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Conserved domains on  [gi|1720415027|ref|XP_030110719|]
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IQ domain-containing protein E isoform X18 [Mus musculus]

Protein Classification

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]; ...
 90-249 1.81e-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: 50.71  E-value: 1.81e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415027  90 EEQEHLQGTVKSLREELGALQEQLLEKDLEMKQLLQSKIDLEKELETAREGEKGRQEQEQALREEVEALTKKCQELEEAK 169
Cdd:COG1196   260 AELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEEL 339

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415027 170 REEKNSFvavtHEAHPELHApspcSRHSEPDSDNSAGEEgssqppapcsEERREAAIRTLQAQWKAHRRKKREAALDEAA 249
Cdd:COG1196   340 EELEEEL----EEAEEELEE----AEAELAEAEEALLEA----------EAELAEAEEELEELAEELLEALRAAAELAAQ 401
IQCD cd23767
IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory ...
 238-269 5.07e-05

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: 40.22  E-value: 5.07e-05
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1720415027 238 RKKREAALDEAATVLQAAFRGHLARSKLVRSK 269
Cdd:cd23767     1 EEEELQRMNRAATLIQALWRGYKVRKELKKKK 32
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 185-502 3.03e-03

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 40.69  E-value: 3.03e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415027  185 PELHAPSPCSRHSEPDSDNSAGEEGSSQPPAPcsEERREAAIRTLqaqwKAHRRKKREAALDEAATVLQAAfrghlaRSK 264
Cdd:PHA03247  2619 PDTHAPDPPPPSPSPAANEPDPHPPPTVPPPE--RPRDDPAPGRV----SRPRRARRLGRAAQASSPPQRP------RRR 2686

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415027  265 LVRSKVPDSRSPSLPGllSPLNQSSPAPRVLSPISPAEENPTQEEaviviQSILRGYLAQARFIASCCREIAASSQRETV 344
Cdd:PHA03247  2687 AARPTVGSLTSLADPP--PPPPTPEPAPHALVSATPLPPGPAAAR-----QASPALPAAPAPPAVPAGPATPGGPARPAR 2759

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415027  345 SLTPSGSASPPSLRAsPEWGPSGKNSEASSGEAAKDEDEAEEPPDLQPYSGVIRKELCASEELRETSASEPAPSVPYSAQ 424
Cdd:PHA03247  2760 PPTTAGPPAPAPPAA-PAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTA 2838

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720415027  425 GGHGDCPSSSSLEAVPSMKDAMCEERSSSPRSAGPSLAEPSPPELQPLSPPPVEDICSDDSDDIIFSPFLPRKKSPSP 502
Cdd:PHA03247  2839 PPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPP 2916
 
Name Accession Description Interval E-value
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 90-249 1.81e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 50.71  E-value: 1.81e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415027  90 EEQEHLQGTVKSLREELGALQEQLLEKDLEMKQLLQSKIDLEKELETAREGEKGRQEQEQALREEVEALTKKCQELEEAK 169
Cdd:COG1196   260 AELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEEL 339

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415027 170 REEKNSFvavtHEAHPELHApspcSRHSEPDSDNSAGEEgssqppapcsEERREAAIRTLQAQWKAHRRKKREAALDEAA 249
Cdd:COG1196   340 EELEEEL----EEAEEELEE----AEAELAEAEEALLEA----------EAELAEAEEELEELAEELLEALRAAAELAAQ 401
IQCD cd23767
IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory ...
 238-269 5.07e-05

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: 40.22  E-value: 5.07e-05
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1720415027 238 RKKREAALDEAATVLQAAFRGHLARSKLVRSK 269
Cdd:cd23767     1 EEEELQRMNRAATLIQALWRGYKVRKELKKKK 32
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 61-257 4.88e-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: 4.88e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415027   61 LVRSPSNISVQKQPKGDQSPEDLPKVAPCEEQehlqgtVKSLREELGALQEQLLEKDLEMKQLLQSKIDLEKELETAREG 140
Cdd:TIGR02168  314 LERQLEELEAQLEELESKLDELAEELAELEEK------LEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSK 387

