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Conserved domains on  [gi|2462592014|ref|XP_054203560|]
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coiled-coil domain-containing protein 14 isoform X9 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Atg16_CCD super family cl46300
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ...
49-552 0e+00

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.


The actual alignment was detected with superfamily member pfam15254:

Pssm-ID: 480640  Cd Length: 857  Bit Score: 929.21  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462592014  49 DSESQAETVHGLDGCASLLRDILRNEDSA-----------------------------------------SSDNKKQIPN 87
Cdd:pfam15254   1 DSESQTETIQGLDGCASLLRDILRNEDSGsetvysenrcnsrplegkrygskkkgpekhtppsvvqkeilSSSNKKQIPN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462592014  88 EASARSERDTSDLEQNWSLQDHYRMYSPIIYQALCEHVQTQMSLMNDLTSKNIPNGIPAVPCHAPSHSESQATPHSSYGL 167
Cdd:pfam15254  81 EASAGSERDASDIPQNWSLQDHYRMYSPIIYQALCEHVQTQMSLMNNLASKNSPNGIPAVPCHTVSGSESQATTASNYGL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462592014 168 CTSTPVWSLQRPPCPPKVHSEVQTDGNSQFASQGKTVSATCT-DVLRNSFNTSPGVPCSLPKTDISAIPTLQQLGLVNGI 246
Cdd:pfam15254 161 PTSTPVLSPQHPACPLVVHSEVQTDSDNQFASQGGTTSVNCTmDVPRNSFSASPGVPCSLPQTDAPAIPTFQQLSLANGI 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462592014 247 LPQQGIHKETDLLKCIQTYLSLFRSHGKEPHLDSQTHRSPTQSQPAFLATNEEKCAREQIREATSERKDLNIHVRDTKTV 326
Cdd:pfam15254 241 LPQQQQLKEADLLKCIQTHLSLLQSHEKDNHPDSQTCQSPTQLQPAFLATNEEKCAREQIEETTSEGKDLNLHVVDIKPV 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462592014 327 KDVQKAKNVNKTAEKVRIIKYLLGELKALVAEQEDSEIQRLITEMEACISVLPTVSGNTDIQVEIALAMQPLRSENAQLR 406
Cdd:pfam15254 321 KDVQKAKNVNQTAEKVRTVKYLLGELKALVADQEDSEVLRLITEVEACVSLLPAVSGNTNIQAEIALALQPLRSENAQLR 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462592014 407 RQLRILNQQLREQQKTQKPSGAVDCNLELFSLQSLNMSLQNQLEESLKSQELLQSKNEELLKVIENQKDENKKFSSIFKD 486
Cdd:pfam15254 401 RQLRILNQQLREQEKTEKTSGSGDCNLELFSLQSLNMSLQNQLQESLKSQELLQSKNEELLKVIENQKEENKKLTKIFKE 480
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462592014 487 KDQTILENKQQYDIEITRIKIELEEALVNVKSSQFKLETAEKENQILGITLRQRDAEVTRLRELTR 552
Cdd:pfam15254 481 KEQTLLENKQQFDIETTRVKIELEEALVNMKSFQFKLEAAEKENQILGITLRQRDAEVTRLRELTR 546
 
Name Accession Description Interval E-value
CCDC14 pfam15254
Coiled-coil domain-containing protein 14; This protein family, Coiled-coil domain-containing ...
49-552 0e+00

Coiled-coil domain-containing protein 14; This protein family, Coiled-coil domain-containing protein 14 (CCDC14) is a domain of unknown function. This family of proteins is found in eukaryotes. Proteins in this family are typically between 301 and 912 amino acids in length.


