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Conserved domains on  [gi|1034612127|ref|XP_016858981|]
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coiled-coil domain-containing protein 138 isoform X2 [Homo sapiens]

Protein Classification

coiled-coil domain-containing protein( domain architecture ID 1000037)

coiled-coil domain-containing protein contains a region with alpha-helical coiled-coil sequence signatures that is being annotated by a variety of protein family models, not necessarily indicating family membership

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Lebercilin super family cl25726
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ...
 191-317 2.47e-06

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.


The actual alignment was detected with superfamily member pfam15619:

Pssm-ID: 464776 [Multi-domain]  Cd Length: 193  Bit Score: 48.36  E-value: 2.47e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612127 191 LQCETAAQQKFAEELQKRERFLlerEQLLFRHENALSKIKGVEEEVLtrfQIIKEHDAEVEHLTEVL------------- 257
Cdd:pfam15619  16 LQNELAELQSKLEELRKENRLL---KRLQKRQEKALGKYEGTESELP---QLIARHNEEVRVLRERLrrlqekerdlerk 89

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034612127 258 -KEKNKETKRLRSSFDALKELNDtlKKQLNEASEENRKIDIQAKRVQA---RLDNLQRKYEFMT 317
Cdd:pfam15619  90 lKEKEAELLRLRDQLKRLEKLSE--DKNLAEREELQKKLEQLEAKLEDkdeKIQDLERKLELEN 151
 
Name Accession Description Interval E-value
Lebercilin pfam15619
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ...
 191-317 2.47e-06

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: 48.36  E-value: 2.47e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612127 191 LQCETAAQQKFAEELQKRERFLlerEQLLFRHENALSKIKGVEEEVLtrfQIIKEHDAEVEHLTEVL------------- 257
Cdd:pfam15619  16 LQNELAELQSKLEELRKENRLL---KRLQKRQEKALGKYEGTESELP---QLIARHNEEVRVLRERLrrlqekerdlerk 89

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034612127 258 -KEKNKETKRLRSSFDALKELNDtlKKQLNEASEENRKIDIQAKRVQA---RLDNLQRKYEFMT 317
Cdd:pfam15619  90 lKEKEAELLRLRDQLKRLEKLSE--DKNLAEREELQKKLEQLEAKLEDkdeKIQDLERKLELEN 151
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 188-314 7.18e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.08  E-value: 7.18e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612127 188 HLKLQCETAAQ-QKFAEELQKRER--FLLEREQLLFRHENALSKIKGVEEEVLTRFQIIKEHDAEVEHLTEVLKEKNKET 264
Cdd:COG1196   204 PLERQAEKAERyRELKEELKELEAelLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELEL 283

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1034612127 265 KRLRSSFDALKELNDTLKKQLNEASEENRKIDIQAKRVQARLDNLQRKYE 314
Cdd:COG1196   284 EEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELE 333
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 194-311 1.21e-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: 42.35  E-value: 1.21e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612127  194 ETAAQQKFAE-ELQKRERFLLEREQLLFRHE--NALSKIKGVEEEVLTRFQIIKEHD-----AEVEHLTEVLKEKNKETK 265
Cdd:TIGR02168  371 ESRLEELEEQlETLRSKVAQLELQIASLNNEieRLEARLERLEDRRERLQQEIEELLkkleeAELKELQAELEELEEELE 450

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1034612127  266 RLRSSFDALKELNDTLKKQLNEASEENRKIDIQAKRVQARLDNLQR 311
Cdd:TIGR02168  451 ELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLER 496
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
203-339 3.46e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.82  E-value: 3.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612127 203 EELQKRERFLLEREQLLFRHENALSKIKGVEEEVLTRFQiikehDAEVEHLTEVLKEKNKETKRLRSSFDALKELNDTLK 282
Cdd:PRK03918  619 KELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYS-----EEEYEELREEYLELSRELAGLRAELEELEKRREEIK 693