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415027  141 EKGRQEQEQALREEVEALTKKCQELEEakREEKNSFVAVTHEAHPELHAPSPCSRHSEpdsdnsagEEGSSQPPAPCSEE 220
Cdd:TIGR02168  388 VAQLELQIASLNNEIERLEARLERLED--RRERLQQEIEELLKKLEEAELKELQAELE--------ELEEELEELQEELE 457

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1720415027  221 RREAAIRTLQAQwkahRRKKREAALDEAATVLQAAFR 257
Cdd:TIGR02168  458 RLEEALEELREE----LEEAEQALDAAERELAQLQAR 490
IQ smart00015
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ...
 245-265 1.86e-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: 1.86e-03
                           10        20
                   ....*....|....*....|.
gi 1720415027  245 LDEAATVLQAAFRGHLARSKL 265
Cdd:smart00015   2 LTRAAIIIQAAWRGYLARKRY 22
PHA03247 PHA03247
large tegument protein UL36; Provisional
 185-502 3.03e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 40.69  E-value: 3.03e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415027  185 PELHAPSPCSRHSEPDSDNSAGEEGSSQPPAPcsEERREAAIRTLqaqwKAHRRKKREAALDEAATVLQAAfrghlaRSK 264
Cdd:PHA03247  2619 PDTHAPDPPPPSPSPAANEPDPHPPPTVPPPE--RPRDDPAPGRV----SRPRRARRLGRAAQASSPPQRP------RRR 2686

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415027  265 LVRSKVPDSRSPSLPGllSPLNQSSPAPRVLSPISPAEENPTQEEaviviQSILRGYLAQARFIASCCREIAASSQRETV 344
Cdd:PHA03247  2687 AARPTVGSLTSLADPP--PPPPTPEPAPHALVSATPLPPGPAAAR-----QASPALPAAPAPPAVPAGPATPGGPARPAR 2759

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415027  345 SLTPSGSASPPSLRAsPEWGPSGKNSEASSGEAAKDEDEAEEPPDLQPYSGVIRKELCASEELRETSASEPAPSVPYSAQ 424
Cdd:PHA03247  2760 PPTTAGPPAPAPPAA-PAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTA 2838

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720415027  425 GGHGDCPSSSSLEAVPSMKDAMCEERSSSPRSAGPSLAEPSPPELQPLSPPPVEDICSDDSDDIIFSPFLPRKKSPSP 502
Cdd:PHA03247  2839 PPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPP 2916
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 92-177 3.12e-03

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


Pssm-ID: 214922 [Multi-domain]  Cd Length: 140  Bit Score: 37.95  E-value: 3.12e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415027   92 QEHLQGTVKSLREELGALQEQLlekdlemKQLLQskiDLEKELETAREGEKGRQEQE-QALREEVEALTKKCQ-ELEEAK 169
Cdd:smart00935  20 QKQLEKEFKKRQAELEKLEKEL-------QKLKE---KLQKDAATLSEAAREKKEKElQKKVQEFQRKQQKLQqDLQKRQ 89


                   ....*...
gi 1720415027  170 REEKNSFV 177
Cdd:smart00935  90 QEELQKIL 97
IQ pfam00612
IQ calmodulin-binding motif; Calmodulin-binding motif.
 247-265 3.56e-03

IQ calmodulin-binding motif; Calmodulin-binding motif.


Pssm-ID: 459869  Cd Length: 21  Bit Score: 34.99  E-value: 3.56e-03
                          10
                  ....*....|....*....
gi 1720415027 247 EAATVLQAAFRGHLARSKL 265
Cdd:pfam00612   2 KAAIKIQAAWRGYLARKRY 20
Adgb_C_mid-like cd22307
C-terminal middle region of Androglobins (Adgbs) and related proteins; including permuted ...
 132-274 4.06e-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: 4.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415027 132 KELETA-----REGEKGRQEQEQALREEVEALTKKCQELEEAKrEEKNSFVAVTHEahpelhaPSPCSRHSEPDSDNSAG 206
Cdd:cd22307    57 KELYRSycpplLWSKEDKKEHHKVFNEALYHLLKKALGRKETP-DELFALRALFLD-------PDIGLEYKESPSSSLRE 128

