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Conserved domains on  [gi|1958795415|ref|XP_038937092|]
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lebercilin isoform X1 [Rattus norvegicus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Lebercilin pfam15619
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ...
 104-296 1.43e-70

Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of eukaryotic ciliary proteins. Mutations in the gene, LCA5, are implicated in the disease Leber congenital amaurosis. In photoreceptors, lebercilin is uniquely localized at the cilium that bridges the inner and outer segments. Lebercilin functions as an integral element of selective protein transport through photoreceptor cilia. Lebercilin specifically interacts with the intraflagellar transport (IFT), and disruption of IFT can lead to Leber congenital amaurosis.


:

Pssm-ID: 464776 [Multi-domain]  Cd Length: 193  Bit Score: 228.63  E-value: 1.43e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795415 104 VTKRVLSARLLKITELQNEVSELQVKLAQLLKENKALKSLQYRQEKALSKFEDAENEISQLIHRHNGEITALKERLRKSQ 183
Cdd:pfam15619   1 VTQRVLSARLHKIKELQNELAELQSKLEELRKENRLLKRLQKRQEKALGKYEGTESELPQLIARHNEEVRVLRERLRRLQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795415 184 EKERMAEKRVKDTEGELFRTKFSLQKLKKISEARHLPERDDLAKKLVSAELKLDNTERKIKELSKNLELSTNSFQRQLLA 263
Cdd:pfam15619  81 EKERDLERKLKEKEAELLRLRDQLKRLEKLSEDKNLAEREELQKKLEQLEAKLEDKDEKIQDLERKLELENKSFRRQLAA 160

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1958795415 264 ERKRAFEAHDENKILQKELQRLHHKLKEKEKEL 296
Cdd:pfam15619 161 EKKKHKEAQEEVKILQEEIERLQQKLKEKEREL 193
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 172-476 7.20e-03

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: 40.04  E-value: 7.20e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795415  172 ITALKERLRKSQEK-ERMAE--KRVKDTEGELFRTKFSLQ-------KLKKISEARHLPERDDLAKKLVSAELKLDNTER 241
Cdd:TIGR02168  167 ISKYKERRKETERKlERTREnlDRLEDILNELERQLKSLErqaekaeRYKELKAELRELELALLVLRLEELREELEELQE 246

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795415  242 KIKELS---KNLELSTNSFQRQLLAERKRAFEAHDENKILQKELQRLHHKLKEKEKELDIKNIYANRLPKSSPKKEKEIA 318
Cdd:TIGR02168  247 ELKEAEeelEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLE 326

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795415  319 RKHASCQSDFTDLCTKAVQTAE-----DFEPEEFPFTAQTVLCYENRWDGSEYLpsyLEYQERN----EHGSESLSSTLE 389
Cdd:TIGR02168  327 ELESKLDELAEELAELEEKLEElkeelESLEAELEELEAELEELESRLEELEEQ---LETLRSKvaqlELQIASLNNEIE 403

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795415  390 QegkYSDDQDSCTAKQETGKSECEWEREELDKVKgKSSLLGRTEKLVLEAGSVQTESYQAQTIDKFQDEAERLKTEMLLA 469
Cdd:TIGR02168  404 R---LEARLERLEDRRERLQQEIEELLKKLEEAE-LKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDA 479


                   ....*..
gi 1958795415  470 KLNEINK 476
Cdd:TIGR02168  480 AERELAQ 486
 
Name Accession Description Interval E-value
Lebercilin pfam15619
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ...
 104-296 1.43e-70

Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of eukaryotic ciliary proteins. Mutations in the gene, LCA5, are implicated in the disease Leber congenital amaurosis. In photoreceptors, lebercilin is uniquely localized at the cilium that bridges the inner and outer segments. Lebercilin functions as an integral element of selective protein transport through photoreceptor cilia. Lebercilin specifically interacts with the intraflagellar transport (IFT), and disruption of IFT can lead to Leber congenital amaurosis.


Pssm-ID: 464776 [Multi-domain]  Cd Length: 193  Bit Score: 228.63  E-value: 1.43e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795415 104 VTKRVLSARLLKITELQNEVSELQVKLAQLLKENKALKSLQYRQEKALSKFEDAENEISQLIHRHNGEITALKERLRKSQ 183
Cdd:pfam15619   1 VTQRVLSARLHKIKELQNELAELQSKLEELRKENRLLKRLQKRQEKALGKYEGTESELPQLIARHNEEVRVLRERLRRLQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795415 184 EKERMAEKRVKDTEGELFRTKFSLQKLKKISEARHLPERDDLAKKLVSAELKLDNTERKIKELSKNLELSTNSFQRQLLA 263
Cdd:pfam15619  81 EKERDLERKLKEKEAELLRLRDQLKRLEKLSEDKNLAEREELQKKLEQLEAKLEDKDEKIQDLERKLELENKSFRRQLAA 160

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1958795415 264 ERKRAFEAHDENKILQKELQRLHHKLKEKEKEL 296
Cdd:pfam15619 161 EKKKHKEAQEEVKILQEEIERLQQKLKEKEREL 193
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 108-326 9.35e-11

