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Conserved domains on  [gi|2024434941|ref|XP_040512450|]
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ankycorbin isoform X9 [Gallus gallus]

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];
1-237 7.56e-51

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 180.92  E-value: 7.56e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941   1 MKSLKAKFRKSDTNEWNKNDDRLLQAVENGDPEKVASLLGKKGASATKQDSEGKTAFHLAATKGHAECLRIMVTHGADVT 80
Cdd:COG0666    35 LLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVN 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  81 AQDGAGHSALHLAVKNSHIDCIKRLLQYKCSVYSTDNSGKTALHYAATCGCLQAVQLLCEHKCPINMKDLDGNIPLLLAV 160
Cdd:COG0666   115 ARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAA 194

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024434941 161 QNGHTEVCKYLLDHGADINTRDKNGRTALMIACEAGSLNMVEVFLRKGADVSLVDVFGQNALHYSKISENTGIQNLL 237
Cdd:COG0666   195 ENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLL 271
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 496-871 4.10e-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: 73.94  E-value: 4.10e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  496 EEVEMLRQELRRALEESERQKEKVRELQKKFEEREQnvtsklsveeceelknsycsvidninQEKALLIERYKEGQEEIK 575
Cdd:TIGR02168  189 DRLEDILNELERQLKSLERQAEKAERYKELKAELRE--------------------------LELALLVLRLEELREELE 242

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  576 RLQDKLTNQTHLESSAESGemKDAMHRMIDELNRQLSELSQLYKEAQAELEDYRKRktlddiavdyIPRDEHEKlmQVTN 655
Cdd:TIGR02168  243 ELQEELKEAEEELEELTAE--LQELEEKLEELRLEVSELEEEIEELQKELYALANE----------ISRLEQQK--QILR 308

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  656 SLKYKAENELLEMKSQYTKVLDEAEELKQMLDTQKQNslpIAEHQQVMNALRSTVKEMEEEINELKELLTNKESEVRNLQ 735
Cdd:TIGR02168  309 ERLANLERQLEELEAQLEELESKLDELAEELAELEEK---LEELKEELESLEAELEELEAELEELESRLEELEEQLETLR 385

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  736 KELLEEKAAINEAMVPRAAYEKLQSSLEGEVSILSSKLKDVIKEKENVSLDvmQLRSEVLHLKEEKEGMHNLLEAKEREV 815
Cdd:TIGR02168  386 SKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELK--ELQAELEELEEELEELQEELERLEEAL 463

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2024434941  816 SGLHQKYHQAQEDLLEMKRYSESSSKLEEDKDKKINEMSKEVSKLKEALNSLSQLS 871
Cdd:TIGR02168  464 EELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLS 519
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 278-583 1.09e-04

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: 46.20  E-value: 1.09e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  278 FADQQEDFSSL---LQDNKDRLSDSTAGADSLLDVSSETEQQDLLMLMQAKIASLTLHNKELQDKLQERTPKEVDSTIDS 354
Cdd:TIGR02168  686 IEELEEKIAELekaLAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEE 765

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  355 YHStQREFDQTADRQSEISAQELKSTLNATQSQ-----EKLTSPSEIkIKYLQEDSKDAQRKLENSETKRKHLEAQVQSR 429
Cdd:TIGR02168  766 LEE-RLEEAEEELAEAEAEIEELEAQIEQLKEElkalrEALDELRAE-LTLLNEEAANLRERLESLERRIAATERRLEDL 843

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  430 VPEADLNNTDISENgSDPSLKIQETQSKYEEAAKEVLNAQKQVKPGLvssesEETCSELSKLKVTCEEVEMLRQELRRAL 509
Cdd:TIGR02168  844 EEQIEELSEDIESL-AAEIEELEELIEELESELEALLNERASLEEAL-----ALLRSELEELSEELRELESKRSELRREL 917

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024434941  510 EESERQKEKVRELQKKFEEREQNVTSKLSVEECEELknsycsviDNINQEKALLIERYKEGQEEIKRLQDKLTN 583
Cdd:TIGR02168  918 EELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTL--------EEAEALENKIEDDEEEARRRLKRLENKIKE 983
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1-237 7.56e-51

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 180.92  E-value: 7.56e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941   1 MKSLKAKFRKSDTNEWNKNDDRLLQAVENGDPEKVASLLGKKGASATKQDSEGKTAFHLAATKGHAECLRIMVTHGADVT 80
Cdd:COG0666    35 LLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVN 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  81 AQDGAGHSALHLAVKNSHIDCIKRLLQYKCSVYSTDNSGKTALHYAATCGCLQAVQLLCEHKCPINMKDLDGNIPLLLAV 160
Cdd:COG0666   115 ARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAA 194

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024434941 161 QNGHTEVCKYLLDHGADINTRDKNGRTALMIACEAGSLNMVEVFLRKGADVSLVDVFGQNALHYSKISENTGIQNLL 237
Cdd:COG0666   195 ENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLL 271
Ank_2 pfam12796
Ankyrin repeats (3 copies);
90-182 8.82e-26

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 101.73  E-value: 8.82e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  90 LHLAVKNSHIDCIKRLLQYKCSVYSTDNSGKTALHYAATCGCLQAVQLLCEHkCPINMKDlDGNIPLLLAVQNGHTEVCK 169
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 2024434941 170 YLLDHGADINTRD 182
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 23-237 1.88e-22

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 101.28  E-value: 1.88e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  23 LLQAVENGDPEKVASLLgKKGASATKQDSEGKTAFHLAATKGHA-----ECLRIMVTHGADVTAQDGAGHSALHLAVKNS 97
Cdd:PHA03100   39 LYLAKEARNIDVVKILL-DNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAISKK 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  98 --HIDCIKRLLQYKCSVYSTDNSGKTALHYAATCGC--LQAVQLLCEHKCPINMKDldgniplllavqnghteVCKYLLD 173
Cdd:PHA03100  118 snSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVDINAKN-----------------RVNYLLS 180

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024434941 174 HGADINTRDKNGRTALMIACEAGSLNMVEVFLRKGADVSLVDVFGQNALHYSKISENTGIQNLL 237
Cdd:PHA03100  181 YGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLL 244
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 496-871 4.10e-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: 73.94  E-value: 4.10e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  496 EEVEMLRQELRRALEESERQKEKVRELQKKFEEREQnvtsklsveeceelknsycsvidninQEKALLIERYKEGQEEIK 575
Cdd:TIGR02168  189 DRLEDILNELERQLKSLERQAEKAERYKELKAELRE--------------------------LELALLVLRLEELREELE 242

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  576 RLQDKLTNQTHLESSAESGemKDAMHRMIDELNRQLSELSQLYKEAQAELEDYRKRktlddiavdyIPRDEHEKlmQVTN 655
Cdd:TIGR02168  243 ELQEELKEAEEELEELTAE--LQELEEKLEELRLEVSELEEEIEELQKELYALANE----------ISRLEQQK--QILR 308

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  656 SLKYKAENELLEMKSQYTKVLDEAEELKQMLDTQKQNslpIAEHQQVMNALRSTVKEMEEEINELKELLTNKESEVRNLQ 735
Cdd:TIGR02168  309 ERLANLERQLEELEAQLEELESKLDELAEELAELEEK---LEELKEELESLEAELEELEAELEELESRLEELEEQLETLR 385

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  736 KELLEEKAAINEAMVPRAAYEKLQSSLEGEVSILSSKLKDVIKEKENVSLDvmQLRSEVLHLKEEKEGMHNLLEAKEREV 815
Cdd:TIGR02168  386 SKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELK--ELQAELEELEEELEELQEELERLEEAL 463

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2024434941  816 SGLHQKYHQAQEDLLEMKRYSESSSKLEEDKDKKINEMSKEVSKLKEALNSLSQLS 871
Cdd:TIGR02168  464 EELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLS 519
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
375-870 1.31e-12

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 72.02  E-value: 1.31e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 375 QELKSTLNATQSQEKLTSPSEIKIKYLQEDSKDAQRKLENSETKRKHLEAQVQsRVPEadlnntdisengsdpslkIQET 454
Cdd:PRK03918  231 KELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVK-ELKE------------------LKEK 291

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 455 QSKYEEAAKEvlnaqkqvkpglvsseSEETCSELSKLKVTCEEVEMLRQELRRALEESERQKEKVRELQKKFEEREQNV- 533
Cdd:PRK03918  292 AEEYIKLSEF----------------YEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLe 355

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 534 ----------TSKLSVEECEELKNSY-CSVIDNINQEKALLIERYKEGQEEIKRLQDKLTNqthLESsaESGEMKDAMHR 602
Cdd:PRK03918  356 eleerhelyeEAKAKKEELERLKKRLtGLTPEKLEKELEELEKAKEEIEEEISKITARIGE---LKK--EIKELKKAIEE 430

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 603 M----------------------IDELNRQLSELSQLYKEAQAELEDYRKRKTLDDIAVDYIPR-----DEHEKLMQVTN 655
Cdd:PRK03918  431 LkkakgkcpvcgrelteehrkelLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESEliklkELAEQLKELEE 510

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 656 SLKYKAENELLEMKSQYTKVLDEAEELKQMLDTQKQNSLPIAEHQQVMNALRSTVKEMEEEINEL-KELLTNKESEVRNL 734
Cdd:PRK03918  511 KLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELlKELEELGFESVEEL 590

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 735 QKELLEEKAAINEAMVPRAAYEKLQSSLEgEVSILSSKLKDVIKEKENVSLDVMQLRSEVLHLK-----EEKEGMHNLLE 809
Cdd:PRK03918  591 EERLKELEPFYNEYLELKDAEKELEREEK-ELKKLEEELDKAFEELAETEKRLEELRKELEELEkkyseEEYEELREEYL 669

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024434941 810 AKEREVSGLHQKYHQAQEDLLEMKRYSEsssKLEEDKdKKINEMSKEVSKLKEALNSLSQL 870
Cdd:PRK03918  670 ELSRELAGLRAELEELEKRREEIKKTLE---KLKEEL-EEREKAKKELEKLEKALERVEEL 726
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 496-833 9.85e-12

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 69.20  E-value: 9.85e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 496 EEVEMLRQELRRALEESERQKE---KVRELQKKFEEREQNVTSKlsveeceelknsycsVIDNINQEKALLIERYKEGQE 572
Cdd:COG1196   189 ERLEDILGELERQLEPLERQAEkaeRYRELKEELKELEAELLLL---------------KLRELEAELEELEAELEELEA 253

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 573 EIKRLQdklTNQTHLESSAESGEMKdamhrmIDELNRQLSELSQLYKEAQAELEDYRKRKTLDDIAVdyipRDEHEKLMQ 652
Cdd:COG1196   254 ELEELE---AELAELEAELEELRLE------LEELELELEEAQAEEYELLAELARLEQDIARLEERR----RELEERLEE 320

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 653 VTNSLKyKAENELLEMKSQYTKVLDEAEELKQMLDTQKQNslpIAEHQQVMNALRSTVKEMEEEINELKELLTNKESEVR 732
Cdd:COG1196   321 LEEELA-ELEEELEELEEELEELEEELEEAEEELEEAEAE---LAEAEEALLEAEAELAEAEEELEELAEELLEALRAAA 396

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 733 NLQKELLEEKAAINEAmvpraayEKLQSSLEGEVSILSSKLKDVIKEKENVSLDVMQLRSEVLHLKEEKEGMHNLLEAKE 812
Cdd:COG1196   397 ELAAQLEELEEAEEAL-------LERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELL 469

                         330       340
                  ....*....|....*....|.
gi 2024434941 813 REVSGLHQKYHQAQEDLLEMK 833
Cdd:COG1196   470 EEAALLEAALAELLEELAEAA 490
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 19-191 7.71e-09

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: 59.26  E-value: 7.71e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  19 NDDRLLQAVENGDPEKVASLLGKKGASATKQDSEGKTAFHLAATKGH-------AECLRIMVTHgaDVTAQDGAGHSALH 91
Cdd:cd22192    17 SESPLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNleaavvlMEAAPELVNE--PMTSDLYQGETALH 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  92 LAVKNSHIDCIKRLLQYKCSVYSTDNSGkTALHYAATCgclqavqlLC---EHkcpinmkdldgniPLLLAVQNGHTEVC 168
Cdd:cd22192    95 IAVVNQNLNLVRELIARGADVVSPRATG-TFFRPGPKN--------LIyygEH-------------PLSFAACVGNEEIV 152

                         170       180
                  ....*....|....*....|...
gi 2024434941 169 KYLLDHGADINTRDKNGRTALMI 191
Cdd:cd22192   153 RLLIEHGADIRAQDSLGNTVLHI 175
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 151-179 1.41e-06

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: 45.27  E-value: 1.41e-06
                           10        20
                   ....*....|....*....|....*....
gi 2024434941  151 DGNIPLLLAVQNGHTEVCKYLLDHGADIN 179
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 275-821 9.58e-06

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 49.73  E-value: 9.58e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  275 QAFFADQQEDFSSLLQDNKDRL----SDSTAGADSLLDVSSETEQQDLLMLMQAKIASLTLHNkelQDKLQERTPKEVDS 350
Cdd:pfam15921  248 EALKSESQNKIELLLQQHQDRIeqliSEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARN---QNSMYMRQLSDLES 324

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  351 TIDSYHSTQREfdqtADRQSEISAQELKSTLNATQSQekLTSPSEIKIKYLQEDSK--DAQRKLENSETKRKH---LEAQ 425
Cdd:pfam15921  325 TVSQLRSELRE----AKRMYEDKIEELEKQLVLANSE--LTEARTERDQFSQESGNldDQLQKLLADLHKREKelsLEKE 398

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  426 VQSRVPEADLNNTdISENGSDPSLKIQETQSKYEEAAKEVLNAQKQVKPGLVSSESEETCSELSKLKVTCEEVEMLRQEL 505
Cdd:pfam15921  399 QNKRLWDRDTGNS-ITIDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEML 477

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  506 RRALEESERQKEKVRELQKKFEEreqnVTSKLSVEEceelknsycSVIDNINQEKALLIERYKEGQEEIKRLQDKLTNQT 585
Cdd:pfam15921  478 RKVVEELTAKKMTLESSERTVSD----LTASLQEKE---------RAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLR 544

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  586 HLESSAESGEMKDA-MHRMIDELNRQLSELSQLY------------KEAQAELEDYRKRKTLDDIAVDYIPRDEHEKLMQ 652
Cdd:pfam15921  545 NVQTECEALKLQMAeKDKVIEILRQQIENMTQLVgqhgrtagamqvEKAQLEKEINDRRLELQEFKILKDKKDAKIRELE 624

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  653 VTNSLKYKAENELLEMKSQYTK-VLDEAEELKQMLDTQKQ-----NSLPiAEHQQVMNALRSTVKEMEEEINELKELLTN 726
Cdd:pfam15921  625 ARVSDLELEKVKLVNAGSERLRaVKDIKQERDQLLNEVKTsrnelNSLS-EDYEVLKRNFRNKSEEMETTTNKLKMQLKS 703

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  727 KESEVRNLQKELLEEKAAINEAMVPRAAYEKLQSSLEGEVSILSSKLK-------DVIKEKENVSLDVMQLRSEVLHLKE 799
Cdd:pfam15921  704 AQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQfleeamtNANKEKHFLKEEKNKLSQELSTVAT 783

                          570       580
                   ....*....|....*....|..
gi 2024434941  800 EKEGMHNLLEAKEREVSGLHQK 821
Cdd:pfam15921  784 EKNKMAGELEVLRSQERRLKEK 805
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 86-231 6.23e-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: 6.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  86 GHSAL-HLAVKNSHIDCIKRLLQYKCSVYStdnsGKTALHyAATCGCLQAVQLLCEHKCPINMKDLD------------- 151
Cdd:TIGR00870  52 GRSALfVAAIENENLELTELLLNLSCRGAV----GDTLLH-AISLEYVDAVEAILLHLLAAFRKSGPlelandqytseft 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 152 -GNIPLLLAVQNGHTEVCKYLLDHGADINTRDK--------------NGRTALMIACEAGSLNMVEVFLRKGADVSLVDV 216
Cdd:TIGR00870 127 pGITALHLAAHRQNYEIVKLLLERGASVPARACgdffvksqgvdsfyHGESPLNAAACLGSPSIVALLSEDPADILTADS 206

                         170
                  ....*....|....*.
gi 2024434941 217 FGQNALHYSKI-SENT 231
Cdd:TIGR00870 207 LGNTLLHLLVMeNEFK 222
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 278-583 1.09e-04

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: 46.20  E-value: 1.09e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  278 FADQQEDFSSL---LQDNKDRLSDSTAGADSLLDVSSETEQQDLLMLMQAKIASLTLHNKELQDKLQERTPKEVDSTIDS 354
Cdd:TIGR02168  686 IEELEEKIAELekaLAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEE 765

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  355 YHStQREFDQTADRQSEISAQELKSTLNATQSQ-----EKLTSPSEIkIKYLQEDSKDAQRKLENSETKRKHLEAQVQSR 429
Cdd:TIGR02168  766 LEE-RLEEAEEELAEAEAEIEELEAQIEQLKEElkalrEALDELRAE-LTLLNEEAANLRERLESLERRIAATERRLEDL 843

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  430 VPEADLNNTDISENgSDPSLKIQETQSKYEEAAKEVLNAQKQVKPGLvssesEETCSELSKLKVTCEEVEMLRQELRRAL 509
Cdd:TIGR02168  844 EEQIEELSEDIESL-AAEIEELEELIEELESELEALLNERASLEEAL-----ALLRSELEELSEELRELESKRSELRREL 917

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024434941  510 EESERQKEKVRELQKKFEEREQNVTSKLSVEECEELknsycsviDNINQEKALLIERYKEGQEEIKRLQDKLTN 583
Cdd:TIGR02168  918 EELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTL--------EEAEALENKIEDDEEEARRRLKRLENKIKE 983
14-3-3_fungi cd11309
Fungal 14-3-3 protein domain; This family containing fungal 14-3-3 domains includes the yeasts ...
 505-643 8.78e-03

Fungal 14-3-3 protein domain; This family containing fungal 14-3-3 domains includes the yeasts Saccharomyces cerevisiae (BMH1 and BMH2) and Schizosaccharomyces pombe (rad24 and rad25) isoforms. They possess distinctively variant C-terminal segments that differentiate them from the mammalian isoforms; the C-terminus is longer and BMH1/2 isoforms contain polyglutamine (polyQ) sequences of unknown function. The C-terminal segments of yeast 14-3-3 isoforms may thus behave in a different manner compared to the higher eukaryote isoforms. Yeast 14-3-3 proteins bind to numerous proteins involved in a variety of yeast cellular processes making them excellent model organisms for elucidating the function of the 14-3-3 protein family. BMH1 and BMH2 are positive regulators of rapamycin-sensitive signaling via TOR kinases while they play an inhibitory role in Rtg3p-dependent transcription involved in retrograde signaling. 14-3-3 domains are an essential part of 14-3-3 proteins, a ubiquitous class of regulatory, phosphoserine/threonine-binding proteins found in all eukaryotic cells, including yeast, protozoa and mammalian cells.