Pssm-ID: 464594  Cd Length: 857  Bit Score: 929.21  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462592014  49 DSESQAETVHGLDGCASLLRDILRNEDSA-----------------------------------------SSDNKKQIPN 87
Cdd:pfam15254   1 DSESQTETIQGLDGCASLLRDILRNEDSGsetvysenrcnsrplegkrygskkkgpekhtppsvvqkeilSSSNKKQIPN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462592014  88 EASARSERDTSDLEQNWSLQDHYRMYSPIIYQALCEHVQTQMSLMNDLTSKNIPNGIPAVPCHAPSHSESQATPHSSYGL 167
Cdd:pfam15254  81 EASAGSERDASDIPQNWSLQDHYRMYSPIIYQALCEHVQTQMSLMNNLASKNSPNGIPAVPCHTVSGSESQATTASNYGL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462592014 168 CTSTPVWSLQRPPCPPKVHSEVQTDGNSQFASQGKTVSATCT-DVLRNSFNTSPGVPCSLPKTDISAIPTLQQLGLVNGI 246
Cdd:pfam15254 161 PTSTPVLSPQHPACPLVVHSEVQTDSDNQFASQGGTTSVNCTmDVPRNSFSASPGVPCSLPQTDAPAIPTFQQLSLANGI 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462592014 247 LPQQGIHKETDLLKCIQTYLSLFRSHGKEPHLDSQTHRSPTQSQPAFLATNEEKCAREQIREATSERKDLNIHVRDTKTV 326
Cdd:pfam15254 241 LPQQQQLKEADLLKCIQTHLSLLQSHEKDNHPDSQTCQSPTQLQPAFLATNEEKCAREQIEETTSEGKDLNLHVVDIKPV 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462592014 327 KDVQKAKNVNKTAEKVRIIKYLLGELKALVAEQEDSEIQRLITEMEACISVLPTVSGNTDIQVEIALAMQPLRSENAQLR 406
Cdd:pfam15254 321 KDVQKAKNVNQTAEKVRTVKYLLGELKALVADQEDSEVLRLITEVEACVSLLPAVSGNTNIQAEIALALQPLRSENAQLR 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462592014 407 RQLRILNQQLREQQKTQKPSGAVDCNLELFSLQSLNMSLQNQLEESLKSQELLQSKNEELLKVIENQKDENKKFSSIFKD 486
Cdd:pfam15254 401 RQLRILNQQLREQEKTEKTSGSGDCNLELFSLQSLNMSLQNQLQESLKSQELLQSKNEELLKVIENQKEENKKLTKIFKE 480
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462592014 487 KDQTILENKQQYDIEITRIKIELEEALVNVKSSQFKLETAEKENQILGITLRQRDAEVTRLRELTR 552
Cdd:pfam15254 481 KEQTLLENKQQFDIETTRVKIELEEALVNMKSFQFKLEAAEKENQILGITLRQRDAEVTRLRELTR 546
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
292-552 9.64e-06

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 48.22  E-value: 9.64e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462592014 292 AFLATNEEKCAREQIREATSERKDLNIHVRdtktvkdvQKAKNVNKTAEKvriIKYLLGELKALvaEQEDSEIQRLITEM 371
Cdd:COG4942     8 ALLLALAAAAQADAAAEAEAELEQLQQEIA--------ELEKELAALKKE---EKALLKQLAAL--ERRIAALARRIRAL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462592014 372 EACISvlptvsgntDIQVEIALAMQPLRSENAQLRRQLRILNQQLREQQKtqkpSGAVDCNLELFSLQSLNmslqnqleE 451
Cdd:COG4942    75 EQELA---------ALEAELAELEKEIAELRAELEAQKEELAELLRALYR----LGRQPPLALLLSPEDFL--------D 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462592014 452 SLKSQELLQSKNEELLKVIENQKdenkkfssifkdKDQTILENKQQydiEITRIKIELEEALVNVKSSQFKLETAEKENQ 531
Cdd:COG4942   134 AVRRLQYLKYLAPARREQAEELR------------ADLAELAALRA---ELEAERAELEALLAELEEERAALEALKAERQ 198
                         250       260
                  ....*....|....*....|..
gi 2462592014 532 ILGITLRQR-DAEVTRLRELTR 552
Cdd:COG4942   199 KLLARLEKElAELAAELAELQQ 220
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
294-552 3.27e-05

