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Conserved domains on  [gi|62632725|ref|NP_001015062|]
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myocilin precursor [Danio rerio]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
OLF pfam02191
Olfactomedin-like domain;
217-470 1.14e-119

Olfactomedin-like domain;


:

Pssm-ID: 460482  Cd Length: 246  Bit Score: 349.91  E-value: 1.14e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62632725   217 LVWVENPEVHRKADsiaGKYGVWMQDPEAKEpygpDMVWRIDSvGSEVRQLFGYENMDQLTRGFPTKVLLLPESVESTGA 296
Cdd:pfam02191   1 LVSVSKPVTVKLSG---GKYGAWMKDPLPPS----DKIYVTDR-GTSGNTLREYASLDDFKNGSPSKKYKLPYPWQGTGH 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62632725   297 TMYKGSLYYQRRLSRTLIRYDLHAESIAARRDLPHAGFHGQFPYSWGGYTDIDLAIDENGLWAIYSTNKAKGAIVISQLD 376
Cdd:pfam02191  73 VVYNGSLYYNKYNSRNIVKYDLTTRTVAARRVLPGAGYNNRFPYSWGGHTDIDLAVDENGLWVIYATEENEGNIVVSKLD 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62632725   377 PHNLEVKGTWETKIRKTSVANAFMICGKLYTVASYTSPNTTVNYMFDTATSQGKAISVPFKNRYRYNSMVDYNSAKRKLY 456
Cdd:pfam02191 153 PETLEVEQTWNTSYPKRSAGNAFMVCGVLYAVRSVNTRREEIFYAFDTYTGKEEAVSIPFPNRYGKISMLDYNPRDKKLY 232

                         250
                  ....*....|....
gi 62632725   457 AWDNYYMVSYSVRL 470
Cdd:pfam02191 233 AWDDGYQVTYPVTF 246
ZapB COG3074
Cell division protein ZapB, interacts with FtsZ [Cell cycle control, cell division, chromosome ...
 101-134 4.72e-06

Cell division protein ZapB, interacts with FtsZ [Cell cycle control, cell division, chromosome partitioning];


:

Pssm-ID: 442308 [Multi-domain]  Cd Length: 79  Bit Score: 44.58  E-value: 4.72e-06
                        10        20        30
                ....*....|....*....|....*....|....
gi 62632725 101 ENAQLKREKQRLDRQVQDLQQRMEELRQEAERLR 134
Cdd:COG3074  26 EVEELKEKNEELEQENEELQSENEELQSENEQLK 59
PRK13729 super family cl42933
conjugal transfer pilus assembly protein TraB; Provisional
 103-187 7.31e-03

conjugal transfer pilus assembly protein TraB; Provisional


The actual alignment was detected with superfamily member PRK13729:

Pssm-ID: 184281 [Multi-domain]  Cd Length: 475  Bit Score: 38.65  E-value: 7.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62632725  103 AQLKREKQRLDRQVQDLQQRMEELRQEAERLRSrpcmQQTSSrvpqKDNSFRPGSGHVPSNLASRP---GNPQEDKSSLR 179
Cdd:PRK13729  86 EEIRRELDVLNKQRGDDQRRIEKLGQDNAALAE----QVKAL----GANPVTATGEPVPQMPASPPgpeGEPQPGNTPVS 157


                 ....*...
gi 62632725  180 DPAwQYSN 187
Cdd:PRK13729 158 FPP-QGSV 164
 
Name Accession Description Interval E-value
OLF pfam02191
Olfactomedin-like domain;
217-470 1.14e-119

Olfactomedin-like domain;


