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Conserved domains on  [gi|2024434935|ref|XP_040512447|]
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ankycorbin isoform X8 [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 2.60e-51

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 182.46  E-value: 2.60e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935   1 MKSLKAKFRKSDTNEWNKNDDRLLQAVENGDPEKVASLLGKKGASATKQDSEGKTAFHLAATKGHAECLRIMVTHGADVT 80
Cdd:COG0666    35 LLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVN 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  81 AQDGAGHSALHLAVKNSHIDCIKRLLQYKCSVYSTDNSGKTALHYAATCGCLQAVQLLCEHKCPINMKDLDGNIPLLLAV 160
Cdd:COG0666   115 ARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAA 194
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024434935 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 ...
524-899 3.15e-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: 74.32  E-value: 3.15e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  524 EEVEMLRQELRRALEESERQKEKVRELQKKFEEREQnvtsklsveeceelknsycsvidninQEKALLIERYKEGQEEIK 603
Cdd:TIGR02168  189 DRLEDILNELERQLKSLERQAEKAERYKELKAELRE--------------------------LELALLVLRLEELREELE 242
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  604 RLQDKLTNQTHLESSAESGemKDAMHRMIDELNRQLSELSQLYKEAQAELEDYRKRktlddiavdyIPRDEHEKlmQVTN 683
Cdd:TIGR02168  243 ELQEELKEAEEELEELTAE--LQELEEKLEELRLEVSELEEEIEELQKELYALANE----------ISRLEQQK--QILR 308
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  684 SLKYKAENELLEMKSQYTKVLDEAEELKQMLDTQKQNslpIAEHQQVMNALRSTVKEMEEEINELKELLTNKESEVRNLQ 763
Cdd:TIGR02168  309 ERLANLERQLEELEAQLEELESKLDELAEELAELEEK---LEELKEELESLEAELEELEAELEELESRLEELEEQLETLR 385
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  764 KELLEEKAAINEAMVPRAAYEKLQSSLEGEVSILSSKLKDVIKEKENVSLDvmQLRSEVLHLKEEKEGMHNLLEAKEREV 843
Cdd:TIGR02168  386 SKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELK--ELQAELEELEEELEELQEELERLEEAL 463
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2024434935  844 SGLHQKYHQAQEDLLEMKRYSESSSKLEEDKDKKINEMSKEVSKLKEALNSLSQLS 899
Cdd:TIGR02168  464 EELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLS 519
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
317-611 1.47e-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: 45.82  E-value: 1.47e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  317 LQDNKDRLSDSTAGADSLLDVSSETEQQDLLMLMQAKIASLTLHNKELQDKLQERTPKEVDSTIDSYHStQREFDQTADR 396
Cdd:TIGR02168  700 LAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEE-RLEEAEEELA 778
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  397 QSEISAQELKSTLNATQSQ-----EKLTSPSEIkIKYLQEDSKDAQRKLENSETKRKHLEAQVQSRVPEADLNNTDISEN 471
Cdd:TIGR02168  779 EAEAEIEELEAQIEQLKEElkalrEALDELRAE-LTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESL 857
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  472 gSDPSLKIQETQSKYEEAAKEVLNAQKQVKPGLvssesEETCSELSKLKVTCEEVEMLRQELRRALEESERQKEKVRELQ 551
Cdd:TIGR02168  858 -AAEIEELEELIEELESELEALLNERASLEEAL-----ALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRL 931
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  552 KKFEEREQNVTSKLSVEECEELknsycsviDNINQEKALLIERYKEGQEEIKRLQDKLTN 611
Cdd:TIGR02168  932 EGLEVRIDNLQERLSEEYSLTL--------EEAEALENKIEDDEEEARRRLKRLENKIKE 983
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1-237 2.60e-51

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 182.46  E-value: 2.60e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935   1 MKSLKAKFRKSDTNEWNKNDDRLLQAVENGDPEKVASLLGKKGASATKQDSEGKTAFHLAATKGHAECLRIMVTHGADVT 80
Cdd:COG0666    35 LLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVN 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  81 AQDGAGHSALHLAVKNSHIDCIKRLLQYKCSVYSTDNSGKTALHYAATCGCLQAVQLLCEHKCPINMKDLDGNIPLLLAV 160
Cdd:COG0666   115 ARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAA 194
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024434935 161 QNGHTEVCKYLLDHGADINTRDKNGRTALMIACEAGSLNMVEVFLRKGADVSLVDVFGQNALHYSKISENTGIQNLL 237
Cdd:COG0666   195 ENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLL 271
Ank_2 pfam12796
Ankyrin repeats (3 copies);
90-182 5.98e-26

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 102.50  E-value: 5.98e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  90 LHLAVKNSHIDCIKRLLQYKCSVYSTDNSGKTALHYAATCGCLQAVQLLCEHkCPINMKDlDGNIPLLLAVQNGHTEVCK 169
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78
                          90
                  ....*....|...
gi 2024434935 170 YLLDHGADINTRD 182
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
23-237 1.36e-22

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 101.67  E-value: 1.36e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  23 LLQAVENGDPEKVASLLgKKGASATKQDSEGKTAFHLAATKGHA-----ECLRIMVTHGADVTAQDGAGHSALHLAVKNS 97
Cdd:PHA03100   39 LYLAKEARNIDVVKILL-DNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAISKK 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  98 --HIDCIKRLLQYKCSVYSTDNSGKTALHYAATCGC--LQAVQLLCEHKCPINMKDldgniplllavqnghteVCKYLLD 173
Cdd:PHA03100  118 snSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVDINAKN-----------------RVNYLLS 180
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024434935 174 HGADINTRDKNGRTALMIACEAGSLNMVEVFLRKGADVSLVDVFGQNALHYSKISENTGIQNLL 237
Cdd:PHA03100  181 YGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLL 244
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
524-899 3.15e-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: 74.32  E-value: 3.15e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  524 EEVEMLRQELRRALEESERQKEKVRELQKKFEEREQnvtsklsveeceelknsycsvidninQEKALLIERYKEGQEEIK 603
Cdd:TIGR02168  189 DRLEDILNELERQLKSLERQAEKAERYKELKAELRE--------------------------LELALLVLRLEELREELE 242
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  604 RLQDKLTNQTHLESSAESGemKDAMHRMIDELNRQLSELSQLYKEAQAELEDYRKRktlddiavdyIPRDEHEKlmQVTN 683
Cdd:TIGR02168  243 ELQEELKEAEEELEELTAE--LQELEEKLEELRLEVSELEEEIEELQKELYALANE----------ISRLEQQK--QILR 308
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  684 SLKYKAENELLEMKSQYTKVLDEAEELKQMLDTQKQNslpIAEHQQVMNALRSTVKEMEEEINELKELLTNKESEVRNLQ 763
Cdd:TIGR02168  309 ERLANLERQLEELEAQLEELESKLDELAEELAELEEK---LEELKEELESLEAELEELEAELEELESRLEELEEQLETLR 385
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  764 KELLEEKAAINEAMVPRAAYEKLQSSLEGEVSILSSKLKDVIKEKENVSLDvmQLRSEVLHLKEEKEGMHNLLEAKEREV 843
Cdd:TIGR02168  386 SKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELK--ELQAELEELEEELEELQEELERLEEAL 463
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2024434935  844 SGLHQKYHQAQEDLLEMKRYSESSSKLEEDKDKKINEMSKEVSKLKEALNSLSQLS 899
Cdd:TIGR02168  464 EELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLS 519
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
403-898 6.93e-13

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 72.79  E-value: 6.93e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 403 QELKSTLNATQSQEKLTSPSEIKIKYLQEDSKDAQRKLENSETKRKHLEAQVQsRVPEadlnntdisengsdpslkIQET 482
Cdd:PRK03918  231 KELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVK-ELKE------------------LKEK 291
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 483 QSKYEEAAKEvlnaqkqvkpglvsseSEETCSELSKLKVTCEEVEMLRQELRRALEESERQKEKVRELQKKFEEREQNV- 561
Cdd:PRK03918  292 AEEYIKLSEF----------------YEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLe 355
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 562 ----------TSKLSVEECEELKNSY-CSVIDNINQEKALLIERYKEGQEEIKRLQDKLTNqthLESsaESGEMKDAMHR 630
Cdd:PRK03918  356 eleerhelyeEAKAKKEELERLKKRLtGLTPEKLEKELEELEKAKEEIEEEISKITARIGE---LKK--EIKELKKAIEE 430
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 631 M----------------------IDELNRQLSELSQLYKEAQAELEDYRKRKTLDDIAVDYIPR-----DEHEKLMQVTN 683
Cdd:PRK03918  431 LkkakgkcpvcgrelteehrkelLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESEliklkELAEQLKELEE 510
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 684 SLKYKAENELLEMKSQYTKVLDEAEELKQMLDTQKQNSLPIAEHQQVMNALRSTVKEMEEEINEL-KELLTNKESEVRNL 762
Cdd:PRK03918  511 KLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELlKELEELGFESVEEL 590
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 763 QKELLEEKAAINEAMVPRAAYEKLQSSLEgEVSILSSKLKDVIKEKENVSLDVMQLRSEVLHLK-----EEKEGMHNLLE 837
Cdd:PRK03918  591 EERLKELEPFYNEYLELKDAEKELEREEK-ELKKLEEELDKAFEELAETEKRLEELRKELEELEkkyseEEYEELREEYL 669
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024434935 838 AKEREVSGLHQKYHQAQEDLLEMKRYSEsssKLEEDKdKKINEMSKEVSKLKEALNSLSQL 898
Cdd:PRK03918  670 ELSRELAGLRAELEELEKRREEIKKTLE---KLKEEL-EEREKAKKELEKLEKALERVEEL 726
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
524-861 6.71e-12

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 69.58  E-value: 6.71e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 524 EEVEMLRQELRRALEESERQKE---KVRELQKKFEEREQNVTSKlsveeceelknsycsVIDNINQEKALLIERYKEGQE 600
Cdd:COG1196   189 ERLEDILGELERQLEPLERQAEkaeRYRELKEELKELEAELLLL---------------KLRELEAELEELEAELEELEA 253
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 601 EIKRLQdklTNQTHLESSAESGEMKdamhrmIDELNRQLSELSQLYKEAQAELEDYRKRKTLDDIAVdyipRDEHEKLMQ 680
Cdd:COG1196   254 ELEELE---AELAELEAELEELRLE------LEELELELEEAQAEEYELLAELARLEQDIARLEERR----RELEERLEE 320
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 681 VTNSLKyKAENELLEMKSQYTKVLDEAEELKQMLDTQKQNslpIAEHQQVMNALRSTVKEMEEEINELKELLTNKESEVR 760
Cdd:COG1196   321 LEEELA-ELEEELEELEEELEELEEELEEAEEELEEAEAE---LAEAEEALLEAEAELAEAEEELEELAEELLEALRAAA 396
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 761 NLQKELLEEKAAINEAmvpraayEKLQSSLEGEVSILSSKLKDVIKEKENVSLDVMQLRSEVLHLKEEKEGMHNLLEAKE 840
Cdd:COG1196   397 ELAAQLEELEEAEEAL-------LERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELL 469
                         330       340
                  ....*....|....*....|.
gi 2024434935 841 REVSGLHQKYHQAQEDLLEMK 861
Cdd:COG1196   470 EEAALLEAALAELLEELAEAA 490
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
19-191 8.01e-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: 8.01e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  19 NDDRLLQAVENGDPEKVASLLGKKGASATKQDSEGKTAFHLAATKGH-------AECLRIMVTHgaDVTAQDGAGHSALH 91
Cdd:cd22192    17 SESPLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNleaavvlMEAAPELVNE--PMTSDLYQGETALH 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  92 LAVKNSHIDCIKRLLQYKCSVYSTDNSGkTALHYAATCgclqavqlLC---EHkcpinmkdldgniPLLLAVQNGHTEVC 168
Cdd:cd22192    95 IAVVNQNLNLVRELIARGADVVSPRATG-TFFRPGPKN--------LIyygEH-------------PLSFAACVGNEEIV 152
                         170       180
                  ....*....|....*....|...
gi 2024434935 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 1.30e-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: 45.66  E-value: 1.30e-06
                           10        20
                   ....*....|....*....|....*....
gi 2024434935  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. ...
310-849 4.42e-05

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: 47.42  E-value: 4.42e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  310 QEDFSSLLQDNKDRL----SDSTAGADSLLDVSSETEQQDLLMLMQAKIASLTLHNkelQDKLQERTPKEVDSTIDSYHS 385
Cdd:pfam15921  255 QNKIELLLQQHQDRIeqliSEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARN---QNSMYMRQLSDLESTVSQLRS 331
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  386 TQREfdqtADRQSEISAQELKSTLNATQSQekLTSPSEIKIKYLQEDSK--DAQRKLENSETKRKH---LEAQVQSRVPE 460
Cdd:pfam15921  332 ELRE----AKRMYEDKIEELEKQLVLANSE--LTEARTERDQFSQESGNldDQLQKLLADLHKREKelsLEKEQNKRLWD 405
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  461 ADLNNTdISENGSDPSLKIQETQSKYEEAAKEVLNAQKQVKPGLVSSESEETCSELSKLKVTCEEVEMLRQELRRALEES 540
Cdd:pfam15921  406 RDTGNS-ITIDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEEL 484
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  541 ERQKEKVRELQKKFEEreqnVTSKLSVEEceelknsycSVIDNINQEKALLIERYKEGQEEIKRLQDKLTNQTHLESSAE 620
Cdd:pfam15921  485 TAKKMTLESSERTVSD----LTASLQEKE---------RAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECE 551
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  621 SGEMKDA-MHRMIDELNRQLSELSQLY------------KEAQAELEDYRKRKTLDDIAVDYIPRDEHEKLMQVTNSLKY 687
Cdd:pfam15921  552 ALKLQMAeKDKVIEILRQQIENMTQLVgqhgrtagamqvEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLE 631
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  688 KAENELLEMKSQYTK-VLDEAEELKQMLDTQKQ-----NSLPiAEHQQVMNALRSTVKEMEEEINELKELLTNKESEVRN 761
Cdd:pfam15921  632 LEKVKLVNAGSERLRaVKDIKQERDQLLNEVKTsrnelNSLS-EDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQ 710
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  762 LQKELLEEKAAINEAMVPRAAYEKLQSSLEGEVSILSSKLK-------DVIKEKENVSLDVMQLRSEVLHLKEEKEGMHN 834
Cdd:pfam15921  711 TRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQfleeamtNANKEKHFLKEEKNKLSQELSTVATEKNKMAG 790
                          570
                   ....*....|....*
gi 2024434935  835 LLEAKEREVSGLHQK 849
Cdd:pfam15921  791 ELEVLRSQERRLKEK 805
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
86-231 5.78e-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: 5.78e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  86 GHSAL-HLAVKNSHIDCIKRLLQYKCSVYStdnsGKTALHyAATCGCLQAVQLLCEHKCPINMKDLD------------- 151
Cdd:TIGR00870  52 GRSALfVAAIENENLELTELLLNLSCRGAV----GDTLLH-AISLEYVDAVEAILLHLLAAFRKSGPlelandqytseft 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 152 -GNIPLLLAVQNGHTEVCKYLLDHGADINTRDK--------------NGRTALMIACEAGSLNMVEVFLRKGADVSLVDV 216
Cdd:TIGR00870 127 pGITALHLAAHRQNYEIVKLLLERGASVPARACgdffvksqgvdsfyHGESPLNAAACLGSPSIVALLSEDPADILTADS 206
                         170
                  ....*....|....*.
gi 2024434935 217 FGQNALHYSKI-SENT 231
Cdd:TIGR00870 207 LGNTLLHLLVMeNEFK 222
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
317-611 1.47e-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: 45.82  E-value: 1.47e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  317 LQDNKDRLSDSTAGADSLLDVSSETEQQDLLMLMQAKIASLTLHNKELQDKLQERTPKEVDSTIDSYHStQREFDQTADR 396
Cdd:TIGR02168  700 LAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEE-RLEEAEEELA 778
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  397 QSEISAQELKSTLNATQSQ-----EKLTSPSEIkIKYLQEDSKDAQRKLENSETKRKHLEAQVQSRVPEADLNNTDISEN 471
Cdd:TIGR02168  779 EAEAEIEELEAQIEQLKEElkalrEALDELRAE-LTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESL 857
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  472 gSDPSLKIQETQSKYEEAAKEVLNAQKQVKPGLvssesEETCSELSKLKVTCEEVEMLRQELRRALEESERQKEKVRELQ 551
Cdd:TIGR02168  858 -AAEIEELEELIEELESELEALLNERASLEEAL-----ALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRL 931
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  552 KKFEEREQNVTSKLSVEECEELknsycsviDNINQEKALLIERYKEGQEEIKRLQDKLTN 611
Cdd:TIGR02168  932 EGLEVRIDNLQERLSEEYSLTL--------EEAEALENKIEDDEEEARRRLKRLENKIKE 983
14-3-3_fungi cd11309
Fungal 14-3-3 protein domain; This family containing fungal 14-3-3 domains includes the yeasts ...
533-671 8.00e-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: 39.21  E-value: 8.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 533 LRRALEESERQKEKVRELQKKFEEREqnvtsKLSVEECEELKNSYCSVI------------------DNINQEKALLIER 594
Cdd:cd11309     7 LAKLAEQAERYEEMVENMKKVASSDQ-----ELTVEERNLLSVAYKNVIgarraswrivssieqkeeSKGNESQVALIKE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 595 YKEGQE-EIKRLQDKLTN--QTHLESSAESGEMKDAMHRMIDELNRQLSELS---QLYKEAQAELEDYrkrKTLDDIAVD 668
Cdd:cd11309    82 YRSKIEsELTKICDDILSvlDKHLIPSATTGESKVFYYKMKGDYHRYLAEFAvgdKRKEAADSSLEAY---KAASDIAVT 158

                  ...
gi 2024434935 669 YIP 671
Cdd:cd11309   159 ELP 161
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1-237 2.60e-51

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 182.46  E-value: 2.60e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935   1 MKSLKAKFRKSDTNEWNKNDDRLLQAVENGDPEKVASLLGKKGASATKQDSEGKTAFHLAATKGHAECLRIMVTHGADVT 80
Cdd:COG0666    35 LLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVN 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  81 AQDGAGHSALHLAVKNSHIDCIKRLLQYKCSVYSTDNSGKTALHYAATCGCLQAVQLLCEHKCPINMKDLDGNIPLLLAV 160
Cdd:COG0666   115 ARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAA 194
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024434935 161 QNGHTEVCKYLLDHGADINTRDKNGRTALMIACEAGSLNMVEVFLRKGADVSLVDVFGQNALHYSKISENTGIQNLL 237
Cdd:COG0666   195 ENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLL 271
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1-237 1.10e-46

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 168.98  E-value: 1.10e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935   1 MKSLKAKFRKSDTNEWNKNDDRLLQAVENGDPEKVASLLGKKGASATKQDSEGKTAFHLAATKGHAECLRIMVTHGADVT 80
Cdd:COG0666     2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  81 AQDGAGHSALHLAVKNSHIDCIKRLLQYKCSVYSTDNSGKTALHYAATCGCLQAVQLLCEHKCPINMKDLDGNIPLLLAV 160
Cdd:COG0666    82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAA 161
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024434935 161 QNGHTEVCKYLLDHGADINTRDKNGRTALMIACEAGSLNMVEVFLRKGADVSLVDVFGQNALHYSKISENTGIQNLL 237
Cdd:COG0666   162 ANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLL 238
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
17-222 2.56e-43

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 159.35  E-value: 2.56e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  17 NKNDDRLLQAVENGDPEKVASLLgKKGASATKQDSEGKTAFHLAATKGHAECLRIMVTHGADVTAQDGAGHSALHLAVKN 96
Cdd:COG0666    85 DGGNTLLHAAARNGDLEIVKLLL-EAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAAN 163
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  97 SHIDCIKRLLQYKCSVYSTDNSGKTALHYAATCGCLQAVQLLCEHKCPINMKDLDGNIPLLLAVQNGHTEVCKYLLDHGA 176
Cdd:COG0666   164 GNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGA 243
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2024434935 177 DINTRDKNGRTALMIACEAGSLNMVEVFLRKGADVSLVDVFGQNAL 222
Cdd:COG0666   244 DLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
33-237 8.68e-35