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: 64.40  E-value: 9.35e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795415 108 VLSARLLKITELQNEVSELQVKLAQLLKENKALKSLQYRQEKALSKFEDAENEISQLIHRHNGEITALKERLRKSQEKER 187
Cdd:COG4942    14 AAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795415 188 MAEKRVKDTEGELFRTKFSLQKLKKISEARHLPERDDLAKKLVSAE-LKLDNTERK--IKELSKNLELSTNSfQRQLLAE 264
Cdd:COG4942    94 ELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQyLKYLAPARReqAEELRADLAELAAL-RAELEAE 172

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958795415 265 RKRAFEAHDENKILQKELQRLhhkLKEKEKELdikniyaNRLPKSSPKKEKEIARKHASCQS 326
Cdd:COG4942   173 RAELEALLAELEEERAALEAL---KAERQKLL-------ARLEKELAELAAELAELQQEAEE 224
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 109-321 8.23e-08

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 55.83  E-value: 8.23e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795415  109 LSARLLKITELQNEVSELQVKLAQLLKENKALKSLQYRQEKALSKFEDAENEISQLIHRHNGEITALKERLRKSQEKERM 188
Cdd:TIGR02168  241 LEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEE 320

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795415  189 AEKRVKDTEGELFRTKFSLQKLKKISEaRHLPERDDLAKKLVSAELKLDNTERKIKELSKNLE-LSTNSFQ--RQLLAER 265
Cdd:TIGR02168  321 LEAQLEELESKLDELAEELAELEEKLE-ELKEELESLEAELEELEAELEELESRLEELEEQLEtLRSKVAQleLQIASLN 399

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958795415  266 KRAFEAHDENKILQKELQRLHHKLKEKEKELDIKNIYANRLPKSSPKKEKEIARKH 321
Cdd:TIGR02168  400 NEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEE 455
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
 112-302 1.70e-06

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 51.47  E-value: 1.70e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795415 112 RLLKITELQNEVSELQVKLAQLLKENKALKSLQYRQEK---------ALSKFEDAENEISQLIHrhngEITALKERLRK- 181
Cdd:PRK05771   44 RLRKLRSLLTKLSEALDKLRSYLPKLNPLREEKKKVSVksleelikdVEEELEKIEKEIKELEE----EISELENEIKEl 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795415 182 SQEKERMaeKRVKDTEGE---LFRTKFSLQKLKKISE--ARHLPERDDLAKKLVSAELKLDNT------ERKIKELSKnl 250
Cdd:PRK05771  120 EQEIERL--EPWGNFDLDlslLLGFKYVSVFVGTVPEdkLEELKLESDVENVEYISTDKGYVYvvvvvlKELSDEVEE-- 195

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958795415 251 ELSTNSFQRQLLAERKRAFEA----HDENKILQKELQRLHHKLKEKEKEL--DIKNIY 302
Cdd:PRK05771  196 ELKKLGFERLELEEEGTPSELireiKEELEEIEKERESLLEELKELAKKYleELLALY 253
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 126-296 1.52e-03

Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 41.02  E-value: 1.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795415 126 LQVKLAQLLKENKAlKSLQYRQEKALSKFEDAENEISQLIH-------RHNGEITALKERLRKSQEKERMAEK------R 192
Cdd:cd16269    99 LEEKKEEFCKQNEE-ASSKRCQALLQELSAPLEEKISQGSYsvpggyqLYLEDREKLVEKYRQVPRKGVKAEEvlqeflQ 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795415 193 VKDTEGE-LFRTKFSL-QKLKKISEARHLPERDDLAKKLVSAELKLdnTERKIKELSKNLELstnsFQRQLLAERKRafe 270
Cdd:cd16269   178 SKEAEAEaILQADQALtEKEKEIEAERAKAEAAEQERKLLEEQQRE--LEQKLEDQERSYEE----HLRQLKEKMEE--- 248

                         170       180
                  ....*....|....*....|....*..
gi 1958795415 271 ahdENKILQKELQRLH-HKLKEKEKEL 296
Cdd:cd16269   249 ---ERENLLKEQERALeSKLKEQEALL 272
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 172-476 7.20e-03

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: 40.04  E-value: 7.20e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795415  172 ITALKERLRKSQEK-ERMAE--KRVKDTEGELFRTKFSLQ-------KLKKISEARHLPERDDLAKKLVSAELKLDNTER 241
Cdd:TIGR02168  167 ISKYKERRKETERKlERTREnlDRLEDILNELERQLKSLErqaekaeRYKELKAELRELELALLVLRLEELREELEELQE 246

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795415  242 KIKELS---KNLELSTNSFQRQLLAERKRAFEAHDENKILQKELQRLHHKLKEKEKELDIKNIYANRLPKSSPKKEKEIA 318
Cdd:TIGR02168  247 ELKEAEeelEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLE 326

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795415  319 RKHASCQSDFTDLCTKAVQTAE-----DFEPEEFPFTAQTVLCYENRWDGSEYLpsyLEYQERN----EHGSESLSSTLE 389
Cdd:TIGR02168  327 ELESKLDELAEELAELEEKLEElkeelESLEAELEELEAELEELESRLEELEEQ---LETLRSKvaqlELQIASLNNEIE 403

