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Conserved domains on  [gi|151101151|ref|NP_001092694|]
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intraflagellar transport protein 74 homolog isoform b [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 101-351 4.77e-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]


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 61.23  E-value: 4.77e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151   101 LRSKISELTTEVNKLQKGIEMYNQENSVYLS-YEKRAETLAVEIKELQGQLADYNMLVDKLNTNTEMEEVMNDYNMLKAQ 179
Cdd:TIGR02168  198 LERQLKSLERQAEKAERYKELKAELRELELAlLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVS 277

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151   180 NDRETqsldviFTERQAKEKQIRSVEEEIEQEKQATDDIIKNMsfENQVKYLEmkTTNEKLLQELDTLQQQLDSQNMKKE 259
Cdd:TIGR02168  278 ELEEE------IEELQKELYALANEISRLEQQKQILRERLANL--ERQLEELE--AQLEELESKLDELAEELAELEEKLE 347

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151   260 SLEAEIAHSQVKQEAvlLHEKLYELESHRDqmiAEDKSIGSPMEEREKLLKQIKDDNQEIASMERQLTDTKEKINQFIEE 339
Cdd:TIGR02168  348 ELKEELESLEAELEE--LEAELEELESRLE---ELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQE 422

                          250
                   ....*....|..
gi 151101151   340 IRQLDMDLEEHQ 351
Cdd:TIGR02168  423 IEELLKKLEEAE 434
dermokine super family cl42387
dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a ...
 7-50 8.52e-04

dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a skin-specific glycoprotein that may play a regulatory role in the crosstalk between barrier dysfunction and inflammation, and therefore play a role in inflammatory diseases such as psoriasis. Dermokine is one of the most highly expressed proteins in differentiating keratinocytes, found mainly in the spinous and granular layers of the epidermis, but also in the epithelia of the small intestine, macrophages of the lung, and endothelial cells of the lung. Mouse dermokine has been reported to be encoded by 22 exons, and its expression leads to alpha, beta, and gamma transcripts.


The actual alignment was detected with superfamily member cd21341:

Pssm-ID: 455732 [Multi-domain]  Cd Length: 139  Bit Score: 39.21  E-value: 8.52e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 151101151   7 SSAARPVSRggvglTGRPPSGI--------RPLSGNIRVATAMPPGTARPGS 50
Cdd:cd21341   66 SQAMRPTTS-----SGRPITGFvrpgtqsgRPGTSRQALRTPRRAGTARPVT 112
 
Name Accession Description Interval E-value
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 101-351 4.77e-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: 61.23  E-value: 4.77e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151   101 LRSKISELTTEVNKLQKGIEMYNQENSVYLS-YEKRAETLAVEIKELQGQLADYNMLVDKLNTNTEMEEVMNDYNMLKAQ 179
Cdd:TIGR02168  198 LERQLKSLERQAEKAERYKELKAELRELELAlLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVS 277

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151   180 NDRETqsldviFTERQAKEKQIRSVEEEIEQEKQATDDIIKNMsfENQVKYLEmkTTNEKLLQELDTLQQQLDSQNMKKE 259
Cdd:TIGR02168  278 ELEEE------IEELQKELYALANEISRLEQQKQILRERLANL--ERQLEELE--AQLEELESKLDELAEELAELEEKLE 347

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151   260 SLEAEIAHSQVKQEAvlLHEKLYELESHRDqmiAEDKSIGSPMEEREKLLKQIKDDNQEIASMERQLTDTKEKINQFIEE 339
Cdd:TIGR02168  348 ELKEELESLEAELEE--LEAELEELESRLE---ELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQE 422

                          250
                   ....*....|..
gi 151101151   340 IRQLDMDLEEHQ 351
Cdd:TIGR02168  423 IEELLKKLEEAE 434
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 133-349 4.68e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 58.02  E-value: 4.68e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151 133 EKRAETLAVEIKELQGQLADYNMLVDKLNTntEMEEVMNDYNMLKAQNDRETQSLDVI---FTERQAKEKQIRSVEEEIE 209
Cdd:COG1196  224 ELEAELLLLKLRELEAELEELEAELEELEA--ELEELEAELAELEAELEELRLELEELeleLEEAQAEEYELLAELARLE 301

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151 210 QEKQATDDIIKnmsfENQVKYLEMKTTNEKLLQELDTLQQQLDSQNMKKESLEAEIAHSQVKQEAVLlhEKLYELESHRD 289
Cdd:COG1196  302 QDIARLEERRR----ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAE--EALLEAEAELA 375

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151 290 QMIAEDKSIgspMEEREKLLKQIKDDNQEIASMERQLTDTKEKINQFIEEIRQLDMDLEE 349
Cdd:COG1196  376 EAEEELEEL---AEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAE 432
46 PHA02562
endonuclease subunit; Provisional
 143-345 2.18e-06

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 49.63  E-value: 2.18e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151 143 IKELQGQLADYNMLVDKLNTNTEMEEvmNDYNMLKAQNDRETQSLDVIFTERQAKEKQIRSVEEEIEQE--------KQA 214
Cdd:PHA02562 176 IRELNQQIQTLDMKIDHIQQQIKTYN--KNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDEllnlvmdiEDP 253

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151 215 TDDIIK--------NMSFENQVKYLEMKTTN-----------------EKLLQELDTLQQQLDSQNMKKESLEaEIAHsQ 269
Cdd:PHA02562 254 SAALNKlntaaakiKSKIEQFQKVIKMYEKGgvcptctqqisegpdriTKIKDKLKELQHSLEKLDTAIDELE-EIMD-E 331

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 151101151 270 VKQEAVLLHEKLYELESHRDQMIAEDKSIGSPMEEREKLLKQIKDDNQEIASMERQLTDTKEKINQFIEEIRQLDM 345
Cdd:PHA02562 332 FNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSELVKEKYHRGI 407
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 70-339 8.61e-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: 44.72  E-value: 8.61e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151    70 RPVTQQgLTGMKTGTKGPQRQILDKSYYLGLLRSKISELTTEVNKLQKGIEMYNQENSVYLSYEKRAETLAVEIKELQGQ 149
Cdd:pfam15921  478 RKVVEE-LTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQ 556

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151   150 LADYNMLVDKLNTNTE-MEEVMNDYN-------MLKAQ-----NDR--ETQSLDVIFTERQAKEKQIRSVEEEIEQEKQA 214
Cdd:pfam15921  557 MAEKDKVIEILRQQIEnMTQLVGQHGrtagamqVEKAQlekeiNDRrlELQEFKILKDKKDAKIRELEARVSDLELEKVK 636

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151   215 tddiIKNMSFENQVKYLEMKTTNEKLLQELDTLQQQLDS---------QNMKKESLEAEIAHSQVKQEavlLHEKLYELE 285
Cdd:pfam15921  637 ----LVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSlsedyevlkRNFRNKSEEMETTTNKLKMQ---LKSAQSELE 709

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 151101151   286 SHRDQMIAEDKSIGSPMEEREKLLKQIKDDNQEIASMERQLtdtkekinQFIEE 339
Cdd:pfam15921  710 QTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKI--------QFLEE 755
TTC8_N cd21341
N-terminal domain of tetratricopeptide repeat domain 8; Tetratricopeptide repeat domain 8 ...
 7-50 8.52e-04

N-terminal domain of tetratricopeptide repeat domain 8; Tetratricopeptide repeat domain 8 (TTC80), also known a BBS8, has been directly linked to Bardet-Biedl syndrome, an autosomal recessive ciliopathy characterized by retinal degeneration, renal failure, obesity, diabetes, male infertility, polydactyly and cognitive impairment. Mutations in BBS8 cause early vision loss. In addition to C-terminal tetratricopeptide repeats, TTC8 also contains an N-terminal domain of unknown function.


