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Conserved domains on  [gi|22325356|ref|NP_671492|]
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PALM2-AKAP2 protein isoform 4 (PALM2-AKAP2) [Homo sapiens]

Protein Classification

Graphical summary

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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 2.61e-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: 2.61e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325356     15 AEKRKRQTEIEGKRQQLDEQILLLQHSKSKVLREKWLLQGIPAGTAEEEEARRRQSEEDEFRVKQLEDNIQRLEQEIQTL 94
Cdd:pfam03285    1 AEKRKRQTEIENKRRQLEDDRRQLQHLKSKALRERWLLEGPPSSASEEDEARRRQEEEDEQKKKLLEEIIRRLEEEIELL 80
                           90       100
                   ....*....|....*....|...
gi 22325356     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 ...
942-1082 4.71e-06

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: 50.13  E-value: 4.71e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325356    942 LRSRKQRTLSMIEEEIRAAQEREEELKRQRQVLQSTQSPRTK--NAPSL-PSRTCYKTApgkiekvkpppspTTEGPSLQ 1018
Cdd:pfam15304  214 LRLGRSQASELLEREVESVLERERELAEQRRNALEVFGPAPFqdSRPSLtASGITGSYS-------------VSESHLFT 280
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22325356   1019 P-DLAPEEAAGTQRPKNLMQTlmedYETHKSKRRERMDDSSVLEATRVNRRKSALALRWEAGIYA 1082
Cdd:pfam15304  281 PiRLHSGLVWTAEAPAPSASG----SHRKKEQWYAGINPLDRVNATRVTRHRNALAERWEAGIYS 341
 
Name Accession Description Interval E-value
Paralemmin pfam03285
Paralemmin;
15-117 2.61e-42

Paralemmin;


Pssm-ID: 460875  Cd Length: 301  Bit Score: 157.21  E-value: 2.61e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325356     15 AEKRKRQTEIEGKRQQLDEQILLLQHSKSKVLREKWLLQGIPAGTAEEEEARRRQSEEDEFRVKQLEDNIQRLEQEIQTL 94
Cdd:pfam03285    1 AEKRKRQTEIENKRRQLEDDRRQLQHLKSKALRERWLLEGPPSSASEEDEARRRQEEEDEQKKKLLEEIIRRLEEEIELL 80
                           90       100
                   ....*....|....*....|...
gi 22325356     95 ESEESQISAKEQIILEKLKETEK 117
Cdd:pfam03285   81 EEESSISAKKENLAEKLLEITVE 103
AKAP2_C pfam15304
A-kinase anchor protein 2 C-terminus; This family includes the C-terminus of A-kinase anchor ...
942-1082 4.71e-06

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: 50.13  E-value: 4.71e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325356    942 LRSRKQRTLSMIEEEIRAAQEREEELKRQRQVLQSTQSPRTK--NAPSL-PSRTCYKTApgkiekvkpppspTTEGPSLQ 1018
Cdd:pfam15304  214 LRLGRSQASELLEREVESVLERERELAEQRRNALEVFGPAPFqdSRPSLtASGITGSYS-------------VSESHLFT 280
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22325356   1019 P-DLAPEEAAGTQRPKNLMQTlmedYETHKSKRRERMDDSSVLEATRVNRRKSALALRWEAGIYA 1082
Cdd:pfam15304  281 PiRLHSGLVWTAEAPAPSASG----SHRKKEQWYAGINPLDRVNATRVTRHRNALAERWEAGIYS 341
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
4-124 4.93e-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: 4.93e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325356    4 AELHKERLQAIAEKRKRQTEIEGKRQQLDEQILLLQHSKSKVLREKwllqgipAGTAEEEEARRRQSEedefRVKQLEDN 83
Cdd:COG1196  249 EELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELL-------AELARLEQDIARLEE----RRRELEER 317
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 22325356   84 IQRLEQEIQTLESEESQISAKEQIILEKLKETEKSFKDFQK 124
Cdd:COG1196  318 LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEA 358
PRK12704 PRK12704
phosphodiesterase; Provisional
17-124 1.14e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 42.84  E-value: 1.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325356    17 KRKRQTEIEGKRQQLdEQILLLQHSKSKVLREKWLLQgipagtAEEEEARRRQSEEDEFRVK--QLEDNIQRLEQEIQTL 94
Cdd:PRK12704   26 KKIAEAKIKEAEEEA-KRILEEAKKEAEAIKKEALLE------AKEEIHKLRNEFEKELRERrnELQKLEKRLLQKEENL 98
                          90       100       110
                  ....*....|....*....|....*....|
gi 22325356    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 2.31e-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: 2.31e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325356      2 AEAELHkERLQAIAEKRKRQTEIEGKRQQLDEQILLLQHSKSKVLREKWLLQGIPAGTAEEEEARRRQSEEDEFRVKQLE 81
Cdd:TIGR02168  237 LREELE-ELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLE 315
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 22325356     82 DNIQRLEQEIQTLESEESQISAKEQIILEKLKETEKSFKDFQK 124
Cdd:TIGR02168  316 RQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEA 358
 
Name Accession Description Interval E-value
Paralemmin pfam03285
Paralemmin;
15-117 2.61e-42

Paralemmin;


Pssm-ID: 460875  Cd Length: 301  Bit Score: 157.21  E-value: 2.61e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325356     15 AEKRKRQTEIEGKRQQLDEQILLLQHSKSKVLREKWLLQGIPAGTAEEEEARRRQSEEDEFRVKQLEDNIQRLEQEIQTL 94
Cdd:pfam03285    1 AEKRKRQTEIENKRRQLEDDRRQLQHLKSKALRERWLLEGPPSSASEEDEARRRQEEEDEQKKKLLEEIIRRLEEEIELL 80
                           90       100
                   ....*....|....*....|...
gi 22325356     95 ESEESQISAKEQIILEKLKETEK 117
Cdd:pfam03285   81 EEESSISAKKENLAEKLLEITVE 103
AKAP2_C pfam15304
A-kinase anchor protein 2 C-terminus; This family includes the C-terminus of A-kinase anchor ...
942-1082 4.71e-06

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: 50.13  E-value: 4.71e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325356    942 LRSRKQRTLSMIEEEIRAAQEREEELKRQRQVLQSTQSPRTK--NAPSL-PSRTCYKTApgkiekvkpppspTTEGPSLQ 1018
Cdd:pfam15304  214 LRLGRSQASELLEREVESVLERERELAEQRRNALEVFGPAPFqdSRPSLtASGITGSYS-------------VSESHLFT 280
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22325356   1019 P-DLAPEEAAGTQRPKNLMQTlmedYETHKSKRRERMDDSSVLEATRVNRRKSALALRWEAGIYA 1082
Cdd:pfam15304  281 PiRLHSGLVWTAEAPAPSASG----SHRKKEQWYAGINPLDRVNATRVTRHRNALAERWEAGIYS 341
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
4-124 4.93e-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: 4.93e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325356    4 AELHKERLQAIAEKRKRQTEIEGKRQQLDEQILLLQHSKSKVLREKwllqgipAGTAEEEEARRRQSEedefRVKQLEDN 83
Cdd:COG1196  249 EELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELL-------AELARLEQDIARLEE----RRRELEER 317
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 22325356   84 IQRLEQEIQTLESEESQISAKEQIILEKLKETEKSFKDFQK 124
Cdd:COG1196  318 LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEA 358
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
8-114 4.68e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 47.60  E-value: 4.68e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325356    8 KERLQA-IAEKRKRQTEIEGKRQQLDEQILLLQHSKSKVLREKWLLQGIPAGTAEEEEARRRQSEEDEF----RVKQLED 82
Cdd:COG4913  340 LEQLEReIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAeaeaALRDLRR 419
                         90       100       110
                 ....*....|....*....|....*....|..
gi 22325356   83 NIQRLEQEIQTLESEESQISAKEQIILEKLKE 114
Cdd:COG4913  420 ELRELEAEIASLERRKSNIPARLLALRDALAE 451
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
9-117 5.68e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 47.07  E-value: 5.68e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325356    9 ERLQAIAEKRKRQTEIEGKRQQLDEQilLLQHSKSkvlREKWLLQGIPAGTAEEEEARRRQSEEDEFRVKQLEDNIQRLE 88
Cdd:COG4717  385 EELRAALEQAEEYQELKEELEELEEQ--LEELLGE---LEELLEALDEEELEEELEELEEELEELEEELEELREELAELE 459
                         90       100       110
                 ....*....|....*....|....*....|.
gi 22325356   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 7.25e-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: 7.25e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325356      1 MAEAELHKERLQAIAEKRKRQTEIEGKRQQLDEqiLLLQHSKskvlrekwllqgipagtaEEEEARRRQSEEdefRVKQL 80
Cdd:pfam15346   53 QVLEELEREREAELEEERRKEEEERKKREELER--ILEENNR------------------KIEEAQRKEAEE---RLAML 109
                           90       100       110
                   ....*....|....*....|....*....|..
gi 22325356     81 EDnIQRLEQEIQTLESEESQISAKEQ-IILEK 111
Cdd:pfam15346  110 EE-QRRMKEERQRREKEEEEREKREQqKILNK 140
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