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1034612127 283 KQLNEASEENRKIdiqaKRVQARLDNLQRKYEFMTIQRLKgsshaVHEMKSLKQEKA 339
Cdd:PRK03918  694 KTLEKLKEELEER----EKAKKELEKLEKALERVEELREK-----VKKYKALLKERA 741
Atg16_CCD cd22887
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ...
 243-294 9.25e-03

Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family includes Saccharomyces cerevisiae Atg16 (also called cytoplasm to vacuole targeting protein 11, CVT11, or SAP18), human autophagy-related protein 16-1 (also called APG16-like 1, ATG16L1, or APG16L) and autophagy-related protein 16-2 (also called APG16-like 2, ATG16L2, WD repeat-containing protein 80 or WDR80), and similar proteins. Atg16 stabilizes the Atg5-Atg12 conjugate and mediates the formation of the 350 kDa complex, which is necessary for autophagy. The Atg5-Atg12/Atg16 complex is required for efficient promotion of Atg8-conjugation to phosphatidylethanolamine and Atg8 localization to the pre-autophagosomal structure (PAS). Similarly, human ATG16L1 plays an essential role in autophagy and acts as a molecular scaffold which mediates protein-protein interactions essential for autophagosome formation. ATG16L2, though structurally similar to ATG16L1 and able to form a complex with the autophagy proteins Atg5 and Atg12, is not essential for autophagy. Single-nucleotide polymorphisms in ATG16L1 is associated with an increased risk of developing Crohn disease. Saccharomyces cerevisiae Atg16 contains an N-terminal domain (NTD) that interacts with the Atg5-Atg12 protein conjugate and a coiled-coil domain (CCD) that dimerizes and mediates self-assembly. Human ATG16L1 and ATG16L2 also contains an N-terminal region that binds Atg5, a CCD homologous to the yeast CCD, and a WD40 domain that represents approximately 50% of the full-length protein. This model corresponds to the CCD of Atg16 family proteins.


Pssm-ID: 439196 [Multi-domain]  Cd Length: 91  Bit Score: 36.00  E-value: 9.25e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1034612127 243 IKEHDAEVEHLTEVLKEKNKETKRLRSSFDALKELNDTLKKQLNEASEENRK 294
Cdd:cd22887    20 LASLEEEIKDLEEELKEKNKANEILNDELIALQIENNLLEEKLRKLQEENDE 71
 
Name Accession Description Interval E-value
Lebercilin pfam15619
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ...
 191-317 2.47e-06

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: 48.36  E-value: 2.47e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612127 191 LQCETAAQQKFAEELQKRERFLlerEQLLFRHENALSKIKGVEEEVLtrfQIIKEHDAEVEHLTEVL------------- 257
Cdd:pfam15619  16 LQNELAELQSKLEELRKENRLL---KRLQKRQEKALGKYEGTESELP---QLIARHNEEVRVLRERLrrlqekerdlerk 89

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034612127 258 -KEKNKETKRLRSSFDALKELNDtlKKQLNEASEENRKIDIQAKRVQA---RLDNLQRKYEFMT 317
Cdd:pfam15619  90 lKEKEAELLRLRDQLKRLEKLSE--DKNLAEREELQKKLEQLEAKLEDkdeKIQDLERKLELEN 151
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 188-314 7.18e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.08  E-value: 7.18e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612127 188 HLKLQCETAAQ-QKFAEELQKRER--FLLEREQLLFRHENALSKIKGVEEEVLTRFQIIKEHDAEVEHLTEVLKEKNKET 264
Cdd:COG1196   204 PLERQAEKAERyRELKEELKELEAelLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELEL 283

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1034612127 265 KRLRSSFDALKELNDTLKKQLNEASEENRKIDIQAKRVQARLDNLQRKYE 314
Cdd:COG1196   284 EEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELE 333
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 186-339 1.85e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.93  E-value: 1.85e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612127 186 QIHLKLQCETAAQQKFAEELQKRERFLLEREQLLFRHENALSKIKGVEEEVLTRFQIIKEHDAEVEHLTEVLKEKNKETK 265
Cdd:COG1196   289 EEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALL 368

