NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2619680066|sp|Q9Y2D5|]
View 

RecName: Full=PALM2-AKAP2 fusion protein; AltName: Full=A-kinase anchor protein 2; Short=AKAP-2; AltName: Full=AKAP-KL; AltName: Full=Paralemmin A kinase anchor protein; AltName: Full=Paralemmin-2; AltName: Full=Protein kinase A-anchoring protein 2; Short=PRKA2

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
MYO6_MIU_linker super family cl46503
MIU-linker domain found in unconventional myosin-VI; Myosins are actin-based motor molecules ...
 15-117 2.29e-42

MIU-linker domain found in unconventional myosin-VI; Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins function in intracellular movements. Myosin-VI, also called unconventional myosin-6 (MYO6), is a reverse-direction motor protein that moves towards the minus-end of actin filaments. It is required for the structural integrity of the Golgi apparatus via the p53-dependent pro-survival pathway. It appears to be involved in a very early step of clathrin-mediated endocytosis in polarized epithelial cells. It modulates RNA polymerase II-dependent transcription. As part of the DISP complex, Myosin-VI may regulate the association of septins with actin and thereby regulate the actin cytoskeleton. Myosin-VI is encoded by the MYO6 gene, the human homologue of the gene responsible for deafness in Snell's waltzer mice. It is mutated in autosomal dominant nonsyndromic hearing loss. This model corresponds to a conserved region of myosin-VI, which consist of three helices: MIU (Motif Interacting with Ubiquitin), a common linker helix (linker-alpha1) and an isoform-specific helix (linker-alpha2).


The actual alignment was detected with superfamily member pfam03285:

Pssm-ID: 480843  Cd Length: 301  Bit Score: 157.21  E-value: 2.29e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619680066   15 AEKRKRQTEIEGKRQQLDEQILLLQHSKSKVLREKWLLQGIPAGTAEEEEARRRQSEEDEFRVKQLEDNIQRLEQEIQTL 94
Cdd:pfam03285    1 AEKRKRQTEIENKRRQLEDDRRQLQHLKSKALRERWLLEGPPSSASEEDEARRRQEEEDEQKKKLLEEIIRRLEEEIELL 80

                           90       100
                   ....*....|....*....|...
gi 2619680066   95 ESEESQISAKEQIILEKLKETEK 117
Cdd:pfam03285   81 EEESSISAKKENLAEKLLEITVE 103
AKAP2_C super family cl21150
A-kinase anchor protein 2 C-terminus; This family includes the C-terminus of A-kinase anchor ...
 942-1095 7.98e-05

A-kinase anchor protein 2 C-terminus; This family includes the C-terminus of A-kinase anchor protein 2 (AKAP2). It includes the site where the regulatory subunits (RII) of protein kinase AII binds.


The actual alignment was detected with superfamily member pfam15304:

Pssm-ID: 464630  Cd Length: 341  Bit Score: 46.28  E-value: 7.98e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619680066  942 LRSRKQRTLSMIEEEIRAAQEREEELKRQRQVLQSTQSPRTK--NAPSL-PSRTCYKTApgkiekvkpppspTTEGPSLQ 1018
Cdd:pfam15304  214 LRLGRSQASELLEREVESVLERERELAEQRRNALEVFGPAPFqdSRPSLtASGITGSYS-------------VSESHLFT 280

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2619680066 1019 P-DLAPEEAAGTQRPKNlmqtlmEDYETHKSKRRERMDDSSytskllsckvtSEVLEATRVNRRKSALALRWEAGIYA 1095
Cdd:pfam15304  281 PiRLHSGLVWTAEAPAP------SASGSHRKKEQWYAGINP-----------LDRVNATRVTRHRNALAERWEAGIYS 341
 
Name Accession Description Interval E-value
Paralemmin pfam03285
Paralemmin;
15-117 2.29e-42

Paralemmin;


Pssm-ID: 460875  Cd Length: 301  Bit Score: 157.21  E-value: 2.29e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619680066   15 AEKRKRQTEIEGKRQQLDEQILLLQHSKSKVLREKWLLQGIPAGTAEEEEARRRQSEEDEFRVKQLEDNIQRLEQEIQTL 94
Cdd:pfam03285    1 AEKRKRQTEIENKRRQLEDDRRQLQHLKSKALRERWLLEGPPSSASEEDEARRRQEEEDEQKKKLLEEIIRRLEEEIELL 80