Pssm-ID: 206763  Cd Length: 231  Bit Score: 38.82  E-value: 8.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 505 LRRALEESERQKEKVRELQKKFEEREqnvtsKLSVEECEELKNSYCSVI------------------DNINQEKALLIER 566
Cdd:cd11309     7 LAKLAEQAERYEEMVENMKKVASSDQ-----ELTVEERNLLSVAYKNVIgarraswrivssieqkeeSKGNESQVALIKE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 567 YKEGQE-EIKRLQDKLTN--QTHLESSAESGEMKDAMHRMIDELNRQLSELS---QLYKEAQAELEDYrkrKTLDDIAVD 640
Cdd:cd11309    82 YRSKIEsELTKICDDILSvlDKHLIPSATTGESKVFYYKMKGDYHRYLAEFAvgdKRKEAADSSLEAY---KAASDIAVT 158


                  ...
gi 2024434941 641 YIP 643
Cdd:cd11309   159 ELP 161
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1-237 7.56e-51

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 180.92  E-value: 7.56e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941   1 MKSLKAKFRKSDTNEWNKNDDRLLQAVENGDPEKVASLLGKKGASATKQDSEGKTAFHLAATKGHAECLRIMVTHGADVT 80
Cdd:COG0666    35 LLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVN 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  81 AQDGAGHSALHLAVKNSHIDCIKRLLQYKCSVYSTDNSGKTALHYAATCGCLQAVQLLCEHKCPINMKDLDGNIPLLLAV 160
Cdd:COG0666   115 ARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAA 194

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024434941 161 QNGHTEVCKYLLDHGADINTRDKNGRTALMIACEAGSLNMVEVFLRKGADVSLVDVFGQNALHYSKISENTGIQNLL 237
Cdd:COG0666   195 ENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLL 271
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1-237 3.22e-46

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 167.82  E-value: 3.22e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941   1 MKSLKAKFRKSDTNEWNKNDDRLLQAVENGDPEKVASLLGKKGASATKQDSEGKTAFHLAATKGHAECLRIMVTHGADVT 80
Cdd:COG0666     2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  81 AQDGAGHSALHLAVKNSHIDCIKRLLQYKCSVYSTDNSGKTALHYAATCGCLQAVQLLCEHKCPINMKDLDGNIPLLLAV 160
Cdd:COG0666    82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAA 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024434941 161 QNGHTEVCKYLLDHGADINTRDKNGRTALMIACEAGSLNMVEVFLRKGADVSLVDVFGQNALHYSKISENTGIQNLL 237
Cdd:COG0666   162 ANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLL 238
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
17-222 6.89e-43

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 158.19  E-value: 6.89e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  17 NKNDDRLLQAVENGDPEKVASLLgKKGASATKQDSEGKTAFHLAATKGHAECLRIMVTHGADVTAQDGAGHSALHLAVKN 96
Cdd:COG0666    85 DGGNTLLHAAARNGDLEIVKLLL-EAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAAN 163

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  97 SHIDCIKRLLQYKCSVYSTDNSGKTALHYAATCGCLQAVQLLCEHKCPINMKDLDGNIPLLLAVQNGHTEVCKYLLDHGA 176
Cdd:COG0666   164 GNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGA 243

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2024434941 177 DINTRDKNGRTALMIACEAGSLNMVEVFLRKGADVSLVDVFGQNAL 222
Cdd:COG0666   244 DLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
33-237 1.90e-34

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 133.54  E-value: 1.90e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  33 EKVASLLGKKGASATKQDSEGKTAFHLAATKGHAECLRIMVTHGADVTAQDGAGHSALHLAVKNSHIDCIKRLLQYKCSV 112
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 113 YSTDNSGKTALHYAATCGCLQAVQLLCEHKCPINMKDLDGNIPLLLAVQNGHTEVCKYLLDHGADINTRDKNGRTALMIA 192
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2024434941 193 CEAGSLNMVEVFLRKGADVSLVDVFGQNALHYSKISENTGIQNLL 237
Cdd:COG0666   161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLL 205
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
12-189 9.37e-32

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 125.84  E-value: 9.37e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  12 DTNEWNKNDDRLLQ-AVENGDPEKVASLLgKKGASATKQDSEGKTAFHLAATKGHAECLRIMVTHGADVTAQDGAGHSAL 90
Cdd:COG0666   112 DVNARDKDGETPLHlAAYNGNLEIVKLLL-EAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPL 190

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  91 HLAVKNSHIDCIKRLLQYKCSVYSTDNSGKTALHYAATCGCLQAVQLLCEHKCPINMKDLDGNIPLLLAVQNGHTEVCKY 170
Cdd:COG0666   191 HLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKL 270

                         170
                  ....*....|....*....
gi 2024434941 171 LLDHGADINTRDKNGRTAL 189
Cdd:COG0666   271 LLLALLLLAAALLDLLTLL 289
Ank_2 pfam12796
Ankyrin repeats (3 copies);
90-182 8.82e-26

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 101.73  E-value: 8.82e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  90 LHLAVKNSHIDCIKRLLQYKCSVYSTDNSGKTALHYAATCGCLQAVQLLCEHkCPINMKDlDGNIPLLLAVQNGHTEVCK 169
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 2024434941 170 YLLDHGADINTRD 182
Cdd:pfam12796  79 LLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
123-215 3.48e-23

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 94.41  E-value: 3.48e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 123 LHYAATCGCLQAVQLLCEHKCPINMKDLDGNIPLLLAVQNGHTEVCKYLLDHgADINTRDkNGRTALMIACEAGSLNMVE 202
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 2024434941 203 VFLRKGADVSLVD 215
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 23-237 1.88e-22

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 101.28  E-value: 1.88e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  23 LLQAVENGDPEKVASLLgKKGASATKQDSEGKTAFHLAATKGHA-----ECLRIMVTHGADVTAQDGAGHSALHLAVKNS 97
Cdd:PHA03100   39 LYLAKEARNIDVVKILL-DNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAISKK 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  98 --HIDCIKRLLQYKCSVYSTDNSGKTALHYAATCGC--LQAVQLLCEHKCPINMKDldgniplllavqnghteVCKYLLD 173
Cdd:PHA03100  118 snSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVDINAKN-----------------RVNYLLS 180

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024434941 174 HGADINTRDKNGRTALMIACEAGSLNMVEVFLRKGADVSLVDVFGQNALHYSKISENTGIQNLL 237
Cdd:PHA03100  181 YGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLL 244
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 1-215 3.19e-22

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 100.51  E-value: 3.19e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941   1 MKSLKAKFRKS-DTNEWNKNDDRLL------QAVENGDPEkVASLLGKKGASATKQDSEGKTAFHLAATK--GHAECLRI 71
Cdd:PHA03100   48 IDVVKILLDNGaDINSSTKNNSTPLhylsniKYNLTDVKE-IVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEY 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  72 MVTHGADVTAQDGAGHSALHLAVKNSHID--CIKRLLQYKCSVYSTDNsgktalhyaatcgclqaVQLLCEHKCPINMKD 149
Cdd:PHA03100  127 LLDNGANVNIKNSDGENLLHLYLESNKIDlkILKLLIDKGVDINAKNR-----------------VNYLLSYGVPINIKD 189

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024434941 150 LDGNIPLLLAVQNGHTEVCKYLLDHGADINTRDKNGRTALMIACEAGSLNMVEVFLRKGADVSLVD 215
Cdd:PHA03100  190 VYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTII 255
Ank_2 pfam12796
Ankyrin repeats (3 copies);
57-149 8.63e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 90.56  E-value: 8.63e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  57 FHLAATKGHAECLRIMVTHGADVTAQDGAGHSALHLAVKNSHIDCIKRLLQYKCSvySTDNSGKTALHYAATCGCLQAVQ 136
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 2024434941 137 LLCEHKCPINMKD 149
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 12-224 1.52e-20

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 95.86  E-value: 1.52e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  12 DTNEWNKNDDRLLQA---VENGDPeKVASLLGKKGASATKQDSEGKTAFH--LAATKGHAECLRIMVTHGADVTAQDGAG 86
Cdd:PHA03095  109 DVNAKDKVGRTPLHVylsGFNINP-KVIRLLLRKGADVNALDLYGMTPLAvlLKSRNANVELLRLLIDAGADVYAVDDRF 187

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  87 HSALHLAVKNSHID--CIKRLLQYKCSVYSTDNSGKTALHYAAT---CGCLQAVQLLcEHKCPINMKDLDGNIPLLLAVQ 161
Cdd:PHA03095  188 RSLLHHHLQSFKPRarIVRELIRAGCDPAATDMLGNTPLHSMATgssCKRSLVLPLL-IAGISINARNRYGQTPLHYAAV 266

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024434941 162 NGHTEVCKYLLDHGADINTRDKNGRTALMIACEAGSLNMVEVFLRKGADVSLVDvfgqNALHY 224
Cdd:PHA03095  267 FNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETVA----ATLNT 325
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 38-214 4.43e-19

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 90.82  E-value: 4.43e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  38 LLGKKGASATKQDSEGKTAFHLAATKGHA---ECLRIMVTHGADVTAQDGagHSALHLAVKNSHIDCIKRLLQYKCS--V 112
Cdd:PHA02875   53 LLMKHGAIPDVKYPDIESELHDAVEEGDVkavEELLDLGKFADDVFYKDG--MTPLHLATILKKLDIMKLLIARGADpdI 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 113 YSTDNSgkTALHYAATCGCLQAVQLLCEHKCPINMKDLDGNIPLLLAVQNGHTEVCKYLLDHGADINTRDKNGRTALM-I 191
Cdd:PHA02875  131 PNTDKF--SPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALcY 208

                         170       180
                  ....*....|....*....|...
gi 2024434941 192 ACEAGSLNMVEVFLRKGADVSLV 214
Cdd:PHA02875  209 AIENNKIDIVRLFIKRGADCNIM 231
PHA03095 PHA03095
ankyrin-like protein; Provisional
 29-232 6.67e-19

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 90.85  E-value: 6.67e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  29 NGDPEKVASLLGKKGASATKQDSEGKTAFHLAATKGH-AECLRIMVTHGADVTAQDGAGHSALH--LAVKNSHIDCIKRL 105
Cdd:PHA03095   59 SEKVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATtLDVIKLLIKAGADVNAKDKVGRTPLHvyLSGFNINPKVIRLL 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 106 LQYKCSVYSTDNSGKTALH-YAATCGC-LQAVQLLCEHKCPINMKDLDGNIPLLLAVQNGHT--EVCKYLLDHGADINTR 181
Cdd:PHA03095  139 LRKGADVNALDLYGMTPLAvLLKSRNAnVELLRLLIDAGADVYAVDDRFRSLLHHHLQSFKPraRIVRELIRAGCDPAAT 218

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2024434941 182 DKNGRTALMIACEAGSLNMVEV--FLRKGADVSLVDVFGQNALHYSKISENTG 232
Cdd:PHA03095  219 DMLGNTPLHSMATGSSCKRSLVlpLLIAGISINARNRYGQTPLHYAAVFNNPR 271
Ank_2 pfam12796
Ankyrin repeats (3 copies);
23-116 5.17e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 79.77  E-value: 5.17e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  23 LLQAVENGDPEKVASLLgKKGASATKQDSEGKTAFHLAATKGHAECLRIMVTHgADVTAQDGaGHSALHLAVKNSHIDCI 102
Cdd:pfam12796   1 LHLAAKNGNLELVKLLL-ENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIV 77

                          90
                  ....*....|....
gi 2024434941 103 KRLLQYKCSVYSTD 116
Cdd:pfam12796  78 KLLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 66-224 2.52e-17

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 85.85  E-value: 2.52e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  66 AECLRIMVTHGADVTAQDGAGHSALHLAVKNSHIDC---IKRLLQYKCSVYSTDNSGKTALHYAATCGC-LQAVQLLCEH 141
Cdd:PHA03095   27 VEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVkdiVRLLLEAGADVNAPERCGFTPLHLYLYNATtLDVIKLLIKA 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 142 KCPINMKDLDGNIPL--LLAVQNGHTEVCKYLLDHGADINTRDKNGRTALMIACEAG--SLNMVEVFLRKGADVSLVDVF 217
Cdd:PHA03095  107 GADVNAKDKVGRTPLhvYLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRnaNVELLRLLIDAGADVYAVDDR 186


                  ....*..
gi 2024434941 218 GQNALHY 224
Cdd:PHA03095  187 FRSLLHH 193
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 1-189 1.27e-16

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 84.92  E-value: 1.27e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941   1 MKSLKAKFRKSDTNEWNKN---DDRLLQAVENGDPEKVASLLgKKGASATKQDSEGKTAFHLAATKGHAECLRIMVTHGA 77
Cdd:PLN03192  504 LHDLNVGDLLGDNGGEHDDpnmASNLLTVASTGNAALLEELL-KAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHAC 582

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  78 DVTAQDGAGHSALHLAVKNSHiDCIKRLLqYKCSVYSTDNSGKTALHYAATCGCLQAVQLLCEHKCPINMKDLDGNIPLL 157
Cdd:PLN03192  583 NVHIRDANGNTALWNAISAKH-HKIFRIL-YHFASISDPHAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQ 660

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2024434941 158 LAVQNGHTEVCKYLLDHGADI---NTRDKNGRTAL 189
Cdd:PLN03192  661 VAMAEDHVDMVRLLIMNGADVdkaNTDDDFSPTEL 695
Ank_2 pfam12796
Ankyrin repeats (3 copies);
156-248 2.56e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 74.77  E-value: 2.56e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 156 LLLAVQNGHTEVCKYLLDHGADINTRDKNGRTALMIACEAGSLNMVEVFLRKgADVSLVDvFGQNALHYSKISENTGI-Q 234
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIvK 78

                          90
                  ....*....|....
gi 2024434941 235 NLLSSKIsqDVDAK 248
Cdd:pfam12796  79 LLLEKGA--DINVK 90
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 31-237 1.29e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 81.26  E-value: 1.29e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  31 DPEKVASLLGKKGASATKQDSEGKTAFHLAATKGHAECLRIMVTHGADVTAQDGAGHSALHLAVKNSHIDCIKRLLQYKC 110
Cdd:PHA02876  156 DELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRS 235

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 111 -----------------------------SVYSTDNSGKTALHYAATCGCL-QAVQLLCEHKCPINMKDLDGNIPLLLAV 160
Cdd:PHA02876  236 ninkndlsllkairnedletslllydagfSVNSIDDCKNTPLHHASQAPSLsRLVPKLLERGADVNAKNIKGETPLYLMA 315

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 161 QNGH-TEVCKYLLDHGADINTRDKNGRTALMiacEAGSL----NMVEVFLRKGADVSLVDVFGQNALHYSKISENTGIQN 235
Cdd:PHA02876  316 KNGYdTENIRTLIMLGADVNAADRLYITPLH---QASTLdrnkDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIIN 392


                  ..
gi 2024434941 236 LL 237
Cdd:PHA02876  393 TL 394
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 3-250 2.58e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 79.24  E-value: 2.58e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941   3 SLKAKFRKSDTNEWNKNDDR----LLQAVENGDPeKVASLLGKKGASATKQDSEGKTAFHLAATKGHAECLRIMVTHGAD 78
Cdd:PHA02874   15 EAIEKIIKNKGNCINISVDEtttpLIDAIRSGDA-KIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVD 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  79 VTAqdgaghsalhLAVKNSHIDCIKRLLQYKCSVYSTDNSGKTALHYAATCGCLQAVQLLCEHKCPINMKDLDGNIPLLL 158
Cdd:PHA02874   94 TSI----------LPIPCIEKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHI 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 159 AVQNGHTEVCKYLLDHGADINTRDKNGRTALMIACEAGSLNMVEVFLRKGADVSLVDVFGQNALHYSKISENTGIQNLLS 238
Cdd:PHA02874  164 AIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRSAIELLIN 243

                         250
                  ....*....|....
gi 2024434941 239 SKI--SQDVDAKSP 250
Cdd:PHA02874  244 NASinDQDIDGSTP 257
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 43-192 8.79e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 77.70  E-value: 8.79e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  43 GASATKQDSEGKTAFHLAATKGHAECLRIMVTHGADVTAQDGAGHSALHLAVKNSHIDCIKRLLQYKCSVYSTDNSGKTA 122
Cdd:PHA02874  114 GIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESP 193

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 123 LHYAATCGCLQAVQLLCEH------KC-------------------------PINMKDLDGNIPLLLAVQNG-HTEVCKY 170
Cdd:PHA02874  194 LHNAAEYGDYACIKLLIDHgnhimnKCkngftplhnaiihnrsaiellinnaSINDQDIDGSTPLHHAINPPcDIDIIDI 273

                         170       180
                  ....*....|....*....|..
gi 2024434941 171 LLDHGADINTRDKNGRTALMIA 192
Cdd:PHA02874  274 LLYHKADISIKDNKGENPIDTA 295
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 496-871 4.10e-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: 73.94  E-value: 4.10e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  496 EEVEMLRQELRRALEESERQKEKVRELQKKFEEREQnvtsklsveeceelknsycsvidninQEKALLIERYKEGQEEIK 575
Cdd:TIGR02168  189 DRLEDILNELERQLKSLERQAEKAERYKELKAELRE--------------------------LELALLVLRLEELREELE 242

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  576 RLQDKLTNQTHLESSAESGemKDAMHRMIDELNRQLSELSQLYKEAQAELEDYRKRktlddiavdyIPRDEHEKlmQVTN 655
Cdd:TIGR02168  243 ELQEELKEAEEELEELTAE--LQELEEKLEELRLEVSELEEEIEELQKELYALANE----------ISRLEQQK--QILR 308

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  656 SLKYKAENELLEMKSQYTKVLDEAEELKQMLDTQKQNslpIAEHQQVMNALRSTVKEMEEEINELKELLTNKESEVRNLQ 735
Cdd:TIGR02168  309 ERLANLERQLEELEAQLEELESKLDELAEELAELEEK---LEELKEELESLEAELEELEAELEELESRLEELEEQLETLR 385

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  736 KELLEEKAAINEAMVPRAAYEKLQSSLEGEVSILSSKLKDVIKEKENVSLDvmQLRSEVLHLKEEKEGMHNLLEAKEREV 815
Cdd:TIGR02168  386 SKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELK--ELQAELEELEEELEELQEELERLEEAL 463

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2024434941  816 SGLHQKYHQAQEDLLEMKRYSESSSKLEEDKDKKINEMSKEVSKLKEALNSLSQLS 871
Cdd:TIGR02168  464 EELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLS 519
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
375-870 1.31e-12

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 72.02  E-value: 1.31e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 375 QELKSTLNATQSQEKLTSPSEIKIKYLQEDSKDAQRKLENSETKRKHLEAQVQsRVPEadlnntdisengsdpslkIQET 454
Cdd:PRK03918  231 KELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVK-ELKE------------------LKEK 291

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 455 QSKYEEAAKEvlnaqkqvkpglvsseSEETCSELSKLKVTCEEVEMLRQELRRALEESERQKEKVRELQKKFEEREQNV- 533
Cdd:PRK03918  292 AEEYIKLSEF----------------YEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLe 355

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 534 ----------TSKLSVEECEELKNSY-CSVIDNINQEKALLIERYKEGQEEIKRLQDKLTNqthLESsaESGEMKDAMHR 602
Cdd:PRK03918  356 eleerhelyeEAKAKKEELERLKKRLtGLTPEKLEKELEELEKAKEEIEEEISKITARIGE---LKK--EIKELKKAIEE 430

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 603 M----------------------IDELNRQLSELSQLYKEAQAELEDYRKRKTLDDIAVDYIPR-----DEHEKLMQVTN 655
Cdd:PRK03918  431 LkkakgkcpvcgrelteehrkelLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESEliklkELAEQLKELEE 510

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 656 SLKYKAENELLEMKSQYTKVLDEAEELKQMLDTQKQNSLPIAEHQQVMNALRSTVKEMEEEINEL-KELLTNKESEVRNL 734
Cdd:PRK03918  511 KLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELlKELEELGFESVEEL 590

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 735 QKELLEEKAAINEAMVPRAAYEKLQSSLEgEVSILSSKLKDVIKEKENVSLDVMQLRSEVLHLK-----EEKEGMHNLLE 809
Cdd:PRK03918  591 EERLKELEPFYNEYLELKDAEKELEREEK-ELKKLEEELDKAFEELAETEKRLEELRKELEELEkkyseEEYEELREEYL 669

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024434941 810 AKEREVSGLHQKYHQAQEDLLEMKRYSEsssKLEEDKdKKINEMSKEVSKLKEALNSLSQL 870
Cdd:PRK03918  670 ELSRELAGLRAELEELEKRREEIKKTLE---KLKEEL-EEREKAKKELEKLEKALERVEEL 726
Ank_4 pfam13637
Ankyrin repeats (many copies);
155-205 3.08e-12