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: 46.97  E-value: 3.27e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462592014  294 LATNEEKCAR--EQIREATSERKDLNIHVRD-TKTVKDVQKAKNvnktaEKVRIIKYLLGELKALVAEQEDSEIQRLITE 370
Cdd:TIGR02168  679 IEELEEKIEEleEKIAELEKALAELRKELEElEEELEQLRKELE-----ELSRQISALRKDLARLEAEVEQLEERIAQLS 753
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462592014  371 MEacisvlptvsgNTDIQVEIALAMQPLRSENAQLRRQLRILnQQLREQQKTQKpsgavdcnLELFSLQSLNMSLQNQLE 450
Cdd:TIGR02168  754 KE-----------LTELEAEIEELEERLEEAEEELAEAEAEI-EELEAQIEQLK--------EELKALREALDELRAELT 813
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462592014  451 ESLKSQELLQSKNEELLKVIENQKDENKKFSSIFKDKDQTILENKQQ---YDIEITRIKIELEEALVNVKSSQFKLETAE 527
Cdd:TIGR02168  814 LLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEieeLEELIEELESELEALLNERASLEEALALLR 893
                          250       260
                   ....*....|....*....|....*
gi 2462592014  528 KENQILGITLRQRDAEVTRLRELTR 552
Cdd:TIGR02168  894 SELEELSEELRELESKRSELRRELE 918
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
336-587 4.45e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.51  E-value: 4.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462592014 336 NKTAEKVRIIKYLLGELKALVAEQEDseIQRLITEMEACIsvlptvsgnTDIQVEIALamqpLRSENAQLRRQLRILNQQ 415
Cdd:PRK03918  165 KNLGEVIKEIKRRIERLEKFIKRTEN--IEELIKEKEKEL---------EEVLREINE----ISSELPELREELEKLEKE 229
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462592014 416 LREQQKTQkpsgavdcnlelfslqslnmSLQNQLEESLKSQELLQSKNEELLKVIENQKDENKKFSSIFKDKDQTI--LE 493
Cdd:PRK03918  230 VKELEELK--------------------EEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELkeLK 289
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462592014 494 NKQQYDIEITRIKIELEEALVNVkssqfKLETAEKENQILGITLRQRDAE--VTRLRELTRLFKTV--DLNVL------- 562
Cdd:PRK03918  290 EKAEEYIKLSEFYEEYLDELREI-----EKRLSRLEEEINGIEERIKELEekEERLEELKKKLKELekRLEELeerhely 364
                         250       260
                  ....*....|....*....|....*
gi 2462592014 563 QSLTQKPNTVHELRKSRTALNKEEV 587
Cdd:PRK03918  365 EEAKAKKEELERLKKRLTGLTPEKL 389
 
Name Accession Description Interval E-value
CCDC14 pfam15254
Coiled-coil domain-containing protein 14; This protein family, Coiled-coil domain-containing ...
49-552 0e+00

Coiled-coil domain-containing protein 14; This protein family, Coiled-coil domain-containing protein 14 (CCDC14) is a domain of unknown function. This family of proteins is found in eukaryotes. Proteins in this family are typically between 301 and 912 amino acids in length.