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034612127 266 RLRSSFDALKELNDTLKKQLNEASEENRKIDIQAKRVQARLDNLQRKYEFMTIQRLKGSSHAVHEMKSLKQEKA 339
Cdd:COG1196   369 EAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEE 442
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 194-311 1.21e-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: 42.35  E-value: 1.21e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612127  194 ETAAQQKFAE-ELQKRERFLLEREQLLFRHE--NALSKIKGVEEEVLTRFQIIKEHD-----AEVEHLTEVLKEKNKETK 265
Cdd:TIGR02168  371 ESRLEELEEQlETLRSKVAQLELQIASLNNEieRLEARLERLEDRRERLQQEIEELLkkleeAELKELQAELEELEEELE 450

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1034612127  266 RLRSSFDALKELNDTLKKQLNEASEENRKIDIQAKRVQARLDNLQR 311
Cdd:TIGR02168  451 ELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLER 496
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
176-321 1.48e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.43  E-value: 1.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612127 176 QISQIYDELFQIHLKLQCETAAQQKFAEELQKRERFLLEREQLLFRHENALSKIKGVEEEVLTRFQIIKEhdaEVEHLTE 255
Cdd:COG4372    39 ELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQE---EAEELQE 115

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034612127 256 VLKEKNKETKRLRSSFDALKELNDTLKKQLNEASEENRKIDIQAKRVQARLDNLQRKYEFMTIQRL 321
Cdd:COG4372   116 ELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEA 181
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 168-339 2.96e-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: 2.96e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612127  168 DKRSLLPHQISQIYDELFQIHLKLQCETAAQQKFAEELQKRERFLLE----REQLLFRHENALSKIKGVEEEVLTRFQII 243
Cdd:TIGR02168  712 EELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTEleaeIEELEERLEEAEEELAEAEAEIEELEAQI 791

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612127  244 KEHDAEVEHLTEVLKEKNKETKRLRSSFDALKELNDTLKKQLNEASEENRKIDIQAKRVQARLDNLQRKYEFMTIQRLKG 323
Cdd:TIGR02168  792 EQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEEL 871

                          170
                   ....*....|....*.
gi 1034612127  324 SShavhEMKSLKQEKA 339
Cdd:TIGR02168  872 ES----ELEALLNERA 883
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
203-339 3.46e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.82  E-value: 3.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612127 203 EELQKRERFLLEREQLLFRHENALSKIKGVEEEVLTRFQiikehDAEVEHLTEVLKEKNKETKRLRSSFDALKELNDTLK 282
Cdd:PRK03918  619 KELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYS-----EEEYEELREEYLELSRELAGLRAELEELEKRREEIK 693

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1034612127 283 KQLNEASEENRKIdiqaKRVQARLDNLQRKYEFMTIQRLKgsshaVHEMKSLKQEKA 339
Cdd:PRK03918  694 KTLEKLKEELEER----EKAKKELEKLEKALERVEELREK-----VKKYKALLKERA 741
PKK pfam12474
Polo kinase kinase; This domain family is found in eukaryotes, and is approximately 140 amino ...
 206-338 3.58e-03

Polo kinase kinase; This domain family is found in eukaryotes, and is approximately 140 amino acids in length. The family is found in association with pfam00069. Polo-like kinase 1 (Plx1) is essential during mitosis for the activation of Cdc25C, for spindle assembly, and for cyclin B degradation. This family is Polo kinase kinase (PKK) which phosphorylates Polo kinase and Polo-like kinase to activate them. PKK is a serine/threonine kinase.


Pssm-ID: 463600 [Multi-domain]  Cd Length: 139  Bit Score: 38.31  E-value: 3.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612127 206 QKRERFLLEREQLLFRHEnalskikgVEEEVLTRFQIIKEHDAEVEHLTevlkEKNKETKRLRSSFDA-LKELNDTLKKQ 284
Cdd:pfam12474   7 QQKDRFEQERQQLKKRYE--------KELEQLERQQKQQIEKLEQRQTQ----ELRRLPKRIRAEQKKrLKMFRESLKQE 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034612127 285 LNEASEEN-------RKIDIQAKRVQARLDNLQRKYEFMtiQRLKGSshAVHEMKSLKQEK 338
Cdd:pfam12474  75 KKELKQEVeklpkfqRKEAKRQRKEELELEQKHEELEFL--QAQSEA--LERELQQLQNEK 131
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
 162-320 5.66e-03

HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.


Pssm-ID: 461694 [Multi-domain]  Cd Length: 528  Bit Score: 39.67  E-value: 5.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612127 162 PKSKASDKRSLLPHQISQIYDELFQIH-----LKLQCETaaQQKFAEELQKR---------ERFLLEREQLLFRHENalS 227
Cdd:pfam05622  53 SGTPGGKKYLLLQKQLEQLQEENFRLEtarddYRIKCEE--LEKEVLELQHRneeltslaeEAQALKDEMDILRESS--D 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612127 228 KIKGVEEEVLT-------------RFQIIKEHDAEVEHLTEVLKEKNKETKRLRSSFDALKELNDTLKKQLNEASEENRK 294
Cdd:pfam05622 129 KVKKLEATVETykkkledlgdlrrQVKLLEERNAEYMQRTLQLEEELKKANALRGQLETYKRQVQELHGKLSEESKKADK 208

                         170       180
                  ....*....|....*....|....*.
gi 1034612127 295 IDIQAKRVQARLDNLQRKYEFMTIQR 320
Cdd:pfam05622 209 LEFEYKKLEEKLEALQKEKERLIIER 234
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 194-311 6.01e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.92  E-value: 6.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612127 194 ETAAQQKFAEELQKRERFLLEREQLLFRHENALSKIKGVEEEVLTRFQIIKEHDAEVEHLTEVLKEKNKETKRLRSSFDA 273
Cdd:COG1196   402 LEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAE 481

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1034612127 274 LKELNDTLKKQLNEASEENRKIDIQAKRVQARLDNLQR 311
Cdd:COG1196   482 LLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGL 519
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 186-337 6.18e-03

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 39.94  E-value: 6.18e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612127  186 QIHLkLQCETAAQQkfAEELQKRERFLLEREQLLFRHENALSKIkgveEEVLTRFQIIKEHDAEVEHLTEVLKEknkETK 265
Cdd:COG3096    882 QANL-LADETLADR--LEELREELDAAQEAQAFIQQHGKALAQL----EPLVAVLQSDPEQFEQLQADYLQAKE---QQR 951

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612127  266 RLRSSFDALKE----------------------LNDTLKKQLNEASEENRKIDIQAKRVQARLDNLQRkyefmTIQRLKG 323
Cdd:COG3096    952 RLKQQIFALSEvvqrrphfsyedavgllgensdLNEKLRARLEQAEEARREAREQLRQAQAQYSQYNQ-----VLASLKS 1026

                          170
                   ....*....|....*
gi 1034612127  324 SSHAVHEM-KSLKQE 337
Cdd:COG3096   1027 SRDAKQQTlQELEQE 1041
RNase_Y_N pfam12072
RNase Y N-terminal region;
204-320 7.13e-03

RNase Y N-terminal region;


Pssm-ID: 463456 [Multi-domain]  Cd Length: 201  Bit Score: 38.33  E-value: 7.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612127 204 ELQKRERFLLEREQLLFRHENALSK----IKGVEEEVLTRFQIIKEHDAEVEhltEVLKEKNKETKRLR--SSFDALKEL 277
Cdd:pfam12072  79 ELQRQERRLLQKEETLDRKDESLEKkeesLEKKEKELEAQQQQLEEKEEELE---ELIEEQRQELERISglTSEEAKEIL 155

