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Conserved domains on  [gi|568938809|ref|XP_006504809|]
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IQ domain-containing protein E isoform X14 [Mus musculus]

Protein Classification

IQ calmodulin-binding motif-containing protein( domain architecture ID 19230579)

IQ calmodulin-binding motif-containing protein may be involved in cooperative interactions with calmodulins or calmodulin-like proteins

Gene Ontology:  GO:0005516

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 159-318 3.19e-06

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


The actual alignment was detected with superfamily member COG1196:

Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 50.32  E-value: 3.19e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938809 159 EEQEHLQGTVKSLREELGALQEQLLEKDLEMKQLLQSKIDLEKELETAREGEKGRQEQEQALREEVEALTKKCQELEEAK 238
Cdd:COG1196  260 AELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEEL 339

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938809 239 REEKNSFvavtHEAHPELHApspcSRHSEPDSDNSAGEEgssqppapcsEERREAAIRTLQAQWKAHRRKKREAALDEAA 318
Cdd:COG1196  340 EELEEEL----EEAEEELEE----AEAELAEAEEALLEA----------EAELAEAEEELEELAEELLEALRAAAELAAQ 401
IQCD cd23767
IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory ...
 307-338 1.75e-04

IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory complex protein 10 (DRC10), belongs to the IQ motif-containing protein family which contains a C-terminal conserved IQ motif domain and two coiled-coil domains. The IQ motif ([ILV]QxxxRxxxx[RK]), where x stands for any amino-acid residue, interacts with calmodulin (CaM) in a calcium-independent manner and is present in proteins with a wide diversity of biological functions. The IQCD protein was found to primarily accumulate in the acrosome area of round and elongating spermatids of the testis during late stage of spermiogenesis and was then localized to the acrosome and tail regions of mature spermatozoa. The expression of IQCD follows the trajectory of acrosome development during spermatogenesis. IQCD is associated with neuroblastoma and neurodegenerative diseases, and is reported to interact with the nuclear retinoid X receptor in the presence of 9-cis-retinoic acid, thereby activating the transcriptional activity of the receptor.


:

Pssm-ID: 467745 [Multi-domain]  Cd Length: 37  Bit Score: 39.06  E-value: 1.75e-04
                         10        20        30
                 ....*....|....*....|....*....|..
gi 568938809 307 RKKREAALDEAATVLQAAFRGHLARSKLVRSK 338
Cdd:cd23767    1 EEEELQRMNRAATLIQALWRGYKVRKELKKKK 32
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 254-571 2.57e-04

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.16  E-value: 2.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938809  254 PELHAPSPCSRHSEPDSDNSAGEEGSSQPPAPcsEERREAAIRTLqaqwKAHRRKKREAALDEAATVLQAaFRGHLARSK 333
Cdd:PHA03247 2619 PDTHAPDPPPPSPSPAANEPDPHPPPTVPPPE--RPRDDPAPGRV----SRPRRARRLGRAAQASSPPQR-PRRRAARPT 2691

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938809  334 LvrSKVPDSRSPSLPGllsplNQSSPAPRVLSPISPAEENPTQEEaviviQSILRGYLAQARFIASCCREIAASSQRETV 413
Cdd:PHA03247 2692 V--GSLTSLADPPPPP-----PTPEPAPHALVSATPLPPGPAAAR-----QASPALPAAPAPPAVPAGPATPGGPARPAR 2759

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938809  414 SLTPSGSASPPSLRAsPEWGPSGKNSEASSGEAAKDEDEAEEPPDLQPYSGVIRKELCASEELRETSASEPAPSVPYSAQ 493
Cdd:PHA03247 2760 PPTTAGPPAPAPPAA-PAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTA 2838

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568938809  494 GGHGDCPSSSSLEAVPSMKDAMCEERSSSPRSAGPSLAEPSPPELQPLSPPPVEDICSDDSDDIIFSPFLPRKKSPSP 571
Cdd:PHA03247 2839 PPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPP 2916
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 46-237 5.62e-04

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


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 43.12  E-value: 5.62e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938809    46 KRQKKMSSALLNLTRSVQELTEENQSLKEDLDRMLSNSPTISkikgygdwskprllRRIAELEKKVSSSESPKQSTSELV 125
Cdd:TIGR02168  684 EKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELS--------------RQISALRKDLARLEAEVEQLEERI 749

