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Conserved domains on  [gi|39725957|ref|NP_945319|]
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cilium assembly protein DZIP1 isoform 2 [Homo sapiens]

Protein Classification

ATP-binding protein; MDR family MFS transporter( domain architecture ID 13845362)

ATP-binding protein containing an AAA (ATPases Associated with various cellular Activities) domain, may function as the toxin for a type IV toxin-antitoxin resistance system| MDR (multi-drug resistance) family major facilitator superfamily (MFS) transporter confers resistance to specific drugs/toxins through their active efflux from the cell

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Dzip-like_N pfam13815
Iguana/Dzip1-like DAZ-interacting protein N-terminal; The DAZ gene-product - Deleted in ...
58-178 6.48e-47

Iguana/Dzip1-like DAZ-interacting protein N-terminal; The DAZ gene-product - Deleted in Azoospermia - and a closely related sequence are required early in germ-cell development in order to maintain germ-cell populations. This family is the N-terminal region that is the only part of the protein in some fungi and lower metazoa.


:

Pssm-ID: 433498 [Multi-domain]  Cd Length: 118  Bit Score: 162.88  E-value: 6.48e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39725957    58 FQFRPRLESVDWRRLSAIDVDKVAGAVDVLTLQENIMNITFCKLEDEKCPHcqsGVDPVLLKLIRLAQFTIEYLLHSQEF 137
Cdd:pfam13815   1 FQFRPRSERLDWRKLASVDVDRVARDTDVDTLQRNIENITFCNLTREEAPH---FVDPHFLKLFRLAQLTIEYLLHSQEC 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 39725957   138 LTSQLHTLEERLRLSHCDGEQSKKLLTKQAGEIKTLKEECK 178
Cdd:pfam13815  78 LATILVKLEERLQEAQQRAEELEKELGRLEEELKKLKKESR 118
PRK03918 super family cl35229
DNA double-strand break repair ATPase Rad50;
144-440 1.99e-04

DNA double-strand break repair ATPase Rad50;


The actual alignment was detected with superfamily member PRK03918:

Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 45.05  E-value: 1.99e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39725957  144 TLEERLRLSHCDGEQSKK---LLTKQAGEIKTLKEECKRRKKMISTQQLMIEAKANyyqchfCDKAFMNQAFLQSHIQRR 220
Cdd:PRK03918 256 KLEEKIRELEERIEELKKeieELEEKVKELKELKEKAEEYIKLSEFYEEYLDELRE------IEKRLSRLEEEINGIEER 329
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39725957  221 HTEENShfeyqKNAQIEKLRSEIVVLKEELqltrSELEAAHhasavrfsKEYEMQKTKEEDFLKLFDRWKEEEKEKLV-- 298
Cdd:PRK03918 330 IKELEE-----KEERLEELKKKLKELEKRL----EELEERH--------ELYEEAKAKKEELERLKKRLTGLTPEKLEke 392
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39725957  299 -DEMEKVKEMFMKEFKELTSKNSALEYQLSEIQKSNMQIKSNIGT------LKDAHEFKEDRSPYPQDFHNV---MQLLD 368
Cdd:PRK03918 393 lEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKcpvcgrELTEEHRKELLEEYTAELKRIekeLKEIE 472
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 39725957  369 SQESKWTARVQAIHQEHKKEkgRLLSHIEKLRTSMIDDLNASNVFYKKRIEELGQRLQEQNELIITQRQQIK 440
Cdd:PRK03918 473 EKERKLRKELRELEKVLKKE--SELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIK 542
 
Name Accession Description Interval E-value
Dzip-like_N pfam13815
Iguana/Dzip1-like DAZ-interacting protein N-terminal; The DAZ gene-product - Deleted in ...
58-178 6.48e-47

Iguana/Dzip1-like DAZ-interacting protein N-terminal; The DAZ gene-product - Deleted in Azoospermia - and a closely related sequence are required early in germ-cell development in order to maintain germ-cell populations. This family is the N-terminal region that is the only part of the protein in some fungi and lower metazoa.