Pssm-ID: 411061 [Multi-domain]  Cd Length: 139  Bit Score: 39.21  E-value: 8.52e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 151101151   7 SSAARPVSRggvglTGRPPSGI--------RPLSGNIRVATAMPPGTARPGS 50
Cdd:cd21341   66 SQAMRPTTS-----SGRPITGFvrpgtqsgRPGTSRQALRTPRRAGTARPVT 112
 
Name Accession Description Interval E-value
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 101-351 4.77e-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: 61.23  E-value: 4.77e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151   101 LRSKISELTTEVNKLQKGIEMYNQENSVYLS-YEKRAETLAVEIKELQGQLADYNMLVDKLNTNTEMEEVMNDYNMLKAQ 179
Cdd:TIGR02168  198 LERQLKSLERQAEKAERYKELKAELRELELAlLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVS 277

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151   180 NDRETqsldviFTERQAKEKQIRSVEEEIEQEKQATDDIIKNMsfENQVKYLEmkTTNEKLLQELDTLQQQLDSQNMKKE 259
Cdd:TIGR02168  278 ELEEE------IEELQKELYALANEISRLEQQKQILRERLANL--ERQLEELE--AQLEELESKLDELAEELAELEEKLE 347

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151   260 SLEAEIAHSQVKQEAvlLHEKLYELESHRDqmiAEDKSIGSPMEEREKLLKQIKDDNQEIASMERQLTDTKEKINQFIEE 339
Cdd:TIGR02168  348 ELKEELESLEAELEE--LEAELEELESRLE---ELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQE 422

                          250
                   ....*....|..
gi 151101151   340 IRQLDMDLEEHQ 351
Cdd:TIGR02168  423 IEELLKKLEEAE 434
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 133-349 4.68e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 58.02  E-value: 4.68e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151 133 EKRAETLAVEIKELQGQLADYNMLVDKLNTntEMEEVMNDYNMLKAQNDRETQSLDVI---FTERQAKEKQIRSVEEEIE 209
Cdd:COG1196  224 ELEAELLLLKLRELEAELEELEAELEELEA--ELEELEAELAELEAELEELRLELEELeleLEEAQAEEYELLAELARLE 301

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151 210 QEKQATDDIIKnmsfENQVKYLEMKTTNEKLLQELDTLQQQLDSQNMKKESLEAEIAHSQVKQEAVLlhEKLYELESHRD 289
Cdd:COG1196  302 QDIARLEERRR----ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAE--EALLEAEAELA 375

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151 290 QMIAEDKSIgspMEEREKLLKQIKDDNQEIASMERQLTDTKEKINQFIEEIRQLDMDLEE 349
Cdd:COG1196  376 EAEEELEEL---AEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAE 432
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
104-285 7.77e-09

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 57.08  E-value: 7.77e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151 104 KISELTTEVNKLQKGIEMYNQENSVYLSYEKRAETLAVEIKELQGQLADYNMLVDKLNTNTEMEEVmndyNMLKAQNDRE 183
Cdd:COG4717   72 ELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEAL----EAELAELPER 147

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151 184 TQSLDVIFTERQAKEKQIRSVEEEIEQEKQATDDIIKNMSFENQVKYLEMKTTNEKLLQELDTLQQQLDSQNMKKESLEA 263
Cdd:COG4717  148 LEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEE 227

                        170       180
                 ....*....|....*....|..
gi 151101151 264 EIAHSQVKQEAVLLHEKLYELE 285
Cdd:COG4717  228 ELEQLENELEAAALEERLKEAR 249
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 101-326 7.97e-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: 57.37  E-value: 7.97e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151   101 LRSKISELTTEVNKLQKGIEMYNQE----NSVYLSYEKRAETLAVEIKELQGQLAdyNMLVDKLNTNTEMEEVMNDYNML 176
Cdd:TIGR02168  272 LRLEVSELEEEIEELQKELYALANEisrlEQQKQILRERLANLERQLEELEAQLE--ELESKLDELAEELAELEEKLEEL 349

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151   177 KAQNDRETQSLDVIFTERQAKEKQIRSVEEEIEQEKQATDDIIKNM-SFENQVKYLEmkTTNEKLLQELDTLQQQLDSQN 255
Cdd:TIGR02168  350 KEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIaSLNNEIERLE--ARLERLEDRRERLQQEIEELL 427

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 151101151   256 MKKESLEAEIAHSQVKQEAVLLHEKLYELESHRDQMIAEDKSIGSPMEEREKLLKQIKDDNQEIASMERQL 326
Cdd:TIGR02168  428 KKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQ 498
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 101-353 5.71e-07

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 51.61  E-value: 5.71e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151   101 LRSKISELTTEVNKLQKGIEMYNQENSvylSYEKRAETLAVEIKELQGQLADYNMLVDKLNTN-TEMEEVMNDYNmlKAQ 179
Cdd:TIGR02169  707 LSQELSDASRKIGEIEKEIEQLEQEEE---KLKERLEELEEDLSSLEQEIENVKSELKELEARiEELEEDLHKLE--EAL 781

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151   180 NDRETQSLDVIFTERQAKEKQIRSVEEEIEQEKQATDDIIKNMSFENQvkYLEmkttnekllQELDTLQQQLDSQNMKKE 259
Cdd:TIGR02169  782 NDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKE--YLE---------KEIQELQEQRIDLKEQIK 850

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151   260 SLEAEIAHSQVKQEavllhEKLYELESHRDQMIAEDKSIGSPMEEREKLLKQIKDDNQEIASMERQLTDTKEKINQFIEE 339
Cdd:TIGR02169  851 SIEKEIENLNGKKE-----ELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAK 925