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938809   126 NPNPLVRSpsNISVQKQPKGDQSPEDLPKVAPCEEQ-EHLQGTVK--------------SLREELGALQEQLLEKDLEMK 190
Cdd:TIGR02168  750 AQLSKELT--ELEAEIEELEERLEEAEEELAEAEAEiEELEAQIEqlkeelkalrealdELRAELTLLNEEAANLRERLE 827

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 568938809   191 QLLQSKIDLEKELETAREGEKGRQEQEQALREEVEALTKKCQELEEA 237
Cdd:TIGR02168  828 SLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESE 874
 
Name Accession Description Interval E-value
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 159-318 3.19e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 50.32  E-value: 3.19e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938809 159 EEQEHLQGTVKSLREELGALQEQLLEKDLEMKQLLQSKIDLEKELETAREGEKGRQEQEQALREEVEALTKKCQELEEAK 238
Cdd:COG1196  260 AELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEEL 339

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938809 239 REEKNSFvavtHEAHPELHApspcSRHSEPDSDNSAGEEgssqppapcsEERREAAIRTLQAQWKAHRRKKREAALDEAA 318
Cdd:COG1196  340 EELEEEL----EEAEEELEE----AEAELAEAEEALLEA----------EAELAEAEEELEELAEELLEALRAAAELAAQ 401
IQCD cd23767
IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory ...
 307-338 1.75e-04

IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory complex protein 10 (DRC10), belongs to the IQ motif-containing protein family which contains a C-terminal conserved IQ motif domain and two coiled-coil domains. The IQ motif ([ILV]QxxxRxxxx[RK]), where x stands for any amino-acid residue, interacts with calmodulin (CaM) in a calcium-independent manner and is present in proteins with a wide diversity of biological functions. The IQCD protein was found to primarily accumulate in the acrosome area of round and elongating spermatids of the testis during late stage of spermiogenesis and was then localized to the acrosome and tail regions of mature spermatozoa. The expression of IQCD follows the trajectory of acrosome development during spermatogenesis. IQCD is associated with neuroblastoma and neurodegenerative diseases, and is reported to interact with the nuclear retinoid X receptor in the presence of 9-cis-retinoic acid, thereby activating the transcriptional activity of the receptor.


Pssm-ID: 467745 [Multi-domain]  Cd Length: 37  Bit Score: 39.06  E-value: 1.75e-04
                         10        20        30
                 ....*....|....*....|....*....|..
gi 568938809 307 RKKREAALDEAATVLQAAFRGHLARSKLVRSK 338
Cdd:cd23767    1 EEEELQRMNRAATLIQALWRGYKVRKELKKKK 32
PHA03247 PHA03247
large tegument protein UL36; Provisional
 254-571 2.57e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.16  E-value: 2.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938809  254 PELHAPSPCSRHSEPDSDNSAGEEGSSQPPAPcsEERREAAIRTLqaqwKAHRRKKREAALDEAATVLQAaFRGHLARSK 333
Cdd:PHA03247 2619 PDTHAPDPPPPSPSPAANEPDPHPPPTVPPPE--RPRDDPAPGRV----SRPRRARRLGRAAQASSPPQR-PRRRAARPT 2691

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938809  334 LvrSKVPDSRSPSLPGllsplNQSSPAPRVLSPISPAEENPTQEEaviviQSILRGYLAQARFIASCCREIAASSQRETV 413
Cdd:PHA03247 2692 V--GSLTSLADPPPPP-----PTPEPAPHALVSATPLPPGPAAAR-----QASPALPAAPAPPAVPAGPATPGGPARPAR 2759

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938809  414 SLTPSGSASPPSLRAsPEWGPSGKNSEASSGEAAKDEDEAEEPPDLQPYSGVIRKELCASEELRETSASEPAPSVPYSAQ 493
Cdd:PHA03247 2760 PPTTAGPPAPAPPAA-PAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTA 2838

