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Conserved domains on  [gi|1002234312|ref|XP_015621368|]
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protein Hook homolog 3 isoform X2 [Oryza sativa Japonica Group]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK05771 super family cl35381
V-type ATP synthase subunit I; Validated
303-595 3.90e-05

V-type ATP synthase subunit I; Validated


The actual alignment was detected with superfamily member PRK05771:

Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 46.84  E-value: 3.90e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002234312 303 SQKVDKLKvlatSLSNSSSKAEKRILDHRRQKEEALnfRAKKENEVSAVEKEltaeISELEKQRDELEARLKkvniSLNA 382
Cdd:PRK05771   56 SEALDKLR----SYLPKLNPLREEKKKVSVKSLEEL--IKDVEEELEKIEKE----IKELEEEISELENEIK----ELEQ 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002234312 383 AIGRLKqtreerdqfdeannqmifSLKAKDNELSKSITSCNVEAGVVKTWINFLEDTWQLQSSYNEQKEKRTND------ 456
Cdd:PRK05771  122 EIERLE------------------PWGNFDLDLSLLLGFKYVSVFVGTVPEDKLEELKLESDVENVEYISTDKGyvyvvv 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002234312 457 ------------ELERCtdNFLKLTKYHLSTFKEILSPSIERICTyvdnlavLQSRDVSTEHDNEELSEKTSPQKSLEEE 524
Cdd:PRK05771  184 vvlkelsdeveeELKKL--GFERLELEEEGTPSELIREIKEELEE-------IEKERESLLEELKELAKKYLEELLALYE 254
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002234312 525 YLETEK---KIVIAFSITDHmkkLFYSEQGVnsrrDDEDVRNLFSEIEKLRERFESVERptLDIEVRRAKVPTK 595
Cdd:PRK05771  255 YLEIELeraEALSKFLKTDK---TFAIEGWV----PEDRVKKLKELIDKATGGSAYVEF--VEPDEEEEEVPTK 319
COG4913 super family cl25907
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
230-374 8.51e-03

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


The actual alignment was detected with superfamily member COG4913:

Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.51  E-value: 8.51e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002234312  230 DAEAVELWKKLNEKETSRVQQTQEDHAKTTERTSATT--VESFKEALSEVRFcSRMEELllKKKTSTAGDSLEIRSQKVD 307
Cdd:COG4913    286 AQRRLELLEAELEELRAELARLEAELERLEARLDALReeLDELEAQIRGNGG-DRLEQL--EREIERLERELEERERRRA 362
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002234312  308 KLKVLATSLSNSSSKAEKRILDHRRQKEEALNFRAKKENEVSAVEKELTAEISELEKQRDELEARLK 374
Cdd:COG4913    363 RLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIA 429
 
Name Accession Description Interval E-value
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
303-595 3.90e-05

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 46.84  E-value: 3.90e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002234312 303 SQKVDKLKvlatSLSNSSSKAEKRILDHRRQKEEALnfRAKKENEVSAVEKEltaeISELEKQRDELEARLKkvniSLNA 382
Cdd:PRK05771   56 SEALDKLR----SYLPKLNPLREEKKKVSVKSLEEL--IKDVEEELEKIEKE----IKELEEEISELENEIK----ELEQ 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002234312 383 AIGRLKqtreerdqfdeannqmifSLKAKDNELSKSITSCNVEAGVVKTWINFLEDTWQLQSSYNEQKEKRTND------ 456
Cdd:PRK05771  122 EIERLE------------------PWGNFDLDLSLLLGFKYVSVFVGTVPEDKLEELKLESDVENVEYISTDKGyvyvvv 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002234312 457 ------------ELERCtdNFLKLTKYHLSTFKEILSPSIERICTyvdnlavLQSRDVSTEHDNEELSEKTSPQKSLEEE 524
Cdd:PRK05771  184 vvlkelsdeveeELKKL--GFERLELEEEGTPSELIREIKEELEE-------IEKERESLLEELKELAKKYLEELLALYE 254
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002234312 525 YLETEK---KIVIAFSITDHmkkLFYSEQGVnsrrDDEDVRNLFSEIEKLRERFESVERptLDIEVRRAKVPTK 595
Cdd:PRK05771  255 YLEIELeraEALSKFLKTDK---TFAIEGWV----PEDRVKKLKELIDKATGGSAYVEF--VEPDEEEEEVPTK 319
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
288-666 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 1002234312  288 LKKKTSTAGDSLEIRSQKVDKLKVLATSLSNSSSKAEKRILDHRRQKEEALNFRAKKENEVSAVEKELTAEISELEKQRD 367
Cdd:TIGR02168  682 LEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEA 761
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002234312  368 ELEARLKKVNiSLNAAIGRLKQTREERDQFDEANNQMIFSLKAKDNELSKSITSCNVEAGVVKTWINFLEDTWQLQSSYN 447
Cdd:TIGR02168  762 EIEELEERLE-EAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRL 840
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002234312  448 EQKEKRTNDELERctdnflkltkyhlstfKEILSPSIERictYVDNLAVLQSRdvsTEHDNEELSEKTSPQKSLEEEYLE 527
Cdd:TIGR02168  841 EDLEEQIEELSED----------------IESLAAEIEE---LEELIEELESE---LEALLNERASLEEALALLRSELEE 898
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002234312  528 TEKKIviafsitdhmkklfyseqgvnsRRDDEDVRNLFSEIEKLRERFESVERPTLDIEVRRAKVPTKERAESSPSpvqv 607
Cdd:TIGR02168  899 LSEEL----------------------RELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLT---- 952
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002234312  608 pstpkaETVVSPKSPAKPDQPLDLDSELAKLEL---EFGQVNKYSPEeisgwEFDELEEELR 666
Cdd:TIGR02168  953 ------LEEAEALENKIEDDEEEARRRLKRLENkikELGPVNLAAIE-----EYEELKERYD 1003
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
230-374 8.51e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.51  E-value: 8.51e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002234312  230 DAEAVELWKKLNEKETSRVQQTQEDHAKTTERTSATT--VESFKEALSEVRFcSRMEELllKKKTSTAGDSLEIRSQKVD 307
Cdd:COG4913    286 AQRRLELLEAELEELRAELARLEAELERLEARLDALReeLDELEAQIRGNGG-DRLEQL--EREIERLERELEERERRRA 362
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002234312  308 KLKVLATSLSNSSSKAEKRILDHRRQKEEALNFRAKKENEVSAVEKELTAEISELEKQRDELEARLK 374
Cdd:COG4913    363 RLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIA 429
 