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 134.70  E-value: 8.68e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  33 EKVASLLGKKGASATKQDSEGKTAFHLAATKGHAECLRIMVTHGADVTAQDGAGHSALHLAVKNSHIDCIKRLLQYKCSV 112
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 113 YSTDNSGKTALHYAATCGCLQAVQLLCEHKCPINMKDLDGNIPLLLAVQNGHTEVCKYLLDHGADINTRDKNGRTALMIA 192
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2024434935 193 CEAGSLNMVEVFLRKGADVSLVDVFGQNALHYSKISENTGIQNLL 237
Cdd:COG0666   161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLL 205
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
12-189 4.12e-32

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 126.99  E-value: 4.12e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  12 DTNEWNKNDDRLLQ-AVENGDPEKVASLLgKKGASATKQDSEGKTAFHLAATKGHAECLRIMVTHGADVTAQDGAGHSAL 90
Cdd:COG0666   112 DVNARDKDGETPLHlAAYNGNLEIVKLLL-EAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPL 190
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  91 HLAVKNSHIDCIKRLLQYKCSVYSTDNSGKTALHYAATCGCLQAVQLLCEHKCPINMKDLDGNIPLLLAVQNGHTEVCKY 170
Cdd:COG0666   191 HLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKL 270
                         170
                  ....*....|....*....
gi 2024434935 171 LLDHGADINTRDKNGRTAL 189
Cdd:COG0666   271 LLLALLLLAAALLDLLTLL 289
Ank_2 pfam12796
Ankyrin repeats (3 copies);
90-182 5.98e-26

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 102.50  E-value: 5.98e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  90 LHLAVKNSHIDCIKRLLQYKCSVYSTDNSGKTALHYAATCGCLQAVQLLCEHkCPINMKDlDGNIPLLLAVQNGHTEVCK 169
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78
                          90
                  ....*....|...
gi 2024434935 170 YLLDHGADINTRD 182
Cdd:pfam12796  79 LLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
123-215 2.53e-23

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 94.80  E-value: 2.53e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 123 LHYAATCGCLQAVQLLCEHKCPINMKDLDGNIPLLLAVQNGHTEVCKYLLDHgADINTRDkNGRTALMIACEAGSLNMVE 202
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78
                          90
                  ....*....|...
gi 2024434935 203 VFLRKGADVSLVD 215
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
23-237 1.36e-22

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 101.67  E-value: 1.36e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  23 LLQAVENGDPEKVASLLgKKGASATKQDSEGKTAFHLAATKGHA-----ECLRIMVTHGADVTAQDGAGHSALHLAVKNS 97
Cdd:PHA03100   39 LYLAKEARNIDVVKILL-DNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAISKK 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  98 --HIDCIKRLLQYKCSVYSTDNSGKTALHYAATCGC--LQAVQLLCEHKCPINMKDldgniplllavqnghteVCKYLLD 173
Cdd:PHA03100  118 snSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVDINAKN-----------------RVNYLLS 180
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024434935 174 HGADINTRDKNGRTALMIACEAGSLNMVEVFLRKGADVSLVDVFGQNALHYSKISENTGIQNLL 237
Cdd:PHA03100  181 YGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLL 244
PHA03100 PHA03100
ankyrin repeat protein; Provisional
1-215 2.51e-22

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 100.89  E-value: 2.51e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935   1 MKSLKAKFRKS-DTNEWNKNDDRLL------QAVENGDPEkVASLLGKKGASATKQDSEGKTAFHLAATK--GHAECLRI 71
Cdd:PHA03100   48 IDVVKILLDNGaDINSSTKNNSTPLhylsniKYNLTDVKE-IVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEY 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  72 MVTHGADVTAQDGAGHSALHLAVKNSHID--CIKRLLQYKCSVYSTDNsgktalhyaatcgclqaVQLLCEHKCPINMKD 149
Cdd:PHA03100  127 LLDNGANVNIKNSDGENLLHLYLESNKIDlkILKLLIDKGVDINAKNR-----------------VNYLLSYGVPINIKD 189
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024434935 150 LDGNIPLLLAVQNGHTEVCKYLLDHGADINTRDKNGRTALMIACEAGSLNMVEVFLRKGADVSLVD 215
Cdd:PHA03100  190 VYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTII 255
Ank_2 pfam12796
Ankyrin repeats (3 copies);
57-149 6.39e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 90.95  E-value: 6.39e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  57 FHLAATKGHAECLRIMVTHGADVTAQDGAGHSALHLAVKNSHIDCIKRLLQYKCSvySTDNSGKTALHYAATCGCLQAVQ 136
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVK 78
                          90
                  ....*....|...
gi 2024434935 137 LLCEHKCPINMKD 149
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
12-224 1.59e-20

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 95.86  E-value: 1.59e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  12 DTNEWNKNDDRLLQA---VENGDPeKVASLLGKKGASATKQDSEGKTAFH--LAATKGHAECLRIMVTHGADVTAQDGAG 86
Cdd:PHA03095  109 DVNAKDKVGRTPLHVylsGFNINP-KVIRLLLRKGADVNALDLYGMTPLAvlLKSRNANVELLRLLIDAGADVYAVDDRF 187
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  87 HSALHLAVKNSHID--CIKRLLQYKCSVYSTDNSGKTALHYAAT---CGCLQAVQLLcEHKCPINMKDLDGNIPLLLAVQ 161
Cdd:PHA03095  188 RSLLHHHLQSFKPRarIVRELIRAGCDPAATDMLGNTPLHSMATgssCKRSLVLPLL-IAGISINARNRYGQTPLHYAAV 266
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024434935 162 NGHTEVCKYLLDHGADINTRDKNGRTALMIACEAGSLNMVEVFLRKGADVSLVDvfgqNALHY 224
Cdd:PHA03095  267 FNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETVA----ATLNT 325
PHA02875 PHA02875
ankyrin repeat protein; Provisional
38-214 3.92e-19

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 91.21  E-value: 3.92e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  38 LLGKKGASATKQDSEGKTAFHLAATKGHA---ECLRIMVTHGADVTAQDGagHSALHLAVKNSHIDCIKRLLQYKCS--V 112
Cdd:PHA02875   53 LLMKHGAIPDVKYPDIESELHDAVEEGDVkavEELLDLGKFADDVFYKDG--MTPLHLATILKKLDIMKLLIARGADpdI 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 113 YSTDNSgkTALHYAATCGCLQAVQLLCEHKCPINMKDLDGNIPLLLAVQNGHTEVCKYLLDHGADINTRDKNGRTALM-I 191
Cdd:PHA02875  131 PNTDKF--SPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALcY 208
                         170       180
                  ....*....|....*....|...
gi 2024434935 192 ACEAGSLNMVEVFLRKGADVSLV 214
Cdd:PHA02875  209 AIENNKIDIVRLFIKRGADCNIM 231
PHA03095 PHA03095
ankyrin-like protein; Provisional
29-232 6.97e-19

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 90.85  E-value: 6.97e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  29 NGDPEKVASLLGKKGASATKQDSEGKTAFHLAATKGH-AECLRIMVTHGADVTAQDGAGHSALH--LAVKNSHIDCIKRL 105
Cdd:PHA03095   59 SEKVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATtLDVIKLLIKAGADVNAKDKVGRTPLHvyLSGFNINPKVIRLL 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 106 LQYKCSVYSTDNSGKTALH-YAATCGC-LQAVQLLCEHKCPINMKDLDGNIPLLLAVQNGHT--EVCKYLLDHGADINTR 181
Cdd:PHA03095  139 LRKGADVNALDLYGMTPLAvLLKSRNAnVELLRLLIDAGADVYAVDDRFRSLLHHHLQSFKPraRIVRELIRAGCDPAAT 218
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2024434935 182 DKNGRTALMIACEAGSLNMVEV--FLRKGADVSLVDVFGQNALHYSKISENTG 232
Cdd:PHA03095  219 DMLGNTPLHSMATGSSCKRSLVlpLLIAGISINARNRYGQTPLHYAAVFNNPR 271
Ank_2 pfam12796
Ankyrin repeats (3 copies);
23-116 4.02e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 80.16  E-value: 4.02e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  23 LLQAVENGDPEKVASLLgKKGASATKQDSEGKTAFHLAATKGHAECLRIMVTHgADVTAQDGaGHSALHLAVKNSHIDCI 102
Cdd:pfam12796   1 LHLAAKNGNLELVKLLL-ENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIV 77
                          90
                  ....*....|....
gi 2024434935 103 KRLLQYKCSVYSTD 116
Cdd:pfam12796  78 KLLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
66-224 2.63e-17

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 85.85  E-value: 2.63e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  66 AECLRIMVTHGADVTAQDGAGHSALHLAVKNSHIDC---IKRLLQYKCSVYSTDNSGKTALHYAATCGC-LQAVQLLCEH 141
Cdd:PHA03095   27 VEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVkdiVRLLLEAGADVNAPERCGFTPLHLYLYNATtLDVIKLLIKA 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 142 KCPINMKDLDGNIPL--LLAVQNGHTEVCKYLLDHGADINTRDKNGRTALMIACEAG--SLNMVEVFLRKGADVSLVDVF 217
Cdd:PHA03095  107 GADVNAKDKVGRTPLhvYLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRnaNVELLRLLIDAGADVYAVDDR 186

                  ....*..
gi 2024434935 218 GQNALHY 224
Cdd:PHA03095  187 FRSLLHH 193
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
1-189 1.33e-16

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 84.92  E-value: 1.33e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935   1 MKSLKAKFRKSDTNEWNKN---DDRLLQAVENGDPEKVASLLgKKGASATKQDSEGKTAFHLAATKGHAECLRIMVTHGA 77
Cdd:PLN03192  504 LHDLNVGDLLGDNGGEHDDpnmASNLLTVASTGNAALLEELL-KAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHAC 582
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  78 DVTAQDGAGHSALHLAVKNSHiDCIKRLLqYKCSVYSTDNSGKTALHYAATCGCLQAVQLLCEHKCPINMKDLDGNIPLL 157
Cdd:PLN03192  583 NVHIRDANGNTALWNAISAKH-HKIFRIL-YHFASISDPHAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQ 660
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2024434935 158 LAVQNGHTEVCKYLLDHGADI---NTRDKNGRTAL 189
Cdd:PLN03192  661 VAMAEDHVDMVRLLIMNGADVdkaNTDDDFSPTEL 695
Ank_2 pfam12796
Ankyrin repeats (3 copies);
156-248 1.95e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 75.15  E-value: 1.95e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 156 LLLAVQNGHTEVCKYLLDHGADINTRDKNGRTALMIACEAGSLNMVEVFLRKgADVSLVDvFGQNALHYSKISENTGI-Q 234
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIvK 78
                          90
                  ....*....|....
gi 2024434935 235 NLLSSKIsqDVDAK 248
Cdd:pfam12796  79 LLLEKGA--DINVK 90
PHA02876 PHA02876
ankyrin repeat protein; Provisional
31-237 1.08e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 81.65  E-value: 1.08e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  31 DPEKVASLLGKKGASATKQDSEGKTAFHLAATKGHAECLRIMVTHGADVTAQDGAGHSALHLAVKNSHIDCIK------- 103
Cdd:PHA02876  156 DELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKaiidnrs 235
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 104 --------------------RLLQYKC--SVYSTDNSGKTALHYAATCGCL-QAVQLLCEHKCPINMKDLDGNIPLLLAV 160
Cdd:PHA02876  236 ninkndlsllkairnedletSLLLYDAgfSVNSIDDCKNTPLHHASQAPSLsRLVPKLLERGADVNAKNIKGETPLYLMA 315
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 161 QNGH-TEVCKYLLDHGADINTRDKNGRTALMiacEAGSL----NMVEVFLRKGADVSLVDVFGQNALHYSKISENTGIQN 235
Cdd:PHA02876  316 KNGYdTENIRTLIMLGADVNAADRLYITPLH---QASTLdrnkDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIIN 392

                  ..
gi 2024434935 236 LL 237
Cdd:PHA02876  393 TL 394
PHA02874 PHA02874
ankyrin repeat protein; Provisional
3-250 2.19e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 79.62  E-value: 2.19e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935   3 SLKAKFRKSDTNEWNKNDDR----LLQAVENGDPeKVASLLGKKGASATKQDSEGKTAFHLAATKGHAECLRIMVTHGAD 78
Cdd:PHA02874   15 EAIEKIIKNKGNCINISVDEtttpLIDAIRSGDA-KIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVD 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  79 VTAqdgaghsalhLAVKNSHIDCIKRLLQYKCSVYSTDNSGKTALHYAATCGCLQAVQLLCEHKCPINMKDLDGNIPLLL 158
Cdd:PHA02874   94 TSI----------LPIPCIEKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHI 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 159 AVQNGHTEVCKYLLDHGADINTRDKNGRTALMIACEAGSLNMVEVFLRKGADVSLVDVFGQNALHYSKISENTGIQNLLS 238
Cdd:PHA02874  164 AIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRSAIELLIN 243
                         250
                  ....*....|....
gi 2024434935 239 SKI--SQDVDAKSP 250
Cdd:PHA02874  244 NASinDQDIDGSTP 257
PHA02874 PHA02874
ankyrin repeat protein; Provisional
43-192 7.88e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 78.08  E-value: 7.88e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  43 GASATKQDSEGKTAFHLAATKGHAECLRIMVTHGADVTAQDGAGHSALHLAVKNSHIDCIKRLLQYKCSVYSTDNSGKTA 122
Cdd:PHA02874  114 GIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESP 193
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 123 LHYAATCGCLQAVQLLCEH------KC-------------------------PINMKDLDGNIPLLLAVQNG-HTEVCKY 170
Cdd:PHA02874  194 LHNAAEYGDYACIKLLIDHgnhimnKCkngftplhnaiihnrsaiellinnaSINDQDIDGSTPLHHAINPPcDIDIIDI 273
                         170       180
                  ....*....|....*....|..
gi 2024434935 171 LLDHGADINTRDKNGRTALMIA 192
Cdd:PHA02874  274 LLYHKADISIKDNKGENPIDTA 295
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
524-899 3.15e-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: 74.32  E-value: 3.15e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  524 EEVEMLRQELRRALEESERQKEKVRELQKKFEEREQnvtsklsveeceelknsycsvidninQEKALLIERYKEGQEEIK 603
Cdd:TIGR02168  189 DRLEDILNELERQLKSLERQAEKAERYKELKAELRE--------------------------LELALLVLRLEELREELE 242
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  604 RLQDKLTNQTHLESSAESGemKDAMHRMIDELNRQLSELSQLYKEAQAELEDYRKRktlddiavdyIPRDEHEKlmQVTN 683
Cdd:TIGR02168  243 ELQEELKEAEEELEELTAE--LQELEEKLEELRLEVSELEEEIEELQKELYALANE----------ISRLEQQK--QILR 308
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  684 SLKYKAENELLEMKSQYTKVLDEAEELKQMLDTQKQNslpIAEHQQVMNALRSTVKEMEEEINELKELLTNKESEVRNLQ 763
Cdd:TIGR02168  309 ERLANLERQLEELEAQLEELESKLDELAEELAELEEK---LEELKEELESLEAELEELEAELEELESRLEELEEQLETLR 385
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  764 KELLEEKAAINEAMVPRAAYEKLQSSLEGEVSILSSKLKDVIKEKENVSLDvmQLRSEVLHLKEEKEGMHNLLEAKEREV 843
Cdd:TIGR02168  386 SKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELK--ELQAELEELEEELEELQEELERLEEAL 463
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2024434935  844 SGLHQKYHQAQEDLLEMKRYSESSSKLEEDKDKKINEMSKEVSKLKEALNSLSQLS 899
Cdd:TIGR02168  464 EELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLS 519
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
403-898 6.93e-13

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 72.79  E-value: 6.93e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 403 QELKSTLNATQSQEKLTSPSEIKIKYLQEDSKDAQRKLENSETKRKHLEAQVQsRVPEadlnntdisengsdpslkIQET 482
Cdd:PRK03918  231 KELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVK-ELKE------------------LKEK 291
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 483 QSKYEEAAKEvlnaqkqvkpglvsseSEETCSELSKLKVTCEEVEMLRQELRRALEESERQKEKVRELQKKFEEREQNV- 561
Cdd:PRK03918  292 AEEYIKLSEF----------------YEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLe 355
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 562 ----------TSKLSVEECEELKNSY-CSVIDNINQEKALLIERYKEGQEEIKRLQDKLTNqthLESsaESGEMKDAMHR 630
Cdd:PRK03918  356 eleerhelyeEAKAKKEELERLKKRLtGLTPEKLEKELEELEKAKEEIEEEISKITARIGE---LKK--EIKELKKAIEE 430
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 631 M----------------------IDELNRQLSELSQLYKEAQAELEDYRKRKTLDDIAVDYIPR-----DEHEKLMQVTN 683
Cdd:PRK03918  431 LkkakgkcpvcgrelteehrkelLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESEliklkELAEQLKELEE 510
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 684 SLKYKAENELLEMKSQYTKVLDEAEELKQMLDTQKQNSLPIAEHQQVMNALRSTVKEMEEEINEL-KELLTNKESEVRNL 762
Cdd:PRK03918  511 KLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELlKELEELGFESVEEL 590
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 763 QKELLEEKAAINEAMVPRAAYEKLQSSLEgEVSILSSKLKDVIKEKENVSLDVMQLRSEVLHLK-----EEKEGMHNLLE 837
Cdd:PRK03918  591 EERLKELEPFYNEYLELKDAEKELEREEK-ELKKLEEELDKAFEELAETEKRLEELRKELEELEkkyseEEYEELREEYL 669
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024434935 838 AKEREVSGLHQKYHQAQEDLLEMKRYSEsssKLEEDKdKKINEMSKEVSKLKEALNSLSQL 898
Cdd:PRK03918  670 ELSRELAGLRAELEELEKRREEIKKTLE---KLKEEL-EEREKAKKELEKLEKALERVEEL 726
Ank_4 pfam13637
Ankyrin repeats (many copies);
155-205 3.17e-12

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 61.91  E-value: 3.17e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2024434935 155 PLLLAVQNGHTEVCKYLLDHGADINTRDKNGRTALMIACEAGSLNMVEVFL 205
Cdd:pfam13637   4 ALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
524-861 6.71e-12

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 69.58  E-value: 6.71e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 524 EEVEMLRQELRRALEESERQKE---KVRELQKKFEEREQNVTSKlsveeceelknsycsVIDNINQEKALLIERYKEGQE 600
Cdd:COG1196   189 ERLEDILGELERQLEPLERQAEkaeRYRELKEELKELEAELLLL---------------KLRELEAELEELEAELEELEA 253
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 601 EIKRLQdklTNQTHLESSAESGEMKdamhrmIDELNRQLSELSQLYKEAQAELEDYRKRKTLDDIAVdyipRDEHEKLMQ 680
Cdd:COG1196   254 ELEELE---AELAELEAELEELRLE------LEELELELEEAQAEEYELLAELARLEQDIARLEERR----RELEERLEE 320
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 681 VTNSLKyKAENELLEMKSQYTKVLDEAEELKQMLDTQKQNslpIAEHQQVMNALRSTVKEMEEEINELKELLTNKESEVR 760
Cdd:COG1196   321 LEEELA-ELEEELEELEEELEELEEELEEAEEELEEAEAE---LAEAEEALLEAEAELAEAEEELEELAEELLEALRAAA 396
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 761 NLQKELLEEKAAINEAmvpraayEKLQSSLEGEVSILSSKLKDVIKEKENVSLDVMQLRSEVLHLKEEKEGMHNLLEAKE 840
Cdd:COG1196   397 ELAAQLEELEEAEEAL-------LERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELL 469
                         330       340
                  ....*....|....*....|.
gi 2024434935 841 REVSGLHQKYHQAQEDLLEMK 861
Cdd:COG1196   470 EEAALLEAALAELLEELAEAA 490
PHA02878 PHA02878
ankyrin repeat protein; Provisional
34-192 7.07e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 68.75  E-value: 7.07e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  34 KVASLLGKKGASATKQD-SEGKTAFHLAATKGHAECLRIMVTHGADVTAQDGAGHSALHLAVKNSHIDCIKRLLQYKCSV 112
Cdd:PHA02878  148 EITKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGAST 227
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 113 YSTDNSGKTALHYA-ATCGCLQAVQLLCEHKCPINMKD-LDGNIPLLLAVQNghTEVCKYLLDHGADINTRDKNGRTALM 190
Cdd:PHA02878  228 DARDKCGNTPLHISvGYCKDYDILKLLLEHGVDVNAKSyILGLTALHSSIKS--ERKLKLLLEYGADINSLNSYKLTPLS 305