                           90       100
                   ....*....|....*....|...
gi 2619680066   95 ESEESQISAKEQIILEKLKETEK 117
Cdd:pfam03285   81 EEESSISAKKENLAEKLLEITVE 103
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 4-124 4.22e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.09  E-value: 4.22e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619680066    4 AELHKERLQAIAEKRKRQTEIEGKRQQLDEQILLLQHSKSKVLREKwllqgipAGTAEEEEARRRQSEedefRVKQLEDN 83
Cdd:COG1196    249 EELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELL-------AELARLEQDIARLEE----RRRELEER 317

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 2619680066   84 IQRLEQEIQTLESEESQISAKEQIILEKLKETEKSFKDFQK 124
Cdd:COG1196    318 LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEA 358
AKAP2_C pfam15304
A-kinase anchor protein 2 C-terminus; This family includes the C-terminus of A-kinase anchor ...
 942-1095 7.98e-05

A-kinase anchor protein 2 C-terminus; This family includes the C-terminus of A-kinase anchor protein 2 (AKAP2). It includes the site where the regulatory subunits (RII) of protein kinase AII binds.


Pssm-ID: 464630  Cd Length: 341  Bit Score: 46.28  E-value: 7.98e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619680066  942 LRSRKQRTLSMIEEEIRAAQEREEELKRQRQVLQSTQSPRTK--NAPSL-PSRTCYKTApgkiekvkpppspTTEGPSLQ 1018
Cdd:pfam15304  214 LRLGRSQASELLEREVESVLERERELAEQRRNALEVFGPAPFqdSRPSLtASGITGSYS-------------VSESHLFT 280

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2619680066 1019 P-DLAPEEAAGTQRPKNlmqtlmEDYETHKSKRRERMDDSSytskllsckvtSEVLEATRVNRRKSALALRWEAGIYA 1095
Cdd:pfam15304  281 PiRLHSGLVWTAEAPAP------SASGSHRKKEQWYAGINP-----------LDRVNATRVTRHRNALAERWEAGIYS 341
PRK12704 PRK12704
phosphodiesterase; Provisional
 17-124 1.08e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 42.84  E-value: 1.08e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619680066   17 KRKRQTEIEGKRQQLdEQILLLQHSKSKVLREKWLLQgipagtAEEEEARRRQSEEDEFRVK--QLEDNIQRLEQEIQTL 94
Cdd:PRK12704    26 KKIAEAKIKEAEEEA-KRILEEAKKEAEAIKKEALLE------AKEEIHKLRNEFEKELRERrnELQKLEKRLLQKEENL 98

                           90       100       110
                   ....*....|....*....|....*....|
gi 2619680066   95 ESEESQISAKEQIILEKLKETEKSFKDFQK 124
Cdd:PRK12704    99 DRKLELLEKREEELEKKEKELEQKQQELEK 128
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 2-124 2.28e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 42.35  E-value: 2.28e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619680066    2 AEAELHkERLQAIAEKRKRQTEIEGKRQQLDEQILLLQHSKSKVLREKWLLQGIPAGTAEEEEARRRQSEEDEFRVKQLE 81
Cdd:TIGR02168  237 LREELE-ELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLE 315

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 2619680066   82 DNIQRLEQEIQTLESEESQISAKEQIILEKLKETEKSFKDFQK 124
Cdd:TIGR02168  316 RQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEA 358
 
Name Accession Description Interval E-value
Paralemmin pfam03285
Paralemmin;
15-117 2.29e-42

Paralemmin;


Pssm-ID: 460875  Cd Length: 301  Bit Score: 157.21  E-value: 2.29e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619680066   15 AEKRKRQTEIEGKRQQLDEQILLLQHSKSKVLREKWLLQGIPAGTAEEEEARRRQSEEDEFRVKQLEDNIQRLEQEIQTL 94
Cdd:pfam03285    1 AEKRKRQTEIENKRRQLEDDRRQLQHLKSKALRERWLLEGPPSSASEEDEARRRQEEEDEQKKKLLEEIIRRLEEEIELL 80