                          250
                   ....*....|....
gi 151101151   340 IRQLDMDLEEHQDP 353
Cdd:TIGR02169  926 LEALEEELSEIEDP 939
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 101-344 6.41e-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: 51.60  E-value: 6.41e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151   101 LRSKISELTTEVNKLQKGIEMYNQENSvylSYEKRAETLAVEIKELQGQLADYNMLVDKLNTNTEMEEVMNdynmlkAQN 180
Cdd:TIGR02168  682 LEEKIEELEEKIAELEKALAELRKELE---ELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERI------AQL 752

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151   181 DRETQSLDVIFTERQAKEKQIRSVEEEIEQEKQATDDIIKNMSFENQvkylEMKTTNEKLLQELDTLQQQLDSQNMKKES 260
Cdd:TIGR02168  753 SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELK----ALREALDELRAELTLLNEEAANLRERLES 828

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151   261 LEAEIAhsQVKQEAVLLHEklyELESHRDQMIAEDKSIGSPMEEREKLLKQIKDDNQEIASMERQLTDTKEKINQFIEEI 340
Cdd:TIGR02168  829 LERRIA--ATERRLEDLEE---QIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEEL 903


                   ....
gi 151101151   341 RQLD 344
Cdd:TIGR02168  904 RELE 907
46 PHA02562
endonuclease subunit; Provisional
 143-345 2.18e-06

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 49.63  E-value: 2.18e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151 143 IKELQGQLADYNMLVDKLNTNTEMEEvmNDYNMLKAQNDRETQSLDVIFTERQAKEKQIRSVEEEIEQE--------KQA 214
Cdd:PHA02562 176 IRELNQQIQTLDMKIDHIQQQIKTYN--KNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDEllnlvmdiEDP 253

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151 215 TDDIIK--------NMSFENQVKYLEMKTTN-----------------EKLLQELDTLQQQLDSQNMKKESLEaEIAHsQ 269
Cdd:PHA02562 254 SAALNKlntaaakiKSKIEQFQKVIKMYEKGgvcptctqqisegpdriTKIKDKLKELQHSLEKLDTAIDELE-EIMD-E 331

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 151101151 270 VKQEAVLLHEKLYELESHRDQMIAEDKSIGSPMEEREKLLKQIKDDNQEIASMERQLTDTKEKINQFIEEIRQLDM 345
Cdd:PHA02562 332 FNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSELVKEKYHRGI 407
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 100-341 4.77e-06

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 48.48  E-value: 4.77e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151  100 LLRSKISELTTEVNKLQKGIEMYNQENSVylsyekraetLAVEIKELQGQLADYNMLVDKLNTNTEMEEvmNDYNMLKAQ 179
Cdd:TIGR04523 409 QKDEQIKKLQQEKELLEKEIERLKETIIK----------NNSEIKDLTNQDSVKELIIKNLDNTRESLE--TQLKVLSRS 476

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151  180 NDRETQSLDVIFTERQAKEKQIRSVEEEIEQEKQATDDIIKNMS-FENQVKYL--EMKTTNEKLLQ---ELDTLQQQLDS 253
Cdd:TIGR04523 477 INKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISsLKEKIEKLesEKKEKESKISDledELNKDDFELKK 556

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151  254 QNMKKESLEAEIAHSQVKQEAVLLHEKLYELESHRDQMIAEDKSIGSPMEEREKL-------LKQIKDDNQEIASMERQL 326
Cdd:TIGR04523 557 ENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKisslekeLEKAKKENEKLSSIIKNI 636

                         250
                  ....*....|....*
gi 151101151  327 TDTKEKINQFIEEIR 341
Cdd:TIGR04523 637 KSKKNKLKQEVKQIK 651
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 127-349 5.43e-06

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 48.53  E-value: 5.43e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151   127 SVYLSYEKRAETLAVEIKELQGQLADynmLVDKLNtntemeEVMNDYNMLKAQNDRETQSLDVIFTERQAKEKQIRSVEE 206
Cdd:TIGR02169  667 LFSRSEPAELQRLRERLEGLKRELSS---LQSELR------RIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKE 737

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151   207 EIEQEKQATDDIiknmsfenQVKYLEMKTTNEKLLQELDTLQQQLDSQNMKKESLEAEIAHSQVKQ-------------- 272
Cdd:TIGR02169  738 RLEELEEDLSSL--------EQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEiqaelskleeevsr 809

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 151101151   273 -EAVLLHEKLYELESHRDQMIAEDKsIGSPMEEREKLLKQIKDDNQEIASMERQLTDTKEKINQFIEEIRQLDMDLEE 349
Cdd:TIGR02169  810 iEARLREIEQKLNRLTLEKEYLEKE-IQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGD 886
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 134-342 2.43e-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: 45.91  E-value: 2.43e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151 134 KRAETLAVEIKELQGQLADYNMLVDKlnTNTEMEEVMNDYNMLKAQNDRETQSLDVIFTERQAKEKQIRSVEEEI----- 208
Cdd:COG4942   20 DAAAEAEAELEQLQQEIAELEKELAA--LKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIaelra 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151 209 --EQEKQATDDIIKNMSFENQVKYLEMKTTNEKLLQ---ELDTLQQQLDSQNMKKESLEAEIAhsQVKQEAVLLHEKLYE 283
Cdd:COG4942   98 elEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDavrRLQYLKYLAPARREQAEELRADLA--ELAALRAELEAERAE 175

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 151101151 284 LESHRDQMIAEDKSIGSPMEEREKLLKQIKDDNQEIASMERQLTDTKEKINQFIEEIRQ 342
Cdd:COG4942  176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEA 234
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
155-352 3.25e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.91  E-value: 3.25e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151 155 MLVDKLNTntEMEEVMNDYNMLKAQNDRETQSLDVIFTERQAKEKQIRSVEEEIEQEKQATDDIIKNMS-FENQVKYLEM 233
Cdd:COG4717   46 MLLERLEK--EADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEeLREELEKLEK 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151 234 KTTNEKLLQELDTLQQQLDSQNMKKESLEAEIAHSQVKQEAVLLHEKlyELESHRDQMIAEDKSIGSPMEER-EKLLKQI 312
Cdd:COG4717  124 LLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEA--ELAELQEELEELLEQLSLATEEElQDLAEEL 201

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 151101151 313 KDDNQEIASMERQLTDTKEKINQFIEEIRQLDMDLEEHQD 352
Cdd:COG4717  202 EELQQRLAELEEELEEAQEELEELEEELEQLENELEAAAL 241
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 195-342 5.95e-05

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: 43.76  E-value: 5.95e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151 195 QAKEKQIRSVEEEIEQEKQATDDIiknmsfENQVKYLEmkTTNEKLLQELDTLQQQLDSQNMKKESLEAEIAHSQVKQEA 274
Cdd:COG1579   13 QELDSELDRLEHRLKELPAELAEL------EDELAALE--ARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGN 84

