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Conserved domains on  [gi|2024443084|ref|XP_040515597|]
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lebercilin-like protein isoform X4 [Gallus gallus]

Protein Classification

Lebercilin domain-containing protein( domain architecture ID 12174059)

Lebercilin domain-containing protein

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 ...
100-292 1.22e-62

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: 205.14  E-value: 1.22e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024443084 100 VAQRILSARLHKIKELKNEISDLQHKLEASNLENQVLKRLLYRHSKAIGGYESSESVLPDLLTRHYSEVSALRKHLRISQ 179
Cdd:pfam15619   1 VTQRVLSARLHKIKELQNELAELQSKLEELRKENRLLKRLQKRQEKALGKYEGTESELPQLIARHNEEVRVLRERLRRLQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024443084 180 EEERRASRKLRKVEAELLKAKDDLQALYKLSEDKTLAERDELYHRLSVLTEKMEVNNKRIQSLEKQLKLNNSTFSRQLAN 259
Cdd:pfam15619  81 EKERDLERKLKEKEAELLRLRDQLKRLEKLSEDKNLAEREELQKKLEQLEAKLEDKDEKIQDLERKLELENKSFRRQLAA 160
                         170       180       190
                  ....*....|....*....|....*....|...
gi 2024443084 260 ENKKAVEAGIITKNLQMEINSLHQKIKEKDRQL 292
Cdd:pfam15619 161 EKKKHKEAQEEVKILQEEIERLQQKLKEKEREL 193
 
Name Accession Description Interval E-value
Lebercilin pfam15619
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ...
100-292 1.22e-62

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: 205.14  E-value: 1.22e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024443084 100 VAQRILSARLHKIKELKNEISDLQHKLEASNLENQVLKRLLYRHSKAIGGYESSESVLPDLLTRHYSEVSALRKHLRISQ 179
Cdd:pfam15619   1 VTQRVLSARLHKIKELQNELAELQSKLEELRKENRLLKRLQKRQEKALGKYEGTESELPQLIARHNEEVRVLRERLRRLQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024443084 180 EEERRASRKLRKVEAELLKAKDDLQALYKLSEDKTLAERDELYHRLSVLTEKMEVNNKRIQSLEKQLKLNNSTFSRQLAN 259
Cdd:pfam15619  81 EKERDLERKLKEKEAELLRLRDQLKRLEKLSEDKNLAEREELQKKLEQLEAKLEDKDEKIQDLERKLELENKSFRRQLAA 160
                         170       180       190
                  ....*....|....*....|....*....|...
gi 2024443084 260 ENKKAVEAGIITKNLQMEINSLHQKIKEKDRQL 292
Cdd:pfam15619 161 EKKKHKEAQEEVKILQEEIERLQQKLKEKEREL 193
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
70-247 5.66e-05

