRPV3 null mice have abnormal hair morphogenesis and compromised skin barrier function. It may play roles in inflammatory skin disorders, such as itch and pain sensation. TRPV3 is also expressed by many neuronal and non-neuronal tissues, showing that TRPV3 might play roles in other unknown cellular and physiological functions. TRPV3 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 42.44  E-value: 1.70e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265   45 ARPTKLDSNGQSPFHLAASKGLTECLTILLANGADI---------NSKNED-----GSTALHLATISCQPQCVKVLLQHG 110
Cdd:cd22194    132 AEYTEEAYEGQTALNIAIERRQGDIVKLLIAKGADVnahakgvffNPKYKHegfyfGETPLALAACTNQPEIVQLLMEKE 211
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2528974265  111 ANEDAV-DAENRSPLHWAASSGCAS------------SVLLLCDHEAFLDVLDNDGRTPLMIASLGGHAAICSQLLQR 175
Cdd:cd22194    212 STDITSqDSRGNTVLHALVTVAEDSktqndfvkrmydMILLKSENKNLETIRNNEGLTPLQLAAKMGKAEILKYILSR 289
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
86-112 1.83e-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: 36.80  E-value: 1.83e-03
                            10        20
                    ....*....|....*....|....*..
gi 2528974265    86 DGSTALHLATISCQPQCVKVLLQHGAN 112
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGAD 27
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
185-211 2.76e-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: 36.03  E-value: 2.76e-03
                            10        20
                    ....*....|....*....|....*..
gi 2528974265   185 NDKSALILACEKGSAEVAELLLSHGAD 211
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGAD 27
PHA02876 PHA02876
ankyrin repeat protein; Provisional
168-231 3.06e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 41.59  E-value: 3.06e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2528974265  168 ICSQLLQRGARVNVTDKNDKSALILACEKGSAEVAELLLSHGADAGAVDSTGHDALHYALHTQD 231
Cdd:PHA02876   160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKN 223
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
778-973 3.42e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 41.16  E-value: 3.42e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  778 QVAALEQDLGKLEEELRA---------VQATMSGKSQEIGKLKQLLYQATEEVAELRAREAASLRQHEKTRGSLVAQAQA 848
Cdd:COG3206    183 QLPELRKELEEAEAALEEfrqknglvdLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQS 262
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  849 wgQELKALLEKYNtacrevgRLREAVAEERRRSGDL--AAQAAEQERQASEmrgrsEQFEKTAELLKEKMEHLIGACRDK 926
Cdd:COG3206    263 --PVIQQLRAQLA-------ELEAELAELSARYTPNhpDVIALRAQIAALR-----AQLQQEAQRILASLEAELEALQAR 328
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 2528974265  927 EAKIKELLKKLEQLSEEVLAIRGENARLALQLQDSQKNHEEIISTYR 973
Cdd:COG3206    329 EASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLE 375
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
603-959 3.48e-03

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 41.26  E-value: 3.48e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  603 KALGGLAKGQLEKEMSVLRLSNSNL--------------------LEELGELGRERQRLQRELQSLSQRLQREFVPKPQA 662
Cdd:pfam15921  436 KAMKSECQGQMERQMAAIQGKNESLekvssltaqlestkemlrkvVEELTAKKMTLESSERTVSDLTASLQEKERAIEAT 515
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  663 QVQLQQLRQSVGLLTNELAMEKEATEKLRKLLAsqssglrglwDCLPADLvgERSAQSKAAESLEELRACISTLVDRH-R 741
Cdd:pfam15921  516 NAEITKLRSRVDLKLQELQHLKNEGDHLRNVQT----------ECEALKL--QMAEKDKVIEILRQQIENMTQLVGQHgR 583
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  742 EAQQVL---ARLQEENQQLRGSLSPCRepgtSLKAPASPQVAALEQDLGKLE-EELRAVQATmSGKSQEIGKLKQLLYQA 817
Cdd:pfam15921  584 TAGAMQvekAQLEKEINDRRLELQEFK----ILKDKKDAKIRELEARVSDLElEKVKLVNAG-SERLRAVKDIKQERDQL 658
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  818 TEEVAELRAREAASLRQHEKTRGSLVAQAQAWGQELKALLEKYNTACREVGRLREAVAEERRRSGDLAAQAAEQERQASE 897
Cdd:pfam15921  659 LNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITA 738
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2528974265  898 MRGRSEQFEKTAELLKEKMEHligacRDKEakiKELLKKLE-QLSEEVLAIRGENARLALQLQ 959
Cdd:pfam15921  739 KRGQIDALQSKIQFLEEAMTN-----ANKE---KHFLKEEKnKLSQELSTVATEKNKMAGELE 793
mukB PRK04863
chromosome partition protein MukB;
711-904 3.93e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 41.48  E-value: 3.93e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  711 DLVGERSAQSKAAESLEELRACISTLVDRHREAQQVLARLQEENQQLrgslspcrepgtslkapasPQVAALEQDLGKLE 790
Cdd:PRK04863   500 ELLRRLREQRHLAEQLQQLRMRLSELEQRLRQQQRAERLLAEFCKRL-------------------GKNLDDEDELEQLQ 560
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  791 EELRAVQATMSgksqeigklkqllyQATEEVAELRAREAASLRQHEKTRGSLVAQAQAWgQELKALLEkyntacrevgRL 870
Cdd:PRK04863   561 EELEARLESLS--------------ESVSEARERRMALRQQLEQLQARIQRLAARAPAW-LAAQDALA----------RL 615
                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 2528974265  871 REAVAEE---RRRSGDLAAQAAEQERQASEMRGRSEQ 904
Cdd:PRK04863   616 REQSGEEfedSQDVTEYMQQLLERERELTVERDELAA 652
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
710-881 4.51e-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: 4.51e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  710 ADLVGERSAQSKAAESLEELRACISTLVDRHREAQQVLARLQEENQQLRGSLSPCREpgtslkapaspQVAALE-QDLGK 788
Cdd:COG4913    274 LEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEA-----------QIRGNGgDRLEQ 342
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  789 LEEELRAVQATMSGKSQEIGKLKQLLYQAT-------EEVAELRAREAASLRQHEKTRGSLVAQAQAWGQELKALLEKYN 861
Cdd:COG4913    343 LEREIERLERELEERERRRARLEALLAALGlplpasaEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELR 422
                          170       180
                   ....*....|....*....|
gi 2528974265  862 TACREVGRLReavaeeRRRS 881
Cdd:COG4913    423 ELEAEIASLE------RRKS 436
PHA02946 PHA02946
ankyin-like protein; Provisional
171-236 4.65e-03