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568938809  494 GGHGDCPSSSSLEAVPSMKDAMCEERSSSPRSAGPSLAEPSPPELQPLSPPPVEDICSDDSDDIIFSPFLPRKKSPSP 571
Cdd:PHA03247 2839 PPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPP 2916
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 46-237 5.62e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 43.12  E-value: 5.62e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938809    46 KRQKKMSSALLNLTRSVQELTEENQSLKEDLDRMLSNSPTISkikgygdwskprllRRIAELEKKVSSSESPKQSTSELV 125
Cdd:TIGR02168  684 EKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELS--------------RQISALRKDLARLEAEVEQLEERI 749

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938809   126 NPNPLVRSpsNISVQKQPKGDQSPEDLPKVAPCEEQ-EHLQGTVK--------------SLREELGALQEQLLEKDLEMK 190
Cdd:TIGR02168  750 AQLSKELT--ELEAEIEELEERLEEAEEELAEAEAEiEELEAQIEqlkeelkalrealdELRAELTLLNEEAANLRERLE 827

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 568938809   191 QLLQSKIDLEKELETAREGEKGRQEQEQALREEVEALTKKCQELEEA 237
Cdd:TIGR02168  828 SLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESE 874
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 60-326 1.15e-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: 41.97  E-value: 1.15e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938809    60 RSVQELTEENQSLKEDLDRMLSNSPT-ISKIKGYgdwsKPRLLRRIAELEKK-------VSSSESPKQSTSElvNPNPLV 131
Cdd:TIGR02168  242 EELQEELKEAEEELEELTAELQELEEkLEELRLE----VSELEEEIEELQKElyalaneISRLEQQKQILRE--RLANLE 315

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938809   132 RSPSNISVQKQPKGDQSPEDLPKVAPCEEQehlqgtVKSLREELGALQEQLLEKDLEMKQLLQSKIDLEKELETAREGEK 211
Cdd:TIGR02168  316 RQLEELEAQLEELESKLDELAEELAELEEK------LEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVA 389

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938809   212 GRQEQEQALREEVEALTKKCQELEEakREEKNSFVAVTHEAHPELHAPSPCSRHSEpdsdnsagEEGSSQPPAPCSEERR 291
Cdd:TIGR02168  390 QLELQIASLNNEIERLEARLERLED--RRERLQQEIEELLKKLEEAELKELQAELE--------ELEEELEELQEELERL 459

                          250       260       270
                   ....*....|....*....|....*....|....*
gi 568938809   292 EAAIRTLQAQwkahRRKKREAALDEAATVLQAAFR 326
Cdd:TIGR02168  460 EEALEELREE----LEEAEQALDAAERELAQLQAR 490
IQ smart00015
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ...
 314-334 2.11e-03

Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln residues.


Pssm-ID: 197470 [Multi-domain]  Cd Length: 23  Bit Score: 35.76  E-value: 2.11e-03
                           10        20
                   ....*....|....*....|.
gi 568938809   314 LDEAATVLQAAFRGHLARSKL 334
Cdd:smart00015   2 LTRAAIIIQAAWRGYLARKRY 22
IQ pfam00612
IQ calmodulin-binding motif; Calmodulin-binding motif.
 316-334 4.03e-03

IQ calmodulin-binding motif; Calmodulin-binding motif.


Pssm-ID: 459869  Cd Length: 21  Bit Score: 34.99  E-value: 4.03e-03
                          10
                  ....*....|....*....
gi 568938809  316 EAATVLQAAFRGHLARSKL 334
Cdd:pfam00612   2 KAAIKIQAAWRGYLARKRY 20
Adgb_C_mid-like cd22307
C-terminal middle region of Androglobins (Adgbs) and related proteins; including permuted ...
 201-343 4.83e-03