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795415  390 QegkYSDDQDSCTAKQETGKSECEWEREELDKVKgKSSLLGRTEKLVLEAGSVQTESYQAQTIDKFQDEAERLKTEMLLA 469
Cdd:TIGR02168  404 R---LEARLERLEDRRERLQQEIEELLKKLEEAE-LKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDA 479


                   ....*..
gi 1958795415  470 KLNEINK 476
Cdd:TIGR02168  480 AERELAQ 486
 
Name Accession Description Interval E-value
Lebercilin pfam15619
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ...
 104-296 1.43e-70

Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of eukaryotic ciliary proteins. Mutations in the gene, LCA5, are implicated in the disease Leber congenital amaurosis. In photoreceptors, lebercilin is uniquely localized at the cilium that bridges the inner and outer segments. Lebercilin functions as an integral element of selective protein transport through photoreceptor cilia. Lebercilin specifically interacts with the intraflagellar transport (IFT), and disruption of IFT can lead to Leber congenital amaurosis.


Pssm-ID: 464776 [Multi-domain]  Cd Length: 193  Bit Score: 228.63  E-value: 1.43e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795415 104 VTKRVLSARLLKITELQNEVSELQVKLAQLLKENKALKSLQYRQEKALSKFEDAENEISQLIHRHNGEITALKERLRKSQ 183
Cdd:pfam15619   1 VTQRVLSARLHKIKELQNELAELQSKLEELRKENRLLKRLQKRQEKALGKYEGTESELPQLIARHNEEVRVLRERLRRLQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795415 184 EKERMAEKRVKDTEGELFRTKFSLQKLKKISEARHLPERDDLAKKLVSAELKLDNTERKIKELSKNLELSTNSFQRQLLA 263
Cdd:pfam15619  81 EKERDLERKLKEKEAELLRLRDQLKRLEKLSEDKNLAEREELQKKLEQLEAKLEDKDEKIQDLERKLELENKSFRRQLAA 160

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1958795415 264 ERKRAFEAHDENKILQKELQRLHHKLKEKEKEL 296
Cdd:pfam15619 161 EKKKHKEAQEEVKILQEEIERLQQKLKEKEREL 193
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 108-326 9.35e-11

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: 64.40  E-value: 9.35e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795415 108 VLSARLLKITELQNEVSELQVKLAQLLKENKALKSLQYRQEKALSKFEDAENEISQLIHRHNGEITALKERLRKSQEKER 187
Cdd:COG4942    14 AAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795415 188 MAEKRVKDTEGELFRTKFSLQKLKKISEARHLPERDDLAKKLVSAE-LKLDNTERK--IKELSKNLELSTNSfQRQLLAE 264
Cdd:COG4942    94 ELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQyLKYLAPARReqAEELRADLAELAAL-RAELEAE 172

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958795415 265 RKRAFEAHDENKILQKELQRLhhkLKEKEKELdikniyaNRLPKSSPKKEKEIARKHASCQS 326
Cdd:COG4942   173 RAELEALLAELEEERAALEAL---KAERQKLL-------ARLEKELAELAAELAELQQEAEE 224
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 109-321 8.23e-08

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 55.83  E-value: 8.23e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795415  109 LSARLLKITELQNEVSELQVKLAQLLKENKALKSLQYRQEKALSKFEDAENEISQLIHRHNGEITALKERLRKSQEKERM 188
Cdd:TIGR02168  241 LEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEE 320

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795415  189 AEKRVKDTEGELFRTKFSLQKLKKISEaRHLPERDDLAKKLVSAELKLDNTERKIKELSKNLE-LSTNSFQ--RQLLAER 265
Cdd:TIGR02168  321 LEAQLEELESKLDELAEELAELEEKLE-ELKEELESLEAELEELEAELEELESRLEELEEQLEtLRSKVAQleLQIASLN 399

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958795415  266 KRAFEAHDENKILQKELQRLHHKLKEKEKELDIKNIYANRLPKSSPKKEKEIARKH 321
Cdd:TIGR02168  400 NEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEE 455
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 115-296 5.30e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 53.40  E-value: 5.30e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795415 115 KITELQNEVSELQVKLAQLLKENKALKSLQYRQEKALS----KFEDAENEISQLIhrhnGEITALKERLRKSQEKERMAE 190
Cdd:COG1196   247 ELEELEAELEELEAELAELEAELEELRLELEELELELEeaqaEEYELLAELARLE----QDIARLEERRRELEERLEELE 322

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795415 191 KRVKDTEGELFRTKFSLQKLKKiSEARHLPERDDLAKKLVSAELKLDNTERKIKELSKNLElstnSFQRQLLAERKRAFE 270
Cdd:COG1196   323 EELAELEEELEELEEELEELEE-ELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELE----ELAEELLEALRAAAE 397

                         170       180
                  ....*....|....*....|....*.
gi 1958795415 271 AHDENKILQKELQRLHHKLKEKEKEL 296
Cdd:COG1196   398 LAAQLEELEEAEEALLERLERLEEEL 423
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
 112-302 1.70e-06