                  ..
gi 2024434935 191 IA 192
Cdd:PHA02878  306 SA 307
PHA02876 PHA02876
ankyrin repeat protein; Provisional
9-247 7.56e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 69.32  E-value: 7.56e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935   9 RKSDTNEWN-KNDDRLLQAVENG-DPEKVASLLgKKGASATKQDSEGKTAFHLAAT-KGHAECLRIMVTHGADVTAQDGA 85
Cdd:PHA02876  296 RGADVNAKNiKGETPLYLMAKNGyDTENIRTLI-MLGADVNAADRLYITPLHQASTlDRNKDIVITLLELGANVNARDYC 374
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  86 GHSALHLAVKNSHIDCIKRLLQYKCSVYSTDNSGKTALHYAaTCGC--LQAVQLLCEHKCPINMKDLDGNIPLLLAVQNG 163
Cdd:PHA02876  375 DKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFA-LCGTnpYMSVKTLIDRGANVNSKNKDLSTPLHYACKKN 453
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 164 -HTEVCKYLLDHGADINTRDKNGRTALMIACEAGSLnmVEVFLRKGADVS----LVDVFGQNALHYSKISENTGIQNLLS 238
Cdd:PHA02876  454 cKLDVIEMLLDNGADVNAINIQNQYPLLIALEYHGI--VNILLHYGAELRdsrvLHKSLNDNMFSFRYIIAHICIQDFIR 531

                  ....*....
gi 2024434935 239 SKISQDVDA 247
Cdd:PHA02876  532 HDIRNEVNP 540
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
424-889 9.34e-12

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 69.32  E-value: 9.34e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 424 IKIKYLQEDSKDAQRKLENSETKRKHLEAQVQSRVPEADLNNTDISEngsdPSLKIQETQSKYEEAAK--EVLNAQKQVK 501
Cdd:PRK03918  296 IKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEE----LKKKLKELEKRLEELEErhELYEEAKAKK 371
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 502 PGLVSSESEETCSELSKLKVTCEEVEMLRQELRRALEESerqKEKVRELQKKFEEREQNVTS-------------KLSVE 568
Cdd:PRK03918  372 EELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKI---TARIGELKKEIKELKKAIEElkkakgkcpvcgrELTEE 448
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 569 ECEELKNSYCSVIDNINQEKALLIERYKEGQEEIKRLQDKLTNQTHLESsaesgemkdaMHRMIDELNRQLSELSQLYKE 648
Cdd:PRK03918  449 HRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIK----------LKELAEQLKELEEKLKKYNLE 518
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 649 -AQAELEDYRK-RKTLDDIAVDYIPRDEHEKLMQVTNSLKYKAENELLEMKSQYTKVLDEAEELKqmldtqkqnslpiae 726
Cdd:PRK03918  519 eLEKKAEEYEKlKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELG--------------- 583
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 727 hqqvmnalRSTVKEMEEEINELKEL------LTNKESEVRNLQKELLEEKAAINEAMVPRAAYEKLQSSLEGEVSILSSK 800
Cdd:PRK03918  584 --------FESVEELEERLKELEPFyneyleLKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKK 655
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 801 LKDviKEKENVSLDVMQLRSEVLHLKEEKEGMHNLLEAKEREVSGLhqkyhqaQEDLLEMKRYSESSSKLEEDKDkKINE 880
Cdd:PRK03918  656 YSE--EEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKL-------KEELEEREKAKKELEKLEKALE-RVEE 725

                  ....*....
gi 2024434935 881 MSKEVSKLK 889
Cdd:PRK03918  726 LREKVKKYK 734
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
451-935 2.41e-11

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 67.78  E-value: 2.41e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 451 EAQVQSRVPEADLNNTDISENGSDPSLKIQETQSKYEEAAKEVLNAQKqvkpglVSSESEETCSELSKLKVTCEEVEMLR 530
Cdd:PRK03918  188 TENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEE------LKEEIEELEKELESLEGSKRKLEEKI 261
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 531 QELRRALEESerqKEKVRELQKKFEEREQNVTSKLSVEECEELKNSYCSVIDNINQEKALLIERYKEGQEEIKRLQDKlt 610
Cdd:PRK03918  262 RELEERIEEL---KKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEK-- 336
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 611 nqthlesSAESGEMKDAMHRMIDELNRqLSELSQLYKEA---QAELEDYRKRKTLDDIavdyiprDEHEKLMQVTNSLKY 687
Cdd:PRK03918  337 -------EERLEELKKKLKELEKRLEE-LEERHELYEEAkakKEELERLKKRLTGLTP-------EKLEKELEELEKAKE 401
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 688 KAENELLEMKSQYTKVLDEAEELKQMLDTQKQNSL-------PIAEHQQ--VMNALRSTVKEMEEEINELKELLTNKESE 758
Cdd:PRK03918  402 EIEEEISKITARIGELKKEIKELKKAIEELKKAKGkcpvcgrELTEEHRkeLLEEYTAELKRIEKELKEIEEKERKLRKE 481
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 759 VRNLQKELLEEKAAINEamvpRAAYEKLQSSLEGEVSILSSKLKDVIKEKENVSLDVMQLRSEVLHLKEEKEGmhnlLEA 838
Cdd:PRK03918  482 LRELEKVLKKESELIKL----KELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEK----LEE 553
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 839 KEREVSGLHQKYHQAQEDLLEMKRysesssKLEEDKDKKINEMSKEVSKLKEALNSLSQLSYSTSAPKRQSQQLEALQQQ 918
Cdd:PRK03918  554 LKKKLAELEKKLDELEEELAELLK------ELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEE 627
                         490
                  ....*....|....*..
gi 2024434935 919 VKQLQNQLTETKKQHQE 935
Cdd:PRK03918  628 LDKAFEELAETEKRLEE 644
Ank_4 pfam13637
Ankyrin repeats (many copies);
121-172 5.10e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 58.83  E-value: 5.10e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2024434935 121 TALHYAATCGCLQAVQLLCEHKCPINMKDLDGNIPLLLAVQNGHTEVCKYLL 172
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
86-138 3.02e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 56.51  E-value: 3.02e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2024434935  86 GHSALHLAVKNSHIDCIKRLLQYKCSVYSTDNSGKTALHYAATCGCLQAVQLL 138
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
581-895 3.10e-10

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 64.31  E-value: 3.10e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  581 IDNINQEKALLIERYKEGQEEIKRLQDKLTNQThlessaesgEMKDAMHRMIDELNRQLSELSQLYKEAQAELEDYRKRK 660
Cdd:TIGR02168  679 IEELEEKIEELEEKIAELEKALAELRKELEELE---------EELEQLRKELEELSRQISALRKDLARLEAEVEQLEERI 749
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  661 TLDDIAVdyiprdeheklmqvtnslkykaeNELLEMKSQYTKVLDEA-EELKQMLDTQKQNSLPIAEHQQVMNALRSTVK 739
Cdd:TIGR02168  750 AQLSKEL-----------------------TELEAEIEELEERLEEAeEELAEAEAEIEELEAQIEQLKEELKALREALD 806
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  740 EMEEEINELKELLTNKESEVRNLQK----------ELLEEKAAINEAMvprAAYEKLQSSLEGEVSILSSKLKDVIKEKE 809
Cdd:TIGR02168  807 ELRAELTLLNEEAANLRERLESLERriaaterrleDLEEQIEELSEDI---ESLAAEIEELEELIEELESELEALLNERA 883
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  810 NVSLDVMQLRSEVLHLKEEKEGMHNLLEAKEREVSGLHQKYHQAQEDLLEMK------------RYS---ESSSKLEEDK 874
Cdd:TIGR02168  884 SLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEvridnlqerlseEYSltlEEAEALENKI 963
                          330       340
                   ....*....|....*....|.
gi 2024434935  875 DKKINEMSKEVSKLKEALNSL 895
Cdd:TIGR02168  964 EDDEEEARRRLKRLENKIKEL 984
Ank_5 pfam13857
Ankyrin repeats (many copies);
171-224 4.30e-10

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 56.20  E-value: 4.30e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2024434935 171 LLDHG-ADINTRDKNGRTALMIACEAGSLNMVEVFLRKGADVSLVDVFGQNALHY 224
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDL 55
Ank_4 pfam13637
Ankyrin repeats (many copies);
55-106 1.18e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 54.97  E-value: 1.18e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2024434935  55 TAFHLAATKGHAECLRIMVTHGADVTAQDGAGHSALHLAVKNSHIDCIKRLL 106
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
518-888 6.35e-09

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 60.07  E-value: 6.35e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  518 KLKVTCEEVEMLRQELRRALEESERQKEKVRELQKKFEEREQNVTSKLS-----VEECEELKNSYCSVIDNINQEKALLI 592
Cdd:TIGR02168  702 ELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAqlskeLTELEAEIEELEERLEEAEEELAEAE 781
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  593 ERYKEGQEEIKRLQDKLTNQThlessaesgemkdamhRMIDELNRQLSELSQLYKEAQAELEDYRKRKtlddiavdyipr 672
Cdd:TIGR02168  782 AEIEELEAQIEQLKEELKALR----------------EALDELRAELTLLNEEAANLRERLESLERRI------------ 833
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  673 DEHEKLMQVTNSLKYKAENELLEMKSQytkVLDEAEELKQMLDTQKQNSLPIAEHQQVMNALRSTVKEMEEEINELKELL 752
Cdd:TIGR02168  834 AATERRLEDLEEQIEELSEDIESLAAE---IEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKR 910
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  753 TNKESEVRNLQKELLEEKAAINEAMVPRAayeKLQSSLEGEVSILsskLKDVIKEKENVSLDVMQLRSEVLHLKEEKEGM 832
Cdd:TIGR02168  911 SELRRELEELREKLAQLELRLEGLEVRID---NLQERLSEEYSLT---LEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2024434935  833 HNL-LEAKE--REVSGLHQKYHQAQEDLLEMKRysesssKLEEdkdkKINEMSKEVSKL 888
Cdd:TIGR02168  985 GPVnLAAIEeyEELKERYDFLTAQKEDLTEAKE------TLEE----AIEEIDREARER 1033
PTZ00121 PTZ00121
MAEBL; Provisional
402-892 6.93e-09

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 60.15  E-value: 6.93e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  402 AQELKSTLNATQSQEKLTSPSEIKIKYLQEDSKDAQRKLENSETKRKHLEAQVQSRvpEADLNNTDISENGSDPSLKIQE 481
Cdd:PTZ00121  1311 AEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKA--EAAEKKKEEAKKKADAAKKKAE 1388
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  482 TQSKYEEAAKEvlnAQKQVKPGLVSSESEETCSELSKLKVTCEEVEMlRQELRRALEEserqKEKVRELQKKFEEREQNV 561
Cdd:PTZ00121  1389 EKKKADEAKKK---AEEDKKKADELKKAAAAKKKADEAKKKAEEKKK-ADEAKKKAEE----AKKADEAKKKAEEAKKAE 1460
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  562 TSKLSVEE---CEELKNsycsvidniNQEKALLIERYKEGQEEIKRLQDKLTNQTHLESSAEsgEMKDAMHRMIDELNRQ 638
Cdd:PTZ00121  1461 EAKKKAEEakkADEAKK---------KAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKAD--EAKKAEEAKKADEAKK 1529
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  639 LSELSQLYKEAQAEledyRKRKTlddiavdyiprDEHEKLMQVTNSLKYKAENELLEMKSQYTKVLDEAEELKQMLDTQK 718
Cdd:PTZ00121  1530 AEEAKKADEAKKAE----EKKKA-----------DELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARI 1594
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  719 QNSLPIAEHQQVMNALR-----------STVKEMEEEINELKELLTNKESEVR---NLQKEllEEKAAINEAMVPRAAYE 784
Cdd:PTZ00121  1595 EEVMKLYEEEKKMKAEEakkaeeakikaEELKKAEEEKKKVEQLKKKEAEEKKkaeELKKA--EEENKIKAAEEAKKAEE 1672
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  785 KLQSSLEGEVSILSSKLK-DVIKEKENVSLDVMQLRSEVlhlKEEKEGMHNLLEAKEREVSGLHQKYHQAQEDllemKRY 863
Cdd:PTZ00121  1673 DKKKAEEAKKAEEDEKKAaEALKKEAEEAKKAEELKKKE---AEEKKKAEELKKAEEENKIKAEEAKKEAEED----KKK 1745
                          490       500
                   ....*....|....*....|....*....
gi 2024434935  864 SESSSKLEEDKdKKINEMSKEVSKLKEAL 892
Cdd:PTZ00121  1746 AEEAKKDEEEK-KKIAHLKKEEEKKAEEI 1773
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
683-937 7.28e-09

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 60.07  E-value: 7.28e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  683 NSLKYKAE--NELLEMKSQYTKV-----LDEAEELKQMLDTQKQNslpIAEHQQVMNALRSTVKEMEEEINELKELLTNK 755
Cdd:TIGR02168  203 KSLERQAEkaERYKELKAELRELelallVLRLEELREELEELQEE---LKEAEEELEELTAELQELEEKLEELRLEVSEL 279
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  756 ESEVRNLQKELLEEKAAINEAMVPRAAYEKLQSSLEGEVSILSSKLKDVIKEKENVSLDVMQLRSEVLHLKEEKEGMHNL 835
Cdd:TIGR02168  280 EEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAE 359
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  836 LEAKEREVSGLHQKYHQAQEDLLEMKRYSESSSKLEEDKDKKINEMSKEVSKLKEALNSLSQlSYSTSAPKRQSQQLEAL 915
Cdd:TIGR02168  360 LEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQ-EIEELLKKLEEAELKEL 438
                          250       260
                   ....*....|....*....|..
gi 2024434935  916 QQQVKQLQNQLTETKKQHQETV 937
Cdd:TIGR02168  439 QAELEELEEELEELQEELERLE 460
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
19-191 8.01e-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: 8.01e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  19 NDDRLLQAVENGDPEKVASLLGKKGASATKQDSEGKTAFHLAATKGH-------AECLRIMVTHgaDVTAQDGAGHSALH 91
Cdd:cd22192    17 SESPLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNleaavvlMEAAPELVNE--PMTSDLYQGETALH 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  92 LAVKNSHIDCIKRLLQYKCSVYSTDNSGkTALHYAATCgclqavqlLC---EHkcpinmkdldgniPLLLAVQNGHTEVC 168
Cdd:cd22192    95 IAVVNQNLNLVRELIARGADVVSPRATG-TFFRPGPKN--------LIyygEH-------------PLSFAACVGNEEIV 152
                         170       180
                  ....*....|....*....|...
gi 2024434935 169 KYLLDHGADINTRDKNGRTALMI 191
Cdd:cd22192   153 RLLIEHGADIRAQDSLGNTVLHI 175
PHA02798 PHA02798
ankyrin-like protein; Provisional
35-256 9.14e-09

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 59.08  E-value: 9.14e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  35 VASLLGKKGASATKQDSEGKTAFHLAATKGH---AECLRIMVTHGADVTAQDGAGHSALHLAVKNSH---IDCIKRLLQY 108
Cdd:PHA02798   91 IVKILIENGADINKKNSDGETPLYCLLSNGYinnLEILLFMIENGADTTLLDKDGFTMLQVYLQSNHhidIEIIKLLLEK 170
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 109 KCSVYSTDNS-GKTALH----YAATCGCLQAVQLLCEHKCPINMKD-------LDGNIPLLLAVQNGHTEVCKYLLDHgA 176
Cdd:PHA02798  171 GVDINTHNNKeKYDTLHcyfkYNIDRIDADILKLFVDNGFIINKENkshkkkfMEYLNSLLYDNKRFKKNILDFIFSY-I 249
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 177 DINTRDKNGRTALMIACEAGSLNMVEVFLRKGADVSLVDVFGQNALHYSKISENTGIQN-LLSSKISQDVDAKSPTKVKQ 255
Cdd:PHA02798  250 DINQVDELGFNPLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCLFTAFENESKFIFNsILNKKPNKNTISYTYYKLRK 329

                  .
gi 2024434935 256 H 256
Cdd:PHA02798  330 H 330
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
526-878 1.01e-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: 1.01e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  526 VEMLRQELRRaLEESERQKEKVRELQKKFEEREQNVTSKlSVEECEELKNSYCSVIDNINQEKALLIERYKEGQEEIKRL 605
Cdd:TIGR02169  193 IDEKRQQLER-LRREREKAERYQALLKEKREYEGYELLK-EKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEI 270
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  606 QDKLtNQTHLESSAESGEMKDAMHRMIDELNRQLSELSQLYKEAQAELEDYRKRKTLDDIAVDYIpRDEHEKLmqvtnsl 685
Cdd:TIGR02169  271 EQLL-EELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKL-LAEIEEL------- 341
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  686 kykaENELLEMKSQYTKVLDEAEELKQMLDTQKQNslpIAEHQQVMNALRSTVKEMEEEINELKELLTNKESEVRNLQKE 765
Cdd:TIGR02169  342 ----EREIEEERKRRDKLTEEYAELKEELEDLRAE---LEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEE 414
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  766 LLEEKAAINEAmvpRAAYEklqsSLEGEVSILSSKLKDVIKEKENVSLDVMQLRSEVLHLKEEKEGMHNLLEAKEREVSG 845
Cdd:TIGR02169  415 LQRLSEELADL---NAAIA----GIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSK 487
                          330       340       350
                   ....*....|....*....|....*....|...
gi 2024434935  846 LHQKYHQAQEDLLEMKRYSESSSKLEEDKDKKI 878
Cdd:TIGR02169  488 LQRELAEAEAQARASEERVRGGRAVEEVLKASI 520
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
88-223 1.92e-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: 1.92e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  88 SALHLAVKNSHIDCIKRLLQYK-CSVYSTDNSGKTALHYAATCGCLQAVQLLCEhKCP--INM---KDL-DGNIPLLLAV 160
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLLKCPsCDLFQRGALGETALHVAALYDNLEAAVVLME-AAPelVNEpmtSDLyQGETALHIAV 97
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024434935 161 QNGHTEVCKYLLDHGADINT----------RDKN----GRTALMIACEAGSLNMVEVFLRKGADVSLVDVFGQNALH 223
Cdd:cd22192    98 VNQNLNLVRELIARGADVVSpratgtffrpGPKNliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLH 174
Ank_5 pfam13857
Ankyrin repeats (many copies);
72-126 2.84e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 50.81  E-value: 2.84e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2024434935  72 MVTHG-ADVTAQDGAGHSALHLAVKNSHIDCIKRLLQYKCSVYSTDNSGKTALHYA 126
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_5 pfam13857
Ankyrin repeats (many copies);
105-159 3.29e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 50.81  E-value: 3.29e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2024434935 105 LLQYK-CSVYSTDNSGKTALHYAATCGCLQAVQLLCEHKCPINMKDLDGNIPLLLA 159
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTZ00121 PTZ00121
MAEBL; Provisional
402-935 3.31e-08