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 151101151 275 V--------LLHEklyeLESHRDQMIAEDKSIGSPMEEREKLLKQIKDDNQEIASMERQLTDTKEKINQFIEEIRQ 342
Cdd:COG1579   85 VrnnkeyeaLQKE----IESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEA 156
PLN02939 PLN02939
transferase, transferring glycosyl groups
 171-349 6.85e-05

transferase, transferring glycosyl groups


Pssm-ID: 215507 [Multi-domain]  Cd Length: 977  Bit Score: 44.89  E-value: 6.85e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151 171 NDYNMLKAQNDRETQSLDVIFTERQAKEKQIRSVE-EEIEQEKQATDdiiKNMSFENQVKYLEMKTTnEKLLQELDTLQQ 249
Cdd:PLN02939  95 DDHNRASMQRDEAIAAIDNEQQTNSKDGEQLSDFQlEDLVGMIQNAE---KNILLLNQARLQALEDL-EKILTEKEALQG 170

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151 250 QLDSQNMKKESLEAEIA-HSQVKQEAVLLHEKLYELESHRDQMIAEDKSIGSPMEEREKLLKQ----IKDDNQEIASMER 324
Cdd:PLN02939 171 KINILEMRLSETDARIKlAAQEKIHVEILEEQLEKLRNELLIRGATEGLCVHSLSKELDVLKEenmlLKDDIQFLKAELI 250

                        170       180
                 ....*....|....*....|....*
gi 151101151 325 QLTDTKEKINQFIEEIRQLDMDLEE 349
Cdd:PLN02939 251 EVAETEERVFKLEKERSLLDASLRE 275
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
104-349 7.36e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 44.67  E-value: 7.36e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151 104 KISELTTEVNKLQKGIEMYNQE--NSVYLSYEKRAETLAVEIKELQGQLADYNMLVDKLNTNTE---------------- 165
Cdd:PRK03918 366 EAKAKKEELERLKKRLTGLTPEklEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEelkkakgkcpvcgrel 445

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151 166 ----MEEVMNDYNmlkaqndRETQSLDVIFTERQAKEKQIRSVEEEIEQEKQATDDIIKNMSFENQVKYLEMKTTN---- 237
Cdd:PRK03918 446 teehRKELLEEYT-------AELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKynle 518

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151 238 --EKLLQELDTLQQQLDSQNMKKESLEAEIAHSQ-VKQEAVLLHEKLYELESHRDQMIAEDKSIG-SPMEEREKLLKQI- 312
Cdd:PRK03918 519 elEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEeLKKKLAELEKKLDELEEELAELLKELEELGfESVEELEERLKELe 598

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 151101151 313 ---------KDDNQEIASMERQLTDTKEKINQFIEEIRQLDMDLEE 349
Cdd:PRK03918 599 pfyneylelKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEE 644
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 70-339 8.61e-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: 44.72  E-value: 8.61e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151    70 RPVTQQgLTGMKTGTKGPQRQILDKSYYLGLLRSKISELTTEVNKLQKGIEMYNQENSVYLSYEKRAETLAVEIKELQGQ 149
Cdd:pfam15921  478 RKVVEE-LTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQ 556

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151   150 LADYNMLVDKLNTNTE-MEEVMNDYN-------MLKAQ-----NDR--ETQSLDVIFTERQAKEKQIRSVEEEIEQEKQA 214
Cdd:pfam15921  557 MAEKDKVIEILRQQIEnMTQLVGQHGrtagamqVEKAQlekeiNDRrlELQEFKILKDKKDAKIRELEARVSDLELEKVK 636

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151   215 tddiIKNMSFENQVKYLEMKTTNEKLLQELDTLQQQLDS---------QNMKKESLEAEIAHSQVKQEavlLHEKLYELE 285
Cdd:pfam15921  637 ----LVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSlsedyevlkRNFRNKSEEMETTTNKLKMQ---LKSAQSELE 709

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 151101151   286 SHRDQMIAEDKSIGSPMEEREKLLKQIKDDNQEIASMERQLtdtkekinQFIEE 339
Cdd:pfam15921  710 QTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKI--------QFLEE 755
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 101-351 9.15e-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: 44.63  E-value: 9.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151  101 LRSKISELTTEVNKLQKGIEMYNQENsvyLSYEKRAETLAVEIKELQGQLADYNMLVDKLNT-NTEMEEVMNDYNMLKAQ 179
Cdd:TIGR04523 150 KEKELEKLNNKYNDLKKQKEELENEL---NLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKkIQKNKSLESQISELKKQ 226

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151  180 NDRETQSLDVIFTERQAKEKQIRSVEEEIEQEKQATDDIIKNMS---------------FENQVKYLEMKTT---NEKLL 241
Cdd:TIGR04523 227 NNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSekqkeleqnnkkikeLEKQLNQLKSEISdlnNQKEQ 306

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151  242 QELDTLQQQLDSQNMKKESLEAEIahSQVKQEAVLLHEKLYELESHRDQMIAEDKSIGSPMEEREKLLKQIKDDNQ---- 317
Cdd:TIGR04523 307 DWNKELKSELKNQEKKLEEIQNQI--SQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQsykq 384

                         250       260       270
                  ....*....|....*....|....*....|....
gi 151101151  318 EIASMERQLTDTKEKINQFIEEIRQLDMDLEEHQ 351
Cdd:TIGR04523 385 EIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQ 418
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
101-349 9.99e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 44.28  E-value: 9.99e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151 101 LRSKISELTTEVNKLQKGIEMYNQENSVYLSYEKRAETLAVEIKELQGQLADYNMLVDKLNTN----TEMEEVMNDYNML 176
Cdd:PRK03918 219 LREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKvkelKELKEKAEEYIKL 298

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151 177 KAQNDRETQSLDVIFTERQAKEKQIRSVEEEIEQ--EKQATDDIIKNMSFENQVKYLEMKtTNEKLLQELDTLQQQLDSQ 254
Cdd:PRK03918 299 SEFYEEYLDELREIEKRLSRLEEEINGIEERIKEleEKEERLEELKKKLKELEKRLEELE-ERHELYEEAKAKKEELERL 377

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151 255 NMKKESLEAEiahsQVKQEAVLLHEKLYELESHRDQMIAEDKSIGSPMEEREKLLKQIKDDNQEIASMERQLTDTKEK-- 332
Cdd:PRK03918 378 KKRLTGLTPE----KLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKel 453

                        250
                 ....*....|....*..
gi 151101151 333 INQFIEEIRQLDMDLEE 349
Cdd:PRK03918 454 LEEYTAELKRIEKELKE 470
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 192-352 2.10e-04

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: 43.52  E-value: 2.10e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151   192 TERQAKEKQIRSVEEEIEQEKQATDDIIKNMSFENQV--------------KYLEMKTTNEKLLQELDTLQQQLDSQNMK 257
Cdd:TIGR02169  237 RQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLleelnkkikdlgeeEQLRVKEKIGELEAEIASLERSIAEKERE 316

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151   258 KESLEAEIAHSQVKQEAVL-----LHEKLYELESHRDQMIAEdksIGSPMEEREKLLKQIKDDNQEIASMERQLTDTKEK 332
Cdd:TIGR02169  317 LEDAEERLAKLEAEIDKLLaeieeLEREIEEERKRRDKLTEE---YAELKEELEDLRAELEEVDKEFAETRDELKDYREK 393

                          170       180
                   ....*....|....*....|
gi 151101151   333 INQFIEEIRQLDMDLEEHQD 352
Cdd:TIGR02169  394 LEKLKREINELKRELDRLQE 413
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
128-345 3.09e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.83  E-value: 3.09e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151 128 VYLSYEKRAETLAVEIKELQGQLADYNMLvdklnTNTEMEEVMNDYNMLKAQNDRETQSLDVIFTERQAKEKQIRSVEEE 207
Cdd:COG4717  288 LLFLLLAREKASLGKEAEELQALPALEEL-----EEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEE 362

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151 208 I-----EQEKQATDDIIKNMSFENQVKYLEMKTTNEKLLQELDTLQQQLDSQNMKKESLEAEIAHSQVKQEAVLLHEKLY 282
Cdd:COG4717  363 LqleelEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELE 442

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 151101151 283 ELESHRDQMIAEdksigspMEEREKLLKQIKDDNqEIASMERQLTDTKEKINQFIEEIRQLDM 345
Cdd:COG4717  443 ELEEELEELREE-------LAELEAELEQLEEDG-ELAELLQELEELKAELRELAEEWAALKL 497
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
194-352 3.19e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.98  E-value: 3.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151  194 RQAKEKQIRSVEEEIEQEKQATddiiknmsfenqvkylemkttnEKLLQELDTLQQQLDSQNMKKESLEAEIAHSQvkqe 273
Cdd:COG4913   612 LAALEAELAELEEELAEAEERL----------------------EALEAELDALQERREALQRLAEYSWDEIDVAS---- 665

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 151101151  274 avlLHEKLYELESHRDQMIAEDKSIGSPMEEREKLLKQIKDDNQEIASMERQLTDTKEKINQFIEEIRQLDMDLEEHQD 352
Cdd:COG4913   666 ---AEREIAELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAED 741
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 194-352 3.63e-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: 42.74  E-value: 3.63e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151   194 RQAKEKQIRSVEEEIEQEKQATDDIIKNMSfENQVKYLEMKTTNEKLLQELDTLQQQLDSQNMKKESLEAEIAhsQVKQE 273
Cdd:TIGR02168  672 ILERRREIEELEEKIEELEEKIAELEKALA-ELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVE--QLEER 748

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 151101151   274 AVLLHEKLYELEshrdqmiaedksigspmEEREKLLKQIKDDNQEIASMERQLTDTKEKINQFIEEIRQLDMDLEEHQD 352
Cdd:TIGR02168  749 IAQLSKELTELE-----------------AEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRA 810
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 193-352 4.63e-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: 41.67  E-value: 4.63e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151 193 ERQAKEKQIRSVEEEIEQEKQATDDIIKNM-SFENQVKYLEMKTtnEKLLQELDTLQQQLDSQNMKKESLEAEIAHSQVK 271
Cdd:COG4942   21 AAAEAEAELEQLQQEIAELEKELAALKKEEkALLKQLAALERRI--AALARRIRALEQELAALEAELAELEKEIAELRAE 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151 272 QEAV--LLHEKLYELESHR--------------DQMIAEDKSIGSPMEEREKLLKQIKDDNQEIASMERQLTDTKEKINQ 335
Cdd:COG4942   99 LEAQkeELAELLRALYRLGrqpplalllspedfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA 178

                        170
                 ....*....|....*..
gi 151101151 336 FIEEIRQLDMDLEEHQD 352
Cdd:COG4942  179 LLAELEEERAALEALKA 195
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 101-343 5.41e-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: 41.93  E-value: 5.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151  101 LRSKISELTTEVNKLQKGIEMYNQENSVY-LSYEKRAETLAVEIKELQGQLADYNMLVDKlntNTEMEEVMNDynmLKAQ 179
Cdd:TIGR04523 445 LTNQDSVKELIIKNLDNTRESLETQLKVLsRSINKIKQNLEQKQKELKSKEKELKKLNEE---KKELEEKVKD---LTKK 518

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151  180 NDRETQSLDVIFTERQAKEKQIRSVEEEIEQEKQA-TDDIIKNMSFENQVKYLEMKTTNEKLLQELDTLQQQLDSQNMKK 258
Cdd:TIGR04523 519 ISSLKEKIEKLESEKKEKESKISDLEDELNKDDFElKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEK 598

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151  259 ESLEAEIAHSQVKQEAvlLHEKLYELESHRDQMIAEDKSIGSPMEEREKLLKQIKDdnqeiasmerQLTDTKEKINQFIE 338
Cdd:TIGR04523 599 KDLIKEIEEKEKKISS--LEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKE----------TIKEIRNKWPEIIK 666


                  ....*
gi 151101151  339 EIRQL 343
Cdd:TIGR04523 667 KIKES 671
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 73-343 6.39e-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: 41.93  E-value: 6.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151   73 TQQGLTGMKTGTKGPQRQILDKSYYLGLLRSKISELTTEVNKLQKGIEMYNQENSVYLSYEKRAETLAVE--IKELQGQL 150
Cdd:TIGR04523 251 TQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELKSELKNQEkkLEEIQNQI 330

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151  151 ADYNMLVDKLNTN-----TEMEEVMNDYNMLKAQNDRETQSLDVIFTERQAKEKQIRSVEEEIEQEKQATDDIIK-NMSF 224
Cdd:TIGR04523 331 SQNNKIISQLNEQisqlkKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKlNQQK 410

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151  225 ENQVKYLEmkTTNEKLLQELDTLQQQLDSQNMKKESLEAEIAhsqvkqEAVLLHEKLYELESHRDQMIAE-DKSIGSPME 303
Cdd:TIGR04523 411 DEQIKKLQ--QEKELLEKEIERLKETIIKNNSEIKDLTNQDS------VKELIIKNLDNTRESLETQLKVlSRSINKIKQ 482

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 151101151  304 EREKLLKQIKDDNQEIASMERQLTDTKEKINQFIEEIRQL 343
Cdd:TIGR04523 483 NLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSL 522
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 101-343 6.67e-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: 41.54  E-value: 6.67e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151  101 LRSKISELTTEVNKLQKGIEMYNQENSvylSYEKRAETLAVEIKELQGQLADYNMLVDKLNTN-----TEMEEVMNDYNM 175
Cdd:TIGR04523 354 SESENSEKQRELEEKQNEIEKLKKENQ---SYKQEIKNLESQINDLESKIQNQEKLNQQKDEQikklqQEKELLEKEIER 430

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151  176 LKAQNDRETQSLDVIFTERQAKEKQIRSVEEEIEQEKQATDDIIKnmsfenqvKYLEMKTTNEKLLQELDTLQQQLDSQN 255
Cdd:TIGR04523 431 LKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSR--------SINKIKQNLEQKQKELKSKEKELKKLN 502

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151  256 MKKESLEAEIahSQVKQEAVLLHEKLYELESHRDQMIAEDKSIGSPMEE------REKLLKQIKDDNQEIASMERQLTDT 329
Cdd:TIGR04523 503 EEKKELEEKV--KDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKddfelkKENLEKEIDEKNKEIEELKQTQKSL 580

                         250
                  ....*....|....
gi 151101151  330 KEKINQFIEEIRQL 343
Cdd:TIGR04523 581 KKKQEEKQELIDQK 594
DUF3450 pfam11932
Protein of unknown function (DUF3450); This family of proteins are functionally ...
 195-338 6.82e-04

Protein of unknown function (DUF3450); This family of proteins are functionally uncharacterized. This protein is found in bacteria and eukaryotes. Proteins in this family are about 260 amino acids in length.


Pssm-ID: 432198 [Multi-domain]  Cd Length: 238  Bit Score: 40.68  E-value: 6.82e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151  195 QAKEKQIRSVEEEIEQEKQATDDIIKNMSFEnqvkYLEMKTTNEKLLQELDTLQQQLDSQNMKKESLEAEIAH-SQVKQE 273
Cdd:pfam11932  19 LDLAEKAVAAAAQSQKKIDKWDDEKQELLAE----YRALKAELESLEVYNRQLERLVASQEQEIASLERQIEEiERTERE 94

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 151101151  274 AVLLhekLYELESHRDQMIAEDKsigsP--MEEREKLLKQIKDdnqeiaSMERQLTDTKEKINQFIE 338
Cdd:pfam11932  95 LVPL---MLKMLDRLEQFVALDL----PflLEERQARLARLRE------LMDDADVSLAEKYRRILE 148
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
107-350 7.51e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.59  E-value: 7.51e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151 107 ELTTEVNKLQKGIEMYNQENSVYLSYEKRAETLAVEIKELQGQLADYNMLVDKLNTNTEmEEVmndynmlkaqnDRETQS 186
Cdd:PRK03918 529 KLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESV-EEL-----------EERLKE 596

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151 187 LDVI---FTERQAKEKQIRSVEEEIEQEKQATDDIIKNMSFENqvKYLEMKttnEKLLQELDTLQQQLDSQNMKKESLEA 263
Cdd:PRK03918 597 LEPFyneYLELKDAEKELEREEKELKKLEEELDKAFEELAETE--KRLEEL---RKELEELEKKYSEEEYEELREEYLEL 671

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151 264 EIAHSQVKqeavllhEKLYELESHRDQMIAEDKSIGSPMEEREKLLKQIKDDNQEIASMERqltdtkekinqFIEEIRQL 343
Cdd:PRK03918 672 SRELAGLR-------AELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERVEE-----------LREKVKKY 733


                 ....*..
gi 151101151 344 DMDLEEH 350
Cdd:PRK03918 734 KALLKER 740
TTC8_N cd21341
N-terminal domain of tetratricopeptide repeat domain 8; Tetratricopeptide repeat domain 8 ...
 7-50 8.52e-04

N-terminal domain of tetratricopeptide repeat domain 8; Tetratricopeptide repeat domain 8 (TTC80), also known a BBS8, has been directly linked to Bardet-Biedl syndrome, an autosomal recessive ciliopathy characterized by retinal degeneration, renal failure, obesity, diabetes, male infertility, polydactyly and cognitive impairment. Mutations in BBS8 cause early vision loss. In addition to C-terminal tetratricopeptide repeats, TTC8 also contains an N-terminal domain of unknown function.


Pssm-ID: 411061 [Multi-domain]  Cd Length: 139  Bit Score: 39.21  E-value: 8.52e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 151101151   7 SSAARPVSRggvglTGRPPSGI--------RPLSGNIRVATAMPPGTARPGS 50
Cdd:cd21341   66 SQAMRPTTS-----SGRPITGFvrpgtqsgRPGTSRQALRTPRRAGTARPVT 112
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 204-352 8.98e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.46  E-value: 8.98e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151 204 VEEEIEQ-----EKQAtddiiknmsfENQVKYLEMKTT-----NEKLLQELDTLQQQLDSQNMKKESLEAEIAHSQVKQE 273
Cdd:COG1196  194 ILGELERqleplERQA----------EKAERYRELKEElkeleAELLLLKLRELEAELEELEAELEELEAELEELEAELA 263

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 151101151 274 AVllhEKlyELESHRDQMIAEDKSIGSPMEEREKLLKQIKDDNQEIASMERQLTDTKEKINQFIEEIRQLDMDLEEHQD 352
Cdd:COG1196  264 EL---EA--ELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEE 337
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 101-274 9.05e-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: 40.90  E-value: 9.05e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151 101 LRSKISELTTEVNKLQKGIEMYNQENSvylSYEKRAETLAVEIKELQGQLADYNMLVDKLNTNTEMEEVMNDYNMLKAQN 180
Cdd:COG4942   60 LERRIAALARRIRALEQELAALEAELA---ELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVR 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151 181 DRE-----TQSLDVIFTERQAKEKQIRSVEEEIEQEKQATDDIIKNMSfENQVKYLEMKTTNEKLLQELDT----LQQQL 251
Cdd:COG4942  137 RLQylkylAPARREQAEELRADLAELAALRAELEAERAELEALLAELE-EERAALEALKAERQKLLARLEKelaeLAAEL 215

                        170       180
                 ....*....|....*....|...
gi 151101151 252 DSQNMKKESLEAEIAHSQVKQEA 274
Cdd:COG4942  216 AELQQEAEELEALIARLEAEAAA 238
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 135-323 1.20e-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: 40.88  E-value: 1.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151  135 RAETLAVEIKELQgQLADYNMLVDKLNTNTEME-EVMNDYNMLKAQNDRETQSLDVIFT-----ERQAKEKQIRSVEEEI 208
Cdd:pfam17380 366 RQEEIAMEISRMR-ELERLQMERQQKNERVRQElEAARKVKILEEERQRKIQQQKVEMEqiraeQEEARQREVRRLEEER 444

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151  209 ----------EQEKQATDDIIKNMSFENQVKYLEMKTTNEK-----------LLQELDTLQQQLDSQNMKKESLEAE--- 264
Cdd:pfam17380 445 aremervrleEQERQQQVERLRQQEEERKRKKLELEKEKRDrkraeeqrrkiLEKELEERKQAMIEEERKRKLLEKEmee 524

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 151101151  265 ----IAHSQVKQEAVLLHEKLYELESHR---DQM--IAEDKSIGSPMEEREKLLKQIKDDNQEIASME 323
Cdd:pfam17380 525 rqkaIYEEERRREAEEERRKQQEMEERRriqEQMrkATEERSRLEAMEREREMMRQIVESEKARAEYE 592
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 93-264 1.33e-03

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: 40.82  E-value: 1.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151    93 DKSYYLGLLRSKISELTTEVNKLQKGIEMYNQENSvylSYEKRAETLAVEIKELQGQLADY-----NMLVDKLNTNTEME 167
Cdd:TIGR02169  823 RLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIE---NLNGKKEELEEELEELEAALRDLesrlgDLKKERDELEAQLR 899

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151   168 EVMNDYNMLKAQNDRETQSLDVIFTERQAKEKQIRSVEEEIEQEKQATDDIIKNMSFENQVKYLE-----MKTTNEKLLQ 242
Cdd:TIGR02169  900 ELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEeeiraLEPVNMLAIQ 979

                          170       180
                   ....*....|....*....|..
gi 151101151   243 ELDTLQQQLDSQNMKKESLEAE 264
Cdd:TIGR02169  980 EYEEVLKRLDELKEKRAKLEEE 1001
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
 114-356 1.35e-03

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


Pssm-ID: 130673 [Multi-domain]  Cd Length: 2757  Bit Score: 40.81  E-value: 1.35e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151   114 KLQKGIEMYNQENSVYLSYEKRAE-TLAVEIKELQGQLADYNMLVDKLNTNtemeEVMNDYNMLKAqnDRETQSLDVIFT 192
Cdd:TIGR01612  946 ILNKNIDTIKESNLIEKSYKDKFDnTLIDKINELDKAFKDASLNDYEAKNN----ELIKYFNDLKA--NLGKNKENMLYH 1019

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151   193 ERQAKEKQIRSVEEEIEqekqatdDIIKNMSFENQVKYLEMKTTNEKLLQELDTLQQQLDSQNMKKesLEAEIAHSQVKQ 272
Cdd:TIGR01612 1020 QFDEKEKATNDIEQKIE-------DANKNIPNIEIAIHTSIYNIIDEIEKEIGKNIELLNKEILEE--AEINITNFNEIK 1090

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151   273 EAVllheKLYELEShrdqmIAEDKSIgSPMEEREKLLKQIKDDNQEIASMERQLTDTKEKINQFIEEIRQLDMDLEEHQD 352
Cdd:TIGR01612 1091 EKL----KHYNFDD-----FGKEENI-KYADEINKIKDDIKNLDQKIDHHIKALEEIKKKSENYIDEIKAQINDLEDVAD 1160


                   ....
gi 151101151   353 PTNY 356
Cdd:TIGR01612 1161 KAIS 1164
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 90-349 1.43e-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: 1.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151   90 QILDKSYYLGLLRSKISELTTEVNKLQKGIEMYNQENSVYLSYEKRAETLAVEIKELQGQLADYNMLVdkLNTNTEMEEV 169
Cdd:TIGR04523 181 EKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEI--SNTQTQLNQL 258

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151  170 MNDYNMLKAQNDRETQSLDVIFTERQAKEKQIRSVEEEIEQ-EKQATDDIIKNM-----SFENQVKYLEMKTTNEKllQE 243
Cdd:TIGR04523 259 KDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDlNNQKEQDWNKELkselkNQEKKLEEIQNQISQNN--KI 336

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151  244 LDTLQQQLdsQNMKKESLEAEIAHSQVKQEAVLLHEKLYELESHRDQMIAEDKSIGSPMEEREKLLKQIKDDNQEIASME 323
Cdd:TIGR04523 337 ISQLNEQI--SQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQI 414

                         250       260
                  ....*....|....*....|....*.
gi 151101151  324 RQLTDTKEKINQFIEEIRQLDMDLEE 349
Cdd:TIGR04523 415 KKLQQEKELLEKEIERLKETIIKNNS 440
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 106-349 1.66e-03

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 40.54  E-value: 1.66e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151   106 SELTTEVNKLQKGIEmynQENSVYLSYEKRAETLAVEIKELQGQLADYNMLVD-----KLNTNTEMEEVMNDYNMLKAQN 180
Cdd:pfam01576  429 AELAEKLSKLQSELE---SVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQeetrqKLNLSTRLRQLEDERNSLQEQL 505

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151   181 DRETQSldvifteRQAKEKQIRSVEEEIEQEKQATDDIIKNMS------------FENQVKYLEMKT--------TNEKL 240
Cdd:pfam01576  506 EEEEEA-------KRNVERQLSTLQAQLSDMKKKLEEDAGTLEaleegkkrlqreLEALTQQLEEKAaaydklekTKNRL 578

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151   241 LQELDTLQQQLDSQNMKKESLEAeiahsqvKQEAVllheklyeleshrDQMIAEDKSIGSPM-EEREKLLKQIKDDNQEI 319
Cdd:pfam01576  579 QQELDDLLVDLDHQRQLVSNLEK-------KQKKF-------------DQMLAEEKAISARYaEERDRAEAEAREKETRA 638

                          250       260       270
                   ....*....|....*....|....*....|
gi 151101151   320 ASMERQLTDTKEKINQFIEEIRQLDMDLEE 349
Cdd:pfam01576  639 LSLARALEEALEAKEELERTNKQLRAEMED 668
PRK12704 PRK12704
phosphodiesterase; Provisional
 197-340 1.79e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 40.15  E-value: 1.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151 197 KEKQIRSVEEEIEQEKQATDDIIKNMsfENQVKYLEmkttnEKLLQELDTLQQQLDSQNMKKESLEAEIAHSQVKQEAvl 276
Cdd:PRK12704  55 KKEALLEAKEEIHKLRNEFEKELRER--RNELQKLE-----KRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQE-- 125

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 151101151 277 LHEKLYELESHRDQMIAEDKSIG--SPMEEREKLLKQIKDD-NQEIASMERQL-TDTKEKINQFIEEI 340
Cdd:PRK12704 126 LEKKEEELEELIEEQLQELERISglTAEEAKEILLEKVEEEaRHEAAVLIKEIeEEAKEEADKKAKEI 193
PRK01156 PRK01156
chromosome segregation protein; Provisional
 72-348 1.98e-03

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 40.27  E-value: 1.98e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151  72 VTQQGLTGMKTGTKGPQRQILDKSYYLGLLRSKISELTTEVNKLQKGIEMYNQENSVYLSYEKRAETLAVEIKELQGQLA 151
Cdd:PRK01156 135 VGQGEMDSLISGDPAQRKKILDEILEINSLERNYDKLKDVIDMLRAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHS 214

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151 152 DynMLVDKLNTNTEMEEVMNDYNMLKAQNDRETQSLDVI------FTERQAKEKQIRSVEEEIEQEKQATDDIIKNMSFE 225
Cdd:PRK01156 215 I--TLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKnryeseIKTAESDLSMELEKNNYYKELEERHMKIINDPVYK 292

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151 226 NQ---VKYLEMKTTNEKLLQELDTLQQQLDS--QNMKK-ESLEAEIAHSQVKQ-EAVLLHEKLYELESHRDQMIAEDKSI 298
Cdd:PRK01156 293 NRnyiNDYFKYKNDIENKKQILSNIDAEINKyhAIIKKlSVLQKDYNDYIKKKsRYDDLNNQILELEGYEMDYNSYLKSI 372

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 151101151 299 GSPMEEREKLLKQIKDDNQEIASMERQLTDTKEKINQFIEEIRQLDMDLE 348
Cdd:PRK01156 373 ESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDIS 422
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 101-274 2.18e-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: 2.18e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151 101 LRSKISELTTEVNKLQKGIEMYNQE----NSVYLSYEKRAETLAVEIKELQGQLADYNMLVDKLNTntEMEEVMNDYnml 176
Cdd:COG3883   21 KQKELSELQAELEAAQAELDALQAEleelNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERRE--ELGERARAL--- 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151 177 kAQNDRETQSLDVIF------------------TERQAKE-KQIRSVEEEIEQEKQATDDIIKnmsfenqvkylEMKTTN 237
Cdd:COG3883   96 -YRSGGSVSYLDVLLgsesfsdfldrlsalskiADADADLlEELKADKAELEAKKAELEAKLA-----------ELEALK 163

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 151101151 238 EKLLQELDTLQQQLDSQNMKKESLEAEIAHSQVKQEA 274
Cdd:COG3883  164 AELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAE 200
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
69-342 2.43e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.90  E-value: 2.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151   69 HRPVTQQGLTGMK--TGTKGPQRQIlDKSYYLG--------LLRSKISELTTEVNKLQKGIEMYNQEnsvYLSYEKRAET 138
Cdd:COG4913   574 PRAITRAGQVKGNgtRHEKDDRRRI-RSRYVLGfdnraklaALEAELAELEEELAEAEERLEALEAE---LDALQERREA 649

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151  139 LA---------VEIKELQGQLADYNMLVDKL-NTNTEMEEVMNDYNMLKAQNDRETQSLDVIFTERQAKEKQIRSVEEEI 208
Cdd:COG4913   650 LQrlaeyswdeIDVASAEREIAELEAELERLdASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEEL 729

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151  209 EQEKQATDDIIKNMSFEnqvkylemkttnekLLQELDTLQQQLDSQNmkKESLEAEIAHSQVKQEAVLLHEKLYELESHR 288
Cdd:COG4913   730 DELQDRLEAAEDLARLE--------------LRALLEERFAAALGDA--VERELRENLEERIDALRARLNRAEEELERAM 793

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 151101151  289 DQMIAEDKSIGSPM-------EEREKLLKQIKDDN-----QEIA-----SMERQLTDTKEKINQFIEEIRQ 342
Cdd:COG4913   794 RAFNREWPAETADLdadleslPEYLALLDRLEEDGlpeyeERFKellneNSIEFVADLLSKLRRAIREIKE 864
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 239-352 4.11e-03

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 38.37  E-value: 4.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151 239 KLLQELDTLQQQLDSQNMKKESLEAEIAhsQVKQEAVLLHEKLYELESHRDQMIAEDKSIGSPMEEREKLLKQIKDD--- 315
Cdd:COG1579   14 ELDSELDRLEHRLKELPAELAELEDELA--ALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNkey 91

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 151101151 316 ---NQEIASMERQLTDTKEKINQFIEEIRQLDMDLEEHQD 352
Cdd:COG1579   92 ealQKEIESLKRRISDLEDEILELMERIEELEEELAELEA 131
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 242-335 5.09e-03

ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 38.91  E-value: 5.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151 242 QELDTLQQQLDSQNMKKESLEAEiAHSQVKQEAVLLHEKLYELESHRDQMIAEDKSIGSPMEEREKLLKQIKDDNQEIAS 321
Cdd:COG0542  411 EELDELERRLEQLEIEKEALKKE-QDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRYGKIPE 489

                         90
                 ....*....|....
gi 151101151 322 MERQLTDTKEKINQ 335
Cdd:COG0542  490 LEKELAELEEELAE 503
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
101-300 5.35e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 38.84  E-value: 5.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151 101 LRSKISELTTEVNKLQKGIEMYNQENSVyLSYEKRAETLAVEIKELQGQLAD-----------YNMLVDKLNTN-TEMEE 168
Cdd:COG3206  180 LEEQLPELRKELEEAEAALEEFRQKNGL-VDLSEEAKLLLQQLSELESQLAEaraelaeaearLAALRAQLGSGpDALPE 258

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151 169 VMND--YNMLKAQ-NDRETQ--SLDVIFTERQAkekQIRSVEEEIEQEKQATDDIIKNMSFENQVKYLEMKTTNEKLLQE 243
Cdd:COG3206  259 LLQSpvIQQLRAQlAELEAElaELSARYTPNHP---DVIALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQ 335

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 151101151 244 LDTLQQQLDSQNmkkeslEAEIAHSQVKQEAVLLhEKLYE--LESHRDQMIAEDKSIGS 300
Cdd:COG3206  336 LAQLEARLAELP------ELEAELRRLEREVEVA-RELYEslLQRLEEARLAEALTVGN 387
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 164-351 5.46e-03

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


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 38.80  E-value: 5.46e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151   164 TEMEEVMNDYNMLKaqndRETQSLDVIFTERQAKEKQIRSVEEEIEQEKQATDDIIKNMSFENQVKYLEMKTTNEKLLQE 243
Cdd:pfam02463  156 LEIEEEAAGSRLKR----KKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDY 231

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151   244 LDTLQQQLDSQNMKKESLEAEIAHSQVKQEAVLlheklyELESHRDQMIAEDKSIGSPMEEREKLL-KQIKDDNQEIASM 322
Cdd:pfam02463  232 LKLNEERIDLLQELLRDEQEEIESSKQEIEKEE------EKLAQVLKENKEEEKEKKLQEEELKLLaKEEEELKSELLKL 305

                          170       180
                   ....*....|....*....|....*....
gi 151101151   323 ERQLTDTKEKINQFIEEIRQLDMDLEEHQ 351
Cdd:pfam02463  306 ERRKVDDEEKLKESEKEKKKAEKELKKEK 334
 
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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