Pssm-ID: 433498 [Multi-domain]  Cd Length: 118  Bit Score: 162.88  E-value: 6.48e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39725957    58 FQFRPRLESVDWRRLSAIDVDKVAGAVDVLTLQENIMNITFCKLEDEKCPHcqsGVDPVLLKLIRLAQFTIEYLLHSQEF 137
Cdd:pfam13815   1 FQFRPRSERLDWRKLASVDVDRVARDTDVDTLQRNIENITFCNLTREEAPH---FVDPHFLKLFRLAQLTIEYLLHSQEC 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 39725957   138 LTSQLHTLEERLRLSHCDGEQSKKLLTKQAGEIKTLKEECK 178
Cdd:pfam13815  78 LATILVKLEERLQEAQQRAEELEKELGRLEEELKKLKKESR 118
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
144-440 1.99e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 45.05  E-value: 1.99e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39725957  144 TLEERLRLSHCDGEQSKK---LLTKQAGEIKTLKEECKRRKKMISTQQLMIEAKANyyqchfCDKAFMNQAFLQSHIQRR 220
Cdd:PRK03918 256 KLEEKIRELEERIEELKKeieELEEKVKELKELKEKAEEYIKLSEFYEEYLDELRE------IEKRLSRLEEEINGIEER 329
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39725957  221 HTEENShfeyqKNAQIEKLRSEIVVLKEELqltrSELEAAHhasavrfsKEYEMQKTKEEDFLKLFDRWKEEEKEKLV-- 298
Cdd:PRK03918 330 IKELEE-----KEERLEELKKKLKELEKRL----EELEERH--------ELYEEAKAKKEELERLKKRLTGLTPEKLEke 392
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39725957  299 -DEMEKVKEMFMKEFKELTSKNSALEYQLSEIQKSNMQIKSNIGT------LKDAHEFKEDRSPYPQDFHNV---MQLLD 368
Cdd:PRK03918 393 lEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKcpvcgrELTEEHRKELLEEYTAELKRIekeLKEIE 472
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 39725957  369 SQESKWTARVQAIHQEHKKEkgRLLSHIEKLRTSMIDDLNASNVFYKKRIEELGQRLQEQNELIITQRQQIK 440
Cdd:PRK03918 473 EKERKLRKELRELEKVLKKE--SELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIK 542
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
224-443 1.41e-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: 1.41e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39725957    224 ENSHFEYQKNaqIEKLRSEIVVLKEELQLTRSELEAAHHAsavrfskeyemQKTKEEDFLKLfdRWKEEEKEKLVDEMEK 303
Cdd:TIGR02168  669 NSSILERRRE--IEELEEKIEELEEKIAELEKALAELRKE-----------LEELEEELEQL--RKELEELSRQISALRK 733
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39725957    304 VKEMFMKEFKELTSKNSALEYQLSEIQKSNMQIKSNIGTLKDA-HEFKEDRSPYPQDFHNVMQLLDSQESKWTArVQAIH 382
Cdd:TIGR02168  734 DLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEElAEAEAEIEELEAQIEQLKEELKALREALDE-LRAEL 812
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 39725957    383 QEHKKEKGRLLSHIEKLRTSMIDdlnasnvfYKKRIEELGQRLQEQNELIITQRQQIKDFT 443
Cdd:TIGR02168  813 TLLNEEAANLRERLESLERRIAA--------TERRLEDLEEQIEELSEDIESLAAEIEELE 865
COG5022 COG5022
Myosin heavy chain [General function prediction only];
178-431 5.58e-03

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 40.45  E-value: 5.58e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39725957  178 KRRKKMISTQQLMieaKANYYQCHFCDKAFMNQAFlqsHIQRRHTEENSHFEY-QKNAQIEKLRSEIV---VLKEELQLT 253
Cdd:COG5022  766 QALKRIKKIQVIQ---HGFRLRRLVDYELKWRLFI---KLQPLLSLLGSRKEYrSYLACIIKLQKTIKrekKLRETEEVE 839
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39725957  254 RSELEAAHHASAVRFSKEYEMQKTKEEDFLKLFDRWKEEEKEK-LVDEMEKVKEmfmkeFKELTSKNSALEYQLSEI--- 329
Cdd:COG5022  840 FSLKAEVLIQKFGRSLKAKKRFSLLKKETIYLQSAQRVELAERqLQELKIDVKS-----ISSLKLVNLELESEIIELkks 914
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39725957  330 QKSNMQIKSnigtlkdahEFKEDRSPYPQDFHNVMQLLDSQEskwtarvqaIHQEHKKEKGRLLSHIEKLRTS------M 403
Cdd:COG5022  915 LSSDLIENL---------EFKTELIARLKKLLNNIDLEEGPS---------IEYVKLPELNKLHEVESKLKETseeyedL 976
                        250       260
                 ....*....|....*....|....*...
gi 39725957  404 IDDLNASNVFYKKRIEELGQRLQEQNEL 431
Cdd:COG5022  977 LKKSTILVREGNKANSELKNFKKELAEL 1004
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
198-221 8.60e-03

Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity site for Sp1 binding to the wt1 promoter.


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 34.58  E-value: 8.60e-03
                          10        20
                  ....*....|....*....|....
gi 39725957   198 YQCHFCDKAFMNQAFLQSHIqRRH 221
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHL-RTH 23
 
Name Accession Description Interval E-value
Dzip-like_N pfam13815
Iguana/Dzip1-like DAZ-interacting protein N-terminal; The DAZ gene-product - Deleted in ...
58-178 6.48e-47

Iguana/Dzip1-like DAZ-interacting protein N-terminal; The DAZ gene-product - Deleted in Azoospermia - and a closely related sequence are required early in germ-cell development in order to maintain germ-cell populations. This family is the N-terminal region that is the only part of the protein in some fungi and lower metazoa.


Pssm-ID: 433498 [Multi-domain]  Cd Length: 118  Bit Score: 162.88  E-value: 6.48e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39725957    58 FQFRPRLESVDWRRLSAIDVDKVAGAVDVLTLQENIMNITFCKLEDEKCPHcqsGVDPVLLKLIRLAQFTIEYLLHSQEF 137
Cdd:pfam13815   1 FQFRPRSERLDWRKLASVDVDRVARDTDVDTLQRNIENITFCNLTREEAPH---FVDPHFLKLFRLAQLTIEYLLHSQEC 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 39725957   138 LTSQLHTLEERLRLSHCDGEQSKKLLTKQAGEIKTLKEECK 178
Cdd:pfam13815  78 LATILVKLEERLQEAQQRAEELEKELGRLEEELKKLKKESR 118
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
144-440 1.99e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 45.05  E-value: 1.99e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39725957  144 TLEERLRLSHCDGEQSKK---LLTKQAGEIKTLKEECKRRKKMISTQQLMIEAKANyyqchfCDKAFMNQAFLQSHIQRR 220
Cdd:PRK03918 256 KLEEKIRELEERIEELKKeieELEEKVKELKELKEKAEEYIKLSEFYEEYLDELRE------IEKRLSRLEEEINGIEER 329
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39725957  221 HTEENShfeyqKNAQIEKLRSEIVVLKEELqltrSELEAAHhasavrfsKEYEMQKTKEEDFLKLFDRWKEEEKEKLV-- 298
Cdd:PRK03918 330 IKELEE-----KEERLEELKKKLKELEKRL----EELEERH--------ELYEEAKAKKEELERLKKRLTGLTPEKLEke 392
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39725957  299 -DEMEKVKEMFMKEFKELTSKNSALEYQLSEIQKSNMQIKSNIGT------LKDAHEFKEDRSPYPQDFHNV---MQLLD 368
Cdd:PRK03918 393 lEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKcpvcgrELTEEHRKELLEEYTAELKRIekeLKEIE 472
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 39725957  369 SQESKWTARVQAIHQEHKKEkgRLLSHIEKLRTSMIDDLNASNVFYKKRIEELGQRLQEQNELIITQRQQIK 440
Cdd:PRK03918 473 EKERKLRKELRELEKVLKKE--SELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIK 542
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
224-443 1.41e-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: 1.41e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39725957    224 ENSHFEYQKNaqIEKLRSEIVVLKEELQLTRSELEAAHHAsavrfskeyemQKTKEEDFLKLfdRWKEEEKEKLVDEMEK 303
Cdd:TIGR02168  669 NSSILERRRE--IEELEEKIEELEEKIAELEKALAELRKE-----------LEELEEELEQL--RKELEELSRQISALRK 733
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39725957    304 VKEMFMKEFKELTSKNSALEYQLSEIQKSNMQIKSNIGTLKDA-HEFKEDRSPYPQDFHNVMQLLDSQESKWTArVQAIH 382
Cdd:TIGR02168  734 DLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEElAEAEAEIEELEAQIEQLKEELKALREALDE-LRAEL 812
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 39725957    383 QEHKKEKGRLLSHIEKLRTSMIDdlnasnvfYKKRIEELGQRLQEQNELIITQRQQIKDFT 443
Cdd:TIGR02168  813 TLLNEEAANLRERLESLERRIAA--------TERRLEDLEEQIEELSEDIESLAAEIEELE 865
COG5022 COG5022
Myosin heavy chain [General function prediction only];
178-431 5.58e-03

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 40.45  E-value: 5.58e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39725957  178 KRRKKMISTQQLMieaKANYYQCHFCDKAFMNQAFlqsHIQRRHTEENSHFEY-QKNAQIEKLRSEIV---VLKEELQLT 253
Cdd:COG5022  766 QALKRIKKIQVIQ---HGFRLRRLVDYELKWRLFI---KLQPLLSLLGSRKEYrSYLACIIKLQKTIKrekKLRETEEVE 839
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39725957  254 RSELEAAHHASAVRFSKEYEMQKTKEEDFLKLFDRWKEEEKEK-LVDEMEKVKEmfmkeFKELTSKNSALEYQLSEI--- 329
Cdd:COG5022  840 FSLKAEVLIQKFGRSLKAKKRFSLLKKETIYLQSAQRVELAERqLQELKIDVKS-----ISSLKLVNLELESEIIELkks 914
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39725957  330 QKSNMQIKSnigtlkdahEFKEDRSPYPQDFHNVMQLLDSQEskwtarvqaIHQEHKKEKGRLLSHIEKLRTS------M 403
Cdd:COG5022  915 LSSDLIENL---------EFKTELIARLKKLLNNIDLEEGPS---------IEYVKLPELNKLHEVESKLKETseeyedL 976
                        250       260
                 ....*....|....*....|....*...
gi 39725957  404 IDDLNASNVFYKKRIEELGQRLQEQNEL 431
Cdd:COG5022  977 LKKSTILVREGNKANSELKNFKKELAEL 1004
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
198-221 8.60e-03

Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity site for Sp1 binding to the wt1 promoter.


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 34.58  E-value: 8.60e-03
                          10        20
                  ....*....|....*....|....
gi 39725957   198 YQCHFCDKAFMNQAFLQSHIqRRH 221
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHL-RTH 23
 
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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