Pssm-ID: 464594  Cd Length: 857  Bit Score: 929.21  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462592014  49 DSESQAETVHGLDGCASLLRDILRNEDSA-----------------------------------------SSDNKKQIPN 87
Cdd:pfam15254   1 DSESQTETIQGLDGCASLLRDILRNEDSGsetvysenrcnsrplegkrygskkkgpekhtppsvvqkeilSSSNKKQIPN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462592014  88 EASARSERDTSDLEQNWSLQDHYRMYSPIIYQALCEHVQTQMSLMNDLTSKNIPNGIPAVPCHAPSHSESQATPHSSYGL 167
Cdd:pfam15254  81 EASAGSERDASDIPQNWSLQDHYRMYSPIIYQALCEHVQTQMSLMNNLASKNSPNGIPAVPCHTVSGSESQATTASNYGL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462592014 168 CTSTPVWSLQRPPCPPKVHSEVQTDGNSQFASQGKTVSATCT-DVLRNSFNTSPGVPCSLPKTDISAIPTLQQLGLVNGI 246
Cdd:pfam15254 161 PTSTPVLSPQHPACPLVVHSEVQTDSDNQFASQGGTTSVNCTmDVPRNSFSASPGVPCSLPQTDAPAIPTFQQLSLANGI 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462592014 247 LPQQGIHKETDLLKCIQTYLSLFRSHGKEPHLDSQTHRSPTQSQPAFLATNEEKCAREQIREATSERKDLNIHVRDTKTV 326
Cdd:pfam15254 241 LPQQQQLKEADLLKCIQTHLSLLQSHEKDNHPDSQTCQSPTQLQPAFLATNEEKCAREQIEETTSEGKDLNLHVVDIKPV 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462592014 327 KDVQKAKNVNKTAEKVRIIKYLLGELKALVAEQEDSEIQRLITEMEACISVLPTVSGNTDIQVEIALAMQPLRSENAQLR 406
Cdd:pfam15254 321 KDVQKAKNVNQTAEKVRTVKYLLGELKALVADQEDSEVLRLITEVEACVSLLPAVSGNTNIQAEIALALQPLRSENAQLR 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462592014 407 RQLRILNQQLREQQKTQKPSGAVDCNLELFSLQSLNMSLQNQLEESLKSQELLQSKNEELLKVIENQKDENKKFSSIFKD 486
Cdd:pfam15254 401 RQLRILNQQLREQEKTEKTSGSGDCNLELFSLQSLNMSLQNQLQESLKSQELLQSKNEELLKVIENQKEENKKLTKIFKE 480
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462592014 487 KDQTILENKQQYDIEITRIKIELEEALVNVKSSQFKLETAEKENQILGITLRQRDAEVTRLRELTR 552
Cdd:pfam15254 481 KEQTLLENKQQFDIETTRVKIELEEALVNMKSFQFKLEAAEKENQILGITLRQRDAEVTRLRELTR 546
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
292-552 9.64e-06

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 48.22  E-value: 9.64e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462592014 292 AFLATNEEKCAREQIREATSERKDLNIHVRdtktvkdvQKAKNVNKTAEKvriIKYLLGELKALvaEQEDSEIQRLITEM 371
Cdd:COG4942     8 ALLLALAAAAQADAAAEAEAELEQLQQEIA--------ELEKELAALKKE---EKALLKQLAAL--ERRIAALARRIRAL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462592014 372 EACISvlptvsgntDIQVEIALAMQPLRSENAQLRRQLRILNQQLREQQKtqkpSGAVDCNLELFSLQSLNmslqnqleE 451
Cdd:COG4942    75 EQELA---------ALEAELAELEKEIAELRAELEAQKEELAELLRALYR----LGRQPPLALLLSPEDFL--------D 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462592014 452 SLKSQELLQSKNEELLKVIENQKdenkkfssifkdKDQTILENKQQydiEITRIKIELEEALVNVKSSQFKLETAEKENQ 531
Cdd:COG4942   134 AVRRLQYLKYLAPARREQAEELR------------ADLAELAALRA---ELEAERAELEALLAELEEERAALEALKAERQ 198
                         250       260
                  ....*....|....*....|..
gi 2462592014 532 ILGITLRQR-DAEVTRLRELTR 552
Cdd:COG4942   199 KLLARLEKElAELAAELAELQQ 220
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
294-552 3.27e-05