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 40.81  E-value: 4.65e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2528974265  171 QLLQRGARVNVTDKNDKSALILACEKGSAEVAELLLSHGADAGAVDSTGHDALHYALHTQDKALWR 236
Cdd:PHA02946    57 ELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDEVIER 122
PHA02798 PHA02798
ankyrin-like protein; Provisional
67-181 4.68e-03

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 40.59  E-value: 4.68e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265   67 TECLTILLANGADINSKNEDGSTAL-----HLATISCQPQCVKVLLQHGANEDAVDAENRSPLHWAASSGCASS---VLL 138
Cdd:PHA02798    51 TDIVKLFINLGANVNGLDNEYSTPLctilsNIKDYKHMLDIVKILIENGADINKKNSDGETPLYCLLSNGYINNleiLLF 130
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 2528974265  139 LCDHEAFLDVLDNDGRTPLMIASLGGHAA---ICSQLLQRGARVNV 181
Cdd:PHA02798   131 MIENGADTTLLDKDGFTMLQVYLQSNHHIdieIIKLLLEKGVDINT 176
PHA02741 PHA02741
hypothetical protein; Provisional
51-127 5.84e-03

hypothetical protein; Provisional


Pssm-ID: 165108 [Multi-domain]  Cd Length: 169  Bit Score: 38.87  E-value: 5.84e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265   51 DSNGQSPFHLAASKG----LTECLTILLANGADINSKNE-DGSTALHLATISCQPQCVKVLL-QHGANEDAVDAENRSPL 124
Cdd:PHA02741    57 DDAGQMCIHIAAEKHeaqlAAEIIDHLIELGADINAQEMlEGDTALHLAAHRRDHDLAEWLCcQPGIDLHFCNADNKSPF 136

                   ...
gi 2528974265  125 HWA 127
Cdd:PHA02741   137 ELA 139
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
612-971 6.93e-03

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 40.54  E-value: 6.93e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  612 QLEKEMSVLRLSNSNLLEELGELGRERQRLQRELQSLSQRLQREFVPKPQAQVQLQqlrqsvglltnELAMEKEATEKLR 691
Cdd:pfam01576  360 ELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQ-----------ELQARLSESERQR 428
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  692 KLLASQSSGLRGLWDCLPADLvgeRSAQSKAAESLEELRACISTLVD----RHREAQQVLA------RLQEENQQLRGSL 761
Cdd:pfam01576  429 AELAEKLSKLQSELESVSSLL---NEAEGKNIKLSKDVSSLESQLQDtqelLQEETRQKLNlstrlrQLEDERNSLQEQL 505
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  762 SPCREPGTSLKAPASPQVAALEQDLGKLEEELRAVQATMSGKSQEIGKLKQLLYQATEEVAELRAREAASLRQHEKTRGS 841
Cdd:pfam01576  506 EEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDL 585
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  842 LVAQAQAwgQELKALLEK----YNTACREVGRLREAVAEERRRSgdlAAQAAEQE-------RQASEMRGRSEQFEKTAE 910
Cdd:pfam01576  586 LVDLDHQ--RQLVSNLEKkqkkFDQMLAEEKAISARYAEERDRA---EAEAREKEtralslaRALEEALEAKEELERTNK 660
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2528974265  911 LLKEKMEHLIG--------------ACRDKEAKIKELLKKLEQLSEEVLAIRGENARLALQLQDSQKNHEEIIST 971
Cdd:pfam01576  661 QLRAEMEDLVSskddvgknvhelerSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNMQALKAQFERDLQA 735
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
612-896 7.25e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 39.81  E-value: 7.25e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  612 QLEKEMSVLRLSNSNLLEELGELGRERQRLQRELQSLSQRLQrefvpkpQAQVQLQQLRQSVGLLTNELAmekEATEKLR 691
Cdd:COG3883     20 AKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELE-------ALQAEIDKLQAEIAEAEAEIE---ERREELG 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  692 KLLAS--QSSGLRGLWDCL-----PADLVGERSAQSKAAESLEELracistlVDRHREAQQVLARLQEENQQlrgslspc 764
Cdd:COG3883     90 ERARAlyRSGGSVSYLDVLlgsesFSDFLDRLSALSKIADADADL-------LEELKADKAELEAKKAELEA-------- 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  765 repgtslkapaspQVAALEQDLGKLEEELRAVQATMSGKSQEIGKLKQLLYQATEEVAELRAREAASLRQHEKTRGSLVA 844
Cdd:COG3883    155 -------------KLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAA 221
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2528974265  845 QAQAWGQELKALLEKYNTACREVGRLREAVAEERRRSGDLAAQAAEQERQAS 896
Cdd:COG3883    222 AAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAG 273
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
778-944 7.25e-03

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 39.14  E-value: 7.25e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  778 QVAALEQDLGKLEEELRAVQATMSGKSQEIGKLKQLLYQATEEVAELRAREAASLRQHEKTRGSLVAQAQAwgQELKALL 857
Cdd:COG1579     18 ELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNN--KEYEALQ 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  858 ekyntacREVGRLREAVAEERRRSGDLAAQAAEQERQASEMRgrsEQFEKTAELLKEKMEHLIGACRDKEAKIKELLKKL 937
Cdd:COG1579     96 -------KEIESLKRRISDLEDEILELMERIEELEEELAELE---AELAELEAELEEKKAELDEELAELEAELEELEAER 165

                   ....*..
gi 2528974265  938 EQLSEEV 944
Cdd:COG1579    166 EELAAKI 172
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
152-181 8.74e-03

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: 34.93  E-value: 8.74e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 2528974265  152 DGRTPLMIASLGGHAAICSQLLQRGARVNV 181
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
612-924 8.98e-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: 39.88  E-value: 8.98e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  612 QLEKEMSVLRLSNSNLLEELGELGRERQRLQRELQSLSQRLQREFVPKPQAQVQLQQLRQSVGLLTNELAMEKEATEKLR 691
Cdd:pfam07888   98 ELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQ 177
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  692 KLLASQSSGLRGLwdclPADLVGERSAQSKAAESLEELRACISTLVDRHREAQQVLArlqeENQQLRGSLSPCREpgtsl 771
Cdd:pfam07888  178 AKLQQTEEELRSL----SKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEA----ENEALLEELRSLQE----- 244
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  772 kapaspQVAALEQDLGKLEEELRAVQATMSGKSQEigklkqlLYQATEEVAELRAREAASLRQHEKTRGSLVAQAQAWGQ 851
Cdd:pfam07888  245 ------RLNASERKVEGLGEELSSMAAQRDRTQAE-------LHQARLQAAQLTLQLADASLALREGRARWAQERETLQQ 311
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265  852 ELKALLEKYNTACREVGRLREAVAEERRRSGDLAA-----------QAAEQERQASEMRGRSEQFEKTAE-LLKEKMEHL 919
Cdd:pfam07888  312 SAEADKDRIEKLSAELQRLEERLQEERMEREKLEVelgrekdcnrvQLSESRRELQELKASLRVAQKEKEqLQAEKQELL 391

                   ....*
gi 2528974265  920 IGACR 924
Cdd:pfam07888  392 EYIRQ 396
PHA02736 PHA02736
Viral ankyrin protein; Provisional
48-127 9.21e-03

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 37.93  E-value: 9.21e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528974265   48 TKLDSNGQSPFHLAASKGLT---ECLTILLANGADINSKNE-DGSTALHLATISCQPQCVKVLL-QHGANEDAVDAENRS 122
Cdd:PHA02736    49 LEYNRHGKQCVHIVSNPDKAdpqEKLKLLMEWGADINGKERvFGNTPLHIAVYTQNYELATWLCnQPGVNMEILNYAFKT 128

                   ....*
gi 2528974265  123 PLHWA 127
Cdd:PHA02736   129 PYYVA 133
 
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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