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720415027 207 EEGSSqppaPCSEERREAAIRtlqaqwkahrrkkreaaLDEAATVLQAAFRGHLARsKLVRSKVPDSR 274
Cdd:cd22307   129 IVEPD----ECDCRTREPTIE-----------------EHEAATKIQAFFRGTLVR-KLLKAHKPGTK 174
Tektin pfam03148
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular ...
 99-165 7.69e-03

Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular sites as centrioles, basal bodies, and along ciliary and flagellar doublet microtubules. Tektins form unique protofilaments, organized as longitudinal polymers of tektin heterodimers with axial periodicity matching tubulin. Tektin polypeptides consist of several alpha-helical regions that are predicted to form coiled coils. Indeed, tektins share considerable structural similarities with intermediate filament proteins. Possible functional roles for tektins are: stabilization of tubulin protofilaments; attachment of A and B-tubules in ciliary/flagellar microtubule doublets and C-tubules in centrioles; binding of axonemal components.


Pssm-ID: 460827 [Multi-domain]  Cd Length: 383  Bit Score: 38.68  E-value: 7.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415027  99 VKSLREELgalQEQLLEKDLEMKQLLQSKIDLEKELE-------------TAREGEKG----RQEQEQALREEVEaLTKK 161
Cdd:pfam03148  55 ITFWKSEL---EKELEELDEEIELLLEEKRRLEKALEaleeplhiaqeclTLREKRQGidlvHDEVEKELLKEVE-LIEG 130


                  ....
gi 1720415027 162 CQEL 165
Cdd:pfam03148 131 IQEL 134
 
Name Accession Description Interval E-value
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 90-249 1.81e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 50.71  E-value: 1.81e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415027  90 EEQEHLQGTVKSLREELGALQEQLLEKDLEMKQLLQSKIDLEKELETAREGEKGRQEQEQALREEVEALTKKCQELEEAK 169
Cdd:COG1196   260 AELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEEL 339

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415027 170 REEKNSFvavtHEAHPELHApspcSRHSEPDSDNSAGEEgssqppapcsEERREAAIRTLQAQWKAHRRKKREAALDEAA 249
Cdd:COG1196   340 EELEEEL----EEAEEELEE----AEAELAEAEEALLEA----------EAELAEAEEELEELAEELLEALRAAAELAAQ 401
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
73-171 9.04e-06

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 48.32  E-value: 9.04e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415027  73 QPKGDQSPEDLPKVAPCEEQEH------LQGTVKSLREELGALQEQLLEKDLEMKqllqskiDLEKELETAR--EGEKGR 144
Cdd:COG2433   390 LPEEEPEAEREKEHEERELTEEeeeirrLEEQVERLEAEVEELEAELEEKDERIE-------RLERELSEARseERREIR 462

                          90       100
                  ....*....|....*....|....*...
gi 1720415027 145 QEQE-QALREEVEALTKKCQELEEAKRE 171
Cdd:COG2433   463 KDREiSRLDREIERLERELEEERERIEE 490
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 90-269 3.44e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.47  E-value: 3.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415027  90 EEQEHLQGTVKSLREELGALQEQLLEKDLEMKQLLQSKIDLEKELETAREGEKGRQEQEQALREEVEALTKKCQELEEAK 169
Cdd:COG1196   281 LELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAEL 360

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415027 170 REEKNSFVAVTHEAHPELHApspcsRHSEPDSDNSAGEEGSSQppapcsEERREAAIRTLQAQwkAHRRKKREAALDEAA 249
Cdd:COG1196   361 AEAEEALLEAEAELAEAEEE-----LEELAEELLEALRAAAEL------AAQLEELEEAEEAL--LERLERLEEELEELE 427