C-terminal middle region of Androglobins (Adgbs) and related proteins; including permuted globin domain and IQ motif; Androglobin (Adgb, also known as Calpain-7-like protein, CAPN7L) is a large multidomain protein consisting of an N-terminal peptidase C2 family calpain-like domain, an IQ calmodulin-binding motif, and an internal, circularly permuted globin domain. The canonical secondary structure of hemoglobins is an 3-over-3 alpha-helical sandwich structure, where the eight alpha-helical segments are conventionally labeled, A-H, according to their sequential order; Adgbs differ from this in having helices C-H followed by A-B. Adgbs and other phylogenetically ancient globins, such as neuroglobins and globin X, form hexacoordinated heme iron complexes. Globins contain various highly conserved residues of the heme pocket: including a Phe in the interhelical position CD1 (Phe CD1, first position in the loop between the helices C and D) that is packed against the heme, a His at the 7th position of the E-helix (His E7) that binds the heme iron distally, and a His at the 8th position of the F-helix (His F8) that binds the heme iron proximally. Unlike other hexacoordinated globins, Adgbs have an E7 Gln; their hexacoordination scheme is [Gln]-Fe-[His]. In mammals, Adgb is mainly expressed in the testes and may play an important role in spermatogenesis. Arthropod Adgbs have degenerate globin domains (DOI:10.3389/fgene.2020.00858). This model spans the permuted globin domain, the IQ motif, and a conserved region of about 200 amino acid residues located C-terminal to the globin domain; it does not include the N-terminal protease domain or the large uncharacterized C-terminal domain of approximately 500 residues.


Pssm-ID: 412094  Cd Length: 416  Bit Score: 39.46  E-value: 4.83e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938809 201 KELETA-----REGEKGRQEQEQALREEVEALTKKCQELEEAKrEEKNSFVAVTHEahpelhaPSPCSRHSEPDSDNSAG 275
Cdd:cd22307   57 KELYRSycpplLWSKEDKKEHHKVFNEALYHLLKKALGRKETP-DELFALRALFLD-------PDIGLEYKESPSSSLRE 128

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568938809 276 EEGSSqppaPCSEERREAAIRtlqaqwkahrrkkreaaLDEAATVLQAAFRGHLARsKLVRSKVPDSR 343
Cdd:cd22307  129 IVEPD----ECDCRTREPTIE-----------------EHEAATKIQAFFRGTLVR-KLLKAHKPGTK 174
 
Name Accession Description Interval E-value
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 159-318 3.19e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 50.32  E-value: 3.19e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938809 159 EEQEHLQGTVKSLREELGALQEQLLEKDLEMKQLLQSKIDLEKELETAREGEKGRQEQEQALREEVEALTKKCQELEEAK 238
Cdd:COG1196  260 AELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEEL 339

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938809 239 REEKNSFvavtHEAHPELHApspcSRHSEPDSDNSAGEEgssqppapcsEERREAAIRTLQAQWKAHRRKKREAALDEAA 318
Cdd:COG1196  340 EELEEEL----EEAEEELEE----AEAELAEAEEALLEA----------EAELAEAEEELEELAEELLEALRAAAELAAQ 401
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
142-240 1.61e-05

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 47.93  E-value: 1.61e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938809 142 QPKGDQSPEDLPKVAPCEEQEH------LQGTVKSLREELGALQEQLLEKDLEMKqllqskiDLEKELETAR--EGEKGR 213
Cdd:COG2433  390 LPEEEPEAEREKEHEERELTEEeeeirrLEEQVERLEAEVEELEAELEEKDERIE-------RLERELSEARseERREIR 462

                         90       100
                 ....*....|....*....|....*...
gi 568938809 214 QEQE-QALREEVEALTKKCQELEEAKRE 240
Cdd:COG2433  463 KDREiSRLDREIERLERELEEERERIEE 490
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 159-334 6.29e-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: 6.29e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938809 159 EEQEHLQGTVKSLREELGALQEQLLEKDLEMKQLLQSKIDLEKELETAREGEKGRQEQEQALREEVEALTKKCQELEEAK 238
Cdd:COG1196  351 EELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEAL 430

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938809 239 REEKNSFVAVTHEAHPELHApspcsrhsepDSDNSAGEEGSSQPPAPCSEERREAAIRTLQAQWKAHRRKKREAALDEAA 318
Cdd:COG1196  431 AELEEEEEEEEEALEEAAEE----------EAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAE 500

                        170
                 ....*....|....*.
gi 568938809 319 TVLQAAFRGHLARSKL 334
Cdd:COG1196  501 ADYEGFLEGVKAALLL 516
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 159-324 1.67e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.54  E-value: 1.67e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938809 159 EEQEHLQGTVKSLREELGALQEQLLEKDLEMKQLLQSKIDLEKELETAREGEKGRQEQEQALREEVEALTKKCQELEEAK 238
Cdd:COG1196  253 AELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEEL 332