1-124 1.57e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.91  E-value: 1.57e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325356    1 MAEAELHKERLQAIAEKRKRQTEIEGKRQQLDEQILLLQHSKSKVLREKWLLQGIPAGTAEEEEARRRQSEEDEFRVKQL 80
Cdd:COG4717  118 LEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDL 197
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 22325356   81 EDNIQRLEQEIQTLESEESQISAKEQIILEKLKETEKSFKDFQK 124
Cdd:COG4717  198 AEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAAL 241
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
2-124 2.34e-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: 2.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325356    2 AEAELHKERLQAIAEKRKRQTEIEGKRQQLDEQILLLQHSKSKVLREKWLLQGIPAGTAEEEEAR----------RRQSE 71
Cdd:COG1196  317 RLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELeelaeelleaLRAAA 396
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 22325356   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 2.73e-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: 2.73e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325356    4 AELHKERLQAIAEKRKRQTEIEGKRQQLDEQILLLQHSKSKVLREKWLLQGIPAGTAEEEEARRRQSEEDEFRVKQLEDN 83
Cdd:COG4942  142 KYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQE 221
                         90       100
                 ....*....|....*....|.
gi 22325356   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 6.71e-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: 6.71e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325356      3 EAELHKERLQAIAEKRKRQTEIEGKRQQLDEQillLQHSKSKVLREKWLLQGIPA-----GTAEEEEARRRQSEEDEFRV 77
Cdd:pfam17380  469 EEERKRKKLELEKEKRDRKRAEEQRRKILEKE---LEERKQAMIEEERKRKLLEKemeerQKAIYEEERRREAEEERRKQ 545
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 22325356     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 9.97e-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: 9.97e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325356    4 AELHKERLQA---IAEKRKRQTEIEGKRQQLDEQILLLQhsksKVLREKWLLQGIPAgtAEEE----EARRRQSEEDEFR 76
Cdd:COG4913  613 AALEAELAELeeeLAEAEERLEALEAELDALQERREALQ----RLAEYSWDEIDVAS--AEREiaelEAELERLDASSDD 686
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22325356   77 VKQLEDNIQRLEQEIQTLESEESQISAKEQIILEKLKETEKSFKDFQKGFSSTDGDAVNYISSQL 141
Cdd:COG4913  687 LAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALL 751
PRK12704 PRK12704
phosphodiesterase; Provisional
17-124 1.14e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 42.84  E-value: 1.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325356    17 KRKRQTEIEGKRQQLdEQILLLQHSKSKVLREKWLLQgipagtAEEEEARRRQSEEDEFRVK--QLEDNIQRLEQEIQTL 94
Cdd:PRK12704   26 KKIAEAKIKEAEEEA-KRILEEAKKEAEAIKKEALLE------AKEEIHKLRNEFEKELRERrnELQKLEKRLLQKEENL 98
                          90       100       110
                  ....*....|....*....|....*....|
gi 22325356    95 ESEESQISAKEQIILEKLKETEKSFKDFQK 124
Cdd:PRK12704   99 DRKLELLEKREEELEKKEKELEQKQQELEK 128
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
2-95 1.31e-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: 1.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325356    2 AEAELHKERLQAIAEKRKRQTEIEGKRQQLDEQILLLQHSKSKVLREKWLLQGIPAGTAEEEEARRRQSEEDEFRVKQLE 81
Cdd:COG1196  687 RLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELE 766
                         90
                 ....*....|....
gi 22325356   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 2.31e-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: 2.31e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325356      2 AEAELHkERLQAIAEKRKRQTEIEGKRQQLDEQILLLQHSKSKVLREKWLLQGIPAGTAEEEEARRRQSEEDEFRVKQLE 81