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 61.91  E-value: 3.08e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2024434941 155 PLLLAVQNGHTEVCKYLLDHGADINTRDKNGRTALMIACEAGSLNMVEVFL 205
Cdd:pfam13637   4 ALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 9-258 7.64e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 69.32  E-value: 7.64e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941   9 RKSDTNEWN-KNDDRLLQAVENG-DPEKVASLLgKKGASATKQDSEGKTAFHLAAT-KGHAECLRIMVTHGADVTAQDGA 85
Cdd:PHA02876  296 RGADVNAKNiKGETPLYLMAKNGyDTENIRTLI-MLGADVNAADRLYITPLHQASTlDRNKDIVITLLELGANVNARDYC 374

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  86 GHSALHLAVKNSHIDCIKRLLQYKCSVYSTDNSGKTALHYAaTCGC--LQAVQLLCEHKCPINMKDLDGNIPLLLAVQNG 163
Cdd:PHA02876  375 DKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFA-LCGTnpYMSVKTLIDRGANVNSKNKDLSTPLHYACKKN 453

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 164 -HTEVCKYLLDHGADINTRDKNGRTALMIACEAGSLnmVEVFLRKGADVS----LVDVFGQNALHYSKISENTGIQNLLS 238
Cdd:PHA02876  454 cKLDVIEMLLDNGADVNAINIQNQYPLLIALEYHGI--VNILLHYGAELRdsrvLHKSLNDNMFSFRYIIAHICIQDFIR 531

                         250       260
                  ....*....|....*....|..
gi 2024434941 239 SKISQDVDA--KSPTKVKQLSD 258
Cdd:PHA02876  532 HDIRNEVNPlkRVPTRFTSLRE 553
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 34-192 8.38e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 68.75  E-value: 8.38e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  34 KVASLLGKKGASATKQD-SEGKTAFHLAATKGHAECLRIMVTHGADVTAQDGAGHSALHLAVKNSHIDCIKRLLQYKCSV 112
Cdd:PHA02878  148 EITKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGAST 227

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 113 YSTDNSGKTALHYA-ATCGCLQAVQLLCEHKCPINMKD-LDGNIPLLLAVQNghTEVCKYLLDHGADINTRDKNGRTALM 190
Cdd:PHA02878  228 DARDKCGNTPLHISvGYCKDYDILKLLLEHGVDVNAKSyILGLTALHSSIKS--ERKLKLLLEYGADINSLNSYKLTPLS 305


                  ..
gi 2024434941 191 IA 192
Cdd:PHA02878  306 SA 307
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 496-833 9.85e-12

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 69.20  E-value: 9.85e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 496 EEVEMLRQELRRALEESERQKE---KVRELQKKFEEREQNVTSKlsveeceelknsycsVIDNINQEKALLIERYKEGQE 572
Cdd:COG1196   189 ERLEDILGELERQLEPLERQAEkaeRYRELKEELKELEAELLLL---------------KLRELEAELEELEAELEELEA 253

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 573 EIKRLQdklTNQTHLESSAESGEMKdamhrmIDELNRQLSELSQLYKEAQAELEDYRKRKTLDDIAVdyipRDEHEKLMQ 652
Cdd:COG1196   254 ELEELE---AELAELEAELEELRLE------LEELELELEEAQAEEYELLAELARLEQDIARLEERR----RELEERLEE 320

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 653 VTNSLKyKAENELLEMKSQYTKVLDEAEELKQMLDTQKQNslpIAEHQQVMNALRSTVKEMEEEINELKELLTNKESEVR 732
Cdd:COG1196   321 LEEELA-ELEEELEELEEELEELEEELEEAEEELEEAEAE---LAEAEEALLEAEAELAEAEEELEELAEELLEALRAAA 396

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 733 NLQKELLEEKAAINEAmvpraayEKLQSSLEGEVSILSSKLKDVIKEKENVSLDVMQLRSEVLHLKEEKEGMHNLLEAKE 812
Cdd:COG1196   397 ELAAQLEELEEAEEAL-------LERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELL 469

                         330       340
                  ....*....|....*....|.
gi 2024434941 813 REVSGLHQKYHQAQEDLLEMK 833
Cdd:COG1196   470 EEAALLEAALAELLEELAEAA 490
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
396-861 1.60e-11

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 68.55  E-value: 1.60e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 396 IKIKYLQEDSKDAQRKLENSETKRKHLEAQVQSRVPEADLNNTDISEngsdPSLKIQETQSKYEEAAK--EVLNAQKQVK 473
Cdd:PRK03918  296 IKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEE----LKKKLKELEKRLEELEErhELYEEAKAKK 371

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 474 PGLVSSESEETCSELSKLKVTCEEVEMLRQELRRALEESerqKEKVRELQKKFEEREQNVTS-------------KLSVE 540
Cdd:PRK03918  372 EELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKI---TARIGELKKEIKELKKAIEElkkakgkcpvcgrELTEE 448

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 541 ECEELKNSYCSVIDNINQEKALLIERYKEGQEEIKRLQDKLTNQTHLESsaesgemkdaMHRMIDELNRQLSELSQLYKE 620
Cdd:PRK03918  449 HRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIK----------LKELAEQLKELEEKLKKYNLE 518

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 621 -AQAELEDYRK-RKTLDDIAVDYIPRDEHEKLMQVTNSLKYKAENELLEMKSQYTKVLDEAEELKqmldtqkqnslpiae 698
Cdd:PRK03918  519 eLEKKAEEYEKlKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELG--------------- 583

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 699 hqqvmnalRSTVKEMEEEINELKEL------LTNKESEVRNLQKELLEEKAAINEAMVPRAAYEKLQSSLEGEVSILSSK 772
Cdd:PRK03918  584 --------FESVEELEERLKELEPFyneyleLKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKK 655

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 773 LKDviKEKENVSLDVMQLRSEVLHLKEEKEGMHNLLEAKEREVSGLhqkyhqaQEDLLEMKRYSESSSKLEEDKDkKINE 852
Cdd:PRK03918  656 YSE--EEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKL-------KEELEEREKAKKELEKLEKALE-RVEE 725


                  ....*....
gi 2024434941 853 MSKEVSKLK 861
Cdd:PRK03918  726 LREKVKKYK 734
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
423-907 3.99e-11

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 67.01  E-value: 3.99e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 423 EAQVQSRVPEADLNNTDISENGSDPSLKIQETQSKYEEAAKEVLNAQKqvkpglVSSESEETCSELSKLKVTCEEVEMLR 502
Cdd:PRK03918  188 TENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEE------LKEEIEELEKELESLEGSKRKLEEKI 261

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 503 QELRRALEESerqKEKVRELQKKFEEREQNVTSKLSVEECEELKNSYCSVIDNINQEKALLIERYKEGQEEIKRLQDKlt 582
Cdd:PRK03918  262 RELEERIEEL---KKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEK-- 336

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 583 nqthlesSAESGEMKDAMHRMIDELNRqLSELSQLYKEA---QAELEDYRKRKTLDDIavdyiprDEHEKLMQVTNSLKY 659
Cdd:PRK03918  337 -------EERLEELKKKLKELEKRLEE-LEERHELYEEAkakKEELERLKKRLTGLTP-------EKLEKELEELEKAKE 401

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 660 KAENELLEMKSQYTKVLDEAEELKQMLDTQKQNSL-------PIAEHQQ--VMNALRSTVKEMEEEINELKELLTNKESE 730
Cdd:PRK03918  402 EIEEEISKITARIGELKKEIKELKKAIEELKKAKGkcpvcgrELTEEHRkeLLEEYTAELKRIEKELKEIEEKERKLRKE 481

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 731 VRNLQKELLEEKAAINEamvpRAAYEKLQSSLEGEVSILSSKLKDVIKEKENVSLDVMQLRSEVLHLKEEKEGmhnlLEA 810
Cdd:PRK03918  482 LRELEKVLKKESELIKL----KELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEK----LEE 553

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 811 KEREVSGLHQKYHQAQEDLLEMKRysesssKLEEDKDKKINEMSKEVSKLKEALNSLSQLSYSTSAPKRQSQQLEALQQQ 890
Cdd:PRK03918  554 LKKKLAELEKKLDELEEELAELLK------ELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEE 627

                         490
                  ....*....|....*..
gi 2024434941 891 VKQLQNQLTETKKQHQE 907
Cdd:PRK03918  628 LDKAFEELAETEKRLEE 644
Ank_4 pfam13637
Ankyrin repeats (many copies);
121-172 4.95e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 58.83  E-value: 4.95e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2024434941 121 TALHYAATCGCLQAVQLLCEHKCPINMKDLDGNIPLLLAVQNGHTEVCKYLL 172
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 450-747 1.40e-10

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 65.46  E-value: 1.40e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  450 KIQETQSKYEEAAKEVLNAQKQVKpglvsSESEETCSELSKLKVTCEEVEMLRQELRRALEESERQKEKVRELQKKFEER 529
Cdd:TIGR02168  692 KIAELEKALAELRKELEELEEELE-----QLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEEL 766

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  530 EQNVT-SKLSVEECEELKNSYCSVIDNINQEKALLIERYKEGQEEIKRLQDKLTNQTHLESSAEsgEMKDAMHRMIDELN 608
Cdd:TIGR02168  767 EERLEeAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLE--RRIAATERRLEDLE 844

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  609 RQLSELSQLYKEAQAELEDYRK--RKTLDDIAVDYIPRDEHEKLMQVTNSLKYKAENELLEMKSQYTKVLDEAEELKQML 686
Cdd:TIGR02168  845 EQIEELSEDIESLAAEIEELEEliEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKL 924

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024434941  687 dtqkqnslpiAEHQQVMNALRSTVKEMEEEINEL--------KELLTNKESEVRNLQKELLEEKAAINE 747
Cdd:TIGR02168  925 ----------AQLELRLEGLEVRIDNLQERLSEEysltleeaEALENKIEDDEEEARRRLKRLENKIKE 983
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 502-860 1.73e-10

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 65.08  E-value: 1.73e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  502 RQELRRALEESERQKEKVRELQKKFEEREQnvtsklSVEECEELKNSYCSVIDNINQEKALLIERYKEGQEEIKRLQDKL 581
Cdd:TIGR02168  676 RREIEELEEKIEELEEKIAELEKALAELRK------ELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERI 749

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  582 TNQTHLESSAEsgEMKDAMHRMIDELNRQLSELSQLYKEAQAELEDYRKRKTLDDIAVDyIPRDEHEKLMQVTNSLKYKA 661
Cdd:TIGR02168  750 AQLSKELTELE--AEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALD-ELRAELTLLNEEAANLRERL 826

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  662 ENELLEMKSQYTKVLDEAEELKQMLDTQKQNSLPIAEHQQVMNALRSTVKE-------MEEEINELKELLTNKESEVRNL 734
Cdd:TIGR02168  827 ESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEAllnerasLEEALALLRSELEELSEELREL 906

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  735 QKELLEEKAAINEAMVPRAAYEKLQSSLEGEVSILSSKL--------KDVIKEKENVSLDVMQLRSEVLHLKEEKEGMHN 806
Cdd:TIGR02168  907 ESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLseeysltlEEAEALENKIEDDEEEARRRLKRLENKIKELGP 986

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2024434941  807 L-LEAKE--REVSGLHQKYHQAQEDLLEMKRysesssKLEEdkdkKINEMSKEVSKL 860
Cdd:TIGR02168  987 VnLAAIEeyEELKERYDFLTAQKEDLTEAKE------TLEE----AIEEIDREARER 1033
Ank_4 pfam13637
Ankyrin repeats (many copies);
86-138 2.93e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 56.51  E-value: 2.93e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2024434941  86 GHSALHLAVKNSHIDCIKRLLQYKCSVYSTDNSGKTALHYAATCGCLQAVQLL 138
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 553-867 4.36e-10

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 63.92  E-value: 4.36e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  553 IDNINQEKALLIERYKEGQEEIKRLQDKLTNQThlessaesgEMKDAMHRMIDELNRQLSELSQLYKEAQAELEDYRKRK 632
Cdd:TIGR02168  679 IEELEEKIEELEEKIAELEKALAELRKELEELE---------EELEQLRKELEELSRQISALRKDLARLEAEVEQLEERI 749

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  633 TLDDIAVdyiprdeheklmqvtnslkykaeNELLEMKSQYTKVLDEA-EELKQMLDTQKQNSLPIAEHQQVMNALRSTVK 711
Cdd:TIGR02168  750 AQLSKEL-----------------------TELEAEIEELEERLEEAeEELAEAEAEIEELEAQIEQLKEELKALREALD 806

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  712 EMEEEINELKELLTNKESEVRNLQK----------ELLEEKAAINEAMvprAAYEKLQSSLEGEVSILSSKLKDVIKEKE 781
Cdd:TIGR02168  807 ELRAELTLLNEEAANLRERLESLERriaaterrleDLEEQIEELSEDI---ESLAAEIEELEELIEELESELEALLNERA 883

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  782 NVSLDVMQLRSEVLHLKEEKEGMHNLLEAKEREVSGLHQKYHQAQEDLLEMK------------RYS---ESSSKLEEDK 846
Cdd:TIGR02168  884 SLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEvridnlqerlseEYSltlEEAEALENKI 963

                          330       340
                   ....*....|....*....|.
gi 2024434941  847 DKKINEMSKEVSKLKEALNSL 867
Cdd:TIGR02168  964 EDDEEEARRRLKRLENKIKEL 984
Ank_5 pfam13857
Ankyrin repeats (many copies);
171-224 4.84e-10

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 55.82  E-value: 4.84e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2024434941 171 LLDHG-ADINTRDKNGRTALMIACEAGSLNMVEVFLRKGADVSLVDVFGQNALHY 224
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDL 55
Ank_4 pfam13637
Ankyrin repeats (many copies);
55-106 1.14e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 54.97  E-value: 1.14e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2024434941  55 TAFHLAATKGHAECLRIMVTHGADVTAQDGAGHSALHLAVKNSHIDCIKRLL 106
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 19-191 7.71e-09

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: 59.26  E-value: 7.71e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  19 NDDRLLQAVENGDPEKVASLLGKKGASATKQDSEGKTAFHLAATKGH-------AECLRIMVTHgaDVTAQDGAGHSALH 91
Cdd:cd22192    17 SESPLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNleaavvlMEAAPELVNE--PMTSDLYQGETALH 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  92 LAVKNSHIDCIKRLLQYKCSVYSTDNSGkTALHYAATCgclqavqlLC---EHkcpinmkdldgniPLLLAVQNGHTEVC 168
Cdd:cd22192    95 IAVVNQNLNLVRELIARGADVVSPRATG-TFFRPGPKN--------LIyygEH-------------PLSFAACVGNEEIV 152

                         170       180
                  ....*....|....*....|...
gi 2024434941 169 KYLLDHGADINTRDKNGRTALMI 191
Cdd:cd22192   153 RLLIEHGADIRAQDSLGNTVLHI 175
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 655-909 8.95e-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: 59.69  E-value: 8.95e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  655 NSLKYKAE--NELLEMKSQYTKV-----LDEAEELKQMLDTQKQNslpIAEHQQVMNALRSTVKEMEEEINELKELLTNK 727
Cdd:TIGR02168  203 KSLERQAEkaERYKELKAELRELelallVLRLEELREELEELQEE---LKEAEEELEELTAELQELEEKLEELRLEVSEL 279

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  728 ESEVRNLQKELLEEKAAINEAMVPRAAYEKLQSSLEGEVSILSSKLKDVIKEKENVSLDVMQLRSEVLHLKEEKEGMHNL 807
Cdd:TIGR02168  280 EEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAE 359

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  808 LEAKEREVSGLHQKYHQAQEDLLEMKRYSESSSKLEEDKDKKINEMSKEVSKLKEALNSLSQlSYSTSAPKRQSQQLEAL 887
Cdd:TIGR02168  360 LEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQ-EIEELLKKLEEAELKEL 438

                          250       260
                   ....*....|....*....|..
gi 2024434941  888 QQQVKQLQNQLTETKKQHQETV 909
Cdd:TIGR02168  439 QAELEELEEELEELQEELERLE 460
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 498-850 1.21e-08

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 59.31  E-value: 1.21e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  498 VEMLRQELRRaLEESERQKEKVRELQKKFEEREQNVTSKlSVEECEELKNSYCSVIDNINQEKALLIERYKEGQEEIKRL 577
Cdd:TIGR02169  193 IDEKRQQLER-LRREREKAERYQALLKEKREYEGYELLK-EKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEI 270

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  578 QDKLtNQTHLESSAESGEMKDAMHRMIDELNRQLSELSQLYKEAQAELEDYRKRKTLDDIAVDYIpRDEHEKLmqvtnsl 657
Cdd:TIGR02169  271 EQLL-EELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKL-LAEIEEL------- 341

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  658 kykaENELLEMKSQYTKVLDEAEELKQMLDTQKQNslpIAEHQQVMNALRSTVKEMEEEINELKELLTNKESEVRNLQKE 737
Cdd:TIGR02169  342 ----EREIEEERKRRDKLTEEYAELKEELEDLRAE---LEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEE 414

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  738 LLEEKAAINEAmvpRAAYEklqsSLEGEVSILSSKLKDVIKEKENVSLDVMQLRSEVLHLKEEKEGMHNLLEAKEREVSG 817
Cdd:TIGR02169  415 LQRLSEELADL---NAAIA----GIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSK 487

                          330       340       350
                   ....*....|....*....|....*....|...
gi 2024434941  818 LHQKYHQAQEDLLEMKRYSESSSKLEEDKDKKI 850
Cdd:TIGR02169  488 LQRELAEAEAQARASEERVRGGRAVEEVLKASI 520
PTZ00121 PTZ00121
MAEBL; Provisional
 374-864 1.28e-08

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 59.38  E-value: 1.28e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  374 AQELKSTLNATQSQEKLTSPSEIKIKYLQEDSKDAQRKLENSETKRKHLEAQVQSRvpEADLNNTDISENGSDPSLKIQE 453
Cdd:PTZ00121  1311 AEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKA--EAAEKKKEEAKKKADAAKKKAE 1388

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  454 TQSKYEEAAKEvlnAQKQVKPGLVSSESEETCSELSKLKVTCEEVEMlRQELRRALEEserqKEKVRELQKKFEEREQNV 533
Cdd:PTZ00121  1389 EKKKADEAKKK---AEEDKKKADELKKAAAAKKKADEAKKKAEEKKK-ADEAKKKAEE----AKKADEAKKKAEEAKKAE 1460

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  534 TSKLSVEE---CEELKNsycsvidniNQEKALLIERYKEGQEEIKRLQDKLTNQTHLESSAEsgEMKDAMHRMIDELNRQ 610
Cdd:PTZ00121  1461 EAKKKAEEakkADEAKK---------KAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKAD--EAKKAEEAKKADEAKK 1529

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  611 LSELSQLYKEAQAEledyRKRKTlddiavdyiprDEHEKLMQVTNSLKYKAENELLEMKSQYTKVLDEAEELKQMLDTQK 690
Cdd:PTZ00121  1530 AEEAKKADEAKKAE----EKKKA-----------DELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARI 1594

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  691 QNSLPIAEHQQVMNALR-----------STVKEMEEEINELKELLTNKESEVR---NLQKEllEEKAAINEAMVPRAAYE 756
Cdd:PTZ00121  1595 EEVMKLYEEEKKMKAEEakkaeeakikaEELKKAEEEKKKVEQLKKKEAEEKKkaeELKKA--EEENKIKAAEEAKKAEE 1672

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  757 KLQSSLEGEVSILSSKLK-DVIKEKENVSLDVMQLRSEVlhlKEEKEGMHNLLEAKEREVSGLHQKYHQAQEDllemKRY 835
Cdd:PTZ00121  1673 DKKKAEEAKKAEEDEKKAaEALKKEAEEAKKAEELKKKE---AEEKKKAEELKKAEEENKIKAEEAKKEAEED----KKK 1745

                          490       500
                   ....*....|....*....|....*....
gi 2024434941  836 SESSSKLEEDKdKKINEMSKEVSKLKEAL 864
Cdd:PTZ00121  1746 AEEAKKDEEEK-KKIAHLKKEEEKKAEEI 1773
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 102-290 1.42e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 58.76  E-value: 1.42e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 102 IKRLLQYKCSVYSTDNSGKTALHYAATcgclqavqllcehkcpinMKDLDGNIPLLLAVQ------NGHTEVCKYLLDHG 175
Cdd:PTZ00322   44 IARIDTHLEALEATENKDATPDHNLTT------------------EEVIDPVVAHMLTVElcqlaaSGDAVGARILLTGG 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 176 ADINTRDKNGRTALMIACEAGSLNMVEVFLRKGADVSLVDVFGQNALHYSKISENTGIQNLLSSKISQDVDAKSPTKVKQ 255
Cdd:PTZ00322  106 ADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFELGANAKPDS 185