                         170       180
                  ....*....|....*....|
gi 1720415027 250 TVLQAAFRGHLARSKLVRSK 269
Cdd:COG1196   428 EALAELEEEEEEEEEALEEA 447
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 90-265 3.59e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.47  E-value: 3.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415027  90 EEQEHLQGTVKSLREELGALQEQLLEKDLEMKQLLQSKIDLEKELETAREGEKGRQEQEQALREEVEALTKKCQELEEAK 169
Cdd:COG1196   351 EELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEAL 430

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415027 170 REEKNSFVAVTHEAHPELHApspcsrhsepDSDNSAGEEGSSQPPAPCSEERREAAIRTLQAQWKAHRRKKREAALDEAA 249
Cdd:COG1196   431 AELEEEEEEEEEALEEAAEE----------EAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAE 500

                         170
                  ....*....|....*.
gi 1720415027 250 TVLQAAFRGHLARSKL 265
Cdd:COG1196   501 ADYEGFLEGVKAALLL 516
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
90-176 4.01e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 45.66  E-value: 4.01e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415027  90 EEQEHLQGTVKSLREELGALQEQLLEKDLEMKQLLQSKIDLEKELETAREGEKGRQEQEQALREEVEALTKKCQELEEAK 169
Cdd:COG4372    59 EELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQI 138


                  ....*..
gi 1720415027 170 REEKNSF 176
Cdd:COG4372   139 AELQSEI 145
IQCD cd23767
IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory ...
 238-269 5.07e-05

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: 40.22  E-value: 5.07e-05
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1720415027 238 RKKREAALDEAATVLQAAFRGHLARSKLVRSK 269
Cdd:cd23767     1 EEEELQRMNRAATLIQALWRGYKVRKELKKKK 32
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 90-255 9.39e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 45.31  E-value: 9.39e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415027  90 EEQEHLQGTVKSLREELGALQEQLLEKDLEMKQLLQSKIDLEKELETAREGEKGRQEQEQALREEVEALTKKCQELEEAK 169
Cdd:COG1196   253 AELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEEL 332

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415027 170 REEKnsfvAVTHEAHPELHApspcsrhSEPDSDNSAGEEGSSQppapCSEERREAAIRTLQAQWKAHRRKKREAALDEAA 249
Cdd:COG1196   333 EELE----EELEELEEELEE-------AEEELEEAEAELAEAE----EALLEAEAELAEAEEELEELAEELLEALRAAAE 397


                  ....*.
gi 1720415027 250 TVLQAA 255
Cdd:COG1196   398 LAAQLE 403
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
90-171 1.51e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 44.12  E-value: 1.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415027  90 EEQEHLQGTVKSLREELGALQEQLLEKDLEMKQLLQSKIDLEKELETAREGEKGRQEQEQALREEVEALTKKCQELEEAK 169
Cdd:COG4372    45 EELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKER 124


                  ..
gi 1720415027 170 RE 171
Cdd:COG4372   125 QD 126
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
90-179 3.24e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.22  E-value: 3.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415027  90 EEQEHLQGTVKSLREELGALQEQL-LEKDLEMKQLLQSKIDLEKELETAREGEKGRQEQEQALREEVEALTKKCQELEEA 168
Cdd:COG4717   163 EELEELEAELAELQEELEELLEQLsLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE 242

                          90
                  ....*....|.
gi 1720415027 169 KREEKNSFVAV 179
Cdd:COG4717   243 ERLKEARLLLL 253
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 61-257 4.88e-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: 4.88e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415027   61 LVRSPSNISVQKQPKGDQSPEDLPKVAPCEEQehlqgtVKSLREELGALQEQLLEKDLEMKQLLQSKIDLEKELETAREG 140
Cdd:TIGR02168  314 LERQLEELEAQLEELESKLDELAEELAELEEK------LEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSK 387

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415027  141 EKGRQEQEQALREEVEALTKKCQELEEakREEKNSFVAVTHEAHPELHAPSPCSRHSEpdsdnsagEEGSSQPPAPCSEE 220
Cdd:TIGR02168  388 VAQLELQIASLNNEIERLEARLERLED--RRERLQQEIEELLKKLEEAELKELQAELE--------ELEEELEELQEELE 457

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1720415027  221 RREAAIRTLQAQwkahRRKKREAALDEAATVLQAAFR 257
Cdd:TIGR02168  458 RLEEALEELREE----LEEAEQALDAAERELAQLQAR 490
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
90-183 5.87e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.45  E-value: 5.87e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415027  90 EEQEHLQGTVKSLREELGAL--QEQLLEKDLEMKQLLQSKIDLEKELETAREgekgRQEQEQALREEVEALTKKCQELEE 167
Cdd:COG4717   102 EELEELEAELEELREELEKLekLLQLLPLYQELEALEAELAELPERLEELEE----RLEELRELEEELEELEAELAELQE 177

                          90
                  ....*....|....*.
gi 1720415027 168 AKREEKNSFVAVTHEA 183
Cdd:COG4717   178 ELEELLEQLSLATEEE 193
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
99-168 1.74e-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: 1.74e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720415027   99 VKSLREELGALQEQL--LEK-DLEMKQLLQSKIDLEKELETAREGEKGRQEQEQALREEVEALTKKCQELEEA 168
Cdd:COG4913    663 VASAEREIAELEAELerLDAsSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDR 735
IQ smart00015
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ...
 245-265 1.86e-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: 1.86e-03
                           10        20
                   ....*....|....*....|.
gi 1720415027  245 LDEAATVLQAAFRGHLARSKL 265
Cdd:smart00015   2 LTRAAIIIQAAWRGYLARKRY 22
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 98-168 1.94e-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: 41.20  E-value: 1.94e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720415027   98 TVKSLREELGALQEQLLEKDLEMKQLLQSKIDLEKELETAREGEKGRQEQEQALREEVEALTKKCQELEEA 168
Cdd:TIGR02168  804 ALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESE 874
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 90-180 2.42e-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: 39.52  E-value: 2.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415027  90 EEQEHLQGTVKSLREELGALQEQLLEKDLEMKQL------LQSKID-----------------LEKELETAREGEKGRQE 146
Cdd:COG1579    31 AELAELEDELAALEARLEAAKTELEDLEKEIKRLeleieeVEARIKkyeeqlgnvrnnkeyeaLQKEIESLKRRISDLED 110

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1720415027 147 QEQALREEVEALTKKCQELEEAKREEKNSFVAVT 180
Cdd:COG1579   111 EILELMERIEELEEELAELEAELAELEAELEEKK 144
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 90-171 3.01e-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: 39.14  E-value: 3.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415027  90 EEQEHLQGTVKSLREELGALQEQLLEKDLEMKQLLQSKIDLEKELETAREGEKGRQEQ--------E-QALREEVEALTK 160
Cdd:COG1579    24 HRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQlgnvrnnkEyEALQKEIESLKR 103

                          90
                  ....*....|.
gi 1720415027 161 KCQELEEAKRE 171
Cdd:COG1579   104 RISDLEDEILE 114
PHA03247 PHA03247
large tegument protein UL36; Provisional
 185-502 3.03e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 40.69  E-value: 3.03e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415027  185 PELHAPSPCSRHSEPDSDNSAGEEGSSQPPAPcsEERREAAIRTLqaqwKAHRRKKREAALDEAATVLQAAfrghlaRSK 264
Cdd:PHA03247  2619 PDTHAPDPPPPSPSPAANEPDPHPPPTVPPPE--RPRDDPAPGRV----SRPRRARRLGRAAQASSPPQRP------RRR 2686

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415027  265 LVRSKVPDSRSPSLPGllSPLNQSSPAPRVLSPISPAEENPTQEEaviviQSILRGYLAQARFIASCCREIAASSQRETV 344
Cdd:PHA03247  2687 AARPTVGSLTSLADPP--PPPPTPEPAPHALVSATPLPPGPAAAR-----QASPALPAAPAPPAVPAGPATPGGPARPAR 2759

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415027  345 SLTPSGSASPPSLRAsPEWGPSGKNSEASSGEAAKDEDEAEEPPDLQPYSGVIRKELCASEELRETSASEPAPSVPYSAQ 424
Cdd:PHA03247  2760 PPTTAGPPAPAPPAA-PAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTA 2838

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720415027  425 GGHGDCPSSSSLEAVPSMKDAMCEERSSSPRSAGPSLAEPSPPELQPLSPPPVEDICSDDSDDIIFSPFLPRKKSPSP 502
Cdd:PHA03247  2839 PPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPP 2916
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 92-177 3.12e-03

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


Pssm-ID: 214922 [Multi-domain]  Cd Length: 140  Bit Score: 37.95  E-value: 3.12e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415027   92 QEHLQGTVKSLREELGALQEQLlekdlemKQLLQskiDLEKELETAREGEKGRQEQE-QALREEVEALTKKCQ-ELEEAK 169
Cdd:smart00935  20 QKQLEKEFKKRQAELEKLEKEL-------QKLKE---KLQKDAATLSEAAREKKEKElQKKVQEFQRKQQKLQqDLQKRQ 89


                   ....*...
gi 1720415027  170 REEKNSFV 177
Cdd:smart00935  90 QEELQKIL 97
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 90-173 3.20e-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: 3.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415027  90 EEQEHLQGTVKSLREELGALQEQLLEKDLEMKQLLQSKIDLEKELETAREGEKGRQEQEQALREEVEALTKKCQELEEAK 169
Cdd:COG1196   239 AELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERL 318


                  ....
gi 1720415027 170 REEK 173
Cdd:COG1196   319 EELE 322
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
98-171 3.30e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 40.00  E-value: 3.30e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720415027  98 TVKSLREELGALQEQLLEkdlEMKQLLQSkidLEKELETAREGEKGRQEQEQALREEVEALTKKCQELEEAKRE 171
Cdd:COG3206   292 DVIALRAQIAALRAQLQQ---EAQRILAS---LEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLERE 359
IQ pfam00612
IQ calmodulin-binding motif; Calmodulin-binding motif.
 247-265 3.56e-03

IQ calmodulin-binding motif; Calmodulin-binding motif.


Pssm-ID: 459869  Cd Length: 21  Bit Score: 34.99  E-value: 3.56e-03
                          10
                  ....*....|....*....
gi 1720415027 247 EAATVLQAAFRGHLARSKL 265
Cdd:pfam00612   2 KAAIKIQAAWRGYLARKRY 20
Adgb_C_mid-like cd22307
C-terminal middle region of Androglobins (Adgbs) and related proteins; including permuted ...
 132-274 4.06e-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: 4.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415027 132 KELETA-----REGEKGRQEQEQALREEVEALTKKCQELEEAKrEEKNSFVAVTHEahpelhaPSPCSRHSEPDSDNSAG 206
Cdd:cd22307    57 KELYRSycpplLWSKEDKKEHHKVFNEALYHLLKKALGRKETP-DELFALRALFLD-------PDIGLEYKESPSSSLRE 128

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720415027 207 EEGSSqppaPCSEERREAAIRtlqaqwkahrrkkreaaLDEAATVLQAAFRGHLARsKLVRSKVPDSR 274
Cdd:cd22307   129 IVEPD----ECDCRTREPTIE-----------------EHEAATKIQAFFRGTLVR-KLLKAHKPGTK 174
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 100-173 4.17e-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: 4.17e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720415027 100 KSLREELGALQEQLLEKDLEMKQLLQSKIDLEKELETAREGEKGRQEQEQALREEVEALTKKCQELEEAKREEK 173
Cdd:COG1196   235 RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLE 308
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
93-262 5.81e-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: 5.81e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415027   93 EHLQGTVKSLREELGALQEQLLEKDLEMKQL----------------------LQSKI-DLEKELETAREGE---KGRQE 146
Cdd:COG4913    613 AALEAELAELEEELAEAEERLEALEAELDALqerrealqrlaeyswdeidvasAEREIaELEAELERLDASSddlAALEE 692

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415027  147 QEQALREEVEALTKKCQELEEAKR---EEKNSFVAVTHEAHPELhapspcsrhsepdsdnSAGEEGSSQPPAPCSEERRE 223
Cdd:COG4913    693 QLEELEAELEELEEELDELKGEIGrleKELEQAEEELDELQDRL----------------EAAEDLARLELRALLEERFA 756