Cdd:TIGR02168  237 LREELE-ELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLE 315
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 22325356     82 DNIQRLEQEIQTLESEESQISAKEQIILEKLKETEKSFKDFQK 124
Cdd:TIGR02168  316 RQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEA 358
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
2-124 2.55e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.85  E-value: 2.55e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325356    2 AEAELHKERLQaIAEKRKRQTEIEGKRQQLDEQILLLQHSKSKVLREKwllqgipAGTAEEEEARRRQSEEDEFRVKQLE 81
Cdd:COG1196  272 LRLELEELELE-LEEAQAEEYELLAELARLEQDIARLEERRRELEERL-------EELEEELAELEEELEELEEELEELE 343
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 22325356   82 DNIQRLEQEIQTLESEESQISAKEQIILEKLKETEKSFKDFQK 124
Cdd:COG1196  344 EELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAE 386
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
8-128 3.18e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.68  E-value: 3.18e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325356    8 KERLQAIAEKRKRQTEIEGKRQQLDEQILLLQHSKSKVLREKWLLQGIpagtAEEEEARRRQSEEDEfRVKQLEDNIQRL 87
Cdd:COG4717   84 EEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLY----QELEALEAELAELPE-RLEELEERLEEL 158
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 22325356   88 EQEIQTLESEESQISAKEQIILEKLK----ETEKSFKDFQKGFSS 128
Cdd:COG4717  159 RELEEELEELEAELAELQEELEELLEqlslATEEELQDLAEELEE 203
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
3-124 4.59e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.20  E-value: 4.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325356     3 EAELHKERlqaIAEKRKRQTEIEGKRQQLDEQILLLQH------SKSKVLREKwlLQGIPAGTAEEEEARRRQSEEDEFR 76
Cdd:PRK03918  232 ELEELKEE---IEELEKELESLEGSKRKLEEKIRELEErieelkKEIEELEEK--VKELKELKEKAEEYIKLSEFYEEYL 306
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 22325356    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 5.39e-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: 5.39e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325356      4 AELHKERLQAIAEKRKRQTEIEGKRQQLDEQI-----------LLLQHSKSKV--LREKWL-LQGIPAGTAEEEEARRRQ 69
Cdd:pfam07888   44 AELLQAQEAANRQREKEKERYKRDREQWERQRrelesrvaelkEELRQSREKHeeLEEKYKeLSASSEELSEEKDALLAQ 123
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22325356     70 SEEDEFRVKQLEDNIQRLEQEIQTLESEESQISAKEQIILEKLKETEKSFKDFQKGFSSTDGD 132
Cdd:pfam07888  124 RAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEE 186
PRK12704 PRK12704
phosphodiesterase; Provisional
3-117 8.04e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 40.15  E-value: 8.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325356     3 EAELHKERLQAIAEKRKRQTEIEGKRQQLDeqiLLLQHSKSKVLREKWLlqgipagtaEEEEARRRQSEEdefrvkQLED 82
Cdd:PRK12704   39 EAKRILEEAKKEAEAIKKEALLEAKEEIHK---LRNEFEKELRERRNEL---------QKLEKRLLQKEE------NLDR 100
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 22325356    83 NIQRLEQEIQTLESEESQISAKEQIILEKLKETEK 117
Cdd:PRK12704  101 KLELLEKREEELEKKEKELEQKQQELEKKEEELEE 135
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
8-107 9.08e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.14  E-value: 9.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325356    8 KERLQAIAEKRKRQTEIEGKRQQLDEQILLLQHSKSkvLREKWLLQGIpAGTAEEEEARRRQSEEdefRVKQLEDNIQRL 87
Cdd:COG4717  152 EERLEELRELEEELEELEAELAELQEELEELLEQLS--LATEEELQDL-AEELEELQQRLAELEE---ELEEAQEELEEL 225
                         90       100
                 ....*....|....*....|
gi 22325356   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.
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