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1034612127 278 NDTLKKQLN-EASEENRKIDIQAKRvQArlDNLQRKYEFMTIQR 320
Cdd:pfam12072 156 LDEVEEELRhEAAVMIKEIEEEAKE-EA--DKKAKEIIALAIQR 196
PRK12705 PRK12705
hypothetical protein; Provisional
 165-320 8.61e-03

hypothetical protein; Provisional


Pssm-ID: 237178 [Multi-domain]  Cd Length: 508  Bit Score: 39.31  E-value: 8.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612127 165 KASDKRSLLPHQISQIYDELFQIHLKLQCETAAQQKFAEELQKRERFLLEREQL------LFRHENALS----KIKGVEE 234
Cdd:PRK12705   26 KKRQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELqreeerLVQKEEQLDaraeKLDNLEN 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612127 235 EVLTRFQIIKEHDAEVEHLTEVLKEKNKETKRLRSsfdalKELNDTLKKQLNEASEENRKIDIQA--KRVQARLDNLQRK 312
Cdd:PRK12705  106 QLEEREKALSARELELEELEKQLDNELYRVAGLTP-----EQARKLLLKLLDAELEEEKAQRVKKieEEADLEAERKAQN 180


                  ....*...
gi 1034612127 313 YEFMTIQR 320
Cdd:PRK12705  181 ILAQAMQR 188
Atg16_CCD cd22887
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ...
 243-294 9.25e-03

Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family includes Saccharomyces cerevisiae Atg16 (also called cytoplasm to vacuole targeting protein 11, CVT11, or SAP18), human autophagy-related protein 16-1 (also called APG16-like 1, ATG16L1, or APG16L) and autophagy-related protein 16-2 (also called APG16-like 2, ATG16L2, WD repeat-containing protein 80 or WDR80), and similar proteins. Atg16 stabilizes the Atg5-Atg12 conjugate and mediates the formation of the 350 kDa complex, which is necessary for autophagy. The Atg5-Atg12/Atg16 complex is required for efficient promotion of Atg8-conjugation to phosphatidylethanolamine and Atg8 localization to the pre-autophagosomal structure (PAS). Similarly, human ATG16L1 plays an essential role in autophagy and acts as a molecular scaffold which mediates protein-protein interactions essential for autophagosome formation. ATG16L2, though structurally similar to ATG16L1 and able to form a complex with the autophagy proteins Atg5 and Atg12, is not essential for autophagy. Single-nucleotide polymorphisms in ATG16L1 is associated with an increased risk of developing Crohn disease. Saccharomyces cerevisiae Atg16 contains an N-terminal domain (NTD) that interacts with the Atg5-Atg12 protein conjugate and a coiled-coil domain (CCD) that dimerizes and mediates self-assembly. Human ATG16L1 and ATG16L2 also contains an N-terminal region that binds Atg5, a CCD homologous to the yeast CCD, and a WD40 domain that represents approximately 50% of the full-length protein. This model corresponds to the CCD of Atg16 family proteins.


Pssm-ID: 439196 [Multi-domain]  Cd Length: 91  Bit Score: 36.00  E-value: 9.25e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1034612127 243 IKEHDAEVEHLTEVLKEKNKETKRLRSSFDALKELNDTLKKQLNEASEENRK 294
Cdd:cd22887    20 LASLEEEIKDLEEELKEKNKANEILNDELIALQIENNLLEEKLRKLQEENDE 71
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
195-314 9.82e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 38.73  E-value: 9.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612127 195 TAAQQKFAEELQKRERFLLEREQLLFRHENALSKIKGVEEEVLTRFQIIKEHDAEVEHLTEVLKEKNKETKRLRSSFDAL 274
Cdd:COG4372    27 AALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESL 106

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1034612127 275 KELNDTLKKQLNEASEENRKIDIQAKRVQARLDNLQRKYE 314
Cdd:COG4372   107 QEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIA 146
 
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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