Pssm-ID: 460482  Cd Length: 246  Bit Score: 349.91  E-value: 1.14e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62632725   217 LVWVENPEVHRKADsiaGKYGVWMQDPEAKEpygpDMVWRIDSvGSEVRQLFGYENMDQLTRGFPTKVLLLPESVESTGA 296
Cdd:pfam02191   1 LVSVSKPVTVKLSG---GKYGAWMKDPLPPS----DKIYVTDR-GTSGNTLREYASLDDFKNGSPSKKYKLPYPWQGTGH 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62632725   297 TMYKGSLYYQRRLSRTLIRYDLHAESIAARRDLPHAGFHGQFPYSWGGYTDIDLAIDENGLWAIYSTNKAKGAIVISQLD 376
Cdd:pfam02191  73 VVYNGSLYYNKYNSRNIVKYDLTTRTVAARRVLPGAGYNNRFPYSWGGHTDIDLAVDENGLWVIYATEENEGNIVVSKLD 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62632725   377 PHNLEVKGTWETKIRKTSVANAFMICGKLYTVASYTSPNTTVNYMFDTATSQGKAISVPFKNRYRYNSMVDYNSAKRKLY 456
Cdd:pfam02191 153 PETLEVEQTWNTSYPKRSAGNAFMVCGVLYAVRSVNTRREEIFYAFDTYTGKEEAVSIPFPNRYGKISMLDYNPRDKKLY 232

                         250
                  ....*....|....
gi 62632725   457 AWDNYYMVSYSVRL 470
Cdd:pfam02191 233 AWDDGYQVTYPVTF 246
OLF smart00284
Olfactomedin-like domains;
215-471 3.48e-110

Olfactomedin-like domains;


Pssm-ID: 128580  Cd Length: 255  Bit Score: 326.40  E-value: 3.48e-110
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62632725    215 GDLVWVENPEVHRKADSiaGKYGVWMQDPEAKEPYgPDMVWRIDSVGSEVRQLFGYENMDQLTRGFPTKVLLLPESVEST 294
Cdd:smart00284   1 GGLAGISKPVTLQTSWK--GKSGAWMKDPLWNTTK-KSLYWYMPLNTRVLRSVREYSSMSDFQMGKNPTDHPLPHAGQGT 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62632725    295 GATMYKGSLYYQRRLSRTLIRYDLHAESIAARRDLPHAGFHGQFPYSWGGYTDIDLAIDENGLWAIYSTNKAKGAIVISQ 374
Cdd:smart00284  78 GVVVYNGSLYFNKFNSHDICRFDLTTETYQKEPLLNGAGYNNRFPYAWGGFSDIDLAVDENGLWVIYATEQNAGKIVISK 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62632725    375 LDPHNLEVKGTWETKIRKTSVANAFMICGKLYTVASYTSPNTTVNYMFDTATSQGKAISVPFKNRYRYNSMVDYNSAKRK 454
Cdd:smart00284 158 LNPATLTIENTWITTYNKRSASNAFMICGILYVTRSLGSKGEKVFYAYDTNTGKEGHLDIPFENMYEYISMLDYNPNDRK 237

                          250
                   ....*....|....*..
gi 62632725    455 LYAWDNYYMVSYSVRLG 471
Cdd:smart00284 238 LYAWNNGHLVHYDIALK 254
ZapB COG3074
Cell division protein ZapB, interacts with FtsZ [Cell cycle control, cell division, chromosome ...
 101-134 4.72e-06

Cell division protein ZapB, interacts with FtsZ [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442308 [Multi-domain]  Cd Length: 79  Bit Score: 44.58  E-value: 4.72e-06
                        10        20        30
                ....*....|....*....|....*....|....
gi 62632725 101 ENAQLKREKQRLDRQVQDLQQRMEELRQEAERLR 134
Cdd:COG3074  26 EVEELKEKNEELEQENEELQSENEELQSENEQLK 59
DUF4482 pfam14818
Domain of unknown function (DUF4482); This family is found in eukaryotes, and is approximately ...
 104-155 7.00e-04

Domain of unknown function (DUF4482); This family is found in eukaryotes, and is approximately 140 amino acids in length. The family is found in association with pfam11365.