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: 46.97  E-value: 3.27e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462592014  294 LATNEEKCAR--EQIREATSERKDLNIHVRD-TKTVKDVQKAKNvnktaEKVRIIKYLLGELKALVAEQEDSEIQRLITE 370
Cdd:TIGR02168  679 IEELEEKIEEleEKIAELEKALAELRKELEElEEELEQLRKELE-----ELSRQISALRKDLARLEAEVEQLEERIAQLS 753
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462592014  371 MEacisvlptvsgNTDIQVEIALAMQPLRSENAQLRRQLRILnQQLREQQKTQKpsgavdcnLELFSLQSLNMSLQNQLE 450
Cdd:TIGR02168  754 KE-----------LTELEAEIEELEERLEEAEEELAEAEAEI-EELEAQIEQLK--------EELKALREALDELRAELT 813
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462592014  451 ESLKSQELLQSKNEELLKVIENQKDENKKFSSIFKDKDQTILENKQQ---YDIEITRIKIELEEALVNVKSSQFKLETAE 527
Cdd:TIGR02168  814 LLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEieeLEELIEELESELEALLNERASLEEALALLR 893
                          250       260
                   ....*....|....*....|....*
gi 2462592014  528 KENQILGITLRQRDAEVTRLRELTR 552
Cdd:TIGR02168  894 SELEELSEELRELESKRSELRRELE 918
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
336-587 4.45e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.51  E-value: 4.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462592014 336 NKTAEKVRIIKYLLGELKALVAEQEDseIQRLITEMEACIsvlptvsgnTDIQVEIALamqpLRSENAQLRRQLRILNQQ 415
Cdd:PRK03918  165 KNLGEVIKEIKRRIERLEKFIKRTEN--IEELIKEKEKEL---------EEVLREINE----ISSELPELREELEKLEKE 229
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462592014 416 LREQQKTQkpsgavdcnlelfslqslnmSLQNQLEESLKSQELLQSKNEELLKVIENQKDENKKFSSIFKDKDQTI--LE 493
Cdd:PRK03918  230 VKELEELK--------------------EEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELkeLK 289
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462592014 494 NKQQYDIEITRIKIELEEALVNVkssqfKLETAEKENQILGITLRQRDAE--VTRLRELTRLFKTV--DLNVL------- 562
Cdd:PRK03918  290 EKAEEYIKLSEFYEEYLDELREI-----EKRLSRLEEEINGIEERIKELEekEERLEELKKKLKELekRLEELeerhely 364
                         250       260
                  ....*....|....*....|....*
gi 2462592014 563 QSLTQKPNTVHELRKSRTALNKEEV 587
Cdd:PRK03918  365 EEAKAKKEELERLKKRLTGLTPEKL 389
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
395-590 1.41e-03

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 41.54  E-value: 1.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462592014 395 MQPLRSENAQLRRQLRILNQQLREQQK--TQKPSGAVDCNLELFSLQSLNMSLQNQLEESLKSQELLQSKNEELLKVIEN 472
Cdd:TIGR04523 309 NKELKSELKNQEKKLEEIQNQISQNNKiiSQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKN 388
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462592014 473 QK----------DENKKFSSIFKDKDQTILENKQQYDIEITRIKIELEEAlvNVKSSQFKLETAEKENQI--LGITlrqR 540
Cdd:TIGR04523 389 LEsqindleskiQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKN--NSEIKDLTNQDSVKELIIknLDNT---R 463
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2462592014 541 DAEVTRLRELTRLFKTVDLN---VLQSLTQKPNTVHELRKSRTALnKEEVGDL 590
Cdd:TIGR04523 464 ESLETQLKVLSRSINKIKQNleqKQKELKSKEKELKKLNEEKKEL-EEKVKDL 515
HAUS-augmin3 pfam14932
HAUS augmin-like complex subunit 3; This domain is subunit three of the augmin complex found ...
381-492 1.53e-03

HAUS augmin-like complex subunit 3; This domain is subunit three of the augmin complex found from Drosophila to humans. The HAUS-augmin complex is made up of eight subunits. The augmin complex interacts with gamma-TuRC, and attenuation of this interaction severely impairs spindle MT generation. Furthermore, we provide evidence that human augmin plays critical and non-redundant roles in the kinetochore-MT attachment and also central spindle formation during anaphase in human cells.The HAUS complex is required for mitotic spindle assembly and for maintenance of centrosome integrity.


Pssm-ID: 464384 [Multi-domain]  Cd Length: 261  Bit Score: 40.76  E-value: 1.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462592014 381 VSGNTDIQVEIALAMQPLRSENAQLRRQLRILNQQLREQQktqkpSGAVDCNLELFSLQSLNMSLQNQLEEslkSQELLQ 460
Cdd:pfam14932  69 VEALEESLEEIREATEDLEAELQELQKTKQLKINRLNKLQ-----AQASSLSQGLRALVAEEEEAAKQLEE---LQEELA 140
                          90       100       110
                  ....*....|....*....|....*....|..
gi 2462592014 461 SKNEELLKVIENQKDENKKFSSIFKDKDQTIL 492
Cdd:pfam14932 141 ALNAKTNNVLQSLQSEVKELASFFSASEPPVF 172
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
334-584 1.83e-03

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


Pssm-ID: 130673 [Multi-domain]  Cd Length: 2757  Bit Score: 41.58  E-value: 1.83e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462592014  334 NVNKTAEKVRIIKYLLGELK---ALVAEQEDSEIQRLITEMeacISVLPTVSGNTDIQ---VEIALAMQPLRSENAQLRR 407
Cdd:TIGR01612 1538 KFAKTKKDSEIIIKEIKDAHkkfILEAEKSEQKIKEIKKEK---FRIEDDAAKNDKSNkaaIDIQLSLENFENKFLKISD 1614
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462592014  408 QLRILNQQLREQQKTQKpsgavdcNLELFSLQSLNMSLQNQLEESLKSQELLQS-KNEEllKVIENQKDE----NKKFSS 482
Cdd:TIGR01612 1615 IKKKINDCLKETESIEK-------KISSFSIDSQDTELKENGDNLNSLQEFLESlKDQK--KNIEDKKKEldelDSEIEK 1685
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462592014  483 IFKDKDQtileNKQQYDIEITRI--------KIELEEALVNVKSSQFKLETAEKENQILGI----TLRQRDAEVTRL-RE 549
Cdd:TIGR01612 1686 IEIDVDQ----HKKNYEIGIIEKikeiaianKEEIESIKELIEPTIENLISSFNTNDLEGIdpneKLEEYNTEIGDIyEE 1761
                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 2462592014  550 LTRLFKTVdLNVLQSLTQKPNTVHELRKSR-TALNK 584
Cdd:TIGR01612 1762 FIELYNII-AGCLETVSKEPITYDEIKNTRiNAQNE 1796
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
445-589 2.05e-03

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 41.03  E-value: 2.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462592014 445 LQNQLEESLKSQELLQSKNEELLKVIENQKDENKKfssifkdkdqtileNKQQYDIEITRIK---IELEEALVNVKSSQF 521
Cdd:pfam07888  32 LQNRLEECLQERAELLQAQEAANRQREKEKERYKR--------------DREQWERQRRELEsrvAELKEELRQSREKHE 97
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462592014 522 KLETAEKENQILG--------ITLRQRDAEVTRLRELTRLFKTVDLNVLQSLTQKpNTVHELRKSRTALNKEEVGD 589
Cdd:pfam07888  98 ELEEKYKELSASSeelseekdALLAQRAAHEARIRELEEDIKTLTQRVLERETEL-ERMKERAKKAGAQRKEEEAE 172
PRK10929 PRK10929
putative mechanosensitive channel protein; Provisional
329-552 2.26e-03