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938809 239 REEKnsfvAVTHEAHPELHApspcsrhSEPDSDNSAGEEGSSQppapCSEERREAAIRTLQAQWKAHRRKKREAALDEAA 318
Cdd:COG1196  333 EELE----EELEELEEELEE-------AEEELEEAEAELAEAE----EALLEAEAELAEAEEELEELAEELLEALRAAAE 397


                 ....*.
gi 568938809 319 TVLQAA 324
Cdd:COG1196  398 LAAQLE 403
IQCD cd23767
IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory ...
 307-338 1.75e-04

IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory complex protein 10 (DRC10), belongs to the IQ motif-containing protein family which contains a C-terminal conserved IQ motif domain and two coiled-coil domains. The IQ motif ([ILV]QxxxRxxxx[RK]), where x stands for any amino-acid residue, interacts with calmodulin (CaM) in a calcium-independent manner and is present in proteins with a wide diversity of biological functions. The IQCD protein was found to primarily accumulate in the acrosome area of round and elongating spermatids of the testis during late stage of spermiogenesis and was then localized to the acrosome and tail regions of mature spermatozoa. The expression of IQCD follows the trajectory of acrosome development during spermatogenesis. IQCD is associated with neuroblastoma and neurodegenerative diseases, and is reported to interact with the nuclear retinoid X receptor in the presence of 9-cis-retinoic acid, thereby activating the transcriptional activity of the receptor.


Pssm-ID: 467745 [Multi-domain]  Cd Length: 37  Bit Score: 39.06  E-value: 1.75e-04
                         10        20        30
                 ....*....|....*....|....*....|..
gi 568938809 307 RKKREAALDEAATVLQAAFRGHLARSKLVRSK 338
Cdd:cd23767    1 EEEELQRMNRAATLIQALWRGYKVRKELKKKK 32
PHA03247 PHA03247
large tegument protein UL36; Provisional
 254-571 2.57e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.16  E-value: 2.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938809  254 PELHAPSPCSRHSEPDSDNSAGEEGSSQPPAPcsEERREAAIRTLqaqwKAHRRKKREAALDEAATVLQAaFRGHLARSK 333
Cdd:PHA03247 2619 PDTHAPDPPPPSPSPAANEPDPHPPPTVPPPE--RPRDDPAPGRV----SRPRRARRLGRAAQASSPPQR-PRRRAARPT 2691

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938809  334 LvrSKVPDSRSPSLPGllsplNQSSPAPRVLSPISPAEENPTQEEaviviQSILRGYLAQARFIASCCREIAASSQRETV 413
Cdd:PHA03247 2692 V--GSLTSLADPPPPP-----PTPEPAPHALVSATPLPPGPAAAR-----QASPALPAAPAPPAVPAGPATPGGPARPAR 2759

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938809  414 SLTPSGSASPPSLRAsPEWGPSGKNSEASSGEAAKDEDEAEEPPDLQPYSGVIRKELCASEELRETSASEPAPSVPYSAQ 493
Cdd:PHA03247 2760 PPTTAGPPAPAPPAA-PAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTA 2838

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568938809  494 GGHGDCPSSSSLEAVPSMKDAMCEERSSSPRSAGPSLAEPSPPELQPLSPPPVEDICSDDSDDIIFSPFLPRKKSPSP 571
Cdd:PHA03247 2839 PPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPP 2916
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
99-248 3.27e-04

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.60  E-value: 3.27e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938809  99 RLLRRIAELEKKVSSSESPKQSTSELVNPNPLVRSPSNISVQKQPKGDQSPEDLPKVAP----CEEQEHLQGTVKSLREE 174
Cdd:COG4717   99 ELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEElrelEEELEELEAELAELQEE 178

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568938809 175 LGALQEQL-LEKDLEMKQLLQSKIDLEKELETAREGEKGRQEQEQALREEVEALTKKCQELEEAKREEKNSFVAV 248
Cdd:COG4717  179 LEELLEQLsLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLL 253
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
159-245 3.66e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.97  E-value: 3.66e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938809 159 EEQEHLQGTVKSLREELGALQEQLLEKDLEMKQLLQSKIDLEKELETAREGEKGRQEQEQALREEVEALTKKCQELEEAK 238
Cdd:COG4372   59 EELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQI 138


                 ....*..
gi 568938809 239 REEKNSF 245
Cdd:COG4372  139 AELQSEI 145
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 46-237 5.62e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 43.12  E-value: 5.62e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938809    46 KRQKKMSSALLNLTRSVQELTEENQSLKEDLDRMLSNSPTISkikgygdwskprllRRIAELEKKVSSSESPKQSTSELV 125
Cdd:TIGR02168  684 EKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELS--------------RQISALRKDLARLEAEVEQLEERI 749

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938809   126 NPNPLVRSpsNISVQKQPKGDQSPEDLPKVAPCEEQ-EHLQGTVK--------------SLREELGALQEQLLEKDLEMK 190
Cdd:TIGR02168  750 AQLSKELT--ELEAEIEELEERLEEAEEELAEAEAEiEELEAQIEqlkeelkalrealdELRAELTLLNEEAANLRERLE 827

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 568938809   191 QLLQSKIDLEKELETAREGEKGRQEQEQALREEVEALTKKCQELEEA 237
Cdd:TIGR02168  828 SLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESE 874
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 60-326 1.15e-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: 41.97  E-value: 1.15e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938809    60 RSVQELTEENQSLKEDLDRMLSNSPT-ISKIKGYgdwsKPRLLRRIAELEKK-------VSSSESPKQSTSElvNPNPLV 131
Cdd:TIGR02168  242 EELQEELKEAEEELEELTAELQELEEkLEELRLE----VSELEEEIEELQKElyalaneISRLEQQKQILRE--RLANLE 315

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938809   132 RSPSNISVQKQPKGDQSPEDLPKVAPCEEQehlqgtVKSLREELGALQEQLLEKDLEMKQLLQSKIDLEKELETAREGEK 211
Cdd:TIGR02168  316 RQLEELEAQLEELESKLDELAEELAELEEK------LEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVA 389

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938809   212 GRQEQEQALREEVEALTKKCQELEEakREEKNSFVAVTHEAHPELHAPSPCSRHSEpdsdnsagEEGSSQPPAPCSEERR 291
Cdd:TIGR02168  390 QLELQIASLNNEIERLEARLERLED--RRERLQQEIEELLKKLEEAELKELQAELE--------ELEEELEELQEELERL 459

                          250       260       270
                   ....*....|....*....|....*....|....*
gi 568938809   292 EAAIRTLQAQwkahRRKKREAALDEAATVLQAAFR 326
Cdd:TIGR02168  460 EEALEELREE----LEEAEQALDAAERELAQLQAR 490
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
159-240 1.28e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.43  E-value: 1.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938809 159 EEQEHLQGTVKSLREELGALQEQLLEKDLEMKQLLQSKIDLEKELETAREGEKGRQEQEQALREEVEALTKKCQELEEAK 238
Cdd:COG4372   45 EELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKER 124


                 ..
gi 568938809 239 RE 240
Cdd:COG4372  125 QD 126
IQ smart00015
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ...
 314-334 2.11e-03

Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln residues.


Pssm-ID: 197470 [Multi-domain]  Cd Length: 23  Bit Score: 35.76  E-value: 2.11e-03
                           10        20
                   ....*....|....*....|.
gi 568938809   314 LDEAATVLQAAFRGHLARSKL 334
Cdd:smart00015   2 LTRAAIIIQAAWRGYLARKRY 22
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
168-237 2.15e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.05  E-value: 2.15e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568938809  168 VKSLREELGALQEQL--LEK-DLEMKQLLQSKIDLEKELETAREGEKGRQEQEQALREEVEALTKKCQELEEA 237
Cdd:COG4913   663 VASAEREIAELEAELerLDAsSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDR 735
IQ pfam00612
IQ calmodulin-binding motif; Calmodulin-binding motif.
 316-334 4.03e-03

IQ calmodulin-binding motif; Calmodulin-binding motif.


Pssm-ID: 459869  Cd Length: 21  Bit Score: 34.99  E-value: 4.03e-03
                          10
                  ....*....|....*....
gi 568938809  316 EAATVLQAAFRGHLARSKL 334
Cdd:pfam00612   2 KAAIKIQAAWRGYLARKRY 20
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 159-242 4.82e-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: 4.82e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938809 159 EEQEHLQGTVKSLREELGALQEQLLEKDLEMKQLLQSKIDLEKELETAREGEKGRQEQEQALREEVEALTKKCQELEEAK 238
Cdd:COG1196  239 AELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERL 318


                 ....
gi 568938809 239 REEK 242
Cdd:COG1196  319 EELE 322
Adgb_C_mid-like cd22307
C-terminal middle region of Androglobins (Adgbs) and related proteins; including permuted ...
 201-343 4.83e-03

C-terminal middle region of Androglobins (Adgbs) and related proteins; including permuted globin domain and IQ motif; Androglobin (Adgb, also known as Calpain-7-like protein, CAPN7L) is a large multidomain protein consisting of an N-terminal peptidase C2 family calpain-like domain, an IQ calmodulin-binding motif, and an internal, circularly permuted globin domain. The canonical secondary structure of hemoglobins is an 3-over-3 alpha-helical sandwich structure, where the eight alpha-helical segments are conventionally labeled, A-H, according to their sequential order; Adgbs differ from this in having helices C-H followed by A-B. Adgbs and other phylogenetically ancient globins, such as neuroglobins and globin X, form hexacoordinated heme iron complexes. Globins contain various highly conserved residues of the heme pocket: including a Phe in the interhelical position CD1 (Phe CD1, first position in the loop between the helices C and D) that is packed against the heme, a His at the 7th position of the E-helix (His E7) that binds the heme iron distally, and a His at the 8th position of the F-helix (His F8) that binds the heme iron proximally. Unlike other hexacoordinated globins, Adgbs have an E7 Gln; their hexacoordination scheme is [Gln]-Fe-[His]. In mammals, Adgb is mainly expressed in the testes and may play an important role in spermatogenesis. Arthropod Adgbs have degenerate globin domains (DOI:10.3389/fgene.2020.00858). This model spans the permuted globin domain, the IQ motif, and a conserved region of about 200 amino acid residues located C-terminal to the globin domain; it does not include the N-terminal protease domain or the large uncharacterized C-terminal domain of approximately 500 residues.


Pssm-ID: 412094  Cd Length: 416  Bit Score: 39.46  E-value: 4.83e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938809 201 KELETA-----REGEKGRQEQEQALREEVEALTKKCQELEEAKrEEKNSFVAVTHEahpelhaPSPCSRHSEPDSDNSAG 275
Cdd:cd22307   57 KELYRSycpplLWSKEDKKEHHKVFNEALYHLLKKALGRKETP-DELFALRALFLD-------PDIGLEYKESPSSSLRE 128

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568938809 276 EEGSSqppaPCSEERREAAIRtlqaqwkahrrkkreaaLDEAATVLQAAFRGHLARsKLVRSKVPDSR 343
Cdd:cd22307  129 IVEPD----ECDCRTREPTIE-----------------EHEAATKIQAFFRGTLVR-KLLKAHKPGTK 174
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
167-240 5.41e-03

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 39.61  E-value: 5.41e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568938809 167 TVKSLREELGALQEQLLEkdlEMKQLLQSkidLEKELETAREGEKGRQEQEQALREEVEALTKKCQELEEAKRE 240
Cdd:COG3206  292 DVIALRAQIAALRAQLQQ---EAQRILAS---LEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLERE 359
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 169-242 6.33e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.53  E-value: 6.33e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568938809 169 KSLREELGALQEQLLEKDLEMKQLLQSKIDLEKELETAREGEKGRQEQEQALREEVEALTKKCQELEEAKREEK 242
Cdd:COG1196  235 RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLE 308
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
162-331 7.05e-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: 7.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938809  162 EHLQGTVKSLREELGALQEQLLEKDLEMKQL----------------------LQSKI-DLEKELETAREGE---KGRQE 215
Cdd:COG4913   613 AALEAELAELEEELAEAEERLEALEAELDALqerrealqrlaeyswdeidvasAEREIaELEAELERLDASSddlAALEE 692

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938809  216 QEQALREEVEALTKKCQELEEAKR---EEKNSFVAVTHEAHPELhapspcsrhsepdsdnSAGEEGSSQPPAPCSEERRE 292
Cdd:COG4913   693 QLEELEAELEELEEELDELKGEIGrleKELEQAEEELDELQDRL----------------EAAEDLARLELRALLEERFA 756

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 568938809  293 AAIRTLQ----AQWKAHRRKKREAALDEAATVLQAAFRGHLAR 331
Cdd:COG4913   757 AALGDAVerelRENLEERIDALRARLNRAEEELERAMRAFNRE 799
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 159-249 8.49e-03

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 37.98  E-value: 8.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938809 159 EEQEHLQGTVKSLREELGALQEQLLEKDLEMKQL------LQSKID-----------------LEKELETAREGEKGRQE 215
Cdd:COG1579   31 AELAELEDELAALEARLEAAKTELEDLEKEIKRLeleieeVEARIKkyeeqlgnvrnnkeyeaLQKEIESLKRRISDLED 110

                         90       100       110
                 ....*....|....*....|....*....|....
gi 568938809 216 QEQALREEVEALTKKCQELEEAKREEKNSFVAVT 249
Cdd:COG1579  111 EILELMERIEELEEELAELEAELAELEAELEEKK 144
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 159-240 9.21e-03

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 37.98  E-value: 9.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938809 159 EEQEHLQGTVKSLREELGALQEQLLEKDLEMKQLLQSKIDLEKELETAREGEKGRQEQ--------E-QALREEVEALTK 229
Cdd:COG1579   24 HRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQlgnvrnnkEyEALQKEIESLKR 103

                         90
                 ....*....|.
gi 568938809 230 KCQELEEAKRE 240
Cdd:COG1579  104 RISDLEDEILE 114
PLN03209 PLN03209
translocon at the inner envelope of chloroplast subunit 62; Provisional
 332-571 9.49e-03

translocon at the inner envelope of chloroplast subunit 62; Provisional


Pssm-ID: 178748 [Multi-domain]  Cd Length: 576  Bit Score: 38.75  E-value: 9.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938809 332 SKLVRSKVPDSRSPSLPGLLSPLNQSSPAPrvlspisPAEENPTQEEAVIviQSILRGYLAQarfiasccreiaassqre 411
Cdd:PLN03209 325 SQRVPPKESDAADGPKPVPTKPVTPEAPSP-------PIEEEPPQPKAVV--PRPLSPYTAY------------------ 377

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938809 412 tVSLTPSGSASPPSlraspewgPSGKNSEASSGEAAKDEDEAEEPPDLQPYSGVIRKELCASEELRETSASEPA------ 485
Cdd:PLN03209 378 -EDLKPPTSPIPTP--------PSSSPASSKSVDAVAKPAEPDVVPSPGSASNVPEVEPAQVEAKKTRPLSPYAryedlk 448

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938809 486 -PSVPySAQGGHGDCPSSSSLEAVPSMKDamceersSSPRSAGPSLAEPSPPELQPLSPPPVEDICSDDSDDIIFSPFLP 564
Cdd:PLN03209 449 pPTSP-SPTAPTGVSPSVSSTSSVPAVPD-------TAPATAATDAAAPPPANMRPLSPYAVYDDLKPPTSPSPAAPVGK 520


                 ....*..
gi 568938809 565 RKKSPSP 571
Cdd:PLN03209 521 VAPSSTN 527
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 5-237 9.58e-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: 38.88  E-value: 9.58e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938809     5 NLEEMRIAMETYYEEIHRLQTLLASSEATGKkpmvEKKLGVKRQKKmssALLNLTRSVQELTEENQSLKEDLDRMLSNSP 84
Cdd:TIGR02168  692 KIAELEKALAELRKELEELEEELEQLRKELE----ELSRQISALRK---DLARLEAEVEQLEERIAQLSKELTELEAEIE 764

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938809    85 TISKIKGYGDWSKPRLLRRIAELEKKVS-SSESPKQSTSELVNPNPLVRSpSNISVQKQPKGDQSPEDlpKVAPCEEQ-- 161
Cdd:TIGR02168  765 ELEERLEEAEEELAEAEAEIEELEAQIEqLKEELKALREALDELRAELTL-LNEEAANLRERLESLER--RIAATERRle 841

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938809   162 ------EHLQGTVKSLREELGALQEQLLEKDLEMKQLLQSKIDLEKELETAREGEKGRQEQEQALREEVEALTKKCQELE 235
Cdd:TIGR02168  842 dleeqiEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELR 921


                   ..
gi 568938809   236 EA 237
Cdd:TIGR02168  922 EK 923
 
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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