Pssm-ID: 464333 [Multi-domain]  Cd Length: 138  Bit Score: 39.67  E-value: 7.00e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 62632725   104 QLKREKQRLDRQVQDLQQRMEELRQEAERLRS-----RPCMQQTSSRVP-QKDNSFRP 155
Cdd:pfam14818  24 RFDRERQEWESQKKIMQKKIEQLQREVSLRRKinmneRAKVIDGEKFVPdQKESSSPP 81
bZIP cd14686
Basic leucine zipper (bZIP) domain of bZIP transcription factors: a DNA-binding and ...
 101-135 3.99e-03

Basic leucine zipper (bZIP) domain of bZIP transcription factors: a DNA-binding and dimerization domain; Basic leucine zipper (bZIP) factors comprise one of the most important classes of enhancer-type transcription factors. They act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes including cell survival, learning and memory, lipid metabolism, and cancer progression, among others. They also play important roles in responses to stimuli or stress signals such as cytokines, genotoxic agents, or physiological stresses. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription.


Pssm-ID: 269834 [Multi-domain]  Cd Length: 52  Bit Score: 35.21  E-value: 3.99e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 62632725 101 ENAQLKREKQR-----LDRQVQDLQQRMEELRQEAERLRS 135
Cdd:cd14686  10 EAARRSRERKKerieeLEEEVEELEEENEELKAELEELRA 49
PRK13729 PRK13729
conjugal transfer pilus assembly protein TraB; Provisional
 103-187 7.31e-03

conjugal transfer pilus assembly protein TraB; Provisional


Pssm-ID: 184281 [Multi-domain]  Cd Length: 475  Bit Score: 38.65  E-value: 7.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62632725  103 AQLKREKQRLDRQVQDLQQRMEELRQEAERLRSrpcmQQTSSrvpqKDNSFRPGSGHVPSNLASRP---GNPQEDKSSLR 179
Cdd:PRK13729  86 EEIRRELDVLNKQRGDDQRRIEKLGQDNAALAE----QVKAL----GANPVTATGEPVPQMPASPPgpeGEPQPGNTPVS 157


                 ....*...
gi 62632725  180 DPAwQYSN 187
Cdd:PRK13729 158 FPP-QGSV 164
PRK13922 PRK13922
rod shape-determining protein MreC; Provisional
 94-134 8.80e-03

rod shape-determining protein MreC; Provisional


Pssm-ID: 237560  Cd Length: 276  Bit Score: 38.04  E-value: 8.80e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 62632725   94 SYNQVMGENAQLKREKQRLDRQVQDLQQrmeeLRQEAERLR 134
Cdd:PRK13922  70 SLFDLREENEELKKELLELESRLQELEQ----LEAENARLR 106
 
Name Accession Description Interval E-value
OLF pfam02191
Olfactomedin-like domain;
217-470 1.14e-119

Olfactomedin-like domain;


Pssm-ID: 460482  Cd Length: 246  Bit Score: 349.91  E-value: 1.14e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62632725   217 LVWVENPEVHRKADsiaGKYGVWMQDPEAKEpygpDMVWRIDSvGSEVRQLFGYENMDQLTRGFPTKVLLLPESVESTGA 296
Cdd:pfam02191   1 LVSVSKPVTVKLSG---GKYGAWMKDPLPPS----DKIYVTDR-GTSGNTLREYASLDDFKNGSPSKKYKLPYPWQGTGH 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62632725   297 TMYKGSLYYQRRLSRTLIRYDLHAESIAARRDLPHAGFHGQFPYSWGGYTDIDLAIDENGLWAIYSTNKAKGAIVISQLD 376
Cdd:pfam02191  73 VVYNGSLYYNKYNSRNIVKYDLTTRTVAARRVLPGAGYNNRFPYSWGGHTDIDLAVDENGLWVIYATEENEGNIVVSKLD 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62632725   377 PHNLEVKGTWETKIRKTSVANAFMICGKLYTVASYTSPNTTVNYMFDTATSQGKAISVPFKNRYRYNSMVDYNSAKRKLY 456
Cdd:pfam02191 153 PETLEVEQTWNTSYPKRSAGNAFMVCGVLYAVRSVNTRREEIFYAFDTYTGKEEAVSIPFPNRYGKISMLDYNPRDKKLY 232

                         250
                  ....*....|....
gi 62632725   457 AWDNYYMVSYSVRL 470
Cdd:pfam02191 233 AWDDGYQVTYPVTF 246
OLF smart00284
Olfactomedin-like domains;
215-471 3.48e-110

Olfactomedin-like domains;


Pssm-ID: 128580  Cd Length: 255  Bit Score: 326.40  E-value: 3.48e-110
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62632725    215 GDLVWVENPEVHRKADSiaGKYGVWMQDPEAKEPYgPDMVWRIDSVGSEVRQLFGYENMDQLTRGFPTKVLLLPESVEST 294
Cdd:smart00284   1 GGLAGISKPVTLQTSWK--GKSGAWMKDPLWNTTK-KSLYWYMPLNTRVLRSVREYSSMSDFQMGKNPTDHPLPHAGQGT 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62632725    295 GATMYKGSLYYQRRLSRTLIRYDLHAESIAARRDLPHAGFHGQFPYSWGGYTDIDLAIDENGLWAIYSTNKAKGAIVISQ 374
Cdd:smart00284  78 GVVVYNGSLYFNKFNSHDICRFDLTTETYQKEPLLNGAGYNNRFPYAWGGFSDIDLAVDENGLWVIYATEQNAGKIVISK 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62632725    375 LDPHNLEVKGTWETKIRKTSVANAFMICGKLYTVASYTSPNTTVNYMFDTATSQGKAISVPFKNRYRYNSMVDYNSAKRK 454
Cdd:smart00284 158 LNPATLTIENTWITTYNKRSASNAFMICGILYVTRSLGSKGEKVFYAYDTNTGKEGHLDIPFENMYEYISMLDYNPNDRK 237

                          250
                   ....*....|....*..
gi 62632725    455 LYAWDNYYMVSYSVRLG 471
Cdd:smart00284 238 LYAWNNGHLVHYDIALK 254
ZapB COG3074
Cell division protein ZapB, interacts with FtsZ [Cell cycle control, cell division, chromosome ...
 101-134 4.72e-06

Cell division protein ZapB, interacts with FtsZ [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442308 [Multi-domain]  Cd Length: 79  Bit Score: 44.58  E-value: 4.72e-06
                        10        20        30
                ....*....|....*....|....*....|....
gi 62632725 101 ENAQLKREKQRLDRQVQDLQQRMEELRQEAERLR 134
Cdd:COG3074  26 EVEELKEKNEELEQENEELQSENEELQSENEQLK 59
DUF4482 pfam14818
Domain of unknown function (DUF4482); This family is found in eukaryotes, and is approximately ...
 104-155 7.00e-04

Domain of unknown function (DUF4482); This family is found in eukaryotes, and is approximately 140 amino acids in length. The family is found in association with pfam11365.


Pssm-ID: 464333 [Multi-domain]  Cd Length: 138  Bit Score: 39.67  E-value: 7.00e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 62632725   104 QLKREKQRLDRQVQDLQQRMEELRQEAERLRS-----RPCMQQTSSRVP-QKDNSFRP 155
Cdd:pfam14818  24 RFDRERQEWESQKKIMQKKIEQLQREVSLRRKinmneRAKVIDGEKFVPdQKESSSPP 81
FtsB COG2919
Cell division protein FtsB [Cell cycle control, cell division, chromosome partitioning];
103-137 2.71e-03

Cell division protein FtsB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442163 [Multi-domain]  Cd Length: 96  Bit Score: 37.17  E-value: 2.71e-03
                        10        20        30
                ....*....|....*....|....*....|....*
gi 62632725 103 AQLKREKQRLDRQVQDLQQRMEELRQEAERLRSRP 137
Cdd:COG2919  32 RELRQEIAELEAENAKLKARNAELEAEVADLKDGP 66
ZapB pfam06005
Cell division protein ZapB; ZapB is a non-essential, abundant cell division factor that is ...
 101-136 3.25e-03

Cell division protein ZapB; ZapB is a non-essential, abundant cell division factor that is required for proper Z-ring formation.