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1720415027  224 AAIRTLQ----AQWKAHRRKKREAALDEAATVLQAAFRGHLAR 262
Cdd:COG4913    757 AALGDAVerelRENLEERIDALRARLNRAEEELERAMRAFNRE 799
Tektin pfam03148
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular ...
 99-165 7.69e-03

Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular sites as centrioles, basal bodies, and along ciliary and flagellar doublet microtubules. Tektins form unique protofilaments, organized as longitudinal polymers of tektin heterodimers with axial periodicity matching tubulin. Tektin polypeptides consist of several alpha-helical regions that are predicted to form coiled coils. Indeed, tektins share considerable structural similarities with intermediate filament proteins. Possible functional roles for tektins are: stabilization of tubulin protofilaments; attachment of A and B-tubules in ciliary/flagellar microtubule doublets and C-tubules in centrioles; binding of axonemal components.


Pssm-ID: 460827 [Multi-domain]  Cd Length: 383  Bit Score: 38.68  E-value: 7.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415027  99 VKSLREELgalQEQLLEKDLEMKQLLQSKIDLEKELE-------------TAREGEKG----RQEQEQALREEVEaLTKK 161
Cdd:pfam03148  55 ITFWKSEL---EKELEELDEEIELLLEEKRRLEKALEaleeplhiaqeclTLREKRQGidlvHDEVEKELLKEVE-LIEG 130


                  ....
gi 1720415027 162 CQEL 165
Cdd:pfam03148 131 IQEL 134
MPS2 pfam17060
Monopolar spindle protein 2; Is a fungal transmembrane protein which is part of the component ...
 39-186 7.81e-03

Monopolar spindle protein 2; Is a fungal transmembrane protein which is part of the component of the spindle pole body (SPB) required for the insertion of the nascent SPB into the nuclear envelope and for the proper execution of spindle pole body (SPB) duplication. It seems that Mps2-Spc24 interaction may contribute to the localization of Spc24 and other kinetochore components to the inner plaque of the SPB.


Pssm-ID: 407228 [Multi-domain]  Cd Length: 340  Bit Score: 38.42  E-value: 7.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415027  39 ARKVSSSESPKQSTSELVNPNPLVRSPSNISVQKQPKGDQSPEDLPKVApcEEQEHLQGTVKSLREELGALQEQLLEKDL 118
Cdd:pfam17060  98 ASFISALELKEDVKSSPRSEADSLGTPIKVDLLRNLKPQESPETPRRIN--RKYKSLELRVESMKDELEFKDETIMEKDR 175

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720415027 119 EMKQL------LQSKIDL---EKELETAREGEKGRQEQEQALREEV--EALTKKCQELEEAKREEKNSFVAVTHEAHPE 186
Cdd:pfam17060 176 ELTELtstiskLKDKYDFlsrEFEFYKQHHEHGGNNSIKTATKHEFiiSELKRKLQEQNRLIRILQEQIQFDPGALHDN 254
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 83-174 7.94e-03

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: 38.59  E-value: 7.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415027  83 LPKVAPCEEQEHLQGTVKSLREELGALQEQLLEKDLEMKQLLQSKIDLEKELETAREGEKGRQEQEQALREEVEALTKKC 162
Cdd:COG4942    13 LAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI 92

                          90
                  ....*....|..
gi 1720415027 163 QELEEAKREEKN 174
Cdd:COG4942    93 AELRAELEAQKE 104
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
81-177 9.76e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 38.60  E-value: 9.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415027  81 EDLPKVAPCEEQEHLQGTVKSLREELGALQEQLLEKDLEMKQLLQSKIDLE---KELETAREGEKGRQEQEQaLREEVEA 157
Cdd:COG4717   409 EQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEaelEQLEEDGELAELLQELEE-LKAELRE 487

                          90       100
                  ....*....|....*....|....*..
gi 1720415027 158 LTKK------CQE-LEEAKREEKNSFV 177
Cdd:COG4717   488 LAEEwaalklALElLEEAREEYREERL 514
 
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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