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 46.07  E-value: 5.66e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024443084  70 GKKLPAKKIPHEKSSFLSLQNNtISQKKNKVAQRIlSARLHKIKELKNEISDLQHKLEA----SNLeNQVLKRLL-YRHS 144
Cdd:PRK05771   69 LNPLREEKKKVSVKSLEELIKD-VEEELEKIEKEI-KELEEEISELENEIKELEQEIERlepwGNF-DLDLSLLLgFKYV 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024443084 145 KAIGGYESSESVLPDLLtrhyseVSALRKHLRISQEEERR------ASRKLRKVEAELLKAkdDLQALyKLSEDKTLAEr 218
Cdd:PRK05771  146 SVFVGTVPEDKLEELKL------ESDVENVEYISTDKGYVyvvvvvLKELSDEVEEELKKL--GFERL-ELEEEGTPSE- 215
                         170       180
                  ....*....|....*....|....*....
gi 2024443084 219 delyhRLSVLTEKMEVNNKRIQSLEKQLK 247
Cdd:PRK05771  216 -----LIREIKEELEEIEKERESLLEELK 239
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
111-386 1.05e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 45.43  E-value: 1.05e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024443084  111 KIKELKNEISDLQH------------KLEASNLENQVLKRLLYRHSKAIGGYESSesvlpdlLTRHYSEVSALRKHLRIS 178
Cdd:TIGR02168  214 RYKELKAELRELELallvlrleelreELEELQEELKEAEEELEELTAELQELEEK-------LEELRLEVSELEEEIEEL 286
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024443084  179 QEEERRASRKLRKVEAELLKAKDDLQALYKlSEDKTLAERDELYHRLSVLTEKMEVNNKRIQSLEKQLKLnnstFSRQLA 258
Cdd:TIGR02168  287 QKELYALANEISRLEQQKQILRERLANLER-QLEELEAQLEELESKLDELAEELAELEEKLEELKEELES----LEAELE 361
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024443084  259 NENKKAVEAGIITKNLQMEINSLHQKIKEKDRQLYIKNiytNRLLKIPKDKGDAVSHKKSLSINTSLQADKQHFRSLQLP 338
Cdd:TIGR02168  362 ELEAELEELESRLEELEEQLETLRSKVAQLELQIASLN---NEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKEL 438
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2024443084  339 QYQPQETEESLVLLHEEK-----KASEGKNQKAKASEAYTDAQCETEKQSSKK 386
Cdd:TIGR02168  439 QAELEELEEELEELQEELerleeALEELREELEEAEQALDAAERELAQLQARL 491
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
111-292 1.56e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 41.29  E-value: 1.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024443084 111 KIKELKNEISDLQHKLEASNLENQVLKRLLYRHSKAIggyesseSVLPDLLTRHYSEVSALRKHLRISQEEERRASRKLR 190
Cdd:COG4942    28 ELEQLQQEIAELEKELAALKKEEKALLKQLAALERRI-------AALARRIRALEQELAALEAELAELEKEIAELRAELE 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024443084 191 KVEAELlkaKDDLQALYKLSEDKTLA------ERDELYHRLSVLTEKMEVNNKRIQSLEKQLKLNNSTfsRQLANENKKA 264
Cdd:COG4942   101 AQKEEL---AELLRALYRLGRQPPLAlllspeDFLDAVRRLQYLKYLAPARREQAEELRADLAELAAL--RAELEAERAE 175
                         170       180
                  ....*....|....*....|....*...
gi 2024443084 265 VEAGIitKNLQMEINSLHQKIKEKDRQL 292
Cdd:COG4942   176 LEALL--AELEEERAALEALKAERQKLL 201
 
Name Accession Description Interval E-value
Lebercilin pfam15619
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ...
100-292 1.22e-62

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: 205.14  E-value: 1.22e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024443084 100 VAQRILSARLHKIKELKNEISDLQHKLEASNLENQVLKRLLYRHSKAIGGYESSESVLPDLLTRHYSEVSALRKHLRISQ 179
Cdd:pfam15619   1 VTQRVLSARLHKIKELQNELAELQSKLEELRKENRLLKRLQKRQEKALGKYEGTESELPQLIARHNEEVRVLRERLRRLQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024443084 180 EEERRASRKLRKVEAELLKAKDDLQALYKLSEDKTLAERDELYHRLSVLTEKMEVNNKRIQSLEKQLKLNNSTFSRQLAN 259
Cdd:pfam15619  81 EKERDLERKLKEKEAELLRLRDQLKRLEKLSEDKNLAEREELQKKLEQLEAKLEDKDEKIQDLERKLELENKSFRRQLAA 160
                         170       180       190
                  ....*....|....*....|....*....|...
gi 2024443084 260 ENKKAVEAGIITKNLQMEINSLHQKIKEKDRQL 292
Cdd:pfam15619 161 EKKKHKEAQEEVKILQEEIERLQQKLKEKEREL 193
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
70-247 5.66e-05

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 46.07  E-value: 5.66e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024443084  70 GKKLPAKKIPHEKSSFLSLQNNtISQKKNKVAQRIlSARLHKIKELKNEISDLQHKLEA----SNLeNQVLKRLL-YRHS 144
Cdd:PRK05771   69 LNPLREEKKKVSVKSLEELIKD-VEEELEKIEKEI-KELEEEISELENEIKELEQEIERlepwGNF-DLDLSLLLgFKYV 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024443084 145 KAIGGYESSESVLPDLLtrhyseVSALRKHLRISQEEERR------ASRKLRKVEAELLKAkdDLQALyKLSEDKTLAEr 218
Cdd:PRK05771  146 SVFVGTVPEDKLEELKL------ESDVENVEYISTDKGYVyvvvvvLKELSDEVEEELKKL--GFERL-ELEEEGTPSE- 215
                         170       180
                  ....*....|....*....|....*....
gi 2024443084 219 delyhRLSVLTEKMEVNNKRIQSLEKQLK 247
Cdd:PRK05771  216 -----LIREIKEELEEIEKERESLLEELK 239
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
111-386 1.05e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 45.43  E-value: 1.05e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024443084  111 KIKELKNEISDLQH------------KLEASNLENQVLKRLLYRHSKAIGGYESSesvlpdlLTRHYSEVSALRKHLRIS 178
Cdd:TIGR02168  214 RYKELKAELRELELallvlrleelreELEELQEELKEAEEELEELTAELQELEEK-------LEELRLEVSELEEEIEEL 286
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024443084  179 QEEERRASRKLRKVEAELLKAKDDLQALYKlSEDKTLAERDELYHRLSVLTEKMEVNNKRIQSLEKQLKLnnstFSRQLA 258
Cdd:TIGR02168  287 QKELYALANEISRLEQQKQILRERLANLER-QLEELEAQLEELESKLDELAEELAELEEKLEELKEELES----LEAELE 361
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024443084  259 NENKKAVEAGIITKNLQMEINSLHQKIKEKDRQLYIKNiytNRLLKIPKDKGDAVSHKKSLSINTSLQADKQHFRSLQLP 338
Cdd:TIGR02168  362 ELEAELEELESRLEELEEQLETLRSKVAQLELQIASLN---NEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKEL 438
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2024443084  339 QYQPQETEESLVLLHEEK-----KASEGKNQKAKASEAYTDAQCETEKQSSKK 386
Cdd:TIGR02168  439 QAELEELEEELEELQEELerleeALEELREELEEAEQALDAAERELAQLQARL 491
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
111-292 1.56e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 41.29  E-value: 1.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024443084 111 KIKELKNEISDLQHKLEASNLENQVLKRLLYRHSKAIggyesseSVLPDLLTRHYSEVSALRKHLRISQEEERRASRKLR 190
Cdd:COG4942    28 ELEQLQQEIAELEKELAALKKEEKALLKQLAALERRI-------AALARRIRALEQELAALEAELAELEKEIAELRAELE 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024443084 191 KVEAELlkaKDDLQALYKLSEDKTLA------ERDELYHRLSVLTEKMEVNNKRIQSLEKQLKLNNSTfsRQLANENKKA 264
Cdd:COG4942   101 AQKEEL---AELLRALYRLGRQPPLAlllspeDFLDAVRRLQYLKYLAPARREQAEELRADLAELAAL--RAELEAERAE 175
                         170       180
                  ....*....|....*....|....*...
gi 2024443084 265 VEAGIitKNLQMEINSLHQKIKEKDRQL 292
Cdd:COG4942   176 LEALL--AELEEERAALEALKAERQKLL 201
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
105-429 2.98e-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: 40.81  E-value: 2.98e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024443084  105 LSARLHKIKELKNEISDLQHKLEASNLENQVLKRLLYRHSKAIGGYESSESVLPDLLTRHYSEVSALRKHLRISQEEERR 184
Cdd:TIGR02168  700 LAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAE 779
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024443084  185 ASRKLRKVEAELLKAKDDLQALyKLSEDKTLAERDELYHRLSVLTEKMEVNNKRIQSLEKQLKlnnsTFSRQLANENKKA 264
Cdd:TIGR02168  780 AEAEIEELEAQIEQLKEELKAL-REALDELRAELTLLNEEAANLRERLESLERRIAATERRLE----DLEEQIEELSEDI 854
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024443084  265 VEAGIITKNLQMEINSLHQKIKEKDRQLYIKNiytnRLLKIPKDKGDAVSHKkslsintsLQADKQHFRSLQlPQYQPQE 344
Cdd:TIGR02168  855 ESLAAEIEELEELIEELESELEALLNERASLE----EALALLRSELEELSEE--------LRELESKRSELR-RELEELR 921
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024443084  345 TEESLVLLHEEKKASEGKNQKAKASEAYTDAQCETEKQSSKKIPKP---ETFSRTHKEYLKENKPLTVHTCLEFISQEER 421
Cdd:TIGR02168  922 EKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEeeaRRRLKRLENKIKELGPVNLAAIEEYEELKER 1001

                   ....*...
gi 2024443084  422 KRDLLKQK 429
Cdd:TIGR02168 1002 YDFLTAQK 1009
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
75-421 3.35e-03

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 40.49  E-value: 3.35e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024443084   75 AKKIpHEKSSFLSLQNNTISQKKNKVAQRILSarlhKIKELKNEISDLQHKLEASNLENQ-VLKRLLYRHSKAIGGYESS 153
Cdd:pfam15921  201 GKKI-YEHDSMSTMHFRSLGSAISKILRELDT----EISYLKGRIFPVEDQLEALKSESQnKIELLLQQHQDRIEQLISE 275
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024443084  154 ESV----LPDLLTRHYSEVSALRKHLRISQEEERRAS----RKLRKVEAELLKAKDDLQALYKLSEDKtlaerdelyhrl 225
Cdd:pfam15921  276 HEVeitgLTEKASSARSQANSIQSQLEIIQEQARNQNsmymRQLSDLESTVSQLRSELREAKRMYEDK------------ 343
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024443084  226 svltekmevnnkrIQSLEKQLKLNNSTFSRQLANENKKAVEAGIITKNLQMEINSLHQKIKEkdrqLYIKNIYTNRLLKi 305
Cdd:pfam15921  344 -------------IEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKE----LSLEKEQNKRLWD- 405
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024443084  306 pKDKGDAVSHKkslsiNTSLQADKQHFRSLQLPQYQPQETEESLVLLHEEKKASEGKNQKAKASEAYTdAQCETEKQSSK 385
Cdd:pfam15921  406 -RDTGNSITID-----HLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLT-AQLESTKEMLR 478
                          330       340       350
                   ....*....|....*....|....*....|....*.
gi 2024443084  386 KIPKpetfSRTHKEYLKENKPLTVHTCLEFISQEER 421
Cdd:pfam15921  479 KVVE----ELTAKKMTLESSERTVSDLTASLQEKER 510
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
65-291 3.74e-03

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


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 40.59  E-value: 3.74e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024443084   65 QNNKGGKKLPAKKIPHEKSSFLslqNNTISQKKNKVAQRILSARlHKIKELKNEISDLQHKLEASNLEnqvlkrllyrHS 144
Cdd:pfam12128  577 ELNLYGVKLDLKRIDVPEWAAS---EEELRERLDKAEEALQSAR-EKQAAAEEQLVQANGELEKASRE----------ET 642
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024443084  145 KAIGGYESSESVLPDLLTRHYSEVSALRKHLrisQEEERRASRKLRKVEAELLKAKDDLQALYKLSEDKTLAERDELYHR 224
Cdd:pfam12128  643 FARTALKNARLDLRRLFDEKQSEKDKKNKAL---AERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAY 719
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024443084  225 LSVLTEKMEVNNKR----IQSLEKQLKLNNSTFSRQLANENKKAVEAGIITKNLQMEINSLHQKIK--EKDRQ 291
Cdd:pfam12128  720 WQVVEGALDAQLALlkaaIAARRSGAKAELKALETWYKRDLASLGVDPDVIAKLKREIRTLERKIEriAVRRQ 792
 
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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