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 57.84  E-value: 3.31e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  402 AQELKSTLNATQSQEKLTSPSEIKIKYLQEDSKDAQR--KLENSETKRKHLEAQVQSRVPEADLNNTDisENGSDPSLKI 479
Cdd:PTZ00121  1208 AEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKaeEERNNEEIRKFEEARMAHFARRQAAIKAE--EARKADELKK 1285
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  480 QETQSKYEEAAKevlnaQKQVKPGLVSSESEETCSELSKLKVTCEEVEMLRQELRRALEESERQKEKVRELQKKFEEREQ 559
Cdd:PTZ00121  1286 AEEKKKADEAKK-----AEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAE 1360
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  560 NVTSKlsvEECEELKNSYCSVIDNINQEKALLIERYKEGQ---EEIKRLQDKLTNQTHLESSAESGEMKDAMHRMIDELN 636
Cdd:PTZ00121  1361 AAEEK---AEAAEKKKEEAKKKADAAKKKAEEKKKADEAKkkaEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAK 1437
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  637 RQLSElSQLYKEAQAELEDYRKRKTLDDIAVDYIPRDEHEKLMQ---VTNSLKYKAEN-----ELLEMKSQYTKVLDE-- 706
Cdd:PTZ00121  1438 KKAEE-AKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEeakKADEAKKKAEEakkkaDEAKKAAEAKKKADEak 1516
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  707 -------AEELKQMLDTQKQNSLPIAEHQQVMNALRST--VKEMEE--EINELKELLTNKESEVRNLQKELLEEKAAINE 775
Cdd:PTZ00121  1517 kaeeakkADEAKKAEEAKKADEAKKAEEKKKADELKKAeeLKKAEEkkKAEEAKKAEEDKNMALRKAEEAKKAEEARIEE 1596
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  776 AMVPRAAYEKLQSSLEGEVSILSSKLKDVIKEKEnVSLDVMQLRSEVlhlKEEKEGMHNLLEAKEREVSGLHQKYHQAQE 855
Cdd:PTZ00121  1597 VMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEE-EKKKVEQLKKKE---AEEKKKAEELKKAEEENKIKAAEEAKKAEE 1672
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  856 DllemKRYSESSSKLEEDKDKKINEMSKEVSKLKEAlnslSQLSYSTSAPKRQSQQL----EALQQQVKQLQNQLTETKK 931
Cdd:PTZ00121  1673 D----KKKAEEAKKAEEDEKKAAEALKKEAEEAKKA----EELKKKEAEEKKKAEELkkaeEENKIKAEEAKKEAEEDKK 1744

                   ....
gi 2024434935  932 QHQE 935
Cdd:PTZ00121  1745 KAEE 1748
PHA02875 PHA02875
ankyrin repeat protein; Provisional
60-250 4.32e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 56.54  E-value: 4.32e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  60 AATKGHAECLRIMVTHGADVTAQDGAGHSALHLAVKNSHIDCIKRLLQYKCSVYSTDNSGKTALHYAATCGCLQAVQLLC 139
Cdd:PHA02875    9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 140 EHKCPINmkDL---DGNIPLLLAVQNGHTEVCKYLLDHGADINTRDKNGRTALMIACEAGSLNMVEVFLRKGADVSLVDV 216
Cdd:PHA02875   89 DLGKFAD--DVfykDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDC 166
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2024434935 217 FGQNALHYSKISENTGI-QNLLSSKISQDVDAKSP 250
Cdd:PHA02875  167 CGCTPLIIAMAKGDIAIcKMLLDSGANIDYFGKNG 201
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
102-247 4.92e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 56.83  E-value: 4.92e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 102 IKRLLQYKCSVYSTDNSGKTALHYAATcgclqavqllcehkcpinMKDLDGNIPLLLAVQ------NGHTEVCKYLLDHG 175
Cdd:PTZ00322   44 IARIDTHLEALEATENKDATPDHNLTT------------------EEVIDPVVAHMLTVElcqlaaSGDAVGARILLTGG 105
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024434935 176 ADINTRDKNGRTALMIACEAGSLNMVEVFLRKGADVSLVDVFGQNALHYSKISENTGIQNLLSSKISQDVDA 247
Cdd:PTZ00322  106 ADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFEL 177
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
630-854 6.66e-08

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 56.56  E-value: 6.66e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 630 RMIDELNRQLSELSQLYKEAQAELEDYRKRKTLDDIAvdyiprDEHEKLMQVTNSLkykaENELLEMKSQYTKVLDEAEE 709
Cdd:COG3206   175 KALEFLEEQLPELRKELEEAEAALEEFRQKNGLVDLS------EEAKLLLQQLSEL----ESQLAEARAELAEAEARLAA 244
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 710 LKQMLDtQKQNSLPIAEHQQVMNALRSTVKEMEEEINELKELLTNKESEVRNLQKELLEEKAAINEAMvpraayEKLQSS 789
Cdd:COG3206   245 LRAQLG-SGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEA------QRILAS 317
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024434935 790 LEGEVSILSSKLKDVIKEKEnvsldvmQLRSEVLHLKEEKEGMHNL---LEAKEREVSGLHQKYHQAQ 854
Cdd:COG3206   318 LEAELEALQAREASLQAQLA-------QLEARLAELPELEAELRRLereVEVARELYESLLQRLEEAR 378
PHA02875 PHA02875
ankyrin repeat protein; Provisional
52-220 9.81e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 55.38  E-value: 9.81e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  52 EGKTAFHLAATKGHAECLRIMVTHGADVTAQDGAGHSALHLAVKNSHIDCIKRLL---QYKCSVYSTDnsGKTALHYAAT 128
Cdd:PHA02875   34 DGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLdlgKFADDVFYKD--GMTPLHLATI 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 129 CGCLQAVQLLCEHKCPINMKDLDGNIPLLLAVQNGHTEVCKYLLDHGADINTRDKNGRTALMIACEAGSLNMVEVFLRKG 208
Cdd:PHA02875  112 LKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSG 191
                         170
                  ....*....|..
gi 2024434935 209 ADvslVDVFGQN 220
Cdd:PHA02875  192 AN---IDYFGKN 200
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
632-935 1.12e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 56.10  E-value: 1.12e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 632 IDELNRQLSELS------QLYKEAQAELEDYRKRKTLddiavdyiprdeheklmqvtnsLKYKAENELLEmksQYTKVLD 705
Cdd:COG1196   195 LGELERQLEPLErqaekaERYRELKEELKELEAELLL----------------------LKLRELEAELE---ELEAELE 249
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 706 EAEELKQMLDTQkqnslpIAEHQQVMNALRSTVKEMEEEINELKELLTNKESEVRNLQKELLEEKAAINEAMVPRAAYEK 785
Cdd:COG1196   250 ELEAELEELEAE------LAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEE 323
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 786 LQSSLEGEVSILSSKLKDVIKEKENVSLDVMQLRSEVLHLKEEKEGMHNLLEAKEREVSGLHQKYHQAQEDLLEMKRYSE 865
Cdd:COG1196   324 ELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLE 403
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 866 SSSKLEEDKDKKINEMSKEVSKLKEALNSLSQLSYSTSAPKRQSQQLEALQQQVKQLQNQLTETKKQHQE 935
Cdd:COG1196   404 ELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAA 473
Ank_5 pfam13857
Ankyrin repeats (many copies);
145-192 1.32e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 48.88  E-value: 1.32e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2024434935 145 INMKDLDGNIPLLLAVQNGHTEVCKYLLDHGADINTRDKNGRTALMIA 192
Cdd:pfam13857   9 LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_5 pfam13857
Ankyrin repeats (many copies);
38-93 3.01e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 48.11  E-value: 3.01e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2024434935  38 LLGKKGASATKQDSEGKTAFHLAATKGHAECLRIMVTHGADVTAQDGAGHSALHLA 93
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
342-895 3.08e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 54.56  E-value: 3.08e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 342 EQQDLLMLMQAKIASLTLHNKELQDKLQERTPKEVDSTIDSYHSTQREfDQTADRQSEISAQELKSTLNATQSQEKLTSP 421
Cdd:COG1196   217 ELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAE-LEAELEELRLELEELELELEEAQAEEYELLA 295
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 422 SEIK----IKYLQEDSKDAQRKLENSETKRKHLEAQVQSRVPEADLNNTDISENGSdpslKIQETQSKYEEAAKEVLNAQ 497
Cdd:COG1196   296 ELARleqdIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEE----ELEEAEAELAEAEEALLEAE 371
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 498 KQVKPglVSSESEETCSELSKLKVTCEEVEMLRQELRRALEESERQKEKVRELQKKFEEREQNVTSKLSVEECEELKNSy 577
Cdd:COG1196   372 AELAE--AEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAA- 448
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 578 cSVIDNINQEKALLIERYKEGQEEIKRLQDKLTNQTHLESSAESgemkdaMHRMIDELNRQLSELSQLYKEAQAELEDYR 657
Cdd:COG1196   449 -EEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAA------RLLLLLEAEADYEGFLEGVKAALLLAGLRG 521
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 658 KRKTLDDIAVD-----------------YIPRDEHEKLMQVTNSLK----YKAENELLEMKSQYTKVLDEAEELKQMLDT 716
Cdd:COG1196   522 LAGAVAVLIGVeaayeaaleaalaaalqNIVVEDDEVAAAAIEYLKaakaGRATFLPLDKIRARAALAAALARGAIGAAV 601
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 717 QKQNSLPIAEHQQVMNALRSTVKEMEEEINELKELLTNKESEVRNLQKELLEEKAAINEAMVpRAAYEKLQSSLEGEVSI 796
Cdd:COG1196   602 DLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLT-GGSRRELLAALLEAEAE 680
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 797 LSSKLKDVIKEKENVSLDVMQLRSEVLHLKEEKEGMHNLLEAKEREVSGLHQKYHQAQEDLLEMKRYSESSSKLEEDKDK 876
Cdd:COG1196   681 LEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPP 760
                         570
                  ....*....|....*....
gi 2024434935 877 KINEMSKEVSKLKEALNSL 895
Cdd:COG1196   761 DLEELERELERLEREIEAL 779
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
151-183 3.97e-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: 3.97e-07
                          10        20        30
                  ....*....|....*....|....*....|....
gi 2024434935 151 DGNIPLLLAV-QNGHTEVCKYLLDHGADINTRDK 183
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
PHA02798 PHA02798
ankyrin-like protein; Provisional
132-234 4.35e-07

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 53.69  E-value: 4.35e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 132 LQAVQLLCEHKCPINMKDLDGNIPLLLAVQN-----GHTEVCKYLLDHGADINTRDKNGRTALMIACEAGSLNMVEVFL- 205
Cdd:PHA02798   51 TDIVKLFINLGANVNGLDNEYSTPLCTILSNikdykHMLDIVKILIENGADINKKNSDGETPLYCLLSNGYINNLEILLf 130
                          90       100       110
                  ....*....|....*....|....*....|..
gi 2024434935 206 --RKGADVSLVDVFGQNALH-YSKISENTGIQ 234
Cdd:PHA02798  131 miENGADTTLLDKDGFTMLQvYLQSNHHIDIE 162
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
362-898 5.90e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 53.91  E-value: 5.90e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  362 KELQDKLQErtpKEVDSTIDSYHSTQREFDQTADRQSEISAQELKSTLNATQSQEKLTSpSEIKIKYLQEDSKDAQRKLE 441
Cdd:TIGR02168  216 KELKAELRE---LELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEE-LRLEVSELEEEIEELQKELY 291
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  442 NSETKRKHLEAQVQSRVPEADLNNTDISEngsdPSLKIQETQSKYEEAAKEV--LNAQKQVKPGLVSSESEETCSELSKL 519
Cdd:TIGR02168  292 ALANEISRLEQQKQILRERLANLERQLEE----LEAQLEELESKLDELAEELaeLEEKLEELKEELESLEAELEELEAEL 367
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  520 KV---TCEEVEMLRQELRRALEESERQKE----KVRELQKKFE------EREQNVTSKLSVEECEELKNSYCSVIDNINQ 586
Cdd:TIGR02168  368 EElesRLEELEEQLETLRSKVAQLELQIAslnnEIERLEARLErledrrERLQQEIEELLKKLEEAELKELQAELEELEE 447
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  587 EKALLIERYKEGQEEIKRLQDKLTNQTHLESSAESGE-----MKDAMHRMIDEL------------NRQ--------LSE 641
Cdd:TIGR02168  448 ELEELQEELERLEEALEELREELEEAEQALDAAERELaqlqaRLDSLERLQENLegfsegvkallkNQSglsgilgvLSE 527
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  642 L--------------------------SQLYKEAQAELEDYRKRKT----LDDIAVDYIPRDEHEKLMQVTNSLKYKaeN 691
Cdd:TIGR02168  528 LisvdegyeaaieaalggrlqavvvenLNAAKKAIAFLKQNELGRVtflpLDSIKGTEIQGNDREILKNIEGFLGVA--K 605
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  692 ELLEMKSQYTKVLDE-------AEELKQMLDTQKQNSLP----------------------------------IAEHQQV 730
Cdd:TIGR02168  606 DLVKFDPKLRKALSYllggvlvVDDLDNALELAKKLRPGyrivtldgdlvrpggvitggsaktnssilerrreIEELEEK 685
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  731 MNALRSTVKEMEEEINELKELLTNKESEVRNLQKELLEEKAAINEAMVPRAAYEKLQSSLEGEVSILSSKLKDVIKEKEN 810
Cdd:TIGR02168  686 IEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEE 765
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  811 VSLDVMQLRSEVLHLKEEKEGMHNL--------------LEAKEREVSGLHQKYHQAQEDLLEMKRYSESSSKLEEDKDK 876
Cdd:TIGR02168  766 LEERLEEAEEELAEAEAEIEELEAQieqlkeelkalreaLDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEE 845
                          650       660
                   ....*....|....*....|..
gi 2024434935  877 KINEMSKEVSKLKEALNSLSQL 898
Cdd:TIGR02168  846 QIEELSEDIESLAAEIEELEEL 867
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
58-141 7.16e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 53.36  E-value: 7.16e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  58 HLAATkGHAECLRIMVTHGADVTAQDGAGHSALHLAVKNSHIDCIKRLLQYKCSVYSTDNSGKTALHYAATCGCLQAVQL 137
Cdd:PTZ00322   88 QLAAS-GDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166

                  ....
gi 2024434935 138 LCEH 141
Cdd:PTZ00322  167 LSRH 170
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
1-120 7.53e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 52.98  E-value: 7.53e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935   1 MKSLKAKFRKSDTNEWNKNDD-------------RLLQAVENGDPEKVASLLgKKGASATKQDSEGKTAFHLAATKGHAE 67
Cdd:PTZ00322   51 LEALEATENKDATPDHNLTTEevidpvvahmltvELCQLAASGDAVGARILL-TGGADPNCRDYDGRTPLHIACANGHVQ 129
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2024434935  68 CLRIMVTHGADVTAQDGAGHSALHLAVKNSHIDCIKRLLQYKCSVYSTDNSGK 120
Cdd:PTZ00322  130 VVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFELGANAK 182
PHA02878 PHA02878
ankyrin repeat protein; Provisional
57-225 7.69e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 52.96  E-value: 7.69e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  57 FHLAATKGHAECLRIMVTHGADVTAQDGAGHSALHLAVKNSHIDCIKRLLQY--KCSVYSTDNSGKTALHY--------- 125
Cdd:PHA02878   41 LHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSinKCSVFYTLVAIKDAFNNrnveifkii 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 126 ------------------AATCGCLQA--VQLLCEHKCPINMKDLD-GNIPLLLAVQNGHTEVCKYLLDHGADINTRDKN 184
Cdd:PHA02878  121 ltnrykniqtidlvyidkKSKDDIIEAeiTKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKT 200
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2024434935 185 GRTALMIACEAGSLNMVEVFLRKGADVSLVDVFGQNALHYS 225
Cdd:PHA02878  201 NNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHIS 241
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
151-179 1.30e-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: 45.66  E-value: 1.30e-06
                           10        20
                   ....*....|....*....|....*....
gi 2024434935  151 DGNIPLLLAVQNGHTEVCKYLLDHGADIN 179
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
Ank_2 pfam12796
Ankyrin repeats (3 copies);
189-251 2.70e-06

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 46.65  E-value: 2.70e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024434935 189 LMIACEAGSLNMVEVFLRKGADVSLVDVFGQNALHYSKISENTGIQNLLSSKISQDVDAKSPT 251
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNGRT 63
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
532-779 2.97e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 51.45  E-value: 2.97e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  532 ELRRALEESERQKEKVRELQKKFEEREQNVTSKLSVEECEELKNSYcsvidNINQEKALLIERYKEGQEEIKRLQDKLtn 611
Cdd:COG4913    239 RAHEALEDAREQIELLEPIRELAERYAAARERLAELEYLRAALRLW-----FAQRRLELLEAELEELRAELARLEAEL-- 311
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  612 qthlessAESGEMKDAMHRMIDELNRQLSELS-QLYKEAQAELEdyRKRKTLDDIavdyipRDEHEKLMQVTNSLKYKAE 690
Cdd:COG4913    312 -------ERLEARLDALREELDELEAQIRGNGgDRLEQLEREIE--RLERELEER------ERRRARLEALLAALGLPLP 376
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  691 NELLEMKSQYTKVLDEAEELKQMLDTQKQNslpIAEHQQVMNALRSTVKEMEEEINELKELLTNKESEVRNLqKELLEEK 770
Cdd:COG4913    377 ASAEEFAALRAEAAALLEALEEELEALEEA---LAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLAL-RDALAEA 452

                   ....*....
gi 2024434935  771 AAINEAMVP 779
Cdd:COG4913    453 LGLDEAELP 461
PRK01156 PRK01156
chromosome segregation protein; Provisional
571-894 3.22e-06

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 51.06  E-value: 3.22e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 571 EELKnSYCSVIDNINQEKALLIERYKEGQEEIKRLQDKLTNqthleSSAESGEMKDAMHRMidelnrqlSELSQLYKEAQ 650
Cdd:PRK01156  190 EKLK-SSNLELENIKKQIADDEKSHSITLKEIERLSIEYNN-----AMDDYNNLKSALNEL--------SSLEDMKNRYE 255
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 651 AELEDYRKRKTLDDIAVDYIPRDEhEKLMQVTNSLKYKAENELLEmksqYTKVLDEAEELKQML---DTQKQNSLPIAEH 727
Cdd:PRK01156  256 SEIKTAESDLSMELEKNNYYKELE-ERHMKIINDPVYKNRNYIND----YFKYKNDIENKKQILsniDAEINKYHAIIKK 330
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 728 QQVMNALRSTVKEMEEEINELKELLTNKESEVRNLQKELLEekaaINEAMVPRAAYEKLQSSLEGEVS----ILSSKLKD 803
Cdd:PRK01156  331 LSVLQKDYNDYIKKKSRYDDLNNQILELEGYEMDYNSYLKS----IESLKKKIEEYSKNIERMSAFISeilkIQEIDPDA 406
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 804 VIKEKENVSLDVMQLRSEVLHLKEEKEGMHNLLEAKEREVSGL--HQKYHQAQEDLLE------MKRYSESSSKLEEDKD 875
Cdd:PRK01156  407 IKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLngQSVCPVCGTTLGEeksnhiINHYNEKKSRLEEKIR 486
                         330       340
                  ....*....|....*....|....*
gi 2024434935 876 ------KKINEMSKEVSKLKEALNS 894
Cdd:PRK01156  487 eieievKDIDEKIVDLKKRKEYLES 511
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
403-776 3.91e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 50.92  E-value: 3.91e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 403 QELKSTLNATQSQEKLTSPSEIKIKYLQEDSKDAQRKLENSETKRKHLEAQVQSRVPEADLNNTDISENGSDPSLK---- 478
Cdd:COG4717    74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEelee 153
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 479 ----IQETQSKYEEAAKEVLNAQKQvkpgLVSSESEETCSELSKLKVTCEEVEMLRQELRRALEESERQKEKVRELQKKF 554
Cdd:COG4717   154 rleeLRELEEELEELEAELAELQEE----LEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEEL 229
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 555 EEREQNVTSKLSVEECEELKNSYCS-----VIDNINQEKALLIERYKE---------GQEEIKRLQDKLTNQTHLESSAE 620
Cdd:COG4717   230 EQLENELEAAALEERLKEARLLLLIaaallALLGLGGSLLSLILTIAGvlflvlgllALLFLLLAREKASLGKEAEELQA 309
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 621 SGEMKDAMHRMIDELNRQLS-ELSQLYKEAQAELEDYRKRKTLDDIAVDYIPRDEHEKLMQVTNSL--KYKAENE----- 692
Cdd:COG4717   310 LPALEELEEEELEELLAALGlPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALlaEAGVEDEeelra 389
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 693 LLEMKSQYTKVLDEAEELKQMLDTQKQNSLPIAEHQqvmnalrsTVKEMEEEINELKELLTNKESEVRNLQKELLEEKAA 772
Cdd:COG4717   390 ALEQAEEYQELKEELEELEEQLEELLGELEELLEAL--------DEEELEEELEELEEELEELEEELEELREELAELEAE 461

                  ....
gi 2024434935 773 INEA 776
Cdd:COG4717   462 LEQL 465
PHA02878 PHA02878
ankyrin repeat protein; Provisional
11-174 6.00e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 49.88  E-value: 6.00e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  11 SDTNEWNKNDDR--LLQAVENGDpEKVASLLGKKGASATKQDSEGKTAFHLAATKGHAECLRIMVTHGADVTAQDGAGHS 88
Cdd:PHA02878  158 ADINMKDRHKGNtaLHYATENKD-QRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNT 236
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  89 ALHLAVKN-SHIDCIKRLLQYKCSVYSTDN-SGKTALHYAATCGclQAVQLLCEHKCPINMKDLDGNIPLLLAV-QNGHT 165
Cdd:PHA02878  237 PLHISVGYcKDYDILKLLLEHGVDVNAKSYiLGLTALHSSIKSE--RKLKLLLEYGADINSLNSYKLTPLSSAVkQYLCI 314

                  ....*....
gi 2024434935 166 EVCKYLLDH 174
Cdd:PHA02878  315 NIGRILISN 323
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
688-898 1.05e-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: 48.99  E-value: 1.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 688 KAENELLEMKSQYTKVLDEAEELKQMLDTQKQNslpIAEHQQVMNALRSTVKEMEEEINELKELLTNKESEVRNLQKELL 767
Cdd:COG4942    24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQ---LAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 768 EEKAAINEAMvpRAAYeKLQSSLEGEVSILSSKLKDVIKEKENVSLDVMQLRSEVLHLKEEKEGMHNLLEAKEREVSGLH 847
Cdd:COG4942   101 AQKEELAELL--RALY-RLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2024434935 848 QKYHQAQEDLLEMKRYSESSSKLEEDKDKKINEMSKEVSKLKEALNSLSQL 898
Cdd:COG4942   178 ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEAL 228
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
588-791 1.16e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 49.38  E-value: 1.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 588 KALLIERYKEGQEEIKRLQDKLT--NQTHLESSAESGEMKDAMHRMIDELNRQLSELSQLYKEAQAELEDYRKRKTLDDI 665
Cdd:COG4717    44 RAMLLERLEKEADELFKPQGRKPelNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEK 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 666 AVDYIPRDEHEKlmqvtnslkyKAENELLEMKSQYTKVLDEAEELKQMLDTQKQNSLPIAEHQQVMN-ALRSTVKEMEEE 744
Cdd:COG4717   124 LLQLLPLYQELE----------ALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEeLLEQLSLATEEE 193
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2024434935 745 INELKELLTNKESEVRNLQKELLEEKAAINEAMVPRAAYEKLQSSLE 791
Cdd:COG4717   194 LQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAA 240
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
403-828 1.18e-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: 49.25  E-value: 1.18e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 403 QELKSTLNATQSQEKLTSPSEIKIKylqEDSKDAQRKLENSETKRKHLEAQVQSRVPE-ADLNNTDISENGSDPSLKIQE 481
Cdd:TIGR04523 242 NEKTTEISNTQTQLNQLKDEQNKIK---KQLSEKQKELEQNNKKIKELEKQLNQLKSEiSDLNNQKEQDWNKELKSELKN 318
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 482 TQSKYEEAAKEVLNAQKQVkpglvssesEETCSELSKLKVTCEEVEMLRQELRRALEESERQKEKV-RELQKKFEEREQN 560
Cdd:TIGR04523 319 QEKKLEEIQNQISQNNKII---------SQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLkKENQSYKQEIKNL 389
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 561 VTSKLSVE----ECEELKNSYCSVIDNINQEKALLIERYKEGQEEIKRLQDKLTNQTHLESSAESgeMKDAMHRMIDELN 636
Cdd:TIGR04523 390 ESQINDLEskiqNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKEL--IIKNLDNTRESLE 467
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 637 RQLSELSQLYKEAQAELEDY-----RKRKTLDDIAVDYIPRDEHEKLMQVTNSLKYKAENELLEMKSQYTKVLDEAEELK 711
Cdd:TIGR04523 468 TQLKVLSRSINKIKQNLEQKqkelkSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDEL 547
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 712 QMLDTQKQNSLpiaehqqvmnaLRSTVKEMEEEINELKELLTNKESEVRNLQKELLEEKAAINEAMVPRAAYEKLQSSLE 791
Cdd:TIGR04523 548 NKDDFELKKEN-----------LEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLE 616
                         410       420       430
                  ....*....|....*....|....*....|....*..
gi 2024434935 792 GEVSILSSKLKDVIKEKENVSLDVMQLRSEVLHLKEE 828
Cdd:TIGR04523 617 KELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKET 653
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
45-191 1.68e-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: 1.68e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  45 SATKQDSEGKTAFHLAATKGHAECLR-IMVTHGAD-------------VTAQDGAGHSALHLAVKNSHIDCIKRLLQYKC 110
Cdd:cd21882    18 SAYQRGATGKTCLHKAALNLNDGVNEaIMLLLEAApdsgnpkelvnapCTDEFYQGQTALHIAIENRNLNLVRLLVENGA 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 111 SVYstdnsgktalhyAATCGclqavQLLCEHKCPINMKdldGNIPLLLAVQNGHTEVCKYLLDHGADI---NTRDKNGRT 187
Cdd:cd21882    98 DVS------------ARATG-----RFFRKSPGNLFYF---GELPLSLAACTNQEEIVRLLLENGAQPaalEAQDSLGNT 157

                  ....
gi 2024434935 188 ALMI 191
Cdd:cd21882   158 VLHA 161
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
581-800 1.79e-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: 48.22  E-value: 1.79e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 581 IDNINQEKALLIERYKEGQEEIKRLQDKLTNQTHLESSAESGemkdamhrmIDELNRQLSELSQLYKEAQAELEdyRKRK 660
Cdd:COG4942    36 IAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQE---------LAALEAELAELEKEIAELRAELE--AQKE 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 661 TLDDIAVDYIPRDEHEKLMQVTNSLKYKAENELLEMKSQYTKVL-DEAEELKQMLDTQKQNSLPIAEHQQvmnALRSTVK 739
Cdd:COG4942   105 ELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARrEQAEELRADLAELAALRAELEAERA---ELEALLA 181
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024434935 740 EMEEEINELKELLTNKESEVRNLQKELLEEKAAINEAMVPRAAYEKLQSSLEGEVSILSSK 800
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 2.16e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 42.19  E-value: 2.16e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 2024434935   52 EGKTAFHLAATKGHAECLRIMVTHGADVTA 81
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
387-749 2.50e-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: 48.53  E-value: 2.50e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  387 QREFDQTADRQSEISaQELKSTLNATQSQEKLTSPSEIKIKYLQEDSKDAQRKLENSETKRKHLEAQVQSRVPEADLNNT 466
Cdd:TIGR02169  687 KRELSSLQSELRRIE-NRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEA 765
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  467 DISEngsdpslkIQETQSKYEEAAKEVlnaqkqvkpglvssESEETCSELSKLKVTCEEVEMLRQELRRALEESErQKEK 546
Cdd:TIGR02169  766 RIEE--------LEEDLHKLEEALNDL--------------EARLSHSRIPEIQAELSKLEEEVSRIEARLREIE-QKLN 822
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  547 VRELQKKFEEREQNvTSKLSVEECEELKNSYCSVIDNINQEKALLIERYKEGQEEIKRLQDKLtnqTHLESSAESGEMK- 625
Cdd:TIGR02169  823 RLTLEKEYLEKEIQ-ELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRL---GDLKKERDELEAQl 898
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  626 DAMHRMIDELNRQLSELSQLYKEAQAELEDYRKR-KTLDDIAVDYIPRDEHEKLMQVTNSLKYKAENELLEMKSQYTKVL 704
Cdd:TIGR02169  899 RELERKIEELEAQIEKKRKRLSELKAKLEALEEElSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEPVNMLAI 978
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*
gi 2024434935  705 DEAEELKQMLDTQKqnslpiaEHQQVMNALRSTVKEMEEEINELK 749
Cdd:TIGR02169  979 QEYEEVLKRLDELK-------EKRAKLEEERKAILERIEEYEKKK 1016
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
591-897 2.84e-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: 48.14  E-value: 2.84e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  591 LIERYKEGQEEIKRLQDKLtnqthlessaesGEMKDAMHRMIDELNRQ---LSELSQLYKEAQAELEDYRKRKTLDDiav 667
Cdd:TIGR02169  665 GILFSRSEPAELQRLRERL------------EGLKRELSSLQSELRRIenrLDELSQELSDASRKIGEIEKEIEQLE--- 729
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  668 dyiprDEHEKLmqvtnslkykaenellemksqytkvldeAEELKQMLDTQKQNSLPIAEHQQVMNALRSTVKEMEEEINE 747
Cdd:TIGR02169  730 -----QEEEKL----------------------------KERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHK 776
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  748 LKELLTNKE-----SEVRNLQKEL--LEEKAAINEAMVprAAYEKLQSSLEGEVSILSSKLKDVIKEKENVSLDVMQLRS 820
Cdd:TIGR02169  777 LEEALNDLEarlshSRIPEIQAELskLEEEVSRIEARL--REIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEK 854
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024434935  821 EVLHLKEEKEGMHNLLEAKEREVSGLHQKYHQAQEDLLEMKRYSESSSKLEEDKDKKINEMSKEVSKLKEALNSLSQ 897
Cdd:TIGR02169  855 EIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEE 931
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
632-856 3.50e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 47.99  E-value: 3.50e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  632 IDELNRQLSELSQLYKEAQAELEDYRKRktlddiavdyipRDEHEKLMQVTNSLK--YKAENELLEMKSQYTKVL---DE 706
Cdd:COG4913    619 LAELEEELAEAEERLEALEAELDALQER------------REALQRLAEYSWDEIdvASAEREIAELEAELERLDassDD 686
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  707 AEELKQMLDTQKQNslpIAEHQQVMNALRSTVKEMEEEINELKELLTNKESEVRNLQK-------ELLEEK-AAINEAMV 778
Cdd:COG4913    687 LAALEEQLEELEAE---LEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDlarlelrALLEERfAAALGDAV 763
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  779 PRAAYEKLQSSLEGEVSILSSKLKDVIK-----------EKENVSLDVM----------QLRSEVLHLKEEKegMHNLL- 836
Cdd:COG4913    764 ERELRENLEERIDALRARLNRAEEELERamrafnrewpaETADLDADLEslpeylalldRLEEDGLPEYEER--FKELLn 841
                          250       260
                   ....*....|....*....|
gi 2024434935  837 EAKEREVSGLHQKYHQAQED 856
Cdd:COG4913    842 ENSIEFVADLLSKLRRAIRE 861
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
310-849 4.42e-05

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: 47.42  E-value: 4.42e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  310 QEDFSSLLQDNKDRL----SDSTAGADSLLDVSSETEQQDLLMLMQAKIASLTLHNkelQDKLQERTPKEVDSTIDSYHS 385
Cdd:pfam15921  255 QNKIELLLQQHQDRIeqliSEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARN---QNSMYMRQLSDLESTVSQLRS 331
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  386 TQREfdqtADRQSEISAQELKSTLNATQSQekLTSPSEIKIKYLQEDSK--DAQRKLENSETKRKH---LEAQVQSRVPE 460
Cdd:pfam15921  332 ELRE----AKRMYEDKIEELEKQLVLANSE--LTEARTERDQFSQESGNldDQLQKLLADLHKREKelsLEKEQNKRLWD 405
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  461 ADLNNTdISENGSDPSLKIQETQSKYEEAAKEVLNAQKQVKPGLVSSESEETCSELSKLKVTCEEVEMLRQELRRALEES 540
Cdd:pfam15921  406 RDTGNS-ITIDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEEL 484
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  541 ERQKEKVRELQKKFEEreqnVTSKLSVEEceelknsycSVIDNINQEKALLIERYKEGQEEIKRLQDKLTNQTHLESSAE 620
Cdd:pfam15921  485 TAKKMTLESSERTVSD----LTASLQEKE---------RAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECE 551
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  621 SGEMKDA-MHRMIDELNRQLSELSQLY------------KEAQAELEDYRKRKTLDDIAVDYIPRDEHEKLMQVTNSLKY 687
Cdd:pfam15921  552 ALKLQMAeKDKVIEILRQQIENMTQLVgqhgrtagamqvEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLE 631
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  688 KAENELLEMKSQYTK-VLDEAEELKQMLDTQKQ-----NSLPiAEHQQVMNALRSTVKEMEEEINELKELLTNKESEVRN 761
Cdd:pfam15921  632 LEKVKLVNAGSERLRaVKDIKQERDQLLNEVKTsrnelNSLS-EDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQ 710
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  762 LQKELLEEKAAINEAMVPRAAYEKLQSSLEGEVSILSSKLK-------DVIKEKENVSLDVMQLRSEVLHLKEEKEGMHN 834
Cdd:pfam15921  711 TRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQfleeamtNANKEKHFLKEEKNKLSQELSTVATEKNKMAG 790
                          570
                   ....*....|....*
gi 2024434935  835 LLEAKEREVSGLHQK 849
Cdd:pfam15921  791 ELEVLRSQERRLKEK 805
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
338-891 4.94e-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: 47.27  E-value: 4.94e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  338 SSETEQQDLLMLMQAKIASLTLHNKELQDKLQERTpKEVDSTIDSYHSTQREFDQTADRQSEISAQELKSTLNATQSQEK 417
Cdd:pfam02463  387 SSAAKLKEEELELKSEEEKEAQLLLELARQLEDLL-KEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDEL 465
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  418 LTSPSEIKIKYLQEDSKDAQRKLENSETKRKHLEAQVQSRVPEADLNNTDISENGSDPSLKIQETQSKYEEAAKEVLNAQ 497
Cdd:pfam02463  466 ELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAI 545
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  498 KQVKPGLVSSESEETCSELSKLKVTCEEVEMLRQ-----ELRRALEESERQKEKVRELQK-KFEEREQNVTSKLSVEECE 571
Cdd:pfam02463  546 STAVIVEVSATADEVEERQKLVRALTELPLGARKlrlliPKLKLPLKSIAVLEIDPILNLaQLDKATLEADEDDKRAKVV 625
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  572 ELKNSYCSVIDNINQEKALLIERYKEGQEEIKRLQDKLTNQTHLESSAESGEM--KDAMHRMIDELNRQLSELSQLYKEA 649
Cdd:pfam02463  626 EGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIqeLQEKAESELAKEEILRRQLEIKKKE 705
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  650 QAELEDYRKRKTLDDIAVDYIPRDEHEKLMQVTNSLKYKAENELLEMKSQYTKVLDEAEELKQMLDTQKQNSLPIAEHQQ 729
Cdd:pfam02463  706 QREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEK 785
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  730 VMNA--LRSTVKEMEEEINELKELLTNKESEVRNLQKELLEEKAAINEAMVPRAAYEKLQSSLEGEVSILSSKLKDVIKE 807
Cdd:pfam02463  786 LKVEeeKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITK 865
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  808 KENVSLdvmQLRSEVLHLKEEKEGMHNLLEAKEREVSGLHQKYHQAQEDLLEMKRYSESSSKLEEDKDKKINEMSKEVSK 887
Cdd:pfam02463  866 EELLQE---LLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLL 942

                   ....
gi 2024434935  888 LKEA 891
Cdd:pfam02463  943 EEAD 946
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
630-899 5.31e-05

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 47.34  E-value: 5.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 630 RMIDELnrqlselSQLYKeaqaeLEDYRKRKTLDDIAVDYIPRDEHEKLMQVTNSLKYKAENELLEMKSQYTKVLDEAEE 709
Cdd:PRK02224  153 DMIDDL-------LQLGK-----LEEYRERASDARLGVERVLSDQRGSLDQLKAQIEEKEEKDLHERLNGLESELAELDE 220
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 710 LKQMLDTQKQN--------SLPIAEHQQVmnalRSTVKEMEEEINELKELLTNKESEVRNL------QKELLEEKAAINE 775
Cdd:PRK02224  221 EIERYEEQREQaretrdeaDEVLEEHEER----REELETLEAEIEDLRETIAETEREREELaeevrdLRERLEELEEERD 296
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 776 AMVPRAAYEklqsslEGEVSILSSKLKDVIKEKENVSLDVMQLRSEVLHLKEEKEGMHNLLEAKEREVSGLHQKYHQAQE 855
Cdd:PRK02224  297 DLLAEAGLD------DADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELES 370
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 2024434935 856 DLLEMKRYSESSSKLEEDKDKKINEMSKEVSKLKEALNSLSQLS 899
Cdd:PRK02224  371 ELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFL 414
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
21-189 5.62e-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: 47.16  E-value: 5.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  21 DRLLQAVENGDPEKVASLLG-------KKGASATKQDSEGKTAFHLAA---TKGHAECLRIMVTHGAD-------VTAQD 83
Cdd:cd22197     8 DRLFSVVSRGNPEELAGLLEylrrtskYLTDSEYTEGSTGKTCLMKAVlnlQDGVNACIMPLLEIDKDsgnpkplVNAQC 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  84 G----AGHSALHLAVKNSHIDCIKRLLQYKCSVYstdnsgktalhyAATCG-CLQAVQLLCEHKcpinmkdldGNIPLLL 158
Cdd:cd22197    88 TdeyyRGHSALHIAIEKRSLQCVKLLVENGADVH------------ARACGrFFQKKQGTCFYF---------GELPLSL 146
                         170       180       190
                  ....*....|....*....|....*....|....
gi 2024434935 159 AVQNGHTEVCKYLLDHGAD---INTRDKNGRTAL 189
Cdd:cd22197   147 AACTKQWDVVNYLLENPHQpasLQAQDSLGNTVL 180
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
86-231 5.78e-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: 5.78e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  86 GHSAL-HLAVKNSHIDCIKRLLQYKCSVYStdnsGKTALHyAATCGCLQAVQLLCEHKCPINMKDLD------------- 151
Cdd:TIGR00870  52 GRSALfVAAIENENLELTELLLNLSCRGAV----GDTLLH-AISLEYVDAVEAILLHLLAAFRKSGPlelandqytseft 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 152 -GNIPLLLAVQNGHTEVCKYLLDHGADINTRDK--------------NGRTALMIACEAGSLNMVEVFLRKGADVSLVDV 216
Cdd:TIGR00870 127 pGITALHLAAHRQNYEIVKLLLERGASVPARACgdffvksqgvdsfyHGESPLNAAACLGSPSIVALLSEDPADILTADS 206
                         170
                  ....*....|....*.
gi 2024434935 217 FGQNALHYSKI-SENT 231
Cdd:TIGR00870 207 LGNTLLHLLVMeNEFK 222
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
395-913 6.68e-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: 46.89  E-value: 6.68e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  395 DRQSEISAQELKSTLNATQSQEKLTSPSEIKIKYLQEDSKDAQRKLENSETKRKHL-EAQVQSRVPEADLNNTDisengs 473
Cdd:TIGR00618  176 DQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLrEALQQTQQSHAYLTQKR------ 249
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  474 dpslKIQETQSKYEEAAKEVLNAQKQVKPGL-VSSESEETCSELSKLKVTCEEVEMLRQELRRALEESERQKEKVRELQK 552
Cdd:TIGR00618  250 ----EAQEEQLKKQQLLKQLRARIEELRAQEaVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAK 325
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  553 KFEEREQNVTSKLSVEECEELKNSYCSVIDNINQ--EKALLI----ERYKEGQEEIKRLQDKLTNQTHLESSAES-GEMK 625
Cdd:TIGR00618  326 LLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDahEVATSIreisCQQHTLTQHIHTLQQQKTTLTQKLQSLCKeLDIL 405
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  626 DAMHRMIDELNRQLSELSQLYKEAQAELEDYRKRKTLDDIAVDYIPRDE-HEKLMQVTNSLKYKAENELLEMKSQYTKVL 704
Cdd:TIGR00618  406 QREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEkLEKIHLQESAQSLKEREQQLQTKEQIHLQE 485
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  705 DE--AEELKQMLDTQ-------KQNSLPIAEHQQVMN--ALRSTVKEMEEEINELKELLTNKESEVRNLQKELLEEKAAI 773
Cdd:TIGR00618  486 TRkkAVVLARLLELQeepcplcGSCIHPNPARQDIDNpgPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQM 565
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  774 NEAMVPRAAYEKLQSSLEGEVSILSSKLKDVIKEKENVSLDVMQLRSEVLHLKEEKEGMHNLLEA------KEREVSGLH 847
Cdd:TIGR00618  566 QEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVrlhlqqCSQELALKL 645
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  848 QKYHQAQEDLLEmKRYSESSSKLEEDKDKKI----NEMSKEVSKLKEALNSLSQLSYSTSAPKRQSQQLE 913
Cdd:TIGR00618  646 TALHALQLTLTQ-ERVREHALSIRVLPKELLasrqLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIE 714
Ank_4 pfam13637
Ankyrin repeats (many copies);
23-73 7.13e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 41.11  E-value: 7.13e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2024434935  23 LLQAVENGDPEKVASLLgKKGASATKQDSEGKTAFHLAATKGHAECLRIMV 73
Cdd:pfam13637   5 LHAAAASGHLELLRLLL-EKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03100 PHA03100
ankyrin repeat protein; Provisional
140-254 8.59e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 46.20  E-value: 8.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 140 EHKCPINMKDLDGNIPLLLAVQNGHTEVCKYLLDHGADINTRDKNGRTALM----------------------------- 190
Cdd:PHA03100   23 MEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHylsnikynltdvkeivkllleyganvnap 102
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024434935 191 -----------IACEAGSLNMVEVFLRKGADVSLVDVFGQNALHY--SKISENTGIQNLLSSKISqDVDAKspTKVK 254
Cdd:PHA03100  103 dnngitpllyaISKKSNSYSIVEYLLDNGANVNIKNSDGENLLHLylESNKIDLKILKLLIDKGV-DINAK--NRVN 176
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
184-215 9.27e-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: 9.27e-05
                          10        20        30
                  ....*....|....*....|....*....|...
gi 2024434935 184 NGRTALMIACE-AGSLNMVEVFLRKGADVSLVD 215
Cdd:pfam00023   1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARD 33
PHA02876 PHA02876
ankyrin repeat protein; Provisional
75-239 9.78e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 46.21  E-value: 9.78e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  75 HGADVTAQDGAGHSALHLAVKNSHIDCIKRLLQYKC-SVYSTDNSGKTALHYAATCGCLQAVQLLCEHKCPINMkdldgN 153
Cdd:PHA02876   30 HGANQCENESIPFTAIHQALQLRQIDIVEEIIQQNPeLIYITDHKCHSTLHTICIIPNVMDIVISLTLDCDIIL-----D 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 154 IPLLLAVQNGHT--EVCKYLLDH---GADINTRDKNGRTALMIAC----EAGSLNMVEVFLRKGADVSLVDVFGQNALHY 224
Cdd:PHA02876  105 IKYASIILNKHKldEACIHILKEaisGNDIHYDKINESIEYMKLIkeriQQDELLIAEMLLEGGADVNAKDIYCITPIHY 184
                         170
                  ....*....|....*
gi 2024434935 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 9.90e-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: 40.26  E-value: 9.90e-05
                           10        20
                   ....*....|....*....|....*...
gi 2024434935  184 NGRTALMIACEAGSLNMVEVFLRKGADV 211
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
52-83 1.06e-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: 40.35  E-value: 1.06e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 2024434935  52 EGKTAFHLAATK-GHAECLRIMVTHGADVTAQD 83
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
397-889 1.07e-04

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


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 46.25  E-value: 1.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 397 QSEISAQELKSTLNATQSQEK---------LTSPSEIKIKYLQEDSKDAQRKLENSETKRKHLEAQvqsrvpeadLNNTD 467
Cdd:pfam05483 232 KKEINDKEKQVSLLLIQITEKenkmkdltfLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKE---------LEDIK 302
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 468 ISENGSDPSLKIQETQSKYEEAAKEVLNAQKQVKPGLVSSESEETCSELSKLKVT-CEEVEMLRQELRRALEESERQKEK 546
Cdd:pfam05483 303 MSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATtCSLEELLRTEQQRLEKNEDQLKII 382
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 547 VRELQKKFEEreqnvtsklsVEECEELKNSycsvidninqeKALLIERYKEGQEEIKRLQDKltnqthlessaesgemKD 626
Cdd:pfam05483 383 TMELQKKSSE----------LEEMTKFKNN-----------KEVELEELKKILAEDEKLLDE----------------KK 425
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 627 AMHRMIDELNRQLSELSQLYKEAQAELEDYrkrktldDIAVDYIPRDEHEKLMQVTNsLKYKAENELL---EMKSQYTKV 703
Cdd:pfam05483 426 QFEKIAEELKGKEQELIFLLQAREKEIHDL-------EIQLTAIKTSEEHYLKEVED-LKTELEKEKLkniELTAHCDKL 497
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 704 LDEAEELKQmldTQKQNSLPIAEHQQVMNALRSTVKEMEEEINELKELLTNKESEVRNLQKELLEE----KAAINEAMVP 779
Cdd:pfam05483 498 LLENKELTQ---EASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKgdevKCKLDKSEEN 574
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 780 RAAYEKLQSSLEGEVSILSSKLKDVIKEKENVSLDVMQLRSEVLHLKEEKEGMHNLLEAKEREVSGLHQKYHQAQEDLLE 859
Cdd:pfam05483 575 ARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEE 654
                         490       500       510
                  ....*....|....*....|....*....|..
gi 2024434935 860 MkryseSSSKLEEDKDKKINE--MSKEVSKLK 889
Cdd:pfam05483 655 I-----IDNYQKEIEDKKISEekLLEEVEKAK 681
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
707-892 1.15e-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: 44.53  E-value: 1.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 707 AEELKQMLDTQKQNSLpIAEHQQVMNALRSTVKEMEEEINELKELLTNKESEVRNLQKELLEEKAAINEAmvpRAAYEKL 786
Cdd:COG1579     3 PEDLRALLDLQELDSE-LDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEV---EARIKKY 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 787 QSSLEgevSILSSK-LKDVIKEKENVSLDVMQLRSEVLHLKEEkegmhnlLEAKEREVSGLHQKYHQAQEDLLEMK-RYS 864
Cdd:COG1579    79 EEQLG---NVRNNKeYEALQKEIESLKRRISDLEDEILELMER-------IEELEEELAELEAELAELEAELEEKKaELD 148
                         170       180
                  ....*....|....*....|....*...
gi 2024434935 865 ESSSKLEEDKDKKINEMSKEVSKLKEAL 892
Cdd:COG1579   149 EELAELEAELEELEAEREELAAKIPPEL 176
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
184-212 1.21e-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: 1.21e-04
                          10        20
                  ....*....|....*....|....*....
gi 2024434935 184 NGRTALMIACEAGSLNMVEVFLRKGADVS 212
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADIN 29
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
317-611 1.47e-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: 45.82  E-value: 1.47e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  317 LQDNKDRLSDSTAGADSLLDVSSETEQQDLLMLMQAKIASLTLHNKELQDKLQERTPKEVDSTIDSYHStQREFDQTADR 396
Cdd:TIGR02168  700 LAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEE-RLEEAEEELA 778
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  397 QSEISAQELKSTLNATQSQ-----EKLTSPSEIkIKYLQEDSKDAQRKLENSETKRKHLEAQVQSRVPEADLNNTDISEN 471
Cdd:TIGR02168  779 EAEAEIEELEAQIEQLKEElkalrEALDELRAE-LTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESL 857
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  472 gSDPSLKIQETQSKYEEAAKEVLNAQKQVKPGLvssesEETCSELSKLKVTCEEVEMLRQELRRALEESERQKEKVRELQ 551
Cdd:TIGR02168  858 -AAEIEELEELIEELESELEALLNERASLEEAL-----ALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRL 931
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  552 KKFEEREQNVTSKLSVEECEELknsycsviDNINQEKALLIERYKEGQEEIKRLQDKLTN 611
Cdd:TIGR02168  932 EGLEVRIDNLQERLSEEYSLTL--------EEAEALENKIEDDEEEARRRLKRLENKIKE 983
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
155-180 1.65e-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: 1.65e-04
                          10        20
                  ....*....|....*....|....*.
gi 2024434935 155 PLLLAVQNGHTEVCKYLLDHGADINT 180
Cdd:pfam13606   5 PLHLAARNGRLEIVKLLLENGADINA 30
AAA_13 pfam13166
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
585-775 1.71e-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: 1.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 585 NQEKALLIERYKEGQEEIKRLQDKLTNQthLESSAESGEMKDAMHRMIDELNRQLSELSQLYKEAQAELEDYRKR----K 660
Cdd:pfam13166 278 DDEFTEFQNRLQKLIEKVESAISSLLAQ--LPAVSDLASLLSAFELDVEDIESEAEVLNSQLDGLRRALEAKRKDpfksI 355
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 661 TLDDIAvdyiprdehEKLMQVTNSLKykAENELLEMKSQYTKVLDEA-EELKQML--DTQKQNSLPIAEHQQVMNALRST 737
Cdd:pfam13166 356 ELDSVD---------AKIESINDLVA--SINELIAKHNEITDNFEEEkNKAKKKLrlHLVEEFKSEIDEYKDKYAGLEKA 424
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2024434935 738 VKEMEEEINELKELLTNKESEVRNLQKELLEEKAAINE 775
Cdd:pfam13166 425 INSLEKEIKNLEAEIKKLREEIKELEAQLRDHKPGADE 462
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
527-890 2.12e-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: 45.20  E-value: 2.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 527 EMLRQELRRALEESERQKEKVRELQKKFEEREQNvtsklsveeceelknsycsvidnINQEKALLIERykegQEEIKRLQ 606
Cdd:pfam10174 112 ELTEENFRRLQSEHERQAKELFLLRKTLEEMELR-----------------------IETQKQTLGAR----DESIKKLL 164
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 607 DKLTNQTHlesSAESGEMKDAMHRMIDELNRQLSELSQLYKEAQAELEDYRKrktlddiavdyiprDEHEKLMQVTNSLK 686
Cdd:pfam10174 165 EMLQSKGL---PKKSGEEDWERTRRIAEAEMQLGHLEVLLDQKEKENIHLRE--------------ELHRRNQLQPDPAK 227
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 687 YKAENELLEMK----SQYTKVLDEAEELKQMLdtqKQNSLPIAEHQQV----MNALRSTVKEMEEEINELKELLTNKESE 758
Cdd:pfam10174 228 TKALQTVIEMKdtkiSSLERNIRDLEDEVQML---KTNGLLHTEDREEeikqMEVYKSHSKFMKNKIDQLKQELSKKESE 304
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 759 VRNLQKEL-------LEEKAAINEAMVPRAAYEKLQSSLEGEVSILSSKLKDVIKEKENVSLDVMQLRSEVLHLKEEKEG 831
Cdd:pfam10174 305 LLALQTKLetltnqnSDCKQHIEVLKESLTAKEQRAAILQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRD 384
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2024434935 832 MHNLLEAKEREVSGLHQKYHQAQEDLlemkrysessskleEDKDKKINEMSKEVSKLKE 890
Cdd:pfam10174 385 LKDMLDVKERKINVLQKKIENLQEQL--------------RDKDKQLAGLKERVKSLQT 429
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
526-760 2.42e-04

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 45.01  E-value: 2.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 526 VEMLRQELRRAL----EESERQKEKVRELQKKFEE-REQNVTSKLSVEEceelkNSYCSVIDNINQEKALLIERYKEGQE 600
Cdd:COG3206   166 LELRREEARKALefleEQLPELRKELEEAEAALEEfRQKNGLVDLSEEA-----KLLLQQLSELESQLAEARAELAEAEA 240
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 601 EIKRLQDKLTNQTHLESSAESGEMKDAMHRMIDELNRQLSELSQLY-------KEAQAELEDYRKRktlddiavdyiprd 673
Cdd:COG3206   241 RLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYtpnhpdvIALRAQIAALRAQ-------------- 306
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 674 ehekLMQVTNSLKYKAENELLEMKSQYTKVLDEAEELKQMLDTQKQNSLPIAEHQQVMNALRSTVKEMEEEINELKELLT 753
Cdd:COG3206   307 ----LQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEARLAEA 382

                  ....*..
gi 2024434935 754 NKESEVR 760
Cdd:COG3206   383 LTVGNVR 389
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
44-172 2.76e-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: 2.76e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  44 ASATKQDSEGKTAFHLAATKGHAECLRIMVTHGADVTAQ-DGA------------GHSALHLAVKNSHIDCIKRLLQYK- 109
Cdd:cd21882    64 APCTDEFYQGQTALHIAIENRNLNLVRLLVENGADVSARaTGRffrkspgnlfyfGELPLSLAACTNQEEIVRLLLENGa 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 110 --CSVYSTDNSGKTALH------------YAATCGCLQAVQLLCEHKCPINMKDL----DGNIPLLLAVQNGHTEVCKYL 171
Cdd:cd21882   144 qpAALEAQDSLGNTVLHalvlqadntpenSAFVCQMYNLLLSYGAHLDPTQQLEEipnhQGLTPLKLAAVEGKIVMFQHI 223

                  .
gi 2024434935 172 L 172
Cdd:cd21882   224 L 224
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
422-895 3.31e-04

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 44.63  E-value: 3.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 422 SEIKIKYLQEDSKDAQRKLENSETKRKHLEAQVQSRVPEADLNNTDISENGSDPSLKIQETQSKYEEAAK---EVLNAQK 498
Cdd:TIGR04523  52 KEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKlevELNKLEK 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 499 QVKPglVSSESEETCSELSKLKVTCEEVEMLRQELRRALEESERQKEKVRELQKKFEEREQNVTSKL--------SVEEC 570
Cdd:TIGR04523 132 QKKE--NKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLlklelllsNLKKK 209
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 571 EELKNSYCSVIDNINQEKALLIERYKEGQEEIKRLQDKL-TNQTHLES-SAESGEMKDAMHRMIDEL---NRQLSELSQL 645
Cdd:TIGR04523 210 IQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEIsNTQTQLNQlKDEQNKIKKQLSEKQKELeqnNKKIKELEKQ 289
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 646 YKEAQAELEDYRKRKTLD-DIAVDYIPRDEHEKLMQVTNSLKY--KAENELLEMKSQYTKVLDEAEELKQMLDTQ---KQ 719
Cdd:TIGR04523 290 LNQLKSEISDLNNQKEQDwNKELKSELKNQEKKLEEIQNQISQnnKIISQLNEQISQLKKELTNSESENSEKQREleeKQ 369
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 720 NSL-----PIAEHQQVMNALRSTVKEMEEEINELKELLTNKESEVRNLQKELLEEKAAINEAMVPRAAYEKLQSSLEGEV 794
Cdd:TIGR04523 370 NEIeklkkENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQD 449
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 795 SILSSKLKDVIKEKENVSLDVMQLRSEVLHLKEEKEGMHNLLEAKEREVSGLHQKYHQAQEDLLEMKRYSESSSKLEEDK 874
Cdd:TIGR04523 450 SVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKL 529
                         490       500
                  ....*....|....*....|.
gi 2024434935 875 DKKINEMSKEVSKLKEALNSL 895
Cdd:TIGR04523 530 ESEKKEKESKISDLEDELNKD 550
COG5022 COG5022
Myosin heavy chain [General function prediction only];
682-953 3.47e-04

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 44.68  E-value: 3.47e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  682 TNSLKYKAENELLEMKSQYTKVLDEAEELKQMLDTQKQNSLPIAEHQQVMNALRSTV--KEMEEEINELKEllTNKEsev 759
Cdd:COG5022    829 EKKLRETEEVEFSLKAEVLIQKFGRSLKAKKRFSLLKKETIYLQSAQRVELAERQLQelKIDVKSISSLKL--VNLE--- 903
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  760 rnLQKELLEEKAAINEAMVpraayEKLQSSLEgevsiLSSKLKDVIKEKENVSLDVMQLRsevlhlkeekegmhnlleaK 839
Cdd:COG5022    904 --LESEIIELKKSLSSDLI-----ENLEFKTE-----LIARLKKLLNNIDLEEGPSIEYV-------------------K 952
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  840 EREVSGLHQKYHQAQEDLLEMKRYSESSSKLEEDKDKKINEMSKEVSKLKEALNSLSQLSYSTSAPKRQSQQLeALQQQV 919
Cdd:COG5022    953 LPELNKLHEVESKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQYGALQESTKQLKELPVEV-AELQSA 1031
                          250       260       270
                   ....*....|....*....|....*....|....
gi 2024434935  920 KQLQNQLTETKKQHQETVSVYRMHLLYAVQGQMD 953
Cdd:COG5022   1032 SKIISSESTELSILKPLQKLKGLLLLENNQLQAR 1065
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
563-897 3.57e-04

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


Pssm-ID: 428797 [Multi-domain]  Cd Length: 542  Bit Score: 44.46  E-value: 3.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 563 SKLSVEECEELKNSYCSVIDNINQEKALLIERYKEGQEEIKRLQDKltnqthlessaesgemkdamhrmIDELNRQLSEL 642
Cdd:pfam06160  84 AKKALDEIEELLDDIEEDIKQILEELDELLESEEKNREEVEELKDK-----------------------YRELRKTLLAN 140
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 643 SQLYKEAQAELEdyrkrKTLDDIAvdyiprDEHEKLMQVTNSLKYKAENELLEMKSQYTKVLDEA-EELKQMLDtQKQNS 721
Cdd:pfam06160 141 RFSYGPAIDELE-----KQLAEIE------EEFSQFEELTESGDYLEAREVLEKLEEETDALEELmEDIPPLYE-ELKTE 208
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 722 LPiaehQQvMNALRSTVKEMEEEINELKELltNKESEVRNLQKELLEEKAAINEAMVPRAAY---------EKLQSSLEG 792
Cdd:pfam06160 209 LP----DQ-LEELKEGYREMEEEGYALEHL--NVDKEIQQLEEQLEENLALLENLELDEAEEaleeieeriDQLYDLLEK 281
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 793 E------VSILSSKLKDVIKEKENVSldvMQLRSEVLHLKEEKEGMHNLLEAK---EREVSGLHQKYHQAQEDLLEMK-R 862
Cdd:pfam06160 282 EvdakkyVEKNLPEIEDYLEHAEEQN---KELKEELERVQQSYTLNENELERVrglEKQLEELEKRYDEIVERLEEKEvA 358
                         330       340       350
                  ....*....|....*....|....*....|....*
gi 2024434935 863 YSESSSKLEEDkDKKINEMSKEVSKLKEALNSLSQ 897
Cdd:pfam06160 359 YSELQEELEEI-LEQLEEIEEEQEEFKESLQSLRK 392
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
479-697 3.64e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.52  E-value: 3.64e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  479 IQETQSKYEEAAKEvLNAQKQVKPGLVSSESEetcselsklkvtcEEVEMLRQELRRALEESERQKEKVRELQKKFEERE 558
Cdd:COG4913    257 IRELAERYAAARER-LAELEYLRAALRLWFAQ-------------RRLELLEAELEELRAELARLEAELERLEARLDALR 322
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  559 qnvtsklsvEECEELKNSYCSV----IDNINQEKALLIERYKEGQEEIKRLQDKLT---------------NQTHLESSA 619
Cdd:COG4913    323 ---------EELDELEAQIRGNggdrLEQLEREIERLERELEERERRRARLEALLAalglplpasaeefaaLRAEAAALL 393
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  620 ES-GEMKDAMHRMIDELNRQLSELSQLYKEAQAELEDYRKRKTLddiavdyIPRDEHEKLMQVTNSLKYKAEN-----EL 693
Cdd:COG4913    394 EAlEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSN-------IPARLLALRDALAEALGLDEAElpfvgEL 466

                   ....
gi 2024434935  694 LEMK 697
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 2024434935  23 LLQAVENGDPEKVASllgkkgASATKQDSEGKTAFHLAATKGHAECLRIMVTHGADVTAQDGA-------------GHSA 89
Cdd:cd22197    70 LEIDKDSGNPKPLVN------AQCTDEYYRGHSALHIAIEKRSLQCVKLLVENGADVHARACGrffqkkqgtcfyfGELP 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  90 LHLAVKNSHIDCIKRLLQYK---CSVYSTDNSGKTALH------------YAATC----GCLQAVQLLCEHKCPINMKDL 150
Cdd:cd22197   144 LSLAACTKQWDVVNYLLENPhqpASLQAQDSLGNTVLHalvmiadnspenSALVIkmydGLLQAGARLCPTVQLEEISNH 223
                         170       180
                  ....*....|....*....|..
gi 2024434935 151 DGNIPLLLAVQNGHTEVCKYLL 172
Cdd:cd22197   224 EGLTPLKLAAKEGKIEIFRHIL 245
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
524-781 4.55e-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: 43.60  E-value: 4.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 524 EEVEMLRQELRRALEESERQKEKVRELQKKfeerEQNVTSKLsvEECEELKNSYCSVIDNINQEKALLIERYKEGQEEIK 603
Cdd:COG4942    20 DAAAEAEAELEQLQQEIAELEKELAALKKE----EKALLKQL--AALERRIAALARRIRALEQELAALEAELAELEKEIA 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 604 RLQDKLTNQthlesSAESGEMKDAMHRM--------------IDELNRQLSELSQLYKEAQAELEDYrkRKTLDDIAvdy 669
Cdd:COG4942    94 ELRAELEAQ-----KEELAELLRALYRLgrqpplalllspedFLDAVRRLQYLKYLAPARREQAEEL--RADLAELA--- 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 670 iprdeheklmqvtnslkyKAENELLEMKSQYTKVLDEAEELKQMLDTQKQnslpiaEHQQVMNALRSTVKEMEEEINELK 749
Cdd:COG4942   164 ------------------ALRAELEAERAELEALLAELEEERAALEALKA------ERQKLLARLEKELAELAAELAELQ 219
                         250       260       270
                  ....*....|....*....|....*....|..
gi 2024434935 750 ELLTNKESEVRNLQKELLEEKAAINEAMVPRA 781
Cdd:COG4942   220 QEAEELEALIARLEAEAAAAAERTPAAGFAAL 251
PHA02946 PHA02946
ankyin-like protein; Provisional
102-230 4.87e-04

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 43.89  E-value: 4.87e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 102 IKRLLQYKCSVYSTDNSGKTALHYAATCGCLQAVQLLCEHKCPINMKDLDGNIPL--LLAVQNGHTEVCKYLLDHGADIN 179
Cdd:PHA02946   55 VEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLyyLSGTDDEVIERINLLVQYGAKIN 134
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2024434935 180 TRDKNGRTALMIACEAGSLNMVEVFLRKGADVSLVDVFGQNALHYSKISEN 230
Cdd:PHA02946  135 NSVDEEGCGPLLACTDPSERVFKKIMSIGFEARIVDKFGKNHIHRHLMSDN 185
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
523-840 4.95e-04

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


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 44.19  E-value: 4.95e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  523 CEEVEMLRQELRRALEESERQKEKVRElqkkfEEREQNVTSKLSVEECEELKNSYCSVIDNINQEKALLIERYKEGQEEI 602
Cdd:pfam02463  193 EELKLQELKLKEQAKKALEYYQLKEKL-----ELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKL 267
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  603 KRLQDKLTNQTHLESSAESGEMKDAMHRMIDELNRQLSELSQLYKEAQAELEDYRKRKTLDDIAVDYIPRDEHEKLMQVT 682
Cdd:pfam02463  268 AQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKEL 347
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  683 NSLKYKAENELLEMKSQYTKVLDEAEELKQMLDTQKQNSLPIAEHQQVMNALRStvkEMEEEINELKELLTNKESEVRNL 762
Cdd:pfam02463  348 EIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKS---EEEKEAQLLLELARQLEDLLKEE 424
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024434935  763 QKELLEEKAAIneamvpraayEKLQSSLEGEVSILSSKLKDVIKEKENVSLDVMQLRSEVLHLKEEKEGMHNLLEAKE 840
Cdd:pfam02463  425 KKEELEILEEE----------EESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSR 492
PRK11281 PRK11281
mechanosensitive channel MscK;
606-897 4.97e-04

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 44.13  E-value: 4.97e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  606 QDKLTnQTHLESSAESGEMKDAMHRMIDELNRQLSELSQLYKEAQAELEDYrKRKTLDDIAVDYiprdehEKLmqvtnSL 685
Cdd:PRK11281    57 EDKLV-QQDLEQTLALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEAL-KDDNDEETRETL------STL-----SL 123
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  686 KykaenellEMKSQYTKVLDEAEELKQMLDTqkQNSLPIAEHQQ---VMNALRSTVKEMEEEINELKELLTNKESEVRNL 762
Cdd:PRK11281   124 R--------QLESRLAQTLDQLQNAQNDLAE--YNSQLVSLQTQperAQAALYANSQRLQQIRNLLKGGKVGGKALRPSQ 193
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  763 QKELLEEKAAINeamvprAAYEKLQSSLEGevsilSSKLKDVIKEKEN-VSLDVMQLRSEVLHLKEekegmhnLLEAKER 841
Cdd:PRK11281   194 RVLLQAEQALLN------AQNDLQRKSLEG-----NTQLQDLLQKQRDyLTARIQRLEHQLQLLQE-------AINSKRL 255
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024434935  842 EVSglHQKYHQAQEdllemkrySESSSKLEED----KDKKIN-EMSKEVSKLKEALNSLSQ 897
Cdd:PRK11281   256 TLS--EKTVQEAQS--------QDEAARIQANplvaQELEINlQLSQRLLKATEKLNTLTQ 306
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
44-172 5.21e-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: 44.02  E-value: 5.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  44 ASATKQDSEGKTAFHLAATKGHAECLRIMVTHGADVTAQDGA--------------GHSALHLAVKNSHIDCIKRLLQ-- 107
Cdd:cd22193    67 AEYTDEYYEGQTALHIAIERRQGDIVALLVENGADVHAHAKGrffqpkyqgegfyfGELPLSLAACTNQPDIVQYLLEne 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 108 -YKCSVYSTDNSGKTALHYAATCG------------CLQAVQLLCEHKCPI----NMKDLDGNIPLLLAVQNGHTEVCKY 170
Cdd:cd22193   147 hQPADIEAQDSRGNTVLHALVTVAdntkentkfvtrMYDMILIRGAKLCPTveleEIRNNDGLTPLQLAAKMGKIEILKY 226

                  ..
gi 2024434935 171 LL 172
Cdd:cd22193   227 IL 228
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
532-791 5.49e-04

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 43.76  E-value: 5.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 532 ELRRALEESERQKEKVRELQKKFEEReqnvtsKLSVEECEELK-NSYCSVIDNINQEKALLIERYKEGQEEIKRLQDKlt 610
Cdd:PRK05771   44 RLRKLRSLLTKLSEALDKLRSYLPKL------NPLREEKKKVSvKSLEELIKDVEEELEKIEKEIKELEEEISELENE-- 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 611 nqthlessaesgemkdamhrmIDELNRQLSELSQLyKEAQAELEDYRKRKTLDdIAVDYIPRDEHEKLMQVTNS------ 684
Cdd:PRK05771  116 ---------------------IKELEQEIERLEPW-GNFDLDLSLLLGFKYVS-VFVGTVPEDKLEELKLESDVenveyi 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 685 -------------LKYK--------AENELLEMKSQYTKVLDEA-EELKQMLDTQKqnslpiAEHQQVMNALRSTVKEME 742
Cdd:PRK05771  173 stdkgyvyvvvvvLKELsdeveeelKKLGFERLELEEEGTPSELiREIKEELEEIE------KERESLLEELKELAKKYL 246
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 2024434935 743 EEINELKELLTNKESEVRNLQKELLEEKAAINEAMVPRAAYEKLQSSLE 791
Cdd:PRK05771  247 EELLALYEYLEIELERAEALSKFLKTDKTFAIEGWVPEDRVKKLKELID 295
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
407-771 8.37e-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: 8.37e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  407 STLNATQSQEKLTSPSEIKIKYLQEDSKDAQRKLENSETKRKHLEAQVQSRVPEADLNNTDISENGSDPSLKIQETQSKY 486
Cdd:pfam02463  652 VSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQ 731
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  487 EEAAKEVLNAQKQVKPGLVSSESEETCSELSKLKVTCEEVEMLRQELRRALEESERQKEKVRELQKKFEEREQNVTSKLS 566
Cdd:pfam02463  732 DKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELK 811
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  567 VEECEELKnsycsviDNINQEKALLIERyKEGQEEIKRLQDKLTNQTHLESSAESGEMKDAMHRMIDELNRQLSELSQL- 645
Cdd:pfam02463  812 EEAELLEE-------EQLLIEQEEKIKE-EELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQk 883
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  646 --YKEAQAELEDYRKRKTLD-DIAVDYIPRDEHEKL---MQVTNSLKYKAENELLEMKSQYTKVLDEAEE-LKQMLDTQK 718
Cdd:pfam02463  884 lkDELESKEEKEKEEKKELEeESQKLNLLEEKENEIeerIKEEAEILLKYEEEPEELLLEEADEKEKEENnKEEEEERNK 963
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2024434935  719 QNSLPIAEHQQVMNALRSTVKEMEEEINELKELLTNKESEVRNLQKELLEEKA 771
Cdd:pfam02463  964 RLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETC 1016
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
119-147 1.05e-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: 1.05e-03
                          10        20
                  ....*....|....*....|....*....
gi 2024434935 119 GKTALHYAATCGCLQAVQLLCEHKCPINM 147
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
341-719 1.19e-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: 42.80  E-value: 1.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 341 TEQQDLLMLMQAKIASLTLHNKELQDKL----QERTPKEVDSTIDSYHSTQREFDQTADRQSEISAQelkSTLNAtqSQE 416
Cdd:pfam17380 266 TENEFLNQLLHIVQHQKAVSERQQQEKFekmeQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQ---AAIYA--EQE 340
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 417 KLTSPSEIKIKYLQEDskdaQRKLENSETKRKHLEAQVqSRVPEADlnntdisengsdpslKIQETQSKYEEAAKEVLNA 496
Cdd:pfam17380 341 RMAMERERELERIRQE----ERKRELERIRQEEIAMEI-SRMRELE---------------RLQMERQQKNERVRQELEA 400
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 497 QKQVKPGLVSSESEETCSELSKLKVTCEEVEMLRQELRRALEESERQKEKVRELQkkfEEREQNVtSKLSVEECEElkns 576
Cdd:pfam17380 401 ARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEE---QERQQQV-ERLRQQEEER---- 472
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 577 ycsvidninQEKALLIERYKEGQEEIKRLQDKLTNQthlessaesgEMKDAMHRMIDELNRQLSELSQLYKEAQAELEDY 656
Cdd:pfam17380 473 ---------KRKKLELEKEKRDRKRAEEQRRKILEK----------ELEERKQAMIEEERKRKLLEKEMEERQKAIYEEE 533
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024434935 657 RKRKTlddiavdyiprdEHEKLMQVTNSLKYKAENELL---EMKSQYTKVLDEAEELKQMLDTQKQ 719
Cdd:pfam17380 534 RRREA------------EEERRKQQEMEERRRIQEQMRkatEERSRLEAMEREREMMRQIVESEKA 587
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
86-113 1.25e-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: 1.25e-03
                           10        20
                   ....*....|....*....|....*...
gi 2024434935   86 GHSALHLAVKNSHIDCIKRLLQYKCSVY 113
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADIN 29
Ank_4 pfam13637
Ankyrin repeats (many copies);
185-224 1.48e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 37.64  E-value: 1.48e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2024434935 185 GRTALMIACEAGSLNMVEVFLRKGADVSLVDVFGQNALHY 224
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHF 40
KpsE COG3524
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
630-758 1.51e-03

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


Pssm-ID: 442746 [Multi-domain]  Cd Length: 370  Bit Score: 42.14  E-value: 1.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 630 RMIDELN------------RQLSELSQLYKEAQAELEDYR-KRKTLDdiavdyiPRDEHEKLMQVTNSLkykaENELLEM 696
Cdd:COG3524   165 ELVNQLSeraredavrfaeEEVERAEERLRDAREALLAFRnRNGILD-------PEATAEALLQLIATL----EGQLAEL 233
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024434935 697 KSQytkvldeaeeLKQMLDTQKQNSLPIAehqqvmnALRSTVKEMEEEINELKELLTNKESE 758
Cdd:COG3524   234 EAE----------LAALRSYLSPNSPQVR-------QLRRRIAALEKQIAAERARLTGASGG 278
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
86-117 1.57e-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: 1.57e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 2024434935  86 GHSALHLAV-KNSHIDCIKRLLQYKCSVYSTDN 117
Cdd:pfam00023   2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
709-932 2.36e-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: 2.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 709 ELKQMLDTQKQNSLPIAEHQQVMNALRSTVKEMEEEINELKELLTNKESEVRNLQKELLEEKAAINEAM-----VPRAAY 783
Cdd:COG3883    17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERReelgeRARALY 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 784 EKLQSSLEGEVSILSSKLKDVIKEKENVSLDVMQLRSEVLHLKEEKEgmhnLLEAKEREVSGLHQKYHQAQEDLLEMKRY 863
Cdd:COG3883    97 RSGGSVSYLDVLLGSESFSDFLDRLSALSKIADADADLLEELKADKA----ELEAKKAELEAKLAELEALKAELEAAKAE 172
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024434935 864 SESsskLEEDKDKKINEMSKEVSKLKEALNSLSQLSYSTSAPKRQSQQLEALQQQVKQLQNQLTETKKQ 932
Cdd:COG3883   173 LEA---QQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 238
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
688-830 2.61e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 41.74  E-value: 2.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 688 KAENELLEMKSQYTKVLDEAEELKQMLDTQKQNSlpiaeHQQVMNALRSTVKEMEEEINELKELLTNKESEVRNlqKELL 767
Cdd:PRK00409  538 EAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEA-----EKEAQQAIKEAKKEADEIIKELRQLQKGGYASVKA--HELI 610
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024434935 768 EEKAAINEAMVPRAA-----YEKLQSSLEG-EVSILSSKLKDVIKEKE-----NVSLDVMQLR---SEVLHLKEEKE 830
Cdd:PRK00409  611 EARKRLNKANEKKEKkkkkqKEKQEELKVGdEVKYLSLGQKGEVLSIPddkeaIVQAGIMKMKvplSDLEKIQKPKK 687
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
522-778 2.70e-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: 41.75  E-value: 2.70e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  522 TCEEVEMLRQELRRALEESERQKEkvrELQKKFEEREQNVTSKLSVEEcEELKNSycsvIDNINQEKALLIERYKEGQEE 601
Cdd:pfam12128  252 TLESAELRLSHLHFGYKSDETLIA---SRQEERQETSAELNQLLRTLD-DQWKEK----RDELNGELSAADAAVAKDRSE 323
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  602 IKRLQDKLT--NQTHLESSAESGEMKDAMHRMIDELNRQLSELSQLYKEAQAE---LEDYRKRKTLDDIAV-----DYIp 671
Cdd:pfam12128  324 LEALEDQHGafLDADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKynrRRSKIKEQNNRDIAGikdklAKI- 402
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  672 RDEHEKLMQVTNSLKYKAENEL-LEMKSQYTKVLDEAEELKQMLDTQK-QNSLPIAEHQQVMNalrstVKEMEEEINELK 749
Cdd:pfam12128  403 REARDRQLAVAEDDLQALESELrEQLEAGKLEFNEEEYRLKSRLGELKlRLNQATATPELLLQ-----LENFDERIERAR 477
                          250       260
                   ....*....|....*....|....*....
gi 2024434935  750 ELLTNKESEVRNLQKELLEEKAAINEAMV 778
Cdd:pfam12128  478 EEQEAANAEVERLQSELRQARKRRDQASE 506
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
683-897 2.91e-03

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 41.54  E-value: 2.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 683 NSLKYKAENELLEMKSQYTKVLDEAEELKQMLDT-----QKQNSL--PIAEHQQVMNALRSTVKEMEEEINELKELLTNK 755
Cdd:TIGR04523  43 KTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKikileQQIKDLndKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKL 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 756 ESEVRNLQKELLEEKAAINEAMVPraayeklQSSLEGEVSILSSKLKDVIKEKENVSLDVMQLRSEVLHLKEEKEGMHNL 835
Cdd:TIGR04523 123 EVELNKLEKQKKENKKNIDKFLTE-------IKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNK 195
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024434935 836 LEAKEREVSGLH---QKYHQAQEDLLEMKRYSESSSKLEEDKDKKINEMSKEVSKLKEALNSLSQ 897
Cdd:TIGR04523 196 LLKLELLLSNLKkkiQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKD 260
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
156-237 3.30e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 41.39  E-value: 3.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 156 LLLAVQNGHTEVCKYLLDHGADINTRDKNGRTALMIACEAGSLNMVEVFLRKGADVSLVDVFGQNALHYSKISENTGIQN 235
Cdd:PLN03192  529 LLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFR 608

                  ..
gi 2024434935 236 LL 237
Cdd:PLN03192  609 IL 610
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
534-893 3.71e-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: 40.99  E-value: 3.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 534 RRALEESERQ----KEKVRELQKKFEE-REQNVTSKLSVEECEELknsYCSVIDNINQEKALLIERYKEGQEEIKRLQDK 608
Cdd:pfam06160  85 KKALDEIEELlddiEEDIKQILEELDElLESEEKNREEVEELKDK---YRELRKTLLANRFSYGPAIDELEKQLAEIEEE 161
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 609 LTNQTHLESSA---ESGEMKDAMHRMIDELNRQLSELSQLYKEAQAELED--------YRKRK----TLDDIAVDyiprd 673
Cdd:pfam06160 162 FSQFEELTESGdylEAREVLEKLEEETDALEELMEDIPPLYEELKTELPDqleelkegYREMEeegyALEHLNVD----- 236
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 674 ehEKLMQVTNSLKyKAENELLEMKsqytkvLDEAEELKQMLDTQkqnslpIAEHQQVMNALRSTVKEMEEEINELKELLT 753
Cdd:pfam06160 237 --KEIQQLEEQLE-ENLALLENLE------LDEAEEALEEIEER------IDQLYDLLEKEVDAKKYVEKNLPEIEDYLE 301
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 754 nkesEVRNLQKELLEEKAAINEAMVPRAAYEKLQSSLEGEVSILSSKLKDVIKEKENVSLDVMQLRSEVLHLKEEKEGMH 833
Cdd:pfam06160 302 ----HAEEQNKELKEELERVQQSYTLNENELERVRGLEKQLEELEKRYDEIVERLEEKEVAYSELQEELEEILEQLEEIE 377
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024434935 834 NLLEAKEREVSGLHQKYHQAQE-------DLLEMKRYSESS--SKLEEDKDKKINEMSKEVSKLKEALN 893
Cdd:pfam06160 378 EEQEEFKESLQSLRKDELEAREkldefklELREIKRLVEKSnlPGLPESYLDYFFDVSDEIEDLADELN 446
Mitofilin pfam09731
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ...
531-848 3.78e-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: 3.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 531 QELRRALEESERQKEKVRELQKKFEEREQNVTSKLSVEECEELKNSYCSVIDNINQEKALLIERYKEGQEEIKRLQDKLT 610
Cdd:pfam09731 124 QEKEKALEEVLKEAISKAESATAVAKEAKDDAIQAVKAHTDSLKEASDTAEISREKATDSALQKAEALAEKLKEVINLAK 203
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 611 NQTHLESSAESGEMKDAMHRMIDELNRQLSELSQLYKEAqAELEDYRKRKTLDdiavdyiPRDEHEKLMQVTNSLKYKAE 690
Cdd:pfam09731 204 QSEEEAAPPLLDAAPETPPKLPEHLDNVEEKVEKAQSLA-KLVDQYKELVASE-------RIVFQQELVSIFPDIIPVLK 275
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 691 NELLEMKSQYTKVLDEA-EELKQMldTQKQNSLPIAEHQQVMNALRSTVKEMEEEINELKELLTNK-ESEVRNLQKELLE 768
Cdd:pfam09731 276 EDNLLSNDDLNSLIAHAhREIDQL--SKKLAELKKREEKHIERALEKQKEELDKLAEELSARLEEVrAADEAQLRLEFER 353
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 769 EKAAINEAMvpraaYEKLQSSLEGEVSILSSKLKDVIKEKEnVSLDVMQLRSEVLHLKEEKEGMHNLLEAKEREVSGLHQ 848
Cdd:pfam09731 354 EREEIRESY-----EEKLRTELERQAEAHEEHLKDVLVEQE-IELQREFLQDIKEKVEEERAGRLLKLNELLANLKGLEK 427
PHA02859 PHA02859
ankyrin repeat protein; Provisional
67-187 3.80e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 39.80  E-value: 3.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  67 ECLRIMVTHGADVTAQ-DGAGHSALHLAV---KNSHIDCIKRLLQYKCSVYSTDNSGKTALH-YAATCGC-LQAVQLLCE 140
Cdd:PHA02859   67 EILKFLIENGADVNFKtRDNNLSALHHYLsfnKNVEPEILKILIDSGSSITEEDEDGKNLLHmYMCNFNVrINVIKLLID 146
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2024434935 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 3.82e-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: 41.28  E-value: 3.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  44 ASATKQDSEGKTAFHLAATKGHAECLRIMVTHGADVTAQ------------DG--AGHSALHLAVKNSHIDCIKRLLQyK 109
Cdd:cd22194   132 AEYTEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAHakgvffnpkykhEGfyFGETPLALAACTNQPEIVQLLME-K 210
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024434935 110 CS--VYSTDNSGKTALHYAATCG------------CLQAVQLLCEHKCPINMKDLDGNIPLLLAVQNGHTEVCKYLL 172
Cdd:cd22194   211 EStdITSQDSRGNTVLHALVTVAedsktqndfvkrMYDMILLKSENKNLETIRNNEGLTPLQLAAKMGKAEILKYIL 287
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
545-893 3.99e-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: 41.19  E-value: 3.99e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  545 EKVRELQKKFEEREQNVTSKLSVEE-----------CEELKNSYCSVIDNINQEKAllIERYKEGQEEIkrLQDKLTNQT 613
Cdd:TIGR01612 1365 DEVKEYTKEIEENNKNIKDELDKSEklikkikddinLEECKSKIESTLDDKDIDEC--IKKIKELKNHI--LSEESNIDT 1440
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  614 HLESSAESGEMKDAMHRMIDELNRQLSELSQLYKEAQAELEDYRKRKTLDDIAVDYIPRDEHEKlmqvtNSLKYKAENEL 693
Cdd:TIGR01612 1441 YFKNADENNENVLLLFKNIEMADNKSQHILKIKKDNATNDHDFNINELKEHIDKSKGCKDEADK-----NAKAIEKNKEL 1515
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  694 LEM-KSQYTKVLDE--AEELKQMLD-TQKQNSLPIAEHQQVMNALRSTVKEMEEEINELKELLTNKESEVRNLQKellEE 769
Cdd:TIGR01612 1516 FEQyKKDVTELLNKysALAIKNKFAkTKKDSEIIIKEIKDAHKKFILEAEKSEQKIKEIKKEKFRIEDDAAKNDK---SN 1592
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  770 KAAINeamvpraayekLQSSLEG------EVSILSSKLKDVIKEKENVsldvmqlrsevlhlkeEKEGMHNLLEAKEREV 843
Cdd:TIGR01612 1593 KAAID-----------IQLSLENfenkflKISDIKKKINDCLKETESI----------------EKKISSFSIDSQDTEL 1645
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|
gi 2024434935  844 SGLHQKYHQAQEDLLEMKryseSSSKLEEDKDKKINEMSKEVSKLKEALN 893
Cdd:TIGR01612 1646 KENGDNLNSLQEFLESLK----DQKKNIEDKKKELDELDSEIEKIEIDVD 1691
PHA02989 PHA02989
ankyrin repeat protein; Provisional
99-205 4.05e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 40.88  E-value: 4.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  99 IDCIKRLLQYKCSVYSTDNSGKTAL------HYAATCGCLQAVQLLCEHkCPINMKDLDGNIPLLLAVQNGHTEVCKYLL 172
Cdd:PHA02989  198 IKVIKYLIKKGVNIETNNNGSESVLesfldnNKILSKKEFKVLNFILKY-IKINKKDKKGFNPLLISAKVDNYEAFNYLL 276
                          90       100       110
                  ....*....|....*....|....*....|...
gi 2024434935 173 DHGADINTRDKNGRTALMIACEAGSLNMVEVFL 205
Cdd:PHA02989  277 KLGDDIYNVSKDGDTVLTYAIKHGNIDMLNRIL 309
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
340-857 5.01e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 40.79  E-value: 5.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 340 ETEQQDLLMLMQAKIASLT--LHNKELQDKLQERTPKEVDSTIDSYHSTQREFDqtaDRQSEISaqELKSTLNATQSqEK 417
Cdd:PRK02224  201 EKDLHERLNGLESELAELDeeIERYEEQREQARETRDEADEVLEEHEERREELE---TLEAEIE--DLRETIAETER-ER 274
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 418 LTspseikikyLQEDSKDAQRKLENSETKRKHLEAQ----------VQSRVPEADLNNTDISENGSDPSLKIQETQSKYE 487
Cdd:PRK02224  275 EE---------LAEEVRDLRERLEELEEERDDLLAEaglddadaeaVEARREELEDRDEELRDRLEECRVAAQAHNEEAE 345
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 488 EAAKEVL-----NAQKQVKPGLVSSESEETCSELSKLKVTCEEVEMLRQELRRALEESERQKEKVRELQKKFEEREQNVT 562
Cdd:PRK02224  346 SLREDADdleerAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELR 425
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 563 SKLSveeceELKNSYCSVIDNINQEKALL-----------------IERYKEGQEEIKRLQDKL----TNQTHLESSAES 621
Cdd:PRK02224  426 EREA-----ELEATLRTARERVEEAEALLeagkcpecgqpvegsphVETIEEDRERVEELEAELedleEEVEEVEERLER 500
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 622 GEMKDAMHRMIDELNRQLSELSQLYKEAQAELEDYR-KRKTLDDIAVDYipRDEHEKLMQVTNSLKYKAENELLEMKSQY 700
Cdd:PRK02224  501 AEDLVEAEDRIERLEERREDLEELIAERRETIEEKReRAEELRERAAEL--EAEAEEKREAAAEAEEEAEEAREEVAELN 578
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 701 TKVLDEAEELKQMLDTQKQNSLpIAEHQQVMNALRSTVKEMEEEINELKELLTNKESEVRNLQKELleEKAAINEAMVPR 780
Cdd:PRK02224  579 SKLAELKERIESLERIRTLLAA-IADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEF--DEARIEEAREDK 655
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 781 AAYEKLQSSLEGEVSILSSKLKDVIKEKENVSLDVMQLRSevlhLKEEKEGMHNLLEAKE---REVSGLHQKYHQAQEDL 857
Cdd:PRK02224  656 ERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEE----LRERREALENRVEALEalyDEAEELESMYGDLRAEL 731
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
733-872 5.04e-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: 5.04e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  733 ALRSTVKEMEEEINELKELLTNKESEVRNLQKElleekaaineamvpRAAYEKLQSSLEGEVSILS-----SKLKDVIKE 807
Cdd:COG4913    614 ALEAELAELEEELAEAEERLEALEAELDALQER--------------REALQRLAEYSWDEIDVASaereiAELEAELER 679
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024434935  808 KENVSLDVMQLRSEVLHLKEEKEGMHNLLEAKEREVSGLHQKYHQAQEDLLEMKRYSESSSKLEE 872
Cdd:COG4913    680 LDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLAR 744
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
637-880 5.31e-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: 5.31e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  637 RQLSELSQLYKEAQAELED-YRKRKTLDDIavdyipRDEHEKlmqvtnslkykaenellemksqYTKVLDEAEELKQMLD 715
Cdd:COG4913    228 DALVEHFDDLERAHEALEDaREQIELLEPI------RELAER----------------------YAAARERLAELEYLRA 279
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  716 TqkqnsLPIAEHQQVMNALRSTVKEMEEEINELKELLTNKESEVRNLQKELLEEKAAINEamvprAAYEKLQsSLEGEVS 795
Cdd:COG4913    280 A-----LRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRG-----NGGDRLE-QLEREIE 348
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  796 ILSSKLKDVIKEKENVSLDVMQLRsevLHLKEEKEGMHNLLEAKEREVSGLHQKYHQAQEDLLEMKRyseSSSKLEEDKD 875
Cdd:COG4913    349 RLERELEERERRRARLEALLAALG---LPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEA---ALRDLRRELR 422

                   ....*
gi 2024434935  876 KKINE 880
Cdd:COG4913    423 ELEAE 427
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
423-895 5.32e-03

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 40.77  E-value: 5.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 423 EIKIKYLQEDSKDAQRKLENSETKRKHLEAQVQSRvpEADLNNTDISENGSDPSL-KIQETQSKYEEAAKEVLNAQKQVK 501
Cdd:TIGR04523 151 EKELEKLNNKYNDLKKQKEELENELNLLEKEKLNI--QKNIDKIKNKLLKLELLLsNLKKKIQKNKSLESQISELKKQNN 228
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 502 pglvsSESEETCSELSKLKVTCEEVEMLRQELRRALEESERQKEKVRELQKKFEEREQNVTSKlsveecEELKNSYCSVI 581
Cdd:TIGR04523 229 -----QLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKEL------EKQLNQLKSEI 297
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 582 DNINQEKALLIEryKEGQEEIKRLQDKLTN-QTHLESSAESgemkdamhrmIDELNRQLSELSQLYKEAQAELEDYRKRK 660
Cdd:TIGR04523 298 SDLNNQKEQDWN--KELKSELKNQEKKLEEiQNQISQNNKI----------ISQLNEQISQLKKELTNSESENSEKQREL 365
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 661 TLDDIAVDYIPRDEHEKLMQVTNslkykAENELLEMKSQytkvLDEAEELKQMLDTQKQNslpiaehqqvmnaLRSTVKE 740
Cdd:TIGR04523 366 EEKQNEIEKLKKENQSYKQEIKN-----LESQINDLESK----IQNQEKLNQQKDEQIKK-------------LQQEKEL 423
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 741 MEEEINELKELLTNKESEVRNLQKELLEEKAAINEAMVPRAAYEKLQSSLEGEVSILSSKLKDV-----IKEKENVSL-- 813
Cdd:TIGR04523 424 LEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKqkelkSKEKELKKLne 503
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 814 DVMQLRSEVLHLKEEKEGMHNLLEAKEREVSGLHQKYHQAQEDLLEMKrYSESSSKLEEDKDKKinemSKEVSKLKEALN 893
Cdd:TIGR04523 504 EKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDD-FELKKENLEKEIDEK----NKEIEELKQTQK 578

                  ..
gi 2024434935 894 SL 895
Cdd:TIGR04523 579 SL 580
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
26-94 6.24e-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: 6.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  26 AVENGDPEKVASLLgKKGASATKQDSEGkTAFHL---------------AATKGHAECLRIMVTHGADVTAQDGAGHSAL 90
Cdd:cd22192    96 AVVNQNLNLVRELI-ARGADVVSPRATG-TFFRPgpknliyygehplsfAACVGNEEIVRLLIEHGADIRAQDSLGNTVL 173

                  ....
gi 2024434935  91 HLAV 94
Cdd:cd22192   174 HILV 177
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
44-172 6.64e-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: 40.45  E-value: 6.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935  44 ASATKQDSEGKTAFHLAATKGHAECLRIMVTHGADVTA------------QDGAGHSALHL----AVKNSHIdcIKRLLQ 107
Cdd:TIGR00870 119 DQYTSEFTPGITALHLAAHRQNYEIVKLLLERGASVPAracgdffvksqgVDSFYHGESPLnaaaCLGSPSI--VALLSE 196
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 108 YKCSVYSTDNSGKTALHYAA------------TCGCLQ-AVQLLcEHKCPIN----MKDLDGNIPLLLAVQNGHTEVCKY 170
Cdd:TIGR00870 197 DPADILTADSLGNTLLHLLVmenefkaeyeelSCQMYNfALSLL-DKLRDSKelevILNHQGLTPLKLAAKEGRIVLFRL 275

                  ..
gi 2024434935 171 LL 172
Cdd:TIGR00870 276 KL 277
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
632-793 7.02e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 39.81  E-value: 7.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 632 IDELNRQLSELSQLYKEAQAELEDYRKR--KTLDDIAVDYIPRDEHEKLMQVTNSLKYKAE------NELLEMKSqYTKV 703
Cdd:COG3883    39 LDALQAELEELNEEYNELQAELEALQAEidKLQAEIAEAEAEIEERREELGERARALYRSGgsvsylDVLLGSES-FSDF 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 704 LDEAEELKQMLDTQKQNslpIAEHQQVMNALRSTVKEMEEEINELKELLTNKESEVRNLQKELLEEKAAINEAMVPRAAY 783
Cdd:COG3883   118 LDRLSALSKIADADADL---LEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAA 194
                         170
                  ....*....|
gi 2024434935 784 EKLQSSLEGE 793
Cdd:COG3883   195 EAQLAELEAE 204
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
396-918 7.79e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.31  E-value: 7.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 396 RQSEI--SAQELKSTLNATQSQEKLtspseIKIKYLQEDSKDAQRKLENSETKRKHLEAQVQSRVPEADLNNTDISENgs 473
Cdd:COG1196   207 RQAEKaeRYRELKEELKELEAELLL-----LKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEEL-- 279
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 474 dpSLKIQETQSKYEEAAKEVLNAQKQVKPGLVSSESEETCSELSKlkvtcEEVEMLRQELRRALEESERQKEKVRELQKK 553
Cdd:COG1196   280 --ELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELE-----EELAELEEELEELEEELEELEEELEEAEEE 352
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 554 FEEREQNVTSKLSVEEceelknsycSVIDNINQEKALLIERYKEGQEEIKRLQDKLTNQTHLESSAESGEMKDAMHR-MI 632
Cdd:COG1196   353 LEEAEAELAEAEEALL---------EAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEeEL 423
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 633 DELNRQLSELSQLYKEAQAELEDYRKR--KTLDDIAVDYIPRDEHEKLMQVTNSLKYKAENELLEMKSQYTKVLDEAEE- 709
Cdd:COG1196   424 EELEEALAELEEEEEEEEEALEEAAEEeaELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADy 503
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 710 --------LKQMLDTQKQNSLPIAEHQQV----------------MNALRSTVKEMEEEINELKE----------LLTNK 755
Cdd:COG1196   504 egflegvkAALLLAGLRGLAGAVAVLIGVeaayeaaleaalaaalQNIVVEDDEVAAAAIEYLKAakagratflpLDKIR 583
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 756 ESEVRNLQKELLEEKAAINEAMVPR----AAYEKLQSSLEGEVSI-------------LSSKLKDVIKEKENVSLDVMQL 818
Cdd:COG1196   584 ARAALAAALARGAIGAAVDLVASDLreadARYYVLGDTLLGRTLVaarleaalrravtLAGRLREVTLEGEGGSAGGSLT 663
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 819 RSEVLHLKEEKEGMHNLLEAKEREVSGLHQKYHQAQEDLLEMKRYSESSSKLEEDKDKKINEMSKEVSKLKEALNSLSQL 898
Cdd:COG1196   664 GGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLE 743
                         570       580
                  ....*....|....*....|....*
gi 2024434935 899 SYSTS-----APKRQSQQLEALQQQ 918
Cdd:COG1196   744 EEELLeeealEELPEPPDLEELERE 768
14-3-3_fungi cd11309
Fungal 14-3-3 protein domain; This family containing fungal 14-3-3 domains includes the yeasts ...
533-671 8.00e-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: 39.21  E-value: 8.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 533 LRRALEESERQKEKVRELQKKFEEREqnvtsKLSVEECEELKNSYCSVI------------------DNINQEKALLIER 594
Cdd:cd11309     7 LAKLAEQAERYEEMVENMKKVASSDQ-----ELTVEERNLLSVAYKNVIgarraswrivssieqkeeSKGNESQVALIKE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 595 YKEGQE-EIKRLQDKLTN--QTHLESSAESGEMKDAMHRMIDELNRQLSELS---QLYKEAQAELEDYrkrKTLDDIAVD 668
Cdd:cd11309    82 YRSKIEsELTKICDDILSvlDKHLIPSATTGESKVFYYKMKGDYHRYLAEFAvgdKRKEAADSSLEAY---KAASDIAVT 158

                  ...
gi 2024434935 669 YIP 671
Cdd:cd11309   159 ELP 161
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
401-666 8.48e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 39.75  E-value: 8.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 401 SAQELKSTLNATQSQekltspseikIKYLQEDSKDAQRKLENSETKRKHLEAQVQSRVPEADLNNTDISENGSdpslKIQ 480
Cdd:COG4942    21 AAAEAEAELEQLQQE----------IAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEA----ELA 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 481 ETQSKYEEAAKEvLNAQKQVKPGLVSSESEETCSELSKLKVTCEEVEMLRQELRRALEESERQKEKVRELQKKFEEREQn 560
Cdd:COG4942    87 ELEKEIAELRAE-LEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAA- 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 561 vtsklsveeceelknsycsVIDNINQEKALLIERYKEGQEEIKRLQDKLTNQTHLESSAESGEMKDAmhRMIDELNRQLS 640
Cdd:COG4942   165 -------------------LRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELA--AELAELQQEAE 223
                         250       260
                  ....*....|....*....|....*.
gi 2024434935 641 ELSQLYKEAQAELEDYRKRKTLDDIA 666
Cdd:COG4942   224 ELEALIARLEAEAAAAAERTPAAGFA 249
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
524-669 8.83e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 40.00  E-value: 8.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 524 EEVEMLRQELRRALEESERQKEKVRELQKKFEEREQNVTSKLSVEECEELKNSYcsviDNINQEKALLIERYKEGQEEIK 603
Cdd:COG3206   219 QQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQL----AELEAELAELSARYTPNHPDVI 294
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024434935 604 RLQDKLTNqthLESsaesgEMKDAMHRMIDELNRQLSELSQLYKEAQAELEDYRKR-KTLDDIAVDY 669
Cdd:COG3206   295 ALRAQIAA---LRA-----QLQQEAQRILASLEAELEALQAREASLQAQLAQLEARlAELPELEAEL 353
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
524-810 9.28e-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: 39.72  E-value: 9.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 524 EEVEMLRQE-LRRALEESERQKEKVRELQKKFEEREQNVTSKLSV-EECEELKNSYCSVIDNINQEK------------- 588
Cdd:pfam17380 291 EKFEKMEQErLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIyAEQERMAMERERELERIRQEErkrelerirqeei 370
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 589 ALLIERYKEGQE-EIKRLQDKLTNQTHLESSAESGEMKDAMHRMIDELNRQLSELSQLYKEAQAE----LEDYRKRKtld 663
Cdd:pfam17380 371 AMEISRMRELERlQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQRevrrLEEERARE--- 447
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024434935 664 diaVDYIPRDEHEKLMQVTNSLKYKAEN--ELLEMKSQYTKvLDEAEELKQMLDTQ--KQNSLPIAEHQQVMNALRstvK 739
Cdd:pfam17380 448 ---MERVRLEEQERQQQVERLRQQEEERkrKKLELEKEKRD-RKRAEEQRRKILEKelEERKQAMIEEERKRKLLE---K 520
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024434935 740 EMEEEINELKELLTNKESEVRNLQKELLEEKAAINEAMVPRAAYEKLQSSLEGEVSILSSklkdvIKEKEN 810
Cdd:pfam17380 521 EMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLEAMEREREMMRQ-----IVESEK 586
 
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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