putative mechanosensitive channel protein; Provisional


Pssm-ID: 236798 [Multi-domain]  Cd Length: 1109  Bit Score: 41.19  E-value: 2.26e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462592014  329 VQKAKNVNKTAEKVRIIKYLLGELKalvaeQEDSEIQRLITEMEACISVLPTVSG------NTDIQVEIA--------LA 394
Cdd:PRK10929   119 LEKSRQAQQEQDRAREISDSLSQLP-----QQQTEARRQLNEIERRLQTLGTPNTplaqaqLTALQAESAalkalvdeLE 193
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462592014  395 MQPLRSENAQLRRQLRILNQQLREQQKtqkpsgavdcNLELFSLQS-LNMSLQNQLEESLKSQELLQSKNEELLKVIENQ 473
Cdd:PRK10929   194 LAQLSANNRQELARLRSELAKKRSQQL----------DAYLQALRNqLNSQRQREAERALESTELLAEQSGDLPKSIVAQ 263
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462592014  474 KDENKKFSSIFKDKDQTI-LENKQQYdiEITRIKIELEEALVNVKssqfklETAE--KENQILGITLRqrdAEVTRLREL 550
Cdd:PRK10929   264 FKINRELSQALNQQAQRMdLIASQQR--QAASQTLQVRQALNTLR------EQSQwlGVSNALGEALR---AQVARLPEM 332

                   ..
gi 2462592014  551 TR 552
Cdd:PRK10929   333 PK 334
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
305-553 3.58e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.31  E-value: 3.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462592014 305 QIREATSERKDLNIHVRDTKTVKDVQKAKNVNKTAEKVRIikyllgELKALVAEQEDSEIQRLITEMEACISvlptvsgn 384
Cdd:COG1196   233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEEL------RLELEELELELEEAQAEEYELLAELA-------- 298
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462592014 385 tdiqvEIALAMQPLRSENAQLRRQLRILNQQLREQQKTQKpsgavdcnlelfslqslnmSLQNQLEESLKSQELLQSKNE 464
Cdd:COG1196   299 -----RLEQDIARLEERRRELEERLEELEEELAELEEELE-------------------ELEEELEELEEELEEAEEELE 354
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462592014 465 ELLKVIENQKDENKKFSSIFKDKDQTILENKQQYdIEITRIKIELEEALVNVKSSQFKLETAEKENQILGITLRQRDAEV 544
Cdd:COG1196   355 EAEAELAEAEEALLEAEAELAEAEEELEELAEEL-LEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAEL 433

                  ....*....
gi 2462592014 545 TRLRELTRL 553
Cdd:COG1196   434 EEEEEEEEE 442
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
337-548 6.01e-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: 39.65  E-value: 6.01e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462592014  337 KTAEKVRIIK---------YLLGELKALVAEQEdsEIQRLITEMEacisvlptvsgntDIQVEIALAMQPLRSENAQLRR 407
Cdd:TIGR02168  210 EKAERYKELKaelrelelaLLVLRLEELREELE--ELQEELKEAE-------------EELEELTAELQELEEKLEELRL 274
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462592014  408 QLRILNQQLREQQKtqkpsgavdcnlELFSLQSLNMSLQNQLEESLKSQELLQSKNEELLKVIEnqKDENKkfssifKDK 487
Cdd:TIGR02168  275 EVSELEEEIEELQK------------ELYALANEISRLEQQKQILRERLANLERQLEELEAQLE--ELESK------LDE 334
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462592014  488 DQTILenkqqydieiTRIKIELEEALVNVKSSQFKLETAEKENQILGITLRQRDAEVTRLR 548
Cdd:TIGR02168  335 LAEEL----------AELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLR 385
 
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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