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 51.47  E-value: 1.70e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795415 112 RLLKITELQNEVSELQVKLAQLLKENKALKSLQYRQEK---------ALSKFEDAENEISQLIHrhngEITALKERLRK- 181
Cdd:PRK05771   44 RLRKLRSLLTKLSEALDKLRSYLPKLNPLREEKKKVSVksleelikdVEEELEKIEKEIKELEE----EISELENEIKEl 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795415 182 SQEKERMaeKRVKDTEGE---LFRTKFSLQKLKKISE--ARHLPERDDLAKKLVSAELKLDNT------ERKIKELSKnl 250
Cdd:PRK05771  120 EQEIERL--EPWGNFDLDlslLLGFKYVSVFVGTVPEdkLEELKLESDVENVEYISTDKGYVYvvvvvlKELSDEVEE-- 195

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958795415 251 ELSTNSFQRQLLAERKRAFEA----HDENKILQKELQRLHHKLKEKEKEL--DIKNIY 302
Cdd:PRK05771  196 ELKKLGFERLELEEEGTPSELireiKEELEEIEKERESLLEELKELAKKYleELLALY 253
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 115-296 2.63e-06

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 50.21  E-value: 2.63e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795415 115 KITELQNEVSELQVKLAQLLKEnkaLKSLQYRQEKALSKFEDAENEISQLihrhNGEITALKERLRKSQEKermAEKRVK 194
Cdd:COG3883    24 ELSELQAELEAAQAELDALQAE---LEELNEEYNELQAELEALQAEIDKL----QAEIAEAEAEIEERREE---LGERAR 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795415 195 DtegeLFRTKFSLQKLKKISEARHLPE---RDDLAKKLVSAELKLDNTERKIKELSKNLELSTNSFQRQLLAERKRAFEA 271
Cdd:COG3883    94 A----LYRSGGSVSYLDVLLGSESFSDfldRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAA 169

                         170       180
                  ....*....|....*....|....*
gi 1958795415 272 HDENKILQKELQRLHHKLKEKEKEL 296
Cdd:COG3883   170 KAELEAQQAEQEALLAQLSAEEAAA 194
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 114-296 3.05e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 50.71  E-value: 3.05e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795415 114 LKITELQNEVSELQVKLAQLLKENKALKSLQYRQEKALSKFEDAENEISQLIHRHNGEITALKERLRKSQEKERMAEKRV 193
Cdd:COG1196   274 LELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEEL 353

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795415 194 KDTEGELfrtKFSLQKLKKISEARHlpERDDLAKKLVSAELKLDNTERKIKELSKNLELSTNSFQRQLLAERKRAFEAHD 273
Cdd:COG1196   354 EEAEAEL---AEAEEALLEAEAELA--EAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEE 428

                         170       180
                  ....*....|....*....|...
gi 1958795415 274 ENKILQKELQRLHHKLKEKEKEL 296
Cdd:COG1196   429 ALAELEEEEEEEEEALEEAAEEE 451
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
109-243 5.90e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 49.91  E-value: 5.90e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795415  109 LSARLLKITELQNEVSELQVKLAQLLKENKALKSLQYRQEKALSKFEDAENEISQLIH---RHNGEITALKERLRKSQEK 185
Cdd:COG4913    656 YSWDEIDVASAEREIAELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGeigRLEKELEQAEEELDELQDR 735

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958795415  186 ERMAEKRVKDTEGELFRTKFSLQKLKKISEArhlpERDDLAKKLVSAELKLDNTERKI 243
Cdd:COG4913    736 LEAAEDLARLELRALLEERFAAALGDAVERE----LRENLEERIDALRARLNRAEEEL 789
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
112-291 2.10e-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: 2.10e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795415  112 RLLKITELQNEVSELQVKLAQLlkenKALKSL--QYRQEKALSKFEDAENEISQLIHRHNGEITALKERLRKSQEKERMA 189
Cdd:COG4913    253 LLEPIRELAERYAAARERLAEL----EYLRAAlrLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDEL 328

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795415  190 EKRVKDTEGElfrtkfSLQKLKK-ISEA-----RHLPERDDLAKKLVSAELKLDNTERKIKELSKNLELSTNSFQRQLLA 263
Cdd:COG4913    329 EAQIRGNGGD------RLEQLEReIERLereleERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEA 402

                          170       180
                   ....*....|....*....|....*...
gi 1958795415  264 ERKRAFEAHDENKILQKELQRLHHKLKE 291
Cdd:COG4913    403 LEEALAEAEAALRDLRRELRELEAEIAS 430
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 111-297 3.81e-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: 45.69  E-value: 3.81e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795415 111 ARLLKITELQNEVSELQVKLAQLLKEnkaLKSLQYRQEKALSKFEDAENEISQL---IHRHNGEITALKERLRKSQEK-- 185
Cdd:COG1579     7 RALLDLQELDSELDRLEHRLKELPAE---LAELEDELAALEARLEAAKTELEDLekeIKRLELEIEEVEARIKKYEEQlg 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795415 186 ERMAEKRVKDTEGElfrtkfsLQKLKKisearhlpERDDLAKKLVSAELKLDNTERKIKELSKNLELstnsfQRQLLAER 265
Cdd:COG1579    84 NVRNNKEYEALQKE-------IESLKR--------RISDLEDEILELMERIEELEEELAELEAELAE-----LEAELEEK 143