                           90       100
                   ....*....|....*....|...
gi 2619680066   95 ESEESQISAKEQIILEKLKETEK 117
Cdd:pfam03285   81 EEESSISAKKENLAEKLLEITVE 103
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 4-124 4.22e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.09  E-value: 4.22e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619680066    4 AELHKERLQAIAEKRKRQTEIEGKRQQLDEQILLLQHSKSKVLREKwllqgipAGTAEEEEARRRQSEedefRVKQLEDN 83
Cdd:COG1196    249 EELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELL-------AELARLEQDIARLEE----RRRELEER 317

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 2619680066   84 IQRLEQEIQTLESEESQISAKEQIILEKLKETEKSFKDFQK 124
Cdd:COG1196    318 LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEA 358
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
8-114 4.04e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 47.99  E-value: 4.04e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619680066    8 KERLQA-IAEKRKRQTEIEGKRQQLDEQILLLQHSKSKVLREKWLLQGIPAGTAEEEEARRRQSEEDEF----RVKQLED 82
Cdd:COG4913    340 LEQLEReIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAeaeaALRDLRR 419

                           90       100       110
                   ....*....|....*....|....*....|..
gi 2619680066   83 NIQRLEQEIQTLESEESQISAKEQIILEKLKE 114
Cdd:COG4913    420 ELRELEAEIASLERRKSNIPARLLALRDALAE 451
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
9-117 5.20e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 47.45  E-value: 5.20e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619680066    9 ERLQAIAEKRKRQTEIEGKRQQLDEQilLLQHSKSkvlREKWLLQGIPAGTAEEEEARRRQSEEDEFRVKQLEDNIQRLE 88
Cdd:COG4717    385 EELRAALEQAEEYQELKEELEELEEQ--LEELLGE---LEELLEALDEEELEEELEELEEELEELEEELEELREELAELE 459

                           90       100       110
                   ....*....|....*....|....*....|.
gi 2619680066   89 QEIQTLESEE--SQISAKEQIILEKLKETEK 117
Cdd:COG4717    460 AELEQLEEDGelAELLQELEELKAELRELAE 490
ARGLU pfam15346
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ...
 1-111 5.96e-05

Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is required for the oestrogen-dependent expression of ESR1 target genes. It functions in cooperation with MED1. The family of proteins is found in eukaryotes.


Pssm-ID: 405931 [Multi-domain]  Cd Length: 151  Bit Score: 44.27  E-value: 5.96e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619680066    1 MAEAELHKERLQAIAEKRKRQTEIEGKRQQLDEqiLLLQHSKskvlrekwllqgipagtaEEEEARRRQSEEdefRVKQL 80
Cdd:pfam15346   53 QVLEELEREREAELEEERRKEEEERKKREELER--ILEENNR------------------KIEEAQRKEAEE---RLAML 109

                           90       100       110
                   ....*....|....*....|....*....|..
gi 2619680066   81 EDnIQRLEQEIQTLESEESQISAKEQ-IILEK 111
Cdd:pfam15346  110 EE-QRRMKEERQRREKEEEEREKREQqKILNK 140
AKAP2_C pfam15304
A-kinase anchor protein 2 C-terminus; This family includes the C-terminus of A-kinase anchor ...
 942-1095 7.98e-05

A-kinase anchor protein 2 C-terminus; This family includes the C-terminus of A-kinase anchor protein 2 (AKAP2). It includes the site where the regulatory subunits (RII) of protein kinase AII binds.


Pssm-ID: 464630  Cd Length: 341  Bit Score: 46.28  E-value: 7.98e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619680066  942 LRSRKQRTLSMIEEEIRAAQEREEELKRQRQVLQSTQSPRTK--NAPSL-PSRTCYKTApgkiekvkpppspTTEGPSLQ 1018
Cdd:pfam15304  214 LRLGRSQASELLEREVESVLERERELAEQRRNALEVFGPAPFqdSRPSLtASGITGSYS-------------VSESHLFT 280

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2619680066 1019 P-DLAPEEAAGTQRPKNlmqtlmEDYETHKSKRRERMDDSSytskllsckvtSEVLEATRVNRRKSALALRWEAGIYA 1095
Cdd:pfam15304  281 PiRLHSGLVWTAEAPAP------SASGSHRKKEQWYAGINP-----------LDRVNATRVTRHRNALAERWEAGIYS 341
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
1-124 1.37e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.91  E-value: 1.37e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619680066    1 MAEAELHKERLQAIAEKRKRQTEIEGKRQQLDEQILLLQHSKSKVLREKWLLQGIPAGTAEEEEARRRQSEEDEFRVKQL 80
Cdd:COG4717    118 LEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDL 197