Name Accession Description Interval E-value
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
303-595 3.90e-05

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 46.84  E-value: 3.90e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002234312 303 SQKVDKLKvlatSLSNSSSKAEKRILDHRRQKEEALnfRAKKENEVSAVEKEltaeISELEKQRDELEARLKkvniSLNA 382
Cdd:PRK05771   56 SEALDKLR----SYLPKLNPLREEKKKVSVKSLEEL--IKDVEEELEKIEKE----IKELEEEISELENEIK----ELEQ 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002234312 383 AIGRLKqtreerdqfdeannqmifSLKAKDNELSKSITSCNVEAGVVKTWINFLEDTWQLQSSYNEQKEKRTND------ 456
Cdd:PRK05771  122 EIERLE------------------PWGNFDLDLSLLLGFKYVSVFVGTVPEDKLEELKLESDVENVEYISTDKGyvyvvv 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002234312 457 ------------ELERCtdNFLKLTKYHLSTFKEILSPSIERICTyvdnlavLQSRDVSTEHDNEELSEKTSPQKSLEEE 524
Cdd:PRK05771  184 vvlkelsdeveeELKKL--GFERLELEEEGTPSELIREIKEELEE-------IEKERESLLEELKELAKKYLEELLALYE 254
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002234312 525 YLETEK---KIVIAFSITDHmkkLFYSEQGVnsrrDDEDVRNLFSEIEKLRERFESVERptLDIEVRRAKVPTK 595
Cdd:PRK05771  255 YLEIELeraEALSKFLKTDK---TFAIEGWV----PEDRVKKLKELIDKATGGSAYVEF--VEPDEEEEEVPTK 319
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
288-666 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 1002234312  288 LKKKTSTAGDSLEIRSQKVDKLKVLATSLSNSSSKAEKRILDHRRQKEEALNFRAKKENEVSAVEKELTAEISELEKQRD 367
Cdd:TIGR02168  682 LEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEA 761
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002234312  368 ELEARLKKVNiSLNAAIGRLKQTREERDQFDEANNQMIFSLKAKDNELSKSITSCNVEAGVVKTWINFLEDTWQLQSSYN 447
Cdd:TIGR02168  762 EIEELEERLE-EAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRL 840
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002234312  448 EQKEKRTNDELERctdnflkltkyhlstfKEILSPSIERictYVDNLAVLQSRdvsTEHDNEELSEKTSPQKSLEEEYLE 527
Cdd:TIGR02168  841 EDLEEQIEELSED----------------IESLAAEIEE---LEELIEELESE---LEALLNERASLEEALALLRSELEE 898
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002234312  528 TEKKIviafsitdhmkklfyseqgvnsRRDDEDVRNLFSEIEKLRERFESVERPTLDIEVRRAKVPTKERAESSPSpvqv 607
Cdd:TIGR02168  899 LSEEL----------------------RELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLT---- 952
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002234312  608 pstpkaETVVSPKSPAKPDQPLDLDSELAKLEL---EFGQVNKYSPEeisgwEFDELEEELR 666
Cdd:TIGR02168  953 ------LEEAEALENKIEDDEEEARRRLKRLENkikELGPVNLAAIE-----EYEELKERYD 1003
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
287-457 8.47e-03

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 39.57  E-value: 8.47e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002234312  287 LLKKKTSTAGDSLEIRSQKV-DKLKVLATSLSN--SSSKAEKRILDHRRQKEEALNFRAKKENEVS---AVEKELTAEIS 360
Cdd:TIGR00618  198 LLTLRSQLLTLCTPCMPDTYhERKQVLEKELKHlrEALQQTQQSHAYLTQKREAQEEQLKKQQLLKqlrARIEELRAQEA 277
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002234312  361 ELEKQRDELEARLKKVNISLNA-AIGRLKQTREERDQFDEANNQMIFSLKAKDNELSKSITSCNVEAGVVKTWI---NFL 436
Cdd:TIGR00618  278 VLEETQERINRARKAAPLAAHIkAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHsqeIHI 357
                          170       180
                   ....*....|....*....|.
gi 1002234312  437 EDTWQLQSSYNEQKEKRTNDE 457
Cdd:TIGR00618  358 RDAHEVATSIREISCQQHTLT 378
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
230-374 8.51e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.51  E-value: 8.51e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002234312  230 DAEAVELWKKLNEKETSRVQQTQEDHAKTTERTSATT--VESFKEALSEVRFcSRMEELllKKKTSTAGDSLEIRSQKVD 307
Cdd:COG4913    286 AQRRLELLEAELEELRAELARLEAELERLEARLDALReeLDELEAQIRGNGG-DRLEQL--EREIERLERELEERERRRA 362
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002234312  308 KLKVLATSLSNSSSKAEKRILDHRRQKEEALNFRAKKENEVSAVEKELTAEISELEKQRDELEARLK 374
Cdd:COG4913    363 RLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIA 429
 
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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