Pssm-ID: 428718 [Multi-domain]  Cd Length: 71  Bit Score: 36.09  E-value: 3.25e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 62632725   101 ENAQLKREKQRLDRQVQDLQQRMEELRQEAERLRSR 136
Cdd:pfam06005  26 ENEELKEENEELKEEANELEEENQQLKQERNQWQER 61
DivIC pfam04977
Septum formation initiator; DivIC from B. subtilis is necessary for both vegetative and ...
 104-137 3.68e-03

Septum formation initiator; DivIC from B. subtilis is necessary for both vegetative and sporulation septum formation. These proteins are mainly composed of an amino terminal coiled-coil.


Pssm-ID: 428231 [Multi-domain]  Cd Length: 69  Bit Score: 36.04  E-value: 3.68e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 62632725   104 QLKREKQRLDRQVQDLQQRMEELRQEAERLRSRP 137
Cdd:pfam04977  10 QLKQEIAQLQAEIAKLKQENEELEAEIKDLKSDP 43
bZIP cd14686
Basic leucine zipper (bZIP) domain of bZIP transcription factors: a DNA-binding and ...
 101-135 3.99e-03

Basic leucine zipper (bZIP) domain of bZIP transcription factors: a DNA-binding and dimerization domain; Basic leucine zipper (bZIP) factors comprise one of the most important classes of enhancer-type transcription factors. They act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes including cell survival, learning and memory, lipid metabolism, and cancer progression, among others. They also play important roles in responses to stimuli or stress signals such as cytokines, genotoxic agents, or physiological stresses. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription.


Pssm-ID: 269834 [Multi-domain]  Cd Length: 52  Bit Score: 35.21  E-value: 3.99e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 62632725 101 ENAQLKREKQR-----LDRQVQDLQQRMEELRQEAERLRS 135
Cdd:cd14686  10 EAARRSRERKKerieeLEEEVEELEEENEELKAELEELRA 49
bZIP_CEBP cd14693
Basic leucine zipper (bZIP) domain of CCAAT/enhancer-binding protein (CEBP) and similar ...
 107-136 4.66e-03

Basic leucine zipper (bZIP) domain of CCAAT/enhancer-binding protein (CEBP) and similar proteins: a DNA-binding and dimerization domain; CEBPs (or C/EBPs) are Basic leucine zipper (bZIP) transcription factors that regulate the cell cycle, differentiation, growth, survival, energy metabolism, innate and adaptive immunity, and inflammation, among others. They are also associated with cancer and viral disease. There are six CEBP proteins in mammalian cells including CEBPA (alpha), CEBPB (beta), CEBPG (gamma), CEBPD (delta), and CEBPE (epsilon), which all contain highly conserved bZIP domains at their C-termini and variations at their N-terminal regions. Each possesses unique properties to regulate cell type-specific growth and differentiation. The sixth isoform, CEBPZ (zeta), lacks an intact DNA-binding domain and is excluded from this subfamily. bZIP factors act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription.


Pssm-ID: 269841 [Multi-domain]  Cd Length: 60  Bit Score: 35.61  E-value: 4.66e-03
                        10        20        30
                ....*....|....*....|....*....|
gi 62632725 107 REKQRldRQVQDLQQRMEELRQEAERLRSR 136
Cdd:cd14693  20 REKAK--QRQLETQQKVQELRKENERLQKR 47
Khc_CBD_cc cd23649
cargo binding coiled-coil domain found in kinesin heavy chains; The family includes Drosophila ...
 97-144 5.13e-03

cargo binding coiled-coil domain found in kinesin heavy chains; The family includes Drosophila kinesin-1, also called kinesin heavy chain (Khc), and Homo sapiens kinesin-1 heavy chain, also called conventional kinesin heavy chain/ubiquitous kinesin heavy chain (UKHC). Kinesin is a microtubule-associated force-producing protein that may play a role in organelle transport. Milt and Miro form an essential protein complex that links Khc to mitochondria for light chain-independent, anterograde transport of mitochondria. The family also includes kinesin heavy chain isoform 5A (KIF5A), also called kinesin heavy chain neuron-specific 1/neuronal kinesin heavy chain (NKHC1), and kinesin heavy chain isoform 5C (KIF5C), also called kinesin heavy chain neuron-specific 2 (NKHC2). KIF5A is a microtubule-dependent motor required for slow axonal transport of neurofilament proteins (NFH, NFM and NFL). It can induce formation of neurite-like membrane protrusions in non-neuronal cells in a ZFYVE27-dependent manner. KIF5C is involved in synaptic transmission and mediates dendritic trafficking of mRNAs. Khc comprises an N-terminal motor-domain, followed by a long coiled-coil stalk that mediates homodimerization, and an unstructured tail with regulatory function. The stalk includes the kinesin light chain (Klc) binding region and an alternative cargo binding region. The model corresponds to the cargo binding region, which is responsible for binding of the atypical tropomyosin, aTm1, a cargo adaptor that plays a stabilizing role in the interaction of Khc with RNA.


Pssm-ID: 467880 [Multi-domain]  Cd Length: 70  Bit Score: 35.64  E-value: 5.13e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 62632725  97 QVMGENAQLKREKQRLDRQ-------VQDLQQRMEELRQEAERLRSRpCMQQTSS 144
Cdd:cd23649  15 QLVRQNSTLKKELALAEKKlaarnerIKSLEALLKEAQEKLEKQNQK-FEEQLQR 68
Spc24 pfam08286
Spc24 subunit of Ndc80; Spc24 is a component of the evolutionarily conserved ...
 104-136 6.83e-03

Spc24 subunit of Ndc80; Spc24 is a component of the evolutionarily conserved kinetochore-associated Ndc80 complex and is involved in chromosome segregation


Pssm-ID: 429899 [Multi-domain]  Cd Length: 107  Bit Score: 36.42  E-value: 6.83e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 62632725   104 QLKREKQRLDRQVQDLQQRMEELRQEAERLRSR 136
Cdd:pfam08286   1 ELDNEKFRLAKELNDLESELERLESELAKLKEE 33
PRK13729 PRK13729
conjugal transfer pilus assembly protein TraB; Provisional
 103-187 7.31e-03

conjugal transfer pilus assembly protein TraB; Provisional


Pssm-ID: 184281 [Multi-domain]  Cd Length: 475  Bit Score: 38.65  E-value: 7.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62632725  103 AQLKREKQRLDRQVQDLQQRMEELRQEAERLRSrpcmQQTSSrvpqKDNSFRPGSGHVPSNLASRP---GNPQEDKSSLR 179
Cdd:PRK13729  86 EEIRRELDVLNKQRGDDQRRIEKLGQDNAALAE----QVKAL----GANPVTATGEPVPQMPASPPgpeGEPQPGNTPVS 157


                 ....*...
gi 62632725  180 DPAwQYSN 187
Cdd:PRK13729 158 FPP-QGSV 164
PRK13922 PRK13922
rod shape-determining protein MreC; Provisional
 94-134 8.80e-03

rod shape-determining protein MreC; Provisional


Pssm-ID: 237560  Cd Length: 276  Bit Score: 38.04  E-value: 8.80e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 62632725   94 SYNQVMGENAQLKREKQRLDRQVQDLQQrmeeLRQEAERLR 134
Cdd:PRK13922  70 SLFDLREENEELKKELLELESRLQELEQ----LEAENARLR 106
 
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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