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1958795415 266 KRAFEAhdENKILQKELQRLHHKLKEKEKELD 297
Cdd:COG1579   144 KAELDE--ELAELEAELEELEAEREELAAKIP 173
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
115-331 5.23e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 46.60  E-value: 5.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795415 115 KITELQNEVSELQVKLAQLLKENKALKSLQYRQEKALSKFEDAENEISQLihrhNGEITALKERLRKSQEKERMAEKRVK 194
Cdd:PRK03918  201 ELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESL----EGSKRKLEEKIRELEERIEELKKEIE 276

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795415 195 DTE---GELFRTKFSLQKLKKISEAR--HLPERDDLAKKLVSAELKLDNTERKIKEL-SKNLELSTNSFQRQLLAERKRA 268
Cdd:PRK03918  277 ELEekvKELKELKEKAEEYIKLSEFYeeYLDELREIEKRLSRLEEEINGIEERIKELeEKEERLEELKKKLKELEKRLEE 356

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958795415 269 FE----AHDENKILQKELQRLHHKLKEKEKELDIKNI-YANRLPKSSPKKEKEIARKHASCQSDFTDL 331
Cdd:PRK03918  357 LEerheLYEEAKAKKEELERLKKRLTGLTPEKLEKELeELEKAKEEIEEEISKITARIGELKKEIKEL 424
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
121-297 8.26e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.91  E-value: 8.26e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795415 121 NEVSELQVKLAQLLKENKALKSLQYRQEKALSKFEDAENEISQLIHRHngeitalkERLRKSQEKeRMAEKRVKDTEGEL 200
Cdd:COG4717    71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREEL--------EKLEKLLQL-LPLYQELEALEAEL 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795415 201 FRTKFSLQKLKkiseaRHLPERDDLAKKLVSAELKLDNTERKIKELSKNLELSTNSFQRQLLAERKRAFEAHDEnkiLQK 280
Cdd:COG4717   142 AELPERLEELE-----ERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAE---LEE 213

                         170
                  ....*....|....*..
gi 1958795415 281 ELQRLHHKLKEKEKELD 297
Cdd:COG4717   214 ELEEAQEELEELEEELE 230
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
79-318 1.25e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 44.89  E-value: 1.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795415  79 NKKGVRVGFRSQSL-NREPLRKDPDIVTKRVLSARLLKITELQNEVSELQVKLAQLLKENKALKSLQYRQEKALSKFEDA 157
Cdd:COG4372     2 DRLGEKVGKARLSLfGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795415 158 ENEISQLIHRHNGEITALKERLRKSQEKERMAEKRVKDTEGELFRTKFSLQKLKKisearhlpERDDLAKKLVSAELKLD 237
Cdd:COG4372    82 LEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEA--------QIAELQSEIAEREEELK 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795415 238 NTERKIKELSKNLELSTNSFQRQLLAERKRAFEAHDENKILQKELQRLHHKLKEKEKELDIKNIYANRLPKSSPKKEKEI 317
Cdd:COG4372   154 ELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGL 233


                  .
gi 1958795415 318 A 318
Cdd:COG4372   234 A 234
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 116-306 1.42e-04

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 45.49  E-value: 1.42e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795415  116 ITELQNEVSELQVKLAQLLKENKALKS-LQYRQEKALSKFEDaenEISQLIHRHNGEITALKERLRKSQEKERMAEKRVK 194
Cdd:pfam15921  226 LRELDTEISYLKGRIFPVEDQLEALKSeSQNKIELLLQQHQD---RIEQLISEHEVEITGLTEKASSARSQANSIQSQLE 302

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795415  195 DTEgELFRTKFSLQklkkiseARHLPERDDLAKKLVSAELKLDNT-ERKIKELSKNLELSTNsfqrQLLAERKRAFEAHD 273
Cdd:pfam15921  303 IIQ-EQARNQNSMY-------MRQLSDLESTVSQLRSELREAKRMyEDKIEELEKQLVLANS----ELTEARTERDQFSQ 370

                          170       180       190
                   ....*....|....*....|....*....|...
gi 1958795415  274 ENKILQKELQRLHHKLKEKEKELDIKNIYANRL 306
Cdd:pfam15921  371 ESGNLDDQLQKLLADLHKREKELSLEKEQNKRL 403
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 106-200 1.75e-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: 44.37  E-value: 1.75e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795415 106 KRVLSARLLKITELQNEVSELQVKLAQLLKENKALKSLQYRQEKALSKFEDAENEISQLIHRHNGEITALKERLRKSQEK 185
Cdd:COG4942   142 KYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQE 221

                          90
                  ....*....|....*
gi 1958795415 186 ERMAEKRVKDTEGEL 200
Cdd:COG4942   222 AEELEALIARLEAEA 236
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 115-296 3.99e-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: 43.90  E-value: 3.99e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795415  115 KITELQNEVSELQVKLAQLLKENKALKSLQYRQEKalsKFEDAENEISQLihrhNGEITALKERLRKSQEK------ERM 188
Cdd:TIGR02169  682 RLEGLKRELSSLQSELRRIENRLDELSQELSDASR---KIGEIEKEIEQL----EQEEEKLKERLEELEEDlssleqEIE 754

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795415  189 AEKR-VKDTEGELFRTKFSLQKLKKIS---EARHLPER--------DDLAKKLVSAELKLDNTERKIKELSKNLELSTNS 256
Cdd:TIGR02169  755 NVKSeLKELEARIEELEEDLHKLEEALndlEARLSHSRipeiqaelSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKE 834

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1958795415  257 FQ-----RQLLAERKRAFEAHDENkiLQKELQRLHHKLKEKEKEL 296
Cdd:TIGR02169  835 IQelqeqRIDLKEQIKSIEKEIEN--LNGKKEELEEELEELEAAL 877
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 116-316 5.56e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.39  E-value: 5.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795415 116 ITELQNEVSELQVKLAQLLKEnkaLKSLQYRQEKALSKFEDAENEISQLIHRHNGEITALKERLRKSQEKERmAEKRVKD 195
Cdd:COG1196   325 LAELEEELEELEEELEELEEE---LEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR-AAAELAA 400

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795415 196 TEGELFRTKFSLQKLKkiseARHLPERDDLAKKLVSAELKLDNTERKIKELSKNLElstNSFQRQLLAERKRAFEAHDEN 275
Cdd:COG1196   401 QLEELEEAEEALLERL----ERLEEELEELEEALAELEEEEEEEEEALEEAAEEEA---ELEEEEEALLELLAELLEEAA 473

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1958795415 276 KILQKELQRLHHKLKEKEKELDIKNIYANRLPKSSPKKEKE 316
Cdd:COG1196   474 LLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAAL 514
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
 153-296 7.42e-04

Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.


Pssm-ID: 464001 [Multi-domain]  Cd Length: 200  Bit Score: 41.43  E-value: 7.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795415 153 KFEDAENEISQLIHRHNGEITALKERLRKSQEKERMAEKRVKDTEGELFRTKFSLQKLKKISEA--RHLPERDDLAKKLV 230
Cdd:pfam13851   9 AFNEIKNYYNDITRNNLELIKSLKEEIAELKKKEERNEKLMSEIQQENKRLTEPLQKAQEEVEElrKQLENYEKDKQSLK 88

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958795415 231 SAELKLDNTERKIKELSKNLELSTNSFQrQLLAER---KRAFEA--HD-------ENKILQKELQRLHHKLKEKEKEL 296
Cdd:pfam13851  89 NLKARLKVLEKELKDLKWEHEVLEQRFE-KVERERdelYDKFEAaiQDvqqktglKNLLLEKKLQALGETLEKKEAQL 165
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
106-317 8.09e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.74  E-value: 8.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795415 106 KRVLSARLLKITELQNEVSELQVKLAQLLKENKALKSLQYRQEKALSKFEDAE--NEISQLIHRHNgeitalKERLRKSQ 183
Cdd:PRK03918  451 KELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEqlKELEEKLKKYN------LEELEKKA 524

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795415 184 EKERMAEKRVKDTEGELFRTKFSLQKLKkisearhlperdDLAKKLVSAELKLDNTERKIKELSKNLELSTNSFQRQL-- 261
Cdd:PRK03918  525 EEYEKLKEKLIKLKGEIKSLKKELEKLE------------ELKKKLAELEKKLDELEEELAELLKELEELGFESVEELee 592

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958795415 262 -LAERKRAFEAHDENKILQKELQRLHHKLKEKEKELDIKNIYANRLPKSSPKKEKEI 317
Cdd:PRK03918  593 rLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKEL 649
PTZ00121 PTZ00121
MAEBL; Provisional
 111-322 1.32e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.44  E-value: 1.32e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795415  111 ARLLKITELQNEVSELQVKLAQLLKENKALKSLQYRQEKALSKFEDAEnEISQLIHRHNGEITALKERLRKSQEKERMAE 190
Cdd:PTZ00121  1292 ADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAE-EAKKAAEAAKAEAEAAADEAEAAEEKAEAAE 1370

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795415  191 KRVKDTEGELFRTKFSLQKLKKISEARHLPERD----DLAKKLVSAELKLDNTERKIKELSKNLELSTNsfqrqllAERK 266
Cdd:PTZ00121  1371 KKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDkkkaDELKKAAAAKKKADEAKKKAEEKKKADEAKKK-------AEEA 1443

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958795415  267 RAFEAHDENKILQKELQRLHHKLKEKEKELDIKNIYANRLPKSSPKKEKEIARKHA 322
Cdd:PTZ00121  1444 KKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKA 1499
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 126-296 1.52e-03

Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 41.02  E-value: 1.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795415 126 LQVKLAQLLKENKAlKSLQYRQEKALSKFEDAENEISQLIH-------RHNGEITALKERLRKSQEKERMAEK------R 192
Cdd:cd16269    99 LEEKKEEFCKQNEE-ASSKRCQALLQELSAPLEEKISQGSYsvpggyqLYLEDREKLVEKYRQVPRKGVKAEEvlqeflQ 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795415 193 VKDTEGE-LFRTKFSL-QKLKKISEARHLPERDDLAKKLVSAELKLdnTERKIKELSKNLELstnsFQRQLLAERKRafe 270
Cdd:cd16269   178 SKEAEAEaILQADQALtEKEKEIEAERAKAEAAEQERKLLEEQQRE--LEQKLEDQERSYEE----HLRQLKEKMEE--- 248

                         170       180
                  ....*....|....*....|....*..
gi 1958795415 271 ahdENKILQKELQRLH-HKLKEKEKEL 296
Cdd:cd16269   249 ---ERENLLKEQERALeSKLKEQEALL 272
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
115-268 1.67e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.68  E-value: 1.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795415 115 KITELQNEVSELQVKLAQLLKENKALKSLQyrqekalsKFEDAENEISQLIHRhngeITALKERLRKSQEKER---MAEK 191
Cdd:COG4717   103 ELEELEAELEELREELEKLEKLLQLLPLYQ--------ELEALEAELAELPER----LEELEERLEELRELEEeleELEA 170

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958795415 192 RVKDTEGELFR--TKFSLQKLKKISEArhLPERDDLAKKLVSAELKLDNTERKIKELSKNLELSTNSFQRQLLAERKRA 268
Cdd:COG4717   171 ELAELQEELEEllEQLSLATEEELQDL--AEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKE 247
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
118-297 1.70e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.97  E-value: 1.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795415 118 ELQNEVSELQVKLAQLLKENKALKSLQYRQEKALSKFEDAENEISQLIHRhngeitaLKERLRKSQEKermAEKRVKDTE 197
Cdd:PRK03918  529 KLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKE-------LEELGFESVEE---LEERLKELE 598

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795415 198 gELFRTKFSLQKLKKISEARhLPERDDLAKKLVSAELKLDNTERKIKELSKNLELSTNSFQRQllaERKRAFEAHDEnki 277
Cdd:PRK03918  599 -PFYNEYLELKDAEKELERE-EKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEE---EYEELREEYLE--- 670

                         170       180
                  ....*....|....*....|
gi 1958795415 278 LQKELQRLHHKLKEKEKELD 297
Cdd:PRK03918  671 LSRELAGLRAELEELEKRRE 690
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
123-297 2.05e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.29  E-value: 2.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795415 123 VSELQVKLAQLLKENKALKSLQyrqekaLSKFEDAENEISQLIHRHnGEITALKERLRKSQEKERMAEKRVKDTEGELFR 202
Cdd:COG4717    48 LERLEKEADELFKPQGRKPELN------LKELKELEEELKEAEEKE-EEYAELQEELEELEEELEELEAELEELREELEK 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795415 203 TKFSLQKLKKISEARHLPER----DDLAKKLVSAELKLDNTERKIKELSKNLELSTNSFQRQL----LAERKRAFEAHDE 274
Cdd:COG4717   121 LEKLLQLLPLYQELEALEAElaelPERLEELEERLEELRELEEELEELEAELAELQEELEELLeqlsLATEEELQDLAEE 200

                         170       180
                  ....*....|....*....|...
gi 1958795415 275 NKILQKELQRLHHKLKEKEKELD 297
Cdd:COG4717   201 LEELQQRLAELEEELEEAQEELE 223
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
88-296 4.48e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 40.39  E-value: 4.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795415  88 RSQSLNREPLRKdpdivTKRVLSARLlkiTELQNEVSELQVKLAqllkenkalkslQYRQEKALSKFEDAENEISQLIHR 167
Cdd:COG3206   164 QNLELRREEARK-----ALEFLEEQL---PELRKELEEAEAALE------------EFRQKNGLVDLSEEAKLLLQQLSE 223

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795415 168 HNGEITALKERLRKSQEKERMAEKRVKDTEGELFRTKFS--LQKLK-KISEARHlpERDDLAKKL-------VSAELKLD 237
Cdd:COG3206   224 LESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSpvIQQLRaQLAELEA--ELAELSARYtpnhpdvIALRAQIA 301

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958795415 238 NTERKIKELSKNLELSTNSfQRQLLAERKRAfeahdenkiLQKELQRLHHKLK---EKEKEL 296
Cdd:COG3206   302 ALRAQLQQEAQRILASLEA-ELEALQAREAS---------LQAQLAQLEARLAelpELEAEL 353
PRK12704 PRK12704
phosphodiesterase; Provisional
 225-320 6.99e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 39.76  E-value: 6.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795415 225 LAKKLVSAelKLDNTERKIKELSKNLELSTNSFQRQLLAERKRAF-----EAHDENKILQKELQRLHHKLKEKEKELDIK 299
Cdd:PRK12704   24 VRKKIAEA--KIKEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIhklrnEFEKELRERRNELQKLEKRLLQKEENLDRK 101

                          90       100
                  ....*....|....*....|.
gi 1958795415 300 NIYANRLPKSSPKKEKEIARK 320
Cdd:PRK12704  102 LELLEKREEELEKKEKELEQK 122
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
107-296 7.12e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 39.66  E-value: 7.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795415 107 RVLSARLLKITELQNEVSELQVKLAQLLKENKALksLQYRQEKALSKFEDAENEISQL--IHRHNGEITALKERLRKSQE 184
Cdd:PRK03918  542 KSLKKELEKLEELKKKLAELEKKLDELEEELAEL--LKELEELGFESVEELEERLKELepFYNEYLELKDAEKELEREEK 619

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795415 185 KERMAEKRVKDTEGELFRTKFSLQKLKKisearhlpERDDLAKKLVSAELKldNTERKIKELSKNLElstnsfqrQLLAE 264
Cdd:PRK03918  620 ELKKLEEELDKAFEELAETEKRLEELRK--------ELEELEKKYSEEEYE--ELREEYLELSRELA--------GLRAE 681

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1958795415 265 RKRAFEAHDENKILQKELQRLHHKLKEKEKEL 296
Cdd:PRK03918  682 LEELEKRREEIKKTLEKLKEELEEREKAKKEL 713
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
115-300 7.12e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 39.66  E-value: 7.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795415 115 KITELQNEVSELQVKLAQLLKENKALKSLQYRQE------KALSKFEDAENEISQLIHRHNGEITALKERLRKSQEKERM 188
Cdd:PRK03918  260 KIRELEERIEELKKEIEELEEKVKELKELKEKAEeyiklsEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEER 339

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795415 189 AE---KRVKDTEGELFRTKFSLQKLKKI----SEARHLPER------DDLAKKLVSAELKLDNTERKIKEL-SKNLELST 254
Cdd:PRK03918  340 LEelkKKLKELEKRLEELEERHELYEEAkakkEELERLKKRltgltpEKLEKELEELEKAKEEIEEEISKItARIGELKK 419

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958795415 255 NSFQRQLLAER-----------KRAFEAHDENKILQK---ELQRLHHKLKE-KEKELDIKN 300
Cdd:PRK03918  420 EIKELKKAIEElkkakgkcpvcGRELTEEHRKELLEEytaELKRIEKELKEiEEKERKLRK 480
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 172-476 7.20e-03

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: 40.04  E-value: 7.20e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795415  172 ITALKERLRKSQEK-ERMAE--KRVKDTEGELFRTKFSLQ-------KLKKISEARHLPERDDLAKKLVSAELKLDNTER 241
Cdd:TIGR02168  167 ISKYKERRKETERKlERTREnlDRLEDILNELERQLKSLErqaekaeRYKELKAELRELELALLVLRLEELREELEELQE 246

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795415  242 KIKELS---KNLELSTNSFQRQLLAERKRAFEAHDENKILQKELQRLHHKLKEKEKELDIKNIYANRLPKSSPKKEKEIA 318
Cdd:TIGR02168  247 ELKEAEeelEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLE 326

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795415  319 RKHASCQSDFTDLCTKAVQTAE-----DFEPEEFPFTAQTVLCYENRWDGSEYLpsyLEYQERN----EHGSESLSSTLE 389
Cdd:TIGR02168  327 ELESKLDELAEELAELEEKLEElkeelESLEAELEELEAELEELESRLEELEEQ---LETLRSKvaqlELQIASLNNEIE 403

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795415  390 QegkYSDDQDSCTAKQETGKSECEWEREELDKVKgKSSLLGRTEKLVLEAGSVQTESYQAQTIDKFQDEAERLKTEMLLA 469
Cdd:TIGR02168  404 R---LEARLERLEDRRERLQQEIEELLKKLEEAE-LKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDA 479


                   ....*..
gi 1958795415  470 KLNEINK 476
Cdd:TIGR02168  480 AERELAQ 486
COG5022 COG5022
Myosin heavy chain [General function prediction only];
103-321 7.93e-03

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 39.68  E-value: 7.93e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795415  103 IVTKRVLSARLLKITELQNEVseLQVKLAQLLKENKALKSLQYRQ--EKALSKFEDAENEISQLiHRHNGEITALKErlr 180
Cdd:COG5022    826 IKREKKLRETEEVEFSLKAEV--LIQKFGRSLKAKKRFSLLKKETiyLQSAQRVELAERQLQEL-KIDVKSISSLKL--- 899

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795415  181 KSQEKERMAEKRVKDTEGELF-RTKFSLQ---KLKKISEARHLPERDDLAKKLVSAELKLDNTERKIKELSKNLEL---S 253
Cdd:COG5022    900 VNLELESEIIELKKSLSSDLIeNLEFKTEliaRLKKLLNNIDLEEGPSIEYVKLPELNKLHEVESKLKETSEEYEDllkK 979

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958795415  254 TNSFQRQLLAER-------KRAFEAHDENKILQ---KELQRLHHKLKEKEKELDIKN-IYANrlpKSSPKKEKEIARKH 321
Cdd:COG5022    980 STILVREGNKANselknfkKELAELSKQYGALQestKQLKELPVEVAELQSASKIISsESTE---LSILKPLQKLKGLL 1055
 
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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