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 2619680066   81 EDNIQRLEQEIQTLESEESQISAKEQIILEKLKETEKSFKDFQK 124
Cdd:COG4717    198 AEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAAL 241
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 2-124 2.22e-04

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: 2.22e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619680066    2 AEAELHKERLQAIAEKRKRQTEIEGKRQQLDEQILLLQHSKSKVLREKWLLQGIPAGTAEEEEAR----------RRQSE 71
Cdd:COG1196    317 RLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELeelaeelleaLRAAA 396

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2619680066   72 EDEFRVKQLEDNIQRLEQEIQTLESEESQISAKEQIILEKLKETEKSFKDFQK 124
Cdd:COG1196    397 ELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAE 449
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 4-104 2.61e-04

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: 44.75  E-value: 2.61e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619680066    4 AELHKERLQAIAEKRKRQTEIEGKRQQLDEQILLLQHSKSKVLREKWLLQGIPAGTAEEEEARRRQSEEDEFRVKQLEDN 83
Cdd:COG4942    142 KYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQE 221

                           90       100
                   ....*....|....*....|.
gi 2619680066   84 IQRLEQEIQTLESEESQISAK 104
Cdd:COG4942    222 AEELEALIARLEAEAAAAAER 242
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 3-123 6.30e-04

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 43.96  E-value: 6.30e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619680066    3 EAELHKERLQAIAEKRKRQTEIEGKRQQLDEQillLQHSKSKVLREKWLLQGIPA-----GTAEEEEARRRQSEEDEFRV 77
Cdd:pfam17380  469 EEERKRKKLELEKEKRDRKRAEEQRRKILEKE---LEERKQAMIEEERKRKLLEKemeerQKAIYEEERRREAEEERRKQ 545

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 2619680066   78 KQLEDNiQRLEQEIQTLESEESQISA--KEQIILEKLKETEKSFKDFQ 123
Cdd:pfam17380  546 QEMEER-RRIQEQMRKATEERSRLEAmeREREMMRQIVESEKARAEYE 592
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
4-141 9.29e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 43.37  E-value: 9.29e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619680066    4 AELHKERLQA---IAEKRKRQTEIEGKRQQLDEQILLLQhsksKVLREKWLLQGIPAgtAEEE----EARRRQSEEDEFR 76
Cdd:COG4913    613 AALEAELAELeeeLAEAEERLEALEAELDALQERREALQ----RLAEYSWDEIDVAS--AEREiaelEAELERLDASSDD 686

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2619680066   77 VKQLEDNIQRLEQEIQTLESEESQISAKEQIILEKLKETEKSFKDFQKGFSSTDGDAVNYISSQL 141
Cdd:COG4913    687 LAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALL 751
PRK12704 PRK12704
phosphodiesterase; Provisional
 17-124 1.08e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 42.84  E-value: 1.08e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619680066   17 KRKRQTEIEGKRQQLdEQILLLQHSKSKVLREKWLLQgipagtAEEEEARRRQSEEDEFRVK--QLEDNIQRLEQEIQTL 94
Cdd:PRK12704    26 KKIAEAKIKEAEEEA-KRILEEAKKEAEAIKKEALLE------AKEEIHKLRNEFEKELRERrnELQKLEKRLLQKEENL 98

                           90       100       110
                   ....*....|....*....|....*....|
gi 2619680066   95 ESEESQISAKEQIILEKLKETEKSFKDFQK 124
Cdd:PRK12704    99 DRKLELLEKREEELEKKEKELEQKQQELEK 128
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 2-95 1.26e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.00  E-value: 1.26e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619680066    2 AEAELHKERLQAIAEKRKRQTEIEGKRQQLDEQILLLQHSKSKVLREKWLLQGIPAGTAEEEEARRRQSEEDEFRVKQLE 81
Cdd:COG1196    687 RLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELE 766

                           90
                   ....*....|....
gi 2619680066   82 DNIQRLEQEIQTLE 95
Cdd:COG1196    767 RELERLEREIEALG 780
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 2-124 2.28e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 42.35  E-value: 2.28e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619680066    2 AEAELHkERLQAIAEKRKRQTEIEGKRQQLDEQILLLQHSKSKVLREKWLLQGIPAGTAEEEEARRRQSEEDEFRVKQLE 81
Cdd:TIGR02168  237 LREELE-ELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLE 315