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2024434941 256 LSDLSSPRSSTSTPMTgkgqaffadqQEDFSSLLQ 290
Cdd:PTZ00322  186 FTGKPPSLEDSPISSH----------HPDFSAVPQ 210
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 88-223 1.85e-08

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: 58.10  E-value: 1.85e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  88 SALHLAVKNSHIDCIKRLLQYK-CSVYSTDNSGKTALHYAATCGCLQAVQLLCEhKCP--INM---KDL-DGNIPLLLAV 160
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLLKCPsCDLFQRGALGETALHVAALYDNLEAAVVLME-AAPelVNEpmtSDLyQGETALHIAV 97

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024434941 161 QNGHTEVCKYLLDHGADINT----------RDKN----GRTALMIACEAGSLNMVEVFLRKGADVSLVDVFGQNALH 223
Cdd:cd22192    98 VNQNLNLVRELIARGADVVSpratgtffrpGPKNliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLH 174
Ank_5 pfam13857
Ankyrin repeats (many copies);
72-126 3.16e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 50.81  E-value: 3.16e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2024434941  72 MVTHG-ADVTAQDGAGHSALHLAVKNSHIDCIKRLLQYKCSVYSTDNSGKTALHYA 126
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_5 pfam13857
Ankyrin repeats (many copies);
105-159 3.66e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 50.42  E-value: 3.66e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2024434941 105 LLQYK-CSVYSTDNSGKTALHYAATCGCLQAVQLLCEHKCPINMKDLDGNIPLLLA 159
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 60-250 4.43e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 56.54  E-value: 4.43e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  60 AATKGHAECLRIMVTHGADVTAQDGAGHSALHLAVKNSHIDCIKRLLQYKCSVYSTDNSGKTALHYAATCGCLQAVQLLC 139
Cdd:PHA02875    9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELL 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 140 EHKCPINmkDL---DGNIPLLLAVQNGHTEVCKYLLDHGADINTRDKNGRTALMIACEAGSLNMVEVFLRKGADVSLVDV 216
Cdd:PHA02875   89 DLGKFAD--DVfykDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDC 166

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2024434941 217 FGQNALHYSKISENTGI-QNLLSSKISQDVDAKSP 250
Cdd:PHA02875  167 CGCTPLIIAMAKGDIAIcKMLLDSGANIDYFGKNG 201
PTZ00121 PTZ00121
MAEBL; Provisional
 374-907 6.16e-08

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 57.07  E-value: 6.16e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  374 AQELKSTLNATQSQEKLTSPSEIKIKYLQEDSKDAQR--KLENSETKRKHLEAQVQSRVPEADLNNTDisENGSDPSLKI 451
Cdd:PTZ00121  1208 AEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKaeEERNNEEIRKFEEARMAHFARRQAAIKAE--EARKADELKK 1285

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  452 QETQSKYEEAAKevlnaQKQVKPGLVSSESEETCSELSKLKVTCEEVEMLRQELRRALEESERQKEKVRELQKKFEEREQ 531
Cdd:PTZ00121  1286 AEEKKKADEAKK-----AEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAE 1360

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  532 NVTSKlsvEECEELKNSYCSVIDNINQEKALLIERYKEGQ---EEIKRLQDKLTNQTHLESSAESGEMKDAMHRMIDELN 608
Cdd:PTZ00121  1361 AAEEK---AEAAEKKKEEAKKKADAAKKKAEEKKKADEAKkkaEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAK 1437

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  609 RQLSElSQLYKEAQAELEDYRKRKTLDDIAVDYIPRDEHEKLMQ---VTNSLKYKAEN-----ELLEMKSQYTKVLDE-- 678
Cdd:PTZ00121  1438 KKAEE-AKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEeakKADEAKKKAEEakkkaDEAKKAAEAKKKADEak 1516

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  679 -------AEELKQMLDTQKQNSLPIAEHQQVMNALRST--VKEMEE--EINELKELLTNKESEVRNLQKELLEEKAAINE 747
Cdd:PTZ00121  1517 kaeeakkADEAKKAEEAKKADEAKKAEEKKKADELKKAeeLKKAEEkkKAEEAKKAEEDKNMALRKAEEAKKAEEARIEE 1596

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  748 AMVPRAAYEKLQSSLEGEVSILSSKLKDVIKEKEnVSLDVMQLRSEVlhlKEEKEGMHNLLEAKEREVSGLHQKYHQAQE 827
Cdd:PTZ00121  1597 VMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEE-EKKKVEQLKKKE---AEEKKKAEELKKAEEENKIKAAEEAKKAEE 1672

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  828 DllemKRYSESSSKLEEDKDKKINEMSKEVSKLKEAlnslSQLSYSTSAPKRQSQQL----EALQQQVKQLQNQLTETKK 903
Cdd:PTZ00121  1673 D----KKKAEEAKKAEEDEKKAAEALKKEAEEAKKA----EELKKKEAEEKKKAEELkkaeEENKIKAEEAKKEAEEDKK 1744


                   ....
gi 2024434941  904 QHQE 907
Cdd:PTZ00121  1745 KAEE 1748
PHA02798 PHA02798
ankyrin-like protein; Provisional
 35-255 6.49e-08

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 56.38  E-value: 6.49e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  35 VASLLGKKGASATKQDSEGKTAFHLAATKGH---AECLRIMVTHGADVTAQDGAGHSALHLAVKNSH---IDCIKRLLQY 108
Cdd:PHA02798   91 IVKILIENGADINKKNSDGETPLYCLLSNGYinnLEILLFMIENGADTTLLDKDGFTMLQVYLQSNHhidIEIIKLLLEK 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 109 KCSVYSTDNS-GKTALH----YAATCGCLQAVQLLCEHKCPINMKD-------LDGNIPLLLAVQNGHTEVCKYLLDHgA 176
Cdd:PHA02798  171 GVDINTHNNKeKYDTLHcyfkYNIDRIDADILKLFVDNGFIINKENkshkkkfMEYLNSLLYDNKRFKKNILDFIFSY-I 249

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 177 DINTRDKNGRTALMIACEAGSLNMVEVFLRKGADVSLVDVFGQNALHYSKISENTGIQN-LLSSKISQDVDAKSPTKVKQ 255
Cdd:PHA02798  250 DINQVDELGFNPLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCLFTAFENESKFIFNsILNKKPNKNTISYTYYKLRK 329
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
602-826 7.88e-08

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 56.18  E-value: 7.88e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 602 RMIDELNRQLSELSQLYKEAQAELEDYRKRKTLDDIAvdyiprDEHEKLMQVTNSLkykaENELLEMKSQYTKVLDEAEE 681
Cdd:COG3206   175 KALEFLEEQLPELRKELEEAEAALEEFRQKNGLVDLS------EEAKLLLQQLSEL----ESQLAEARAELAEAEARLAA 244

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 682 LKQMLDtQKQNSLPIAEHQQVMNALRSTVKEMEEEINELKELLTNKESEVRNLQKELLEEKAAINEAMvpraayEKLQSS 761
Cdd:COG3206   245 LRAQLG-SGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEA------QRILAS 317

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024434941 762 LEGEVSILSSKLKDVIKEKEnvsldvmQLRSEVLHLKEEKEGMHNL---LEAKEREVSGLHQKYHQAQ 826
Cdd:COG3206   318 LEAELEALQAREASLQAQLA-------QLEARLAELPELEAELRRLereVEVARELYESLLQRLEEAR 378
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 52-220 1.01e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 55.38  E-value: 1.01e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  52 EGKTAFHLAATKGHAECLRIMVTHGADVTAQDGAGHSALHLAVKNSHIDCIKRLL---QYKCSVYSTDnsGKTALHYAAT 128
Cdd:PHA02875   34 DGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLdlgKFADDVFYKD--GMTPLHLATI 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 129 CGCLQAVQLLCEHKCPINMKDLDGNIPLLLAVQNGHTEVCKYLLDHGADINTRDKNGRTALMIACEAGSLNMVEVFLRKG 208
Cdd:PHA02875  112 LKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSG 191

                         170
                  ....*....|..
gi 2024434941 209 ADvslVDVFGQN 220
Cdd:PHA02875  192 AN---IDYFGKN 200
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 604-907 1.40e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 55.71  E-value: 1.40e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 604 IDELNRQLSELS------QLYKEAQAELEDYRKRKTLddiavdyiprdeheklmqvtnsLKYKAENELLEmksQYTKVLD 677
Cdd:COG1196   195 LGELERQLEPLErqaekaERYRELKEELKELEAELLL----------------------LKLRELEAELE---ELEAELE 249

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 678 EAEELKQMLDTQkqnslpIAEHQQVMNALRSTVKEMEEEINELKELLTNKESEVRNLQKELLEEKAAINEAMVPRAAYEK 757
Cdd:COG1196   250 ELEAELEELEAE------LAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEE 323

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 758 LQSSLEGEVSILSSKLKDVIKEKENVSLDVMQLRSEVLHLKEEKEGMHNLLEAKEREVSGLHQKYHQAQEDLLEMKRYSE 837
Cdd:COG1196   324 ELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLE 403

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 838 SSSKLEEDKDKKINEMSKEVSKLKEALNSLSQLSYSTSAPKRQSQQLEALQQQVKQLQNQLTETKKQHQE 907
Cdd:COG1196   404 ELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAA 473
Ank_5 pfam13857
Ankyrin repeats (many copies);
145-192 1.43e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 48.88  E-value: 1.43e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2024434941 145 INMKDLDGNIPLLLAVQNGHTEVCKYLLDHGADINTRDKNGRTALMIA 192
Cdd:pfam13857   9 LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_5 pfam13857
Ankyrin repeats (many copies);
38-93 3.07e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 48.11  E-value: 3.07e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2024434941  38 LLGKKGASATKQDSEGKTAFHLAATKGHAECLRIMVTHGADVTAQDGAGHSALHLA 93
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 151-183 4.09e-07

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 46.90  E-value: 4.09e-07
                          10        20        30
                  ....*....|....*....|....*....|....
gi 2024434941 151 DGNIPLLLAV-QNGHTEVCKYLLDHGADINTRDK 183
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 314-867 4.42e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 54.17  E-value: 4.42e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 314 EQQDLLMLMQAKIASLTLHNKELQDKLQERTPKEVDSTIDSYHSTQREfDQTADRQSEISAQELKSTLNATQSQEKLTSP 393
Cdd:COG1196   217 ELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAE-LEAELEELRLELEELELELEEAQAEEYELLA 295

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 394 SEIK----IKYLQEDSKDAQRKLENSETKRKHLEAQVQSRVPEADLNNTDISENGSdpslKIQETQSKYEEAAKEVLNAQ 469
Cdd:COG1196   296 ELARleqdIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEE----ELEEAEAELAEAEEALLEAE 371

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 470 KQVKPglVSSESEETCSELSKLKVTCEEVEMLRQELRRALEESERQKEKVRELQKKFEEREQNVTSKLSVEECEELKNSy 549
Cdd:COG1196   372 AELAE--AEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAA- 448

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 550 cSVIDNINQEKALLIERYKEGQEEIKRLQDKLTNQTHLESSAESgemkdaMHRMIDELNRQLSELSQLYKEAQAELEDYR 629
Cdd:COG1196   449 -EEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAA------RLLLLLEAEADYEGFLEGVKAALLLAGLRG 521

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 630 KRKTLDDIAVD-----------------YIPRDEHEKLMQVTNSLK----YKAENELLEMKSQYTKVLDEAEELKQMLDT 688
Cdd:COG1196   522 LAGAVAVLIGVeaayeaaleaalaaalqNIVVEDDEVAAAAIEYLKaakaGRATFLPLDKIRARAALAAALARGAIGAAV 601

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 689 QKQNSLPIAEHQQVMNALRSTVKEMEEEINELKELLTNKESEVRNLQKELLEEKAAINEAMVpRAAYEKLQSSLEGEVSI 768
Cdd:COG1196   602 DLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLT-GGSRRELLAALLEAEAE 680

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 769 LSSKLKDVIKEKENVSLDVMQLRSEVLHLKEEKEGMHNLLEAKEREVSGLHQKYHQAQEDLLEMKRYSESSSKLEEDKDK 848
Cdd:COG1196   681 LEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPP 760

                         570
                  ....*....|....*....
gi 2024434941 849 KINEMSKEVSKLKEALNSL 867
Cdd:COG1196   761 DLEELERELERLEREIEAL 779
PHA02798 PHA02798
ankyrin-like protein; Provisional
 132-234 4.53e-07

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 53.69  E-value: 4.53e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 132 LQAVQLLCEHKCPINMKDLDGNIPLLLAVQN-----GHTEVCKYLLDHGADINTRDKNGRTALMIACEAGSLNMVEVFL- 205
Cdd:PHA02798   51 TDIVKLFINLGANVNGLDNEYSTPLCTILSNikdykHMLDIVKILIENGADINKKNSDGETPLYCLLSNGYINNLEILLf 130

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2024434941 206 --RKGADVSLVDVFGQNALH-YSKISENTGIQ 234
Cdd:PHA02798  131 miENGADTTLLDKDGFTMLQvYLQSNHHIDIE 162
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 58-141 6.90e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 53.36  E-value: 6.90e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  58 HLAATkGHAECLRIMVTHGADVTAQDGAGHSALHLAVKNSHIDCIKRLLQYKCSVYSTDNSGKTALHYAATCGCLQAVQL 137
Cdd:PTZ00322   88 QLAAS-GDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166


                  ....
gi 2024434941 138 LCEH 141
Cdd:PTZ00322  167 LSRH 170
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 1-120 7.20e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 52.98  E-value: 7.20e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941   1 MKSLKAKFRKSDTNEWNKNDD-------------RLLQAVENGDPEKVASLLgKKGASATKQDSEGKTAFHLAATKGHAE 67
Cdd:PTZ00322   51 LEALEATENKDATPDHNLTTEevidpvvahmltvELCQLAASGDAVGARILL-TGGADPNCRDYDGRTPLHIACANGHVQ 129

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2024434941  68 CLRIMVTHGADVTAQDGAGHSALHLAVKNSHIDCIKRLLQYKCSVYSTDNSGK 120
Cdd:PTZ00322  130 VVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFELGANAK 182
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 57-225 8.59e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 52.57  E-value: 8.59e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  57 FHLAATKGHAECLRIMVTHGADVTAQDGAGHSALHLAVKNSHIDCIKRLLQY--KCSVYSTDNSGKTALHY--------- 125
Cdd:PHA02878   41 LHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSinKCSVFYTLVAIKDAFNNrnveifkii 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 126 ------------------AATCGCLQA--VQLLCEHKCPINMKDLD-GNIPLLLAVQNGHTEVCKYLLDHGADINTRDKN 184
Cdd:PHA02878  121 ltnrykniqtidlvyidkKSKDDIIEAeiTKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKT 200

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2024434941 185 GRTALMIACEAGSLNMVEVFLRKGADVSLVDVFGQNALHYS 225
Cdd:PHA02878  201 NNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHIS 241
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 334-870 9.94e-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: 52.75  E-value: 9.94e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  334 KELQDKLQErtpKEVDSTIDSYHSTQREFDQTADRQSEISAQELKSTLNATQSQEKLTSpSEIKIKYLQEDSKDAQRKLE 413
Cdd:TIGR02168  216 KELKAELRE---LELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEE-LRLEVSELEEEIEELQKELY 291

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  414 NSETKRKHLEAQVQSRVPEADLNNTDISEngsdPSLKIQETQSKYEEAAKEV--LNAQKQVKPGLVSSESEETCSELSKL 491
Cdd:TIGR02168  292 ALANEISRLEQQKQILRERLANLERQLEE----LEAQLEELESKLDELAEELaeLEEKLEELKEELESLEAELEELEAEL 367

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  492 KV---TCEEVEMLRQELRRALEESERQKE----KVRELQKKFE------EREQNVTSKLSVEECEELKNSYCSVIDNINQ 558
Cdd:TIGR02168  368 EElesRLEELEEQLETLRSKVAQLELQIAslnnEIERLEARLErledrrERLQQEIEELLKKLEEAELKELQAELEELEE 447

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  559 EKALLIERYKEGQEEIKRLQDKLTNQTHLESSAESGE-----MKDAMHRMIDEL------------NRQ--------LSE 613
Cdd:TIGR02168  448 ELEELQEELERLEEALEELREELEEAEQALDAAERELaqlqaRLDSLERLQENLegfsegvkallkNQSglsgilgvLSE 527

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  614 L--------------------------SQLYKEAQAELEDYRKRKT----LDDIAVDYIPRDEHEKLMQVTNSLKYKaeN 663
Cdd:TIGR02168  528 LisvdegyeaaieaalggrlqavvvenLNAAKKAIAFLKQNELGRVtflpLDSIKGTEIQGNDREILKNIEGFLGVA--K 605

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  664 ELLEMKSQYTKVLDE-------AEELKQMLDTQKQNSLP----------------------------------IAEHQQV 702
Cdd:TIGR02168  606 DLVKFDPKLRKALSYllggvlvVDDLDNALELAKKLRPGyrivtldgdlvrpggvitggsaktnssilerrreIEELEEK 685

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  703 MNALRSTVKEMEEEINELKELLTNKESEVRNLQKELLEEKAAINEAMVPRAAYEKLQSSLEGEVSILSSKLKDVIKEKEN 782
Cdd:TIGR02168  686 IEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEE 765

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  783 VSLDVMQLRSEVLHLKEEKEGMHNL--------------LEAKEREVSGLHQKYHQAQEDLLEMKRYSESSSKLEEDKDK 848
Cdd:TIGR02168  766 LEERLEEAEEELAEAEAEIEELEAQieqlkeelkalreaLDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEE 845

                          650       660
                   ....*....|....*....|..
gi 2024434941  849 KINEMSKEVSKLKEALNSLSQL 870
Cdd:TIGR02168  846 QIEELSEDIESLAAEIEELEEL 867
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 151-179 1.41e-06

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: 45.27  E-value: 1.41e-06
                           10        20
                   ....*....|....*....|....*....
gi 2024434941  151 DGNIPLLLAVQNGHTEVCKYLLDHGADIN 179
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
Ank_2 pfam12796
Ankyrin repeats (3 copies);
189-251 2.95e-06

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 46.26  E-value: 2.95e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024434941 189 LMIACEAGSLNMVEVFLRKGADVSLVDVFGQNALHYSKISENTGIQNLLSSKISQDVDAKSPT 251
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNGRT 63
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
504-751 3.88e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 51.07  E-value: 3.88e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  504 ELRRALEESERQKEKVRELQKKFEEREQNVTSKLSVEECEELKNSYcsvidNINQEKALLIERYKEGQEEIKRLQDKLtn 583
Cdd:COG4913    239 RAHEALEDAREQIELLEPIRELAERYAAARERLAELEYLRAALRLW-----FAQRRLELLEAELEELRAELARLEAEL-- 311

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  584 qthlessAESGEMKDAMHRMIDELNRQLSELS-QLYKEAQAELEdyRKRKTLDDIavdyipRDEHEKLMQVTNSLKYKAE 662
Cdd:COG4913    312 -------ERLEARLDALREELDELEAQIRGNGgDRLEQLEREIE--RLERELEER------ERRRARLEALLAALGLPLP 376

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  663 NELLEMKSQYTKVLDEAEELKQMLDTQKQNslpIAEHQQVMNALRSTVKEMEEEINELKELLTNKESEVRNLqKELLEEK 742
Cdd:COG4913    377 ASAEEFAALRAEAAALLEALEEELEALEEA---LAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLAL-RDALAEA 452


                   ....*....
gi 2024434941  743 AAINEAMVP 751
Cdd:COG4913    453 LGLDEAELP 461
PRK01156 PRK01156
chromosome segregation protein; Provisional
 543-866 3.98e-06

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 51.06  E-value: 3.98e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 543 EELKnSYCSVIDNINQEKALLIERYKEGQEEIKRLQDKLTNqthleSSAESGEMKDAMHRMidelnrqlSELSQLYKEAQ 622
Cdd:PRK01156  190 EKLK-SSNLELENIKKQIADDEKSHSITLKEIERLSIEYNN-----AMDDYNNLKSALNEL--------SSLEDMKNRYE 255

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 623 AELEDYRKRKTLDDIAVDYIPRDEhEKLMQVTNSLKYKAENELLEmksqYTKVLDEAEELKQML---DTQKQNSLPIAEH 699
Cdd:PRK01156  256 SEIKTAESDLSMELEKNNYYKELE-ERHMKIINDPVYKNRNYIND----YFKYKNDIENKKQILsniDAEINKYHAIIKK 330

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 700 QQVMNALRSTVKEMEEEINELKELLTNKESEVRNLQKELLEekaaINEAMVPRAAYEKLQSSLEGEVS----ILSSKLKD 775
Cdd:PRK01156  331 LSVLQKDYNDYIKKKSRYDDLNNQILELEGYEMDYNSYLKS----IESLKKKIEEYSKNIERMSAFISeilkIQEIDPDA 406

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 776 VIKEKENVSLDVMQLRSEVLHLKEEKEGMHNLLEAKEREVSGL--HQKYHQAQEDLLE------MKRYSESSSKLEEDKD 847
Cdd:PRK01156  407 IKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLngQSVCPVCGTTLGEeksnhiINHYNEKKSRLEEKIR 486

                         330       340
                  ....*....|....*....|....*
gi 2024434941 848 ------KKINEMSKEVSKLKEALNS 866
Cdd:PRK01156  487 eieievKDIDEKIVDLKKRKEYLES 511
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
375-748 5.88e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 50.15  E-value: 5.88e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 375 QELKSTLNATQSQEKLTSPSEIKIKYLQEDSKDAQRKLENSETKRKHLEAQVQSRVPEADLNNTDISENGSDPSLK---- 450
Cdd:COG4717    74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEelee 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 451 ----IQETQSKYEEAAKEVLNAQKQvkpgLVSSESEETCSELSKLKVTCEEVEMLRQELRRALEESERQKEKVRELQKKF 526
Cdd:COG4717   154 rleeLRELEEELEELEAELAELQEE----LEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEEL 229

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 527 EEREQNVTSKLSVEECEELKNSYCS-----VIDNINQEKALLIERYKE---------GQEEIKRLQDKLTNQTHLESSAE 592
Cdd:COG4717   230 EQLENELEAAALEERLKEARLLLLIaaallALLGLGGSLLSLILTIAGvlflvlgllALLFLLLAREKASLGKEAEELQA 309

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 593 SGEMKDAMHRMIDELNRQLS-ELSQLYKEAQAELEDYRKRKTLDDIAVDYIPRDEHEKLMQVTNSL--KYKAENE----- 664
Cdd:COG4717   310 LPALEELEEEELEELLAALGlPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALlaEAGVEDEeelra 389

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 665 LLEMKSQYTKVLDEAEELKQMLDTQKQNSLPIAEHQqvmnalrsTVKEMEEEINELKELLTNKESEVRNLQKELLEEKAA 744
Cdd:COG4717   390 ALEQAEEYQELKEELEELEEQLEELLGELEELLEAL--------DEEELEEELEELEEELEELEEELEELREELAELEAE 461


                  ....
gi 2024434941 745 INEA 748
Cdd:COG4717   462 LEQL 465
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 11-174 7.05e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 49.49  E-value: 7.05e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  11 SDTNEWNKNDDR--LLQAVENGDpEKVASLLGKKGASATKQDSEGKTAFHLAATKGHAECLRIMVTHGADVTAQDGAGHS 88
Cdd:PHA02878  158 ADINMKDRHKGNtaLHYATENKD-QRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNT 236

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  89 ALHLAVKN-SHIDCIKRLLQYKCSVYSTDN-SGKTALHYAATCGclQAVQLLCEHKCPINMKDLDGNIPLLLAV-QNGHT 165
Cdd:PHA02878  237 PLHISVGYcKDYDILKLLLEHGVDVNAKSYiLGLTALHSSIKSE--RKLKLLLEYGADINSLNSYKLTPLSSAVkQYLCI 314


                  ....*....
gi 2024434941 166 EVCKYLLDH 174
Cdd:PHA02878  315 NIGRILISN 323
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 275-821 9.58e-06

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 49.73  E-value: 9.58e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  275 QAFFADQQEDFSSLLQDNKDRL----SDSTAGADSLLDVSSETEQQDLLMLMQAKIASLTLHNkelQDKLQERTPKEVDS 350
Cdd:pfam15921  248 EALKSESQNKIELLLQQHQDRIeqliSEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARN---QNSMYMRQLSDLES 324

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  351 TIDSYHSTQREfdqtADRQSEISAQELKSTLNATQSQekLTSPSEIKIKYLQEDSK--DAQRKLENSETKRKH---LEAQ 425
Cdd:pfam15921  325 TVSQLRSELRE----AKRMYEDKIEELEKQLVLANSE--LTEARTERDQFSQESGNldDQLQKLLADLHKREKelsLEKE 398

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  426 VQSRVPEADLNNTdISENGSDPSLKIQETQSKYEEAAKEVLNAQKQVKPGLVSSESEETCSELSKLKVTCEEVEMLRQEL 505
Cdd:pfam15921  399 QNKRLWDRDTGNS-ITIDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEML 477

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  506 RRALEESERQKEKVRELQKKFEEreqnVTSKLSVEEceelknsycSVIDNINQEKALLIERYKEGQEEIKRLQDKLTNQT 585
Cdd:pfam15921  478 RKVVEELTAKKMTLESSERTVSD----LTASLQEKE---------RAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLR 544

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  586 HLESSAESGEMKDA-MHRMIDELNRQLSELSQLY------------KEAQAELEDYRKRKTLDDIAVDYIPRDEHEKLMQ 652
Cdd:pfam15921  545 NVQTECEALKLQMAeKDKVIEILRQQIENMTQLVgqhgrtagamqvEKAQLEKEINDRRLELQEFKILKDKKDAKIRELE 624

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  653 VTNSLKYKAENELLEMKSQYTK-VLDEAEELKQMLDTQKQ-----NSLPiAEHQQVMNALRSTVKEMEEEINELKELLTN 726
Cdd:pfam15921  625 ARVSDLELEKVKLVNAGSERLRaVKDIKQERDQLLNEVKTsrnelNSLS-EDYEVLKRNFRNKSEEMETTTNKLKMQLKS 703

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  727 KESEVRNLQKELLEEKAAINEAMVPRAAYEKLQSSLEGEVSILSSKLK-------DVIKEKENVSLDVMQLRSEVLHLKE 799
Cdd:pfam15921  704 AQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQfleeamtNANKEKHFLKEEKNKLSQELSTVAT 783

                          570       580
                   ....*....|....*....|..
gi 2024434941  800 EKEGMHNLLEAKEREVSGLHQK 821
Cdd:pfam15921  784 EKNKMAGELEVLRSQERRLKEK 805
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 660-870 1.16e-05

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 48.61  E-value: 1.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 660 KAENELLEMKSQYTKVLDEAEELKQMLDTQKQNslpIAEHQQVMNALRSTVKEMEEEINELKELLTNKESEVRNLQKELL 739
Cdd:COG4942    24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQ---LAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 740 EEKAAINEAMvpRAAYeKLQSSLEGEVSILSSKLKDVIKEKENVSLDVMQLRSEVLHLKEEKEGMHNLLEAKEREVSGLH 819
Cdd:COG4942   101 AQKEELAELL--RALY-RLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2024434941 820 QKYHQAQEDLLEMKRYSESSSKLEEDKDKKINEMSKEVSKLKEALNSLSQL 870
Cdd:COG4942   178 ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEAL 228
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
560-763 1.60e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 48.61  E-value: 1.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 560 KALLIERYKEGQEEIKRLQDKLT--NQTHLESSAESGEMKDAMHRMIDELNRQLSELSQLYKEAQAELEDYRKRKTLDDI 637
Cdd:COG4717    44 RAMLLERLEKEADELFKPQGRKPelNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEK 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 638 AVDYIPRDEHEKlmqvtnslkyKAENELLEMKSQYTKVLDEAEELKQMLDTQKQNSLPIAEHQQVMN-ALRSTVKEMEEE 716
Cdd:COG4717   124 LLQLLPLYQELE----------ALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEeLLEQLSLATEEE 193

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2024434941 717 INELKELLTNKESEVRNLQKELLEEKAAINEAMVPRAAYEKLQSSLE 763
Cdd:COG4717   194 LQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAA 240
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 45-191 1.62e-05

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: 48.72  E-value: 1.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  45 SATKQDSEGKTAFHLAATKGHAECLR-IMVTHGAD-------------VTAQDGAGHSALHLAVKNSHIDCIKRLLQYKC 110
Cdd:cd21882    18 SAYQRGATGKTCLHKAALNLNDGVNEaIMLLLEAApdsgnpkelvnapCTDEFYQGQTALHIAIENRNLNLVRLLVENGA 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 111 SVYstdnsgktalhyAATCGclqavQLLCEHKCPINMKdldGNIPLLLAVQNGHTEVCKYLLDHGADI---NTRDKNGRT 187
Cdd:cd21882    98 DVS------------ARATG-----RFFRKSPGNLFYF---GELPLSLAACTNQEEIVRLLLENGAQPaalEAQDSLGNT 157


                  ....
gi 2024434941 188 ALMI 191
Cdd:cd21882   158 VLHA 161
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 375-800 1.97e-05

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: 48.48  E-value: 1.97e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 375 QELKSTLNATQSQEKLTSPSEIKIKylqEDSKDAQRKLENSETKRKHLEAQVQSRVPE-ADLNNTDISENGSDPSLKIQE 453
Cdd:TIGR04523 242 NEKTTEISNTQTQLNQLKDEQNKIK---KQLSEKQKELEQNNKKIKELEKQLNQLKSEiSDLNNQKEQDWNKELKSELKN 318

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 454 TQSKYEEAAKEVLNAQKQVkpglvssesEETCSELSKLKVTCEEVEMLRQELRRALEESERQKEKV-RELQKKFEEREQN 532
Cdd:TIGR04523 319 QEKKLEEIQNQISQNNKII---------SQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLkKENQSYKQEIKNL 389

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 533 VTSKLSVE----ECEELKNSYCSVIDNINQEKALLIERYKEGQEEIKRLQDKLTNQTHLESSAESgeMKDAMHRMIDELN 608
Cdd:TIGR04523 390 ESQINDLEskiqNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKEL--IIKNLDNTRESLE 467

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 609 RQLSELSQLYKEAQAELEDY-----RKRKTLDDIAVDYIPRDEHEKLMQVTNSLKYKAENELLEMKSQYTKVLDEAEELK 683
Cdd:TIGR04523 468 TQLKVLSRSINKIKQNLEQKqkelkSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDEL 547

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 684 QMLDTQKQNSLpiaehqqvmnaLRSTVKEMEEEINELKELLTNKESEVRNLQKELLEEKAAINEAMVPRAAYEKLQSSLE 763
Cdd:TIGR04523 548 NKDDFELKKEN-----------LEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLE 616

                         410       420       430
                  ....*....|....*....|....*....|....*..
gi 2024434941 764 GEVSILSSKLKDVIKEKENVSLDVMQLRSEVLHLKEE 800
Cdd:TIGR04523 617 KELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKET 653
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 553-772 2.07e-05

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 47.84  E-value: 2.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 553 IDNINQEKALLIERYKEGQEEIKRLQDKLTNQTHLESSAESGemkdamhrmIDELNRQLSELSQLYKEAQAELEdyRKRK 632
Cdd:COG4942    36 IAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQE---------LAALEAELAELEKEIAELRAELE--AQKE 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 633 TLDDIAVDYIPRDEHEKLMQVTNSLKYKAENELLEMKSQYTKVL-DEAEELKQMLDTQKQNSLPIAEHQQvmnALRSTVK 711
Cdd:COG4942   105 ELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARrEQAEELRADLAELAALRAELEAERA---ELEALLA 181

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024434941 712 EMEEEINELKELLTNKESEVRNLQKELLEEKAAINEAMVPRAAYEKLQSSLEGEVSILSSK 772
Cdd:COG4942   182 ELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 52-81 2.27e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 41.80  E-value: 2.27e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 2024434941   52 EGKTAFHLAATKGHAECLRIMVTHGADVTA 81
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 359-721 3.33e-05

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: 47.76  E-value: 3.33e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  359 QREFDQTADRQSEISaQELKSTLNATQSQEKLTSPSEIKIKYLQEDSKDAQRKLENSETKRKHLEAQVQSRVPEADLNNT 438
Cdd:TIGR02169  687 KRELSSLQSELRRIE-NRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEA 765

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  439 DISEngsdpslkIQETQSKYEEAAKEVlnaqkqvkpglvssESEETCSELSKLKVTCEEVEMLRQELRRALEESErQKEK 518
Cdd:TIGR02169  766 RIEE--------LEEDLHKLEEALNDL--------------EARLSHSRIPEIQAELSKLEEEVSRIEARLREIE-QKLN 822

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  519 VRELQKKFEEREQNvTSKLSVEECEELKNSYCSVIDNINQEKALLIERYKEGQEEIKRLQDKLtnqTHLESSAESGEMK- 597
Cdd:TIGR02169  823 RLTLEKEYLEKEIQ-ELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRL---GDLKKERDELEAQl 898

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  598 DAMHRMIDELNRQLSELSQLYKEAQAELEDYRKR-KTLDDIAVDYIPRDEHEKLMQVTNSLKYKAENELLEMKSQYTKVL 676
Cdd:TIGR02169  899 RELERKIEELEAQIEKKRKRLSELKAKLEALEEElSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEPVNMLAI 978

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*
gi 2024434941  677 DEAEELKQMLDTQKqnslpiaEHQQVMNALRSTVKEMEEEINELK 721
Cdd:TIGR02169  979 QEYEEVLKRLDELK-------EKRAKLEEERKAILERIEEYEKKK 1016
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 276-863 3.60e-05

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


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 47.66  E-value: 3.60e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  276 AFFADQQEDFSSLLQDNKDRLSDSTAGAdslldvSSETEQQDLLMLMQAKIASLTLHNKELQDKLQERTpKEVDSTIDSY 355
Cdd:pfam02463  359 EELEKLQEKLEQLEEELLAKKKLESERL------SSAAKLKEEELELKSEEEKEAQLLLELARQLEDLL-KEEKKEELEI 431

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  356 HSTQREFDQTADRQSEISAQELKSTLNATQSQEKLTSPSEIKIKYLQEDSKDAQRKLENSETKRKHLEAQVQSRVPEADL 435
Cdd:pfam02463  432 LEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKV 511

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  436 NNTDISENGSDPSLKIQETQSKYEEAAKEVLNAQKQVKPGLVSSESEETCSELSKLKVTCEEVEMLRQ-----ELRRALE 510
Cdd:pfam02463  512 LLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKlrlliPKLKLPL 591

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  511 ESERQKEKVRELQK-KFEEREQNVTSKLSVEECEELKNSYCSVIDNINQEKALLIERYKEGQEEIKRLQDKLTNQTHLES 589
Cdd:pfam02463  592 KSIAVLEIDPILNLaQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSEL 671

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  590 SAESGEM--KDAMHRMIDELNRQLSELSQLYKEAQAELEDYRKRKTLDDIAVDYIPRDEHEKLMQVTNSLKYKAENELLE 667
Cdd:pfam02463  672 TKELLEIqeLQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEE 751

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  668 MKSQYTKVLDEAEELKQMLDTQKQNSLPIAEHQQVMNA--LRSTVKEMEEEINELKELLTNKESEVRNLQKELLEEKAAI 745
Cdd:pfam02463  752 EEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEeeKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIK 831

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  746 NEAMVPRAAYEKLQSSLEGEVSILSSKLKDVIKEKENVSLdvmQLRSEVLHLKEEKEGMHNLLEAKEREVSGLHQKYHQA 825
Cdd:pfam02463  832 EEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQE---LLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQK 908

                          570       580       590
                   ....*....|....*....|....*....|....*...
gi 2024434941  826 QEDLLEMKRYSESSSKLEEDKDKKINEMSKEVSKLKEA 863
Cdd:pfam02463  909 LNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEAD 946
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 563-869 3.74e-05

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: 47.76  E-value: 3.74e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  563 LIERYKEGQEEIKRLQDKLtnqthlessaesGEMKDAMHRMIDELNRQ---LSELSQLYKEAQAELEDYRKRKTLDDiav 639
Cdd:TIGR02169  665 GILFSRSEPAELQRLRERL------------EGLKRELSSLQSELRRIenrLDELSQELSDASRKIGEIEKEIEQLE--- 729

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  640 dyiprDEHEKLmqvtnslkykaenellemksqytkvldeAEELKQMLDTQKQNSLPIAEHQQVMNALRSTVKEMEEEINE 719
Cdd:TIGR02169  730 -----QEEEKL----------------------------KERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHK 776

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  720 LKELLTNKE-----SEVRNLQKELLEEKAAINEAMVPRAAYEKLQSSLEGEVSILSSKLKDVIKEKENVSLDVMQLRSEV 794
Cdd:TIGR02169  777 LEEALNDLEarlshSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEI 856

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024434941  795 LHLKEEKEGMHNLLEAKEREVSGLHQKYHQAQEDLLEMKRYSESSSKLEEDKDKKINEMSKEVSKLKEALNSLSQ 869
Cdd:TIGR02169  857 ENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEE 931
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
604-828 4.21e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 47.60  E-value: 4.21e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  604 IDELNRQLSELSQLYKEAQAELEDYRKRktlddiavdyipRDEHEKLMQVTNSLK--YKAENELLEMKSQYTKVL---DE 678
Cdd:COG4913    619 LAELEEELAEAEERLEALEAELDALQER------------REALQRLAEYSWDEIdvASAEREIAELEAELERLDassDD 686

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  679 AEELKQMLDTQKQNslpIAEHQQVMNALRSTVKEMEEEINELKELLTNKESEVRNLQK-------ELLEEK-AAINEAMV 750
Cdd:COG4913    687 LAALEEQLEELEAE---LEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDlarlelrALLEERfAAALGDAV 763

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  751 PRAAYEKLQSSLEGEVSILSSKLKDVIK-----------EKENVSLDVM----------QLRSEVLHLKEEKegMHNLL- 808
Cdd:COG4913    764 ERELRENLEERIDALRARLNRAEEELERamrafnrewpaETADLDADLEslpeylalldRLEEDGLPEYEER--FKELLn 841

                          250       260
                   ....*....|....*....|
gi 2024434941  809 EAKEREVSGLHQKYHQAQED 828
Cdd:COG4913    842 ENSIEFVADLLSKLRRAIRE 861
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
602-871 5.82e-05

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 46.96  E-value: 5.82e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 602 RMIDELnrqlselSQLYKeaqaeLEDYRKRKTLDDIAVDYIPRDEHEKLMQVTNSLKYKAENELLEMKSQYTKVLDEAEE 681
Cdd:PRK02224  153 DMIDDL-------LQLGK-----LEEYRERASDARLGVERVLSDQRGSLDQLKAQIEEKEEKDLHERLNGLESELAELDE 220

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 682 LKQMLDTQKQN--------SLPIAEHQQVmnalRSTVKEMEEEINELKELLTNKESEVRNL------QKELLEEKAAINE 747
Cdd:PRK02224  221 EIERYEEQREQaretrdeaDEVLEEHEER----REELETLEAEIEDLRETIAETEREREELaeevrdLRERLEELEEERD 296

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 748 AMVPRAAYEklqsslEGEVSILSSKLKDVIKEKENVSLDVMQLRSEVLHLKEEKEGMHNLLEAKEREVSGLHQKYHQAQE 827
Cdd:PRK02224  297 DLLAEAGLD------DADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELES 370

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 2024434941 828 DLLEMKRYSESSSKLEEDKDKKINEMSKEVSKLKEALNSLSQLS 871
Cdd:PRK02224  371 ELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFL 414
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 21-189 5.91e-05

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely related to TRPV1, sharing high sequence identity (>50%), but TRPV2 shows a higher temperature threshold and sensitivity for activation than TRPV1. TRPV2 can be stimulated by ligands or lipids, and is involved in osmosensation and mechanosensation. TRPV2 is expressed in both neuronal and non-neuronal tissues, and it has been implicated in diverse physiological and pathophysiological processes, including cardiac-structure maintenance, innate immunity, and cancer. TRPV2 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 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.


Pssm-ID: 411981 [Multi-domain]  Cd Length: 640  Bit Score: 46.77  E-value: 5.91e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  21 DRLLQAVENGDPEKVASLLG-------KKGASATKQDSEGKTAFHLAA---TKGHAECLRIMVTHGAD-------VTAQD 83
Cdd:cd22197     8 DRLFSVVSRGNPEELAGLLEylrrtskYLTDSEYTEGSTGKTCLMKAVlnlQDGVNACIMPLLEIDKDsgnpkplVNAQC 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  84 G----AGHSALHLAVKNSHIDCIKRLLQYKCSVYstdnsgktalhyAATCG-CLQAVQLLCEHKcpinmkdldGNIPLLL 158
Cdd:cd22197    88 TdeyyRGHSALHIAIEKRSLQCVKLLVENGADVH------------ARACGrFFQKKQGTCFYF---------GELPLSL 146

                         170       180       190
                  ....*....|....*....|....*....|....
gi 2024434941 159 AVQNGHTEVCKYLLDHGAD---INTRDKNGRTAL 189
Cdd:cd22197   147 AACTKQWDVVNYLLENPHQpasLQAQDSLGNTVL 180
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 86-231 6.23e-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: 6.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  86 GHSAL-HLAVKNSHIDCIKRLLQYKCSVYStdnsGKTALHyAATCGCLQAVQLLCEHKCPINMKDLD------------- 151
Cdd:TIGR00870  52 GRSALfVAAIENENLELTELLLNLSCRGAV----GDTLLH-AISLEYVDAVEAILLHLLAAFRKSGPlelandqytseft 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 152 -GNIPLLLAVQNGHTEVCKYLLDHGADINTRDK--------------NGRTALMIACEAGSLNMVEVFLRKGADVSLVDV 216
Cdd:TIGR00870 127 pGITALHLAAHRQNYEIVKLLLERGASVPARACgdffvksqgvdsfyHGESPLNAAACLGSPSIVALLSEDPADILTADS 206

                         170
                  ....*....|....*.
gi 2024434941 217 FGQNALHYSKI-SENT 231
Cdd:TIGR00870 207 LGNTLLHLLVMeNEFK 222
Ank_4 pfam13637
Ankyrin repeats (many copies);
23-73 6.92e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 41.11  E-value: 6.92e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2024434941  23 LLQAVENGDPEKVASLLgKKGASATKQDSEGKTAFHLAATKGHAECLRIMV 73
Cdd:pfam13637   5 LHAAAASGHLELLRLLL-EKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 140-256 7.35e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 46.20  E-value: 7.35e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 140 EHKCPINMKDLDGNIPLLLAVQNGHTEVCKYLLDHGADINTRDKNGRTALM----------------------------- 190
Cdd:PHA03100   23 MEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHylsnikynltdvkeivkllleyganvnap 102

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024434941 191 -----------IACEAGSLNMVEVFLRKGADVSLVDVFGQNALHY--SKISENTGIQNLLSSKISqDVDAKspTKVKQL 256
Cdd:PHA03100  103 dnngitpllyaISKKSNSYSIVEYLLDNGANVNIKNSDGENLLHLylESNKIDLKILKLLIDKGV-DINAK--NRVNYL 178
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 184-215 9.65e-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: 9.65e-05
                          10        20        30
                  ....*....|....*....|....*....|...
gi 2024434941 184 NGRTALMIACE-AGSLNMVEVFLRKGADVSLVD 215
Cdd:pfam00023   1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARD 33
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 367-885 9.77e-05

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 46.50  E-value: 9.77e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  367 DRQSEISAQELKSTLNATQSQEKLTSPSEIKIKYLQEDSKDAQRKLENSETKRKHL-EAQVQSRVPEADLNNTDisengs 445
Cdd:TIGR00618  176 DQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLrEALQQTQQSHAYLTQKR------ 249

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  446 dpslKIQETQSKYEEAAKEVLNAQKQVKPGL-VSSESEETCSELSKLKVTCEEVEMLRQELRRALEESERQKEKVRELQK 524
Cdd:TIGR00618  250 ----EAQEEQLKKQQLLKQLRARIEELRAQEaVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAK 325

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  525 KFEEREQNVTSKLSVEECEELKNSYCSVIDNINQ--EKALLI----ERYKEGQEEIKRLQDKLTNQTHLESSAES-GEMK 597
Cdd:TIGR00618  326 LLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDahEVATSIreisCQQHTLTQHIHTLQQQKTTLTQKLQSLCKeLDIL 405

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  598 DAMHRMIDELNRQLSELSQLYKEAQAELEDYRKRKTLDDIAVDYIPRDE-HEKLMQVTNSLKYKAENELLEMKSQYTKVL 676
Cdd:TIGR00618  406 QREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEkLEKIHLQESAQSLKEREQQLQTKEQIHLQE 485

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  677 DE--AEELKQMLDTQ-------KQNSLPIAEHQQVMN--ALRSTVKEMEEEINELKELLTNKESEVRNLQKELLEEKAAI 745
Cdd:TIGR00618  486 TRkkAVVLARLLELQeepcplcGSCIHPNPARQDIDNpgPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQM 565

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  746 NEAMVPRAAYEKLQSSLEGEVSILSSKLKDVIKEKENVSLDVMQLRSEVLHLKEEKEGMHNLLEA------KEREVSGLH 819
Cdd:TIGR00618  566 QEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVrlhlqqCSQELALKL 645

                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  820 QKYHQAQEDLLEmKRYSESSSKLEEDKDKKI----NEMSKEVSKLKEALNSLSQLSYSTSAPKRQSQQLE 885
Cdd:TIGR00618  646 TALHALQLTLTQ-ERVREHALSIRVLPKELLasrqLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIE 714
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 75-239 1.02e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 46.21  E-value: 1.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  75 HGADVTAQDGAGHSALHLAVKNSHIDCIKRLLQYKC-SVYSTDNSGKTALHYAATCGCLQAVQLLCEHKCPINMkdldgN 153
Cdd:PHA02876   30 HGANQCENESIPFTAIHQALQLRQIDIVEEIIQQNPeLIYITDHKCHSTLHTICIIPNVMDIVISLTLDCDIIL-----D 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 154 IPLLLAVQNGHT--EVCKYLLDH---GADINTRDKNGRTALMIA----CEAGSLNMVEVFLRKGADVSLVDVFGQNALHY 224
Cdd:PHA02876  105 IKYASIILNKHKldEACIHILKEaisGNDIHYDKINESIEYMKLikerIQQDELLIAEMLLEGGADVNAKDIYCITPIHY 184

                         170
                  ....*....|....*
gi 2024434941 225 SKISENTGIQNLLSS 239
Cdd:PHA02876  185 AAERGNAKMVNLLLS 199
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 184-211 1.04e-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: 40.26  E-value: 1.04e-04
                           10        20
                   ....*....|....*....|....*...
gi 2024434941  184 NGRTALMIACEAGSLNMVEVFLRKGADV 211
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 52-83 1.09e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 39.97  E-value: 1.09e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 2024434941  52 EGKTAFHLAATK-GHAECLRIMVTHGADVTAQD 83
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 278-583 1.09e-04

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: 46.20  E-value: 1.09e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  278 FADQQEDFSSL---LQDNKDRLSDSTAGADSLLDVSSETEQQDLLMLMQAKIASLTLHNKELQDKLQERTPKEVDSTIDS 354
Cdd:TIGR02168  686 IEELEEKIAELekaLAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEE 765

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  355 YHStQREFDQTADRQSEISAQELKSTLNATQSQ-----EKLTSPSEIkIKYLQEDSKDAQRKLENSETKRKHLEAQVQSR 429
Cdd:TIGR02168  766 LEE-RLEEAEEELAEAEAEIEELEAQIEQLKEElkalrEALDELRAE-LTLLNEEAANLRERLESLERRIAATERRLEDL 843

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  430 VPEADLNNTDISENgSDPSLKIQETQSKYEEAAKEVLNAQKQVKPGLvssesEETCSELSKLKVTCEEVEMLRQELRRAL 509
Cdd:TIGR02168  844 EEQIEELSEDIESL-AAEIEELEELIEELESELEALLNERASLEEAL-----ALLRSELEELSEELRELESKRSELRREL 917

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024434941  510 EESERQKEKVRELQKKFEEREQNVTSKLSVEECEELknsycsviDNINQEKALLIERYKEGQEEIKRLQDKLTN 583
Cdd:TIGR02168  918 EELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTL--------EEAEALENKIEDDEEEARRRLKRLENKIKE 983
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 184-212 1.17e-04

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 39.93  E-value: 1.17e-04
                          10        20
                  ....*....|....*....|....*....
gi 2024434941 184 NGRTALMIACEAGSLNMVEVFLRKGADVS 212
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADIN 29
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 369-870 1.49e-04

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


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 45.87  E-value: 1.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 369 QSEISAQELKSTLNATQSQEK---------LTSPSEIKIKYLQEDSKDAQRKLENSETKRKHLEAQvqsrvpeadLNNTD 439
Cdd:pfam05483 232 KKEINDKEKQVSLLLIQITEKenkmkdltfLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKE---------LEDIK 302

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 440 ISENGSDPSLKIQETQSKYEEAAKEVLNAQKQVKPGLVSSESEETCSELSKLKVT-CEEVEMLRQELRRALEESERQKEK 518
Cdd:pfam05483 303 MSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATtCSLEELLRTEQQRLEKNEDQLKII 382

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 519 VRELQKKFEEreqnvtsklsVEECEELKNSycsvidninqeKALLIERYKEGQEEIKRLQDKltnqthlessaesgemKD 598
Cdd:pfam05483 383 TMELQKKSSE----------LEEMTKFKNN-----------KEVELEELKKILAEDEKLLDE----------------KK 425

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 599 AMHRMIDELNRQLSELSQLYKEAQAELEDYrkrktldDIAVDYIPRDEHEKLMQVTNsLKYKAENELL---EMKSQYTKV 675
Cdd:pfam05483 426 QFEKIAEELKGKEQELIFLLQAREKEIHDL-------EIQLTAIKTSEEHYLKEVED-LKTELEKEKLkniELTAHCDKL 497

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 676 LDEAEELKQmldTQKQNSLPIAEHQQVMNALRSTVKEMEEEINELKELLTNKESEVRNLQKELLEE----KAAINEAMVP 751
Cdd:pfam05483 498 LLENKELTQ---EASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKgdevKCKLDKSEEN 574

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 752 RAAYEKLQSSLEGEVSILSSKLKDVIKEKENVSLDVMQLRSEVLHLKEEKEGMHNLLEAKEREVSGLHQKYHQAQEDLLE 831
Cdd:pfam05483 575 ARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEE 654

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|.
gi 2024434941 832 MkryseSSSKLEEDKDKKINE--MSKEVSKLKEALNSLSQL 870
Cdd:pfam05483 655 I-----IDNYQKEIEDKKISEekLLEEVEKAKAIADEAVKL 690
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 155-180 1.61e-04

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 39.55  E-value: 1.61e-04
                          10        20
                  ....*....|....*....|....*.
gi 2024434941 155 PLLLAVQNGHTEVCKYLLDHGADINT 180
Cdd:pfam13606   5 PLHLAARNGRLEIVKLLLENGADINA 30
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 679-864 1.67e-04

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: 44.15  E-value: 1.67e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 679 AEELKQMLDTQKQNSLpIAEHQQVMNALRSTVKEMEEEINELKELLTNKESEVRNLQKELLEEKAAINEAmvpRAAYEKL 758
Cdd:COG1579     3 PEDLRALLDLQELDSE-LDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEV---EARIKKY 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 759 QSSLEgevSILSSK-LKDVIKEKENVSLDVMQLRSEVLHLKEEkegmhnlLEAKEREVSGLHQKYHQAQEDLLEMK-RYS 836
Cdd:COG1579    79 EEQLG---NVRNNKeYEALQKEIESLKRRISDLEDEILELMER-------IEELEEELAELEAELAELEAELEEKKaELD 148

                         170       180
                  ....*....|....*....|....*...
gi 2024434941 837 ESSSKLEEDKDKKINEMSKEVSKLKEAL 864
Cdd:COG1579   149 EELAELEAELEELEAEREELAAKIPPEL 176
AAA_13 pfam13166
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
 557-747 1.89e-04

AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins. This family includes the PrrC protein that is thought to be the active component of the anticodon nuclease.


Pssm-ID: 463796 [Multi-domain]  Cd Length: 712  Bit Score: 45.44  E-value: 1.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 557 NQEKALLIERYKEGQEEIKRLQDKLTNQthLESSAESGEMKDAMHRMIDELNRQLSELSQLYKEAQAELEDYRKR----K 632
Cdd:pfam13166 278 DDEFTEFQNRLQKLIEKVESAISSLLAQ--LPAVSDLASLLSAFELDVEDIESEAEVLNSQLDGLRRALEAKRKDpfksI 355

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 633 TLDDIAvdyiprdehEKLMQVTNSLKykAENELLEMKSQYTKVLDEA-EELKQML--DTQKQNSLPIAEHQQVMNALRST 709
Cdd:pfam13166 356 ELDSVD---------AKIESINDLVA--SINELIAKHNEITDNFEEEkNKAKKKLrlHLVEEFKSEIDEYKDKYAGLEKA 424

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2024434941 710 VKEMEEEINELKELLTNKESEVRNLQKELLEEKAAINE 747
Cdd:pfam13166 425 INSLEKEIKNLEAEIKKLREEIKELEAQLRDHKPGADE 462
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 499-862 2.62e-04

RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 44.81  E-value: 2.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 499 EMLRQELRRALEESERQKEKVRELQKKFEEREQNvtsklsveeceelknsycsvidnINQEKALLIERykegQEEIKRLQ 578
Cdd:pfam10174 112 ELTEENFRRLQSEHERQAKELFLLRKTLEEMELR-----------------------IETQKQTLGAR----DESIKKLL 164

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 579 DKLTNQTHlesSAESGEMKDAMHRMIDELNRQLSELSQLYKEAQAELEDYRKrktlddiavdyiprDEHEKLMQVTNSLK 658
Cdd:pfam10174 165 EMLQSKGL---PKKSGEEDWERTRRIAEAEMQLGHLEVLLDQKEKENIHLRE--------------ELHRRNQLQPDPAK 227

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 659 YKAENELLEMK----SQYTKVLDEAEELKQMLdtqKQNSLPIAEHQQV----MNALRSTVKEMEEEINELKELLTNKESE 730
Cdd:pfam10174 228 TKALQTVIEMKdtkiSSLERNIRDLEDEVQML---KTNGLLHTEDREEeikqMEVYKSHSKFMKNKIDQLKQELSKKESE 304

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 731 VRNLQKEL-------LEEKAAINEAMVPRAAYEKLQSSLEGEVSILSSKLKDVIKEKENVSLDVMQLRSEVLHLKEEKEG 803
Cdd:pfam10174 305 LLALQTKLetltnqnSDCKQHIEVLKESLTAKEQRAAILQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRD 384

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2024434941 804 MHNLLEAKEREVSGLHQKYHQAQEDLlemkrysessskleEDKDKKINEMSKEVSKLKE 862
Cdd:pfam10174 385 LKDMLDVKERKINVLQKKIENLQEQL--------------RDKDKQLAGLKERVKSLQT 429
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 44-172 2.66e-04

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: 44.87  E-value: 2.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  44 ASATKQDSEGKTAFHLAATKGHAECLRIMVTHGADVTAQ-DGA------------GHSALHLAVKNSHIDCIKRLLQYK- 109
Cdd:cd21882    64 APCTDEFYQGQTALHIAIENRNLNLVRLLVENGADVSARaTGRffrkspgnlfyfGELPLSLAACTNQEEIVRLLLENGa 143

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 110 --CSVYSTDNSGKTALH------------YAATCGCLQAVQLLCEHKCPINMKDL----DGNIPLLLAVQNGHTEVCKYL 171
Cdd:cd21882   144 qpAALEAQDSLGNTVLHalvlqadntpenSAFVCQMYNLLLSYGAHLDPTQQLEEipnhQGLTPLKLAAVEGKIVMFQHI 223


                  .
gi 2024434941 172 L 172
Cdd:cd21882   224 L 224
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
498-732 2.94e-04

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 44.62  E-value: 2.94e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 498 VEMLRQELRRAL----EESERQKEKVRELQKKFEE-REQNVTSKLSVEEceelkNSYCSVIDNINQEKALLIERYKEGQE 572
Cdd:COG3206   166 LELRREEARKALefleEQLPELRKELEEAEAALEEfRQKNGLVDLSEEA-----KLLLQQLSELESQLAEARAELAEAEA 240

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 573 EIKRLQDKLTNQTHLESSAESGEMKDAMHRMIDELNRQLSELSQLY-------KEAQAELEDYRKRktlddiavdyiprd 645
Cdd:COG3206   241 RLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYtpnhpdvIALRAQIAALRAQ-------------- 306

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 646 ehekLMQVTNSLKYKAENELLEMKSQYTKVLDEAEELKQMLDTQKQNSLPIAEHQQVMNALRSTVKEMEEEINELKELLT 725
Cdd:COG3206   307 ----LQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEARLAEA 382


                  ....*..
gi 2024434941 726 NKESEVR 732
Cdd:COG3206   383 LTVGNVR 389
COG5022 COG5022
Myosin heavy chain [General function prediction only];
654-925 3.61e-04

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 44.68  E-value: 3.61e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  654 TNSLKYKAENELLEMKSQYTKVLDEAEELKQMLDTQKQNSLPIAEHQQVMNALRSTV--KEMEEEINELKEllTNKEsev 731
Cdd:COG5022    829 EKKLRETEEVEFSLKAEVLIQKFGRSLKAKKRFSLLKKETIYLQSAQRVELAERQLQelKIDVKSISSLKL--VNLE--- 903

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  732 rnLQKELLEEKAAINEAMVpraayEKLQSSLEgevsiLSSKLKDVIKEKENVSLDVMQLRsevlhlkeekegmhnlleaK 811
Cdd:COG5022    904 --LESEIIELKKSLSSDLI-----ENLEFKTE-----LIARLKKLLNNIDLEEGPSIEYV-------------------K 952

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  812 EREVSGLHQKYHQAQEDLLEMKRYSESSSKLEEDKDKKINEMSKEVSKLKEALNSLSQLSYSTSAPKRQSQQLeALQQQV 891
Cdd:COG5022    953 LPELNKLHEVESKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQYGALQESTKQLKELPVEV-AELQSA 1031

                          250       260       270
                   ....*....|....*....|....*....|....
gi 2024434941  892 KQLQNQLTETKKQHQETVSVYRMHLLYAVQGQMD 925
Cdd:COG5022   1032 SKIISSESTELSILKPLQKLKGLLLLENNQLQAR 1065
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
451-669 4.24e-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: 4.24e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  451 IQETQSKYEEAAKEvLNAQKQVKPGLVSSESEetcselsklkvtcEEVEMLRQELRRALEESERQKEKVRELQKKFEERE 530
Cdd:COG4913    257 IRELAERYAAARER-LAELEYLRAALRLWFAQ-------------RRLELLEAELEELRAELARLEAELERLEARLDALR 322

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  531 qnvtsklsvEECEELKNSYCSV----IDNINQEKALLIERYKEGQEEIKRLQDKLT---------------NQTHLESSA 591
Cdd:COG4913    323 ---------EELDELEAQIRGNggdrLEQLEREIERLERELEERERRRARLEALLAalglplpasaeefaaLRAEAAALL 393

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  592 ES-GEMKDAMHRMIDELNRQLSELSQLYKEAQAELEDYRKRKTLddiavdyIPRDEHEKLMQVTNSLKYKAEN-----EL 665
Cdd:COG4913    394 EAlEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSN-------IPARLLALRDALAEALGLDEAElpfvgEL 466


                   ....
gi 2024434941  666 LEMK 669
Cdd:COG4913    467 IEVR 470
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 23-172 4.52e-04

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely related to TRPV1, sharing high sequence identity (>50%), but TRPV2 shows a higher temperature threshold and sensitivity for activation than TRPV1. TRPV2 can be stimulated by ligands or lipids, and is involved in osmosensation and mechanosensation. TRPV2 is expressed in both neuronal and non-neuronal tissues, and it has been implicated in diverse physiological and pathophysiological processes, including cardiac-structure maintenance, innate immunity, and cancer. TRPV2 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 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.


Pssm-ID: 411981 [Multi-domain]  Cd Length: 640  Bit Score: 44.08  E-value: 4.52e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  23 LLQAVENGDPEKVASllgkkgASATKQDSEGKTAFHLAATKGHAECLRIMVTHGADVTAQDGA-------------GHSA 89
Cdd:cd22197    70 LEIDKDSGNPKPLVN------AQCTDEYYRGHSALHIAIEKRSLQCVKLLVENGADVHARACGrffqkkqgtcfyfGELP 143

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  90 LHLAVKNSHIDCIKRLLQYK---CSVYSTDNSGKTALH------------YAATC----GCLQAVQLLCEHKCPINMKDL 150
Cdd:cd22197   144 LSLAACTKQWDVVNYLLENPhqpASLQAQDSLGNTVLHalvmiadnspenSALVIkmydGLLQAGARLCPTVQLEEISNH 223

                         170       180
                  ....*....|....*....|..
gi 2024434941 151 DGNIPLLLAVQNGHTEVCKYLL 172
Cdd:cd22197   224 EGLTPLKLAAKEGKIEIFRHIL 245
PHA02946 PHA02946
ankyin-like protein; Provisional
 102-230 4.67e-04

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 43.89  E-value: 4.67e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 102 IKRLLQYKCSVYSTDNSGKTALHYAATCGCLQAVQLLCEHKCPINMKDLDGNIPL--LLAVQNGHTEVCKYLLDHGADIN 179
Cdd:PHA02946   55 VEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLyyLSGTDDEVIERINLLVQYGAKIN 134

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2024434941 180 TRDKNGRTALMIACEAGSLNMVEVFLRKGADVSLVDVFGQNALHYSKISEN 230
Cdd:PHA02946  135 NSVDEEGCGPLLACTDPSERVFKKIMSIGFEARIVDKFGKNHIHRHLMSDN 185
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
 504-763 5.30e-04

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 43.76  E-value: 5.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 504 ELRRALEESERQKEKVRELQKKFEEReqnvtsKLSVEECEELK-NSYCSVIDNINQEKALLIERYKEGQEEIKRLQDKlt 582
Cdd:PRK05771   44 RLRKLRSLLTKLSEALDKLRSYLPKL------NPLREEKKKVSvKSLEELIKDVEEELEKIEKEIKELEEEISELENE-- 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 583 nqthlessaesgemkdamhrmIDELNRQLSELSQLyKEAQAELEDYRKRKTLDdIAVDYIPRDEHEKLMQVTNS------ 656
Cdd:PRK05771  116 ---------------------IKELEQEIERLEPW-GNFDLDLSLLLGFKYVS-VFVGTVPEDKLEELKLESDVenveyi 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 657 -------------LKYK--------AENELLEMKSQYTKVLDEA-EELKQMLDTQKqnslpiAEHQQVMNALRSTVKEME 714
Cdd:PRK05771  173 stdkgyvyvvvvvLKELsdeveeelKKLGFERLELEEEGTPSELiREIKEELEEIE------KERESLLEELKELAKKYL 246

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 2024434941 715 EEINELKELLTNKESEVRNLQKELLEEKAAINEAMVPRAAYEKLQSSLE 763
Cdd:PRK05771  247 EELLALYEYLEIELERAEALSKFLKTDKTFAIEGWVPEDRVKKLKELID 295
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 44-172 5.57e-04

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are thermo-sensing channels that function directly in temperature-sensing and nociception; they share substantial structural and functional properties. Transient Receptor Potential (TRP) ion channels activated by temperature (thermo TRPs) are important molecular players in acute, inflammatory, and chronic pain states. So far, 11 TRP channels in mammalian cells have been identified as thermosensitive TRP (thermo-TRP) channels. TRPV1-4 channels are activated by different heat temperatures, for example, TRPV1 and TRPV2 are activated by high temperatures (>43C and >55C, respectively). TRPV1-4 belong 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: 411977 [Multi-domain]  Cd Length: 607  Bit Score: 43.63  E-value: 5.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  44 ASATKQDSEGKTAFHLAATKGHAECLRIMVTHGADVTAQDGA--------------GHSALHLAVKNSHIDCIKRLLQ-- 107
Cdd:cd22193    67 AEYTDEYYEGQTALHIAIERRQGDIVALLVENGADVHAHAKGrffqpkyqgegfyfGELPLSLAACTNQPDIVQYLLEne 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 108 -YKCSVYSTDNSGKTALHYAATCG------------CLQAVQLLCEHKCPI----NMKDLDGNIPLLLAVQNGHTEVCKY 170
Cdd:cd22193   147 hQPADIEAQDSRGNTVLHALVTVAdntkentkfvtrMYDMILIRGAKLCPTveleEIRNNDGLTPLQLAAKMGKIEILKY 226


                  ..
gi 2024434941 171 LL 172
Cdd:cd22193   227 IL 228
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 496-753 5.66e-04

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 43.21  E-value: 5.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 496 EEVEMLRQELRRALEESERQKEKVRELQKKfeerEQNVTSKLsvEECEELKNSYCSVIDNINQEKALLIERYKEGQEEIK 575
Cdd:COG4942    20 DAAAEAEAELEQLQQEIAELEKELAALKKE----EKALLKQL--AALERRIAALARRIRALEQELAALEAELAELEKEIA 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 576 RLQDKLTNQthlesSAESGEMKDAMHRM--------------IDELNRQLSELSQLYKEAQAELEDYrkRKTLDDIAvdy 641
Cdd:COG4942    94 ELRAELEAQ-----KEELAELLRALYRLgrqpplalllspedFLDAVRRLQYLKYLAPARREQAEEL--RADLAELA--- 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 642 iprdeheklmqvtnslkyKAENELLEMKSQYTKVLDEAEELKQMLDTQKQnslpiaEHQQVMNALRSTVKEMEEEINELK 721
Cdd:COG4942   164 ------------------ALRAELEAERAELEALLAELEEERAALEALKA------ERQKLLARLEKELAELAAELAELQ 219

                         250       260       270
                  ....*....|....*....|....*....|..
gi 2024434941 722 ELLTNKESEVRNLQKELLEEKAAINEAMVPRA 753
Cdd:COG4942   220 QEAEELEALIARLEAEAAAAAERTPAAGFAAL 251
PRK11281 PRK11281
mechanosensitive channel MscK;
578-869 5.93e-04

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 43.75  E-value: 5.93e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  578 QDKLTnQTHLESSAESGEMKDAMHRMIDELNRQLSELSQLYKEAQAELEDYrKRKTLDDIAVDYiprdehEKLmqvtnSL 657
Cdd:PRK11281    57 EDKLV-QQDLEQTLALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEAL-KDDNDEETRETL------STL-----SL 123

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  658 KykaenellEMKSQYTKVLDEAEELKQMLDTqkQNSLPIAEHQQ---VMNALRSTVKEMEEEINELKELLTNKESEVRNL 734
Cdd:PRK11281   124 R--------QLESRLAQTLDQLQNAQNDLAE--YNSQLVSLQTQperAQAALYANSQRLQQIRNLLKGGKVGGKALRPSQ 193

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  735 QKELLEEKAAINeamvprAAYEKLQSSLEGevsilSSKLKDVIKEKEN-VSLDVMQLRSEVLHLKEekegmhnLLEAKER 813
Cdd:PRK11281   194 RVLLQAEQALLN------AQNDLQRKSLEG-----NTQLQDLLQKQRDyLTARIQRLEHQLQLLQE-------AINSKRL 255

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024434941  814 EVSglHQKYHQAQEdllemkrySESSSKLEED----KDKKIN-EMSKEVSKLKEALNSLSQ 869
Cdd:PRK11281   256 TLS--EKTVQEAQS--------QDEAARIQANplvaQELEINlQLSQRLLKATEKLNTLTQ 306
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
 535-869 6.23e-04

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


Pssm-ID: 428797 [Multi-domain]  Cd Length: 542  Bit Score: 43.30  E-value: 6.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 535 SKLSVEECEELKNSYCSVIDNINQEKALLIERYKEGQEEIKRLQDKltnqthlessaesgemkdamhrmIDELNRQLSEL 614
Cdd:pfam06160  84 AKKALDEIEELLDDIEEDIKQILEELDELLESEEKNREEVEELKDK-----------------------YRELRKTLLAN 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 615 SQLYKEAQAELEdyrkrKTLDDIAvdyiprDEHEKLMQVTNSLKYKAENELLEMKSQYTKVLDEA-EELKQMLDtQKQNS 693
Cdd:pfam06160 141 RFSYGPAIDELE-----KQLAEIE------EEFSQFEELTESGDYLEAREVLEKLEEETDALEELmEDIPPLYE-ELKTE 208

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 694 LPiaehQQvMNALRSTVKEMEEEINELKELltNKESEVRNLQKELLEEKAAINEAMVPRAAY---------EKLQSSLEG 764
Cdd:pfam06160 209 LP----DQ-LEELKEGYREMEEEGYALEHL--NVDKEIQQLEEQLEENLALLENLELDEAEEaleeieeriDQLYDLLEK 281

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 765 E------VSILSSKLKDVIKEKENVSldvMQLRSEVLHLKEEKEGMHNLLEAK---EREVSGLHQKYHQAQEDLLEMK-R 834
Cdd:pfam06160 282 EvdakkyVEKNLPEIEDYLEHAEEQN---KELKEELERVQQSYTLNENELERVrglEKQLEELEKRYDEIVERLEEKEvA 358

                         330       340       350
                  ....*....|....*....|....*....|....*
gi 2024434941 835 YSESSSKLEEDkDKKINEMSKEVSKLKEALNSLSQ 869
Cdd:pfam06160 359 YSELQEELEEI-LEQLEEIEEEQEEFKESLQSLRK 392
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 394-867 6.38e-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: 43.47  E-value: 6.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 394 SEIKIKYLQEDSKDAQRKLENSETKRKHLEAQVQSRVPEADLNNTDISENGSDPSLKIQETQSKYEEAAK---EVLNAQK 470
Cdd:TIGR04523  52 KEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKlevELNKLEK 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 471 QVKPglVSSESEETCSELSKLKVTCEEVEMLRQELRRALEESERQKEKVRELQKKFEEREQNVTSKL--------SVEEC 542
Cdd:TIGR04523 132 QKKE--NKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLlklelllsNLKKK 209

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 543 EELKNSYCSVIDNINQEKALLIERYKEGQEEIKRLQDKL-TNQTHLES-SAESGEMKDAMHRMIDEL---NRQLSELSQL 617
Cdd:TIGR04523 210 IQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEIsNTQTQLNQlKDEQNKIKKQLSEKQKELeqnNKKIKELEKQ 289

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 618 YKEAQAELEDYRKRKTLD-DIAVDYIPRDEHEKLMQVTNSLKY--KAENELLEMKSQYTKVLDEAEELKQMLDTQ---KQ 691
Cdd:TIGR04523 290 LNQLKSEISDLNNQKEQDwNKELKSELKNQEKKLEEIQNQISQnnKIISQLNEQISQLKKELTNSESENSEKQREleeKQ 369

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 692 NSL-----PIAEHQQVMNALRSTVKEMEEEINELKELLTNKESEVRNLQKELLEEKAAINEAMVPRAAYEKLQSSLEGEV 766
Cdd:TIGR04523 370 NEIeklkkENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQD 449

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 767 SILSSKLKDVIKEKENVSLDVMQLRSEVLHLKEEKEGMHNLLEAKEREVSGLHQKYHQAQEDLLEMKRYSESSSKLEEDK 846
Cdd:TIGR04523 450 SVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKL 529

                         490       500
                  ....*....|....*....|.
gi 2024434941 847 DKKINEMSKEVSKLKEALNSL 867
Cdd:TIGR04523 530 ESEKKEKESKISDLEDELNKD 550
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 495-812 7.30e-04

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


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 43.42  E-value: 7.30e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  495 CEEVEMLRQELRRALEESERQKEKVRElqkkfEEREQNVTSKLSVEECEELKNSYCSVIDNINQEKALLIERYKEGQEEI 574
Cdd:pfam02463  193 EELKLQELKLKEQAKKALEYYQLKEKL-----ELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKL 267

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  575 KRLQDKLTNQTHLESSAESGEMKDAMHRMIDELNRQLSELSQLYKEAQAELEDYRKRKTLDDIAVDYIPRDEHEKLMQVT 654
Cdd:pfam02463  268 AQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKEL 347

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  655 NSLKYKAENELLEMKSQYTKVLDEAEELKQMLDTQKQNSLPIAEHQQVMNALRStvkEMEEEINELKELLTNKESEVRNL 734
Cdd:pfam02463  348 EIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKS---EEEKEAQLLLELARQLEDLLKEE 424

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024434941  735 QKELLEEKAAIneamvpraayEKLQSSLEGEVSILSSKLKDVIKEKENVSLDVMQLRSEVLHLKEEKEGMHNLLEAKE 812
Cdd:pfam02463  425 KKEELEILEEE----------EESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSR 492
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 119-147 1.02e-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: 37.24  E-value: 1.02e-03
                          10        20
                  ....*....|....*....|....*....
gi 2024434941 119 GKTALHYAATCGCLQAVQLLCEHKCPINM 147
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 379-743 1.23e-03

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


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 42.65  E-value: 1.23e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  379 STLNATQSQEKLTSPSEIKIKYLQEDSKDAQRKLENSETKRKHLEAQVQSRVPEADLNNTDISENGSDPSLKIQETQSKY 458
Cdd:pfam02463  652 VSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQ 731

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  459 EEAAKEVLNAQKQVKPGLVSSESEETCSELSKLKVTCEEVEMLRQELRRALEESERQKEKVRELQKKFEEREQNVTSKLS 538
Cdd:pfam02463  732 DKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELK 811

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  539 VEECEELKnsycsviDNINQEKALLIERyKEGQEEIKRLQDKLTNQTHLESSAESGEMKDAMHRMIDELNRQLSELSQL- 617
Cdd:pfam02463  812 EEAELLEE-------EQLLIEQEEKIKE-EELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQk 883

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  618 --YKEAQAELEDYRKRKTLD-DIAVDYIPRDEHEKL---MQVTNSLKYKAENELLEMKSQYTKVLDEAEE-LKQMLDTQK 690
Cdd:pfam02463  884 lkDELESKEEKEKEEKKELEeESQKLNLLEEKENEIeerIKEEAEILLKYEEEPEELLLEEADEKEKEENnKEEEEERNK 963

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2024434941  691 QNSLPIAEHQQVMNALRSTVKEMEEEINELKELLTNKESEVRNLQKELLEEKA 743
Cdd:pfam02463  964 RLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETC 1016
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 86-113 1.30e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 37.18  E-value: 1.30e-03
                           10        20
                   ....*....|....*....|....*...
gi 2024434941   86 GHSALHLAVKNSHIDCIKRLLQYKCSVY 113
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADIN 29
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 313-691 1.35e-03

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 42.42  E-value: 1.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 313 TEQQDLLMLMQAKIASLTLHNKELQDKL----QERTPKEVDSTIDSYHSTQREFDQTADRQSEISAQelkSTLNAtqSQE 388
Cdd:pfam17380 266 TENEFLNQLLHIVQHQKAVSERQQQEKFekmeQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQ---AAIYA--EQE 340

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 389 KLTSPSEIKIKYLQEDskdaQRKLENSETKRKHLEAQVqSRVPEADlnntdisengsdpslKIQETQSKYEEAAKEVLNA 468
Cdd:pfam17380 341 RMAMERERELERIRQE----ERKRELERIRQEEIAMEI-SRMRELE---------------RLQMERQQKNERVRQELEA 400

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 469 QKQVKPGLVSSESEETCSELSKLKVTCEEVEMLRQELRRALEESERQKEKVRELQkkfEEREQNVtSKLSVEECEElkns 548
Cdd:pfam17380 401 ARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEE---QERQQQV-ERLRQQEEER---- 472

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 549 ycsvidninQEKALLIERYKEGQEEIKRLQDKLTNQthlessaesgEMKDAMHRMIDELNRQLSELSQLYKEAQAELEDY 628
Cdd:pfam17380 473 ---------KRKKLELEKEKRDRKRAEEQRRKILEK----------ELEERKQAMIEEERKRKLLEKEMEERQKAIYEEE 533

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024434941 629 RKRKTlddiavdyiprdEHEKLMQVTNSLKYKAENELL---EMKSQYTKVLDEAEELKQMLDTQKQ 691
Cdd:pfam17380 534 RRREA------------EEERRKQQEMEERRRIQEQMRkatEERSRLEAMEREREMMRQIVESEKA 587
Ank_4 pfam13637
Ankyrin repeats (many copies);
185-224 1.43e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 37.64  E-value: 1.43e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2024434941 185 GRTALMIACEAGSLNMVEVFLRKGADVSLVDVFGQNALHY 224
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHF 40
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 86-117 1.61e-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. 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: 36.88  E-value: 1.61e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 2024434941  86 GHSALHLAV-KNSHIDCIKRLLQYKCSVYSTDN 117
Cdd:pfam00023   2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
KpsE COG3524
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
602-730 1.67e-03

Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442746 [Multi-domain]  Cd Length: 370  Bit Score: 41.76  E-value: 1.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 602 RMIDELN------------RQLSELSQLYKEAQAELEDYR-KRKTLDdiavdyiPRDEHEKLMQVTNSLkykaENELLEM 668
Cdd:COG3524   165 ELVNQLSeraredavrfaeEEVERAEERLRDAREALLAFRnRNGILD-------PEATAEALLQLIATL----EGQLAEL 233

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024434941 669 KSQytkvldeaeeLKQMLDTQKQNSLPIAehqqvmnALRSTVKEMEEEINELKELLTNKESE 730
Cdd:COG3524   234 EAE----------LAALRSYLSPNSPQVR-------QLRRRIAALEKQIAAERARLTGASGG 278
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 660-802 2.70e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 41.74  E-value: 2.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 660 KAENELLEMKSQYTKVLDEAEELKQMLDTQKQNSlpiaeHQQVMNALRSTVKEMEEEINELKELLTNKESEVRNlqKELL 739
Cdd:PRK00409  538 EAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEA-----EKEAQQAIKEAKKEADEIIKELRQLQKGGYASVKA--HELI 610

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024434941 740 EEKAAINEAMVPRAA-----YEKLQSSLEG-EVSILSSKLKDVIKEKE-----NVSLDVMQLR---SEVLHLKEEKE 802
Cdd:PRK00409  611 EARKRLNKANEKKEKkkkkqKEKQEELKVGdEVKYLSLGQKGEVLSIPddkeaIVQAGIMKMKvplSDLEKIQKPKK 687
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 681-904 2.71e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 41.35  E-value: 2.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 681 ELKQMLDTQKQNSLPIAEHQQVMNALRSTVKEMEEEINELKELLTNKESEVRNLQKELLEEKAAINEAM-----VPRAAY 755
Cdd:COG3883    17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERReelgeRARALY 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 756 EKLQSSLEGEVSILSSKLKDVIKEKENVSLDVMQLRSEVLHLKEEKEgmhnLLEAKEREVSGLHQKYHQAQEDLLEMKRY 835
Cdd:COG3883    97 RSGGSVSYLDVLLGSESFSDFLDRLSALSKIADADADLLEELKADKA----ELEAKKAELEAKLAELEALKAELEAAKAE 172

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024434941 836 SESsskLEEDKDKKINEMSKEVSKLKEALNSLSQLSYSTSAPKRQSQQLEALQQQVKQLQNQLTETKKQ 904
Cdd:COG3883   173 LEA---QQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 238
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 494-750 3.04e-03

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 41.36  E-value: 3.04e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  494 TCEEVEMLRQELRRALEESERQKEkvrELQKKFEEREQNVTSKLSVEEcEELKNSycsvIDNINQEKALLIERYKEGQEE 573
Cdd:pfam12128  252 TLESAELRLSHLHFGYKSDETLIA---SRQEERQETSAELNQLLRTLD-DQWKEK----RDELNGELSAADAAVAKDRSE 323

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  574 IKRLQDKLT--NQTHLESSAESGEMKDAMHRMIDELNRQLSELSQLYKEAQAE---LEDYRKRKTLDDIAV-----DYIp 643
Cdd:pfam12128  324 LEALEDQHGafLDADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKynrRRSKIKEQNNRDIAGikdklAKI- 402

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  644 RDEHEKLMQVTNSLKYKAENEL-LEMKSQYTKVLDEAEELKQMLDTQK-QNSLPIAEHQQVMNalrstVKEMEEEINELK 721
Cdd:pfam12128  403 REARDRQLAVAEDDLQALESELrEQLEAGKLEFNEEEYRLKSRLGELKlRLNQATATPELLLQ-----LENFDERIERAR 477

                          250       260
                   ....*....|....*....|....*....
gi 2024434941  722 ELLTNKESEVRNLQKELLEEKAAINEAMV 750
Cdd:pfam12128  478 EEQEAANAEVERLQSELRQARKRRDQASE 506
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 156-237 3.16e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 41.39  E-value: 3.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 156 LLLAVQNGHTEVCKYLLDHGADINTRDKNGRTALMIACEAGSLNMVEVFLRKGADVSLVDVFGQNALHYSKISENTGIQN 235
Cdd:PLN03192  529 LLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFR 608


                  ..
gi 2024434941 236 LL 237
Cdd:PLN03192  609 IL 610
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 67-187 4.03e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 39.80  E-value: 4.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  67 ECLRIMVTHGADVTAQ-DGAGHSALHLAV---KNSHIDCIKRLLQYKCSVYSTDNSGKTALH-YAATCGC-LQAVQLLCE 140
Cdd:PHA02859   67 EILKFLIENGADVNFKtRDNNLSALHHYLsfnKNVEPEILKILIDSGSSITEEDEDGKNLLHmYMCNFNVrINVIKLLID 146

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2024434941 141 HKCPINMKDLDG-NIPLLLAVQNGHTEVCKYLLDHGADINTRDKNGRT 187
Cdd:PHA02859  147 SGVSFLNKDFDNnNILYSYILFHSDKKIFDFLTSLGIDINETNKSGYN 194
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 44-172 4.09e-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: 40.90  E-value: 4.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  44 ASATKQDSEGKTAFHLAATKGHAECLRIMVTHGADVTAQ------------DG--AGHSALHLAVKNSHIDCIKRLLQyK 109
Cdd:cd22194   132 AEYTEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAHakgvffnpkykhEGfyFGETPLALAACTNQPEIVQLLME-K 210

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024434941 110 CS--VYSTDNSGKTALHYAATCG------------CLQAVQLLCEHKCPINMKDLDGNIPLLLAVQNGHTEVCKYLL 172
Cdd:cd22194   211 EStdITSQDSRGNTVLHALVTVAedsktqndfvkrMYDMILLKSENKNLETIRNNEGLTPLQLAAKMGKAEILKYIL 287
PHA02989 PHA02989
ankyrin repeat protein; Provisional
 99-205 4.12e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 40.88  E-value: 4.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  99 IDCIKRLLQYKCSVYSTDNSGKTAL------HYAATCGCLQAVQLLCEHkCPINMKDLDGNIPLLLAVQNGHTEVCKYLL 172
Cdd:PHA02989  198 IKVIKYLIKKGVNIETNNNGSESVLesfldnNKILSKKEFKVLNFILKY-IKINKKDKKGFNPLLISAKVDNYEAFNYLL 276

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2024434941 173 DHGADINTRDKNGRTALMIACEAGSLNMVEVFL 205
Cdd:PHA02989  277 KLGDDIYNVSKDGDTVLTYAIKHGNIDMLNRIL 309
Mitofilin pfam09731
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ...
 503-820 4.33e-03

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


Pssm-ID: 430783 [Multi-domain]  Cd Length: 618  Bit Score: 40.90  E-value: 4.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 503 QELRRALEESERQKEKVRELQKKFEEREQNVTSKLSVEECEELKNSYCSVIDNINQEKALLIERYKEGQEEIKRLQDKLT 582
Cdd:pfam09731 124 QEKEKALEEVLKEAISKAESATAVAKEAKDDAIQAVKAHTDSLKEASDTAEISREKATDSALQKAEALAEKLKEVINLAK 203

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 583 NQTHLESSAESGEMKDAMHRMIDELNRQLSELSQLYKEAqAELEDYRKRKTLDdiavdyiPRDEHEKLMQVTNSLKYKAE 662
Cdd:pfam09731 204 QSEEEAAPPLLDAAPETPPKLPEHLDNVEEKVEKAQSLA-KLVDQYKELVASE-------RIVFQQELVSIFPDIIPVLK 275

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 663 NELLEMKSQYTKVLDEA-EELKQMldTQKQNSLPIAEHQQVMNALRSTVKEMEEEINELKELLTNK-ESEVRNLQKELLE 740
Cdd:pfam09731 276 EDNLLSNDDLNSLIAHAhREIDQL--SKKLAELKKREEKHIERALEKQKEELDKLAEELSARLEEVrAADEAQLRLEFER 353

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 741 EKAAINEAMvpraaYEKLQSSLEGEVSILSSKLKDVIKEKEnVSLDVMQLRSEVLHLKEEKEGMHNLLEAKEREVSGLHQ 820
Cdd:pfam09731 354 EREEIRESY-----EEKLRTELERQAEAHEEHLKDVLVEQE-IELQREFLQDIKEKVEEERAGRLLKLNELLANLKGLEK 427
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 655-869 4.45e-03

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 40.77  E-value: 4.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 655 NSLKYKAENELLEMKSQYTKVLDEAEELKQMLDT-----QKQNSL--PIAEHQQVMNALRSTVKEMEEEINELKELLTNK 727
Cdd:TIGR04523  43 KTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKikileQQIKDLndKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKL 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 728 ESEVRNLQKELLEEKAAINEAMVPraayeklQSSLEGEVSILSSKLKDVIKEKENVSLDVMQLRSEVLHLKEEKEGMHNL 807
Cdd:TIGR04523 123 EVELNKLEKQKKENKKNIDKFLTE-------IKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNK 195

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024434941 808 LEAKEREVSGLH---QKYHQAQEDLLEMKRYSESSSKLEEDKDKKINEMSKEVSKLKEALNSLSQ 869
Cdd:TIGR04523 196 LLKLELLLSNLKkkiQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKD 260
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
705-844 5.35e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.67  E-value: 5.35e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  705 ALRSTVKEMEEEINELKELLTNKESEVRNLQKElleekaaineamvpRAAYEKLQSSLEGEVSILS-----SKLKDVIKE 779
Cdd:COG4913    614 ALEAELAELEEELAEAEERLEALEAELDALQER--------------REALQRLAEYSWDEIDVASaereiAELEAELER 679

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024434941  780 KENVSLDVMQLRSEVLHLKEEKEGMHNLLEAKEREVSGLHQKYHQAQEDLLEMKRYSESSSKLEE 844
Cdd:COG4913    680 LDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLAR 744
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
 506-865 5.83e-03

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


Pssm-ID: 428797 [Multi-domain]  Cd Length: 542  Bit Score: 40.22  E-value: 5.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 506 RRALEESERQ----KEKVRELQKKFEE-REQNVTSKLSVEECEELknsYCSVIDNINQEKALLIERYKEGQEEIKRLQDK 580
Cdd:pfam06160  85 KKALDEIEELlddiEEDIKQILEELDElLESEEKNREEVEELKDK---YRELRKTLLANRFSYGPAIDELEKQLAEIEEE 161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 581 LTNQTHLESSA---ESGEMKDAMHRMIDELNRQLSELSQLYKEAQAELED--------YRKRK----TLDDIAVDyiprd 645
Cdd:pfam06160 162 FSQFEELTESGdylEAREVLEKLEEETDALEELMEDIPPLYEELKTELPDqleelkegYREMEeegyALEHLNVD----- 236

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 646 ehEKLMQVTNSLKyKAENELLEMKsqytkvLDEAEELKQMLDTQkqnslpIAEHQQVMNALRSTVKEMEEEINELKELLT 725
Cdd:pfam06160 237 --KEIQQLEEQLE-ENLALLENLE------LDEAEEALEEIEER------IDQLYDLLEKEVDAKKYVEKNLPEIEDYLE 301

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 726 nkesEVRNLQKELLEEKAAINEAMVPRAAYEKLQSSLEGEVSILSSKLKDVIKEKENVSLDVMQLRSEVLHLKEEKEGMH 805
Cdd:pfam06160 302 ----HAEEQNKELKEELERVQQSYTLNENELERVRGLEKQLEELEKRYDEIVERLEEKEVAYSELQEELEEILEQLEEIE 377

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024434941 806 NLLEAKEREVSGLHQKYHQAQE-------DLLEMKRYSESS--SKLEEDKDKKINEMSKEVSKLKEALN 865
Cdd:pfam06160 378 EEQEEFKESLQSLRKDELEAREkldefklELREIKRLVEKSnlPGLPESYLDYFFDVSDEIEDLADELN 446
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
609-852 5.87e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.67  E-value: 5.87e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  609 RQLSELSQLYKEAQAELED-YRKRKTLDDIavdyipRDEHEKlmqvtnslkykaenellemksqYTKVLDEAEELKQMLD 687
Cdd:COG4913    228 DALVEHFDDLERAHEALEDaREQIELLEPI------RELAER----------------------YAAARERLAELEYLRA 279

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  688 TqkqnsLPIAEHQQVMNALRSTVKEMEEEINELKELLTNKESEVRNLQKELLEEKAAINEamvprAAYEKLQsSLEGEVS 767
Cdd:COG4913    280 A-----LRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRG-----NGGDRLE-QLEREIE 348

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  768 ILSSKLKDVIKEKENVSLDVMQLRsevLHLKEEKEGMHNLLEAKEREVSGLHQKYHQAQEDLLEMKRyseSSSKLEEDKD 847
Cdd:COG4913    349 RLERELEERERRRARLEALLAALG---LPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEA---ALRDLRRELR 422


                   ....*
gi 2024434941  848 KKINE 852
Cdd:COG4913    423 ELEAE 427
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 26-94 6.03e-03

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: 40.38  E-value: 6.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  26 AVENGDPEKVASLLgKKGASATKQDSEGkTAFHL---------------AATKGHAECLRIMVTHGADVTAQDGAGHSAL 90
Cdd:cd22192    96 AVVNQNLNLVRELI-ARGADVVSPRATG-TFFRPgpknliyygehplsfAACVGNEEIVRLLIEHGADIRAQDSLGNTVL 173


                  ....
gi 2024434941  91 HLAV 94
Cdd:cd22192   174 HILV 177
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
 517-865 6.24e-03

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


Pssm-ID: 130673 [Multi-domain]  Cd Length: 2757  Bit Score: 40.81  E-value: 6.24e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  517 EKVRELQKKFEEREQNVTSKLSVEE-----------CEELKNSYCSVIDNINQEKAllIERYKEGQEEIkrLQDKLTNQT 585
Cdd:TIGR01612 1365 DEVKEYTKEIEENNKNIKDELDKSEklikkikddinLEECKSKIESTLDDKDIDEC--IKKIKELKNHI--LSEESNIDT 1440

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  586 HLESSAESGEMKDAMHRMIDELNRQLSELSQLYKEAQAELEDYRKRKTLDDIAVDYIPRDEHEKlmqvtNSLKYKAENEL 665
Cdd:TIGR01612 1441 YFKNADENNENVLLLFKNIEMADNKSQHILKIKKDNATNDHDFNINELKEHIDKSKGCKDEADK-----NAKAIEKNKEL 1515

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  666 LEM-KSQYTKVLDE--AEELKQMLD-TQKQNSLPIAEHQQVMNALRSTVKEMEEEINELKELLTNKESEVRNLQKellEE 741
Cdd:TIGR01612 1516 FEQyKKDVTELLNKysALAIKNKFAkTKKDSEIIIKEIKDAHKKFILEAEKSEQKIKEIKKEKFRIEDDAAKNDK---SN 1592

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  742 KAAINeamvpraayekLQSSLEG------EVSILSSKLKDVIKEKENVsldvmqlrsevlhlkeEKEGMHNLLEAKEREV 815
Cdd:TIGR01612 1593 KAAID-----------IQLSLENfenkflKISDIKKKINDCLKETESI----------------EKKISSFSIDSQDTEL 1645

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|
gi 2024434941  816 SGLHQKYHQAQEDLLEMKryseSSSKLEEDKDKKINEMSKEVSKLKEALN 865
Cdd:TIGR01612 1646 KENGDNLNSLQEFLESLK----DQKKNIEDKKKELDELDSEIEKIEIDVD 1691
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 44-172 7.04e-03

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: 40.06  E-value: 7.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941  44 ASATKQDSEGKTAFHLAATKGHAECLRIMVTHGADVTA------------QDGAGHSALHL----AVKNSHIdcIKRLLQ 107
Cdd:TIGR00870 119 DQYTSEFTPGITALHLAAHRQNYEIVKLLLERGASVPAracgdffvksqgVDSFYHGESPLnaaaCLGSPSI--VALLSE 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 108 YKCSVYSTDNSGKTALHYAA------------TCGCLQ-AVQLLcEHKCPIN----MKDLDGNIPLLLAVQNGHTEVCKY 170
Cdd:TIGR00870 197 DPADILTADSLGNTLLHLLVmenefkaeyeelSCQMYNfALSLL-DKLRDSKelevILNHQGLTPLKLAAKEGRIVLFRL 275


                  ..
gi 2024434941 171 LL 172
Cdd:TIGR00870 276 KL 277
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
312-829 7.34e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 40.02  E-value: 7.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 312 ETEQQDLLMLMQAKIASLT--LHNKELQDKLQERTPKEVDSTIDSYHSTQREFDqtaDRQSEISaqELKSTLNATQSqEK 389
Cdd:PRK02224  201 EKDLHERLNGLESELAELDeeIERYEEQREQARETRDEADEVLEEHEERREELE---TLEAEIE--DLRETIAETER-ER 274

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 390 LTspseikikyLQEDSKDAQRKLENSETKRKHLEAQ----------VQSRVPEADLNNTDISENGSDPSLKIQETQSKYE 459
Cdd:PRK02224  275 EE---------LAEEVRDLRERLEELEEERDDLLAEaglddadaeaVEARREELEDRDEELRDRLEECRVAAQAHNEEAE 345

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 460 EAAKEVL-----NAQKQVKPGLVSSESEETCSELSKLKVTCEEVEMLRQELRRALEESERQKEKVRELQKKFEEREQNVT 534
Cdd:PRK02224  346 SLREDADdleerAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELR 425

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 535 SKLSveeceELKNSYCSVIDNINQEKALL-----------------IERYKEGQEEIKRLQDKL----TNQTHLESSAES 593
Cdd:PRK02224  426 EREA-----ELEATLRTARERVEEAEALLeagkcpecgqpvegsphVETIEEDRERVEELEAELedleEEVEEVEERLER 500

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 594 GEMKDAMHRMIDELNRQLSELSQLYKEAQAELEDYR-KRKTLDDIAVDYipRDEHEKLMQVTNSLKYKAENELLEMKSQY 672
Cdd:PRK02224  501 AEDLVEAEDRIERLEERREDLEELIAERRETIEEKReRAEELRERAAEL--EAEAEEKREAAAEAEEEAEEAREEVAELN 578

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 673 TKVLDEAEELKQMLDTQKQNSLpIAEHQQVMNALRSTVKEMEEEINELKELLTNKESEVRNLQKELleEKAAINEAMVPR 752
Cdd:PRK02224  579 SKLAELKERIESLERIRTLLAA-IADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEF--DEARIEEAREDK 655

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 753 AAYEKLQSSLEGEVSILSSKLKDVIKEKENVSLDVMQLRSevlhLKEEKEGMHNLLEAKE---REVSGLHQKYHQAQEDL 829
Cdd:PRK02224  656 ERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEE----LRERREALENRVEALEalyDEAEELESMYGDLRAEL 731
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 604-765 8.07e-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: 8.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 604 IDELNRQLSELSQLYKEAQAELEDYRKR--KTLDDIAVDYIPRDEHEKLMQVTNSLKYKAE------NELLEMKSqYTKV 675
Cdd:COG3883    39 LDALQAELEELNEEYNELQAELEALQAEidKLQAEIAEAEAEIEERREELGERARALYRSGgsvsylDVLLGSES-FSDF 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 676 LDEAEELKQMLDTQKQNslpIAEHQQVMNALRSTVKEMEEEINELKELLTNKESEVRNLQKELLEEKAAINEAMVPRAAY 755
Cdd:COG3883   118 LDRLSALSKIADADADL---LEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAA 194

                         170
                  ....*....|
gi 2024434941 756 EKLQSSLEGE 765
Cdd:COG3883   195 EAQLAELEAE 204
14-3-3_fungi cd11309
Fungal 14-3-3 protein domain; This family containing fungal 14-3-3 domains includes the yeasts ...
 505-643 8.78e-03

Fungal 14-3-3 protein domain; This family containing fungal 14-3-3 domains includes the yeasts Saccharomyces cerevisiae (BMH1 and BMH2) and Schizosaccharomyces pombe (rad24 and rad25) isoforms. They possess distinctively variant C-terminal segments that differentiate them from the mammalian isoforms; the C-terminus is longer and BMH1/2 isoforms contain polyglutamine (polyQ) sequences of unknown function. The C-terminal segments of yeast 14-3-3 isoforms may thus behave in a different manner compared to the higher eukaryote isoforms. Yeast 14-3-3 proteins bind to numerous proteins involved in a variety of yeast cellular processes making them excellent model organisms for elucidating the function of the 14-3-3 protein family. BMH1 and BMH2 are positive regulators of rapamycin-sensitive signaling via TOR kinases while they play an inhibitory role in Rtg3p-dependent transcription involved in retrograde signaling. 14-3-3 domains are an essential part of 14-3-3 proteins, a ubiquitous class of regulatory, phosphoserine/threonine-binding proteins found in all eukaryotic cells, including yeast, protozoa and mammalian cells.


Pssm-ID: 206763  Cd Length: 231  Bit Score: 38.82  E-value: 8.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 505 LRRALEESERQKEKVRELQKKFEEREqnvtsKLSVEECEELKNSYCSVI------------------DNINQEKALLIER 566
Cdd:cd11309     7 LAKLAEQAERYEEMVENMKKVASSDQ-----ELTVEERNLLSVAYKNVIgarraswrivssieqkeeSKGNESQVALIKE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 567 YKEGQE-EIKRLQDKLTN--QTHLESSAESGEMKDAMHRMIDELNRQLSELS---QLYKEAQAELEDYrkrKTLDDIAVD 640
Cdd:cd11309    82 YRSKIEsELTKICDDILSvlDKHLIPSATTGESKVFYYKMKGDYHRYLAEFAvgdKRKEAADSSLEAY---KAASDIAVT 158


                  ...
gi 2024434941 641 YIP 643
Cdd:cd11309   159 ELP 161
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
496-641 9.86e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 39.61  E-value: 9.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434941 496 EEVEMLRQELRRALEESERQKEKVRELQKKFEEREQNVTSKLSVEECEELKNSYcsviDNINQEKALLIERYKEGQEEIK 575
Cdd:COG3206   219 QQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQL----AELEAELAELSARYTPNHPDVI 294

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024434941 576 RLQDKLTNqthLESsaesgEMKDAMHRMIDELNRQLSELSQLYKEAQAELEDYRKR-KTLDDIAVDY 641
Cdd:COG3206   295 ALRAQIAA---LRA-----QLQQEAQRILASLEAELEALQAREASLQAQLAQLEARlAELPELEAEL 353
 
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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