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 2619680066   82 DNIQRLEQEIQTLESEESQISAKEQIILEKLKETEKSFKDFQK 124
Cdd:TIGR02168  316 RQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEA 358
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 2-124 2.34e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.23  E-value: 2.34e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619680066    2 AEAELHKERLQ------AIAEKRKRQTEIEGKRQQLDEQILLLQHSKSKVLREKwllqgipAGTAEEEEARRRQSEEDEF 75
Cdd:COG1196    265 LEAELEELRLEleelelELEEAQAEEYELLAELARLEQDIARLEERRRELEERL-------EELEEELAELEEELEELEE 337

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 2619680066   76 RVKQLEDNIQRLEQEIQTLESEESQISAKEQIILEKLKETEKSFKDFQK 124
Cdd:COG1196    338 ELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAE 386
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
8-128 2.99e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.68  E-value: 2.99e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619680066    8 KERLQAIAEKRKRQTEIEGKRQQLDEQILLLQHSKSKVLREKWLLQGIpagtAEEEEARRRQSEEDEfRVKQLEDNIQRL 87
Cdd:COG4717     84 EEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLY----QELEALEAELAELPE-RLEELEERLEEL 158

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 2619680066   88 EQEIQTLESEESQISAKEQIILEKLK----ETEKSFKDFQKGFSS 128
Cdd:COG4717    159 RELEEELEELEAELAELQEELEELLEqlslATEEELQDLAEELEE 203
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
3-124 4.73e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.20  E-value: 4.73e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619680066    3 EAELHKERlqaIAEKRKRQTEIEGKRQQLDEQILLLQH------SKSKVLREKwlLQGIPAGTAEEEEARRRQSEEDEFR 76
Cdd:PRK03918   232 ELEELKEE---IEELEKELESLEGSKRKLEEKIRELEErieelkKEIEELEEK--VKELKELKEKAEEYIKLSEFYEEYL 306

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 2619680066   77 VK--QLEDNIQRLEQEIQTLESEESQISAKEqiilEKLKETEKSFKDFQK 124
Cdd:PRK03918   307 DElrEIEKRLSRLEEEINGIEERIKELEEKE----ERLEELKKKLKELEK 352
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 4-132 5.10e-03

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


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 40.65  E-value: 5.10e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619680066    4 AELHKERLQAIAEKRKRQTEIEGKRQQLDEQI-----------LLLQHSKSKV--LREKWL-LQGIPAGTAEEEEARRRQ 69
Cdd:pfam07888   44 AELLQAQEAANRQREKEKERYKRDREQWERQRrelesrvaelkEELRQSREKHeeLEEKYKeLSASSEELSEEKDALLAQ 123

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2619680066   70 SEEDEFRVKQLEDNIQRLEQEIQTLESEESQISAKEQIILEKLKETEKSFKDFQKGFSSTDGD 132
Cdd:pfam07888  124 RAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEE 186
PRK12704 PRK12704
phosphodiesterase; Provisional
 3-117 7.81e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 40.15  E-value: 7.81e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619680066    3 EAELHKERLQAIAEKRKRQTEIEGKRQQLDeqiLLLQHSKSKVLREKWLlqgipagtaEEEEARRRQSEEdefrvkQLED 82
Cdd:PRK12704    39 EAKRILEEAKKEAEAIKKEALLEAKEEIHK---LRNEFEKELRERRNEL---------QKLEKRLLQKEE------NLDR 100

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 2619680066   83 NIQRLEQEIQTLESEESQISAKEQIILEKLKETEK 117
Cdd:PRK12704   101 KLELLEKREEELEKKEKELEQKQQELEKKEEELEE 135
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
8-107 8.17e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.14  E-value: 8.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619680066    8 KERLQAIAEKRKRQTEIEGKRQQLDEQILLLQHSKSkvLREKWLLQGIpAGTAEEEEARRRQSEEdefRVKQLEDNIQRL 87
Cdd:COG4717    152 EERLEELRELEEELEELEAELAELQEELEELLEQLS--LATEEELQDL-AEELEELQQRLAELEE---ELEEAQEELEEL 225

                           90       100
                   ....*....|....*....|
gi 2619680066   88 EQEIQTLESEESQISAKEQI 107
Cdd:COG4717    226 EEELEQLENELEAAALEERL 245
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH