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Conserved domains on  [gi|156546890|ref|NP_079225|]
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protein WWC2 isoform 2 [Homo sapiens]

Protein Classification

WW and C2_Kibra domain-containing protein( domain architecture ID 13628918)

protein containing domains WW, Smc, C2_Kibra, and PRK10929

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
C2_Kibra cd08680
C2 domain found in Human protein Kibra; Kibra is thought to be a regulator of the Salvador ...
 700-823 2.31e-60

C2 domain found in Human protein Kibra; Kibra is thought to be a regulator of the Salvador (Sav)/Warts (Wts)/Hippo (Hpo) (SWH) signaling network, which limits tissue growth by inhibiting cell proliferation and promoting apoptosis. The core of the pathway consists of a MST and LATS family kinase cascade that ultimately phosphorylates and inactivates the YAP/Yorkie (Yki) transcription coactivator. The FERM domain proteins Merlin (Mer) and Expanded (Ex) are part of the upstream regulation controlling pathway mechanism. Kibra colocalizes and associates with Mer and Ex and is thought to transduce an extracellular signal via the SWH network. The apical scaffold machinery that contains Hpo, Wts, and Ex recruits Yki to the apical membrane facilitating its inhibitory phosphorlyation by Wts. Since Kibra associates with Ex and is apically located it is hypothesized that KIBRA is part of the scaffold, helps in the Hpo/Wts complex, and helps recruit Yki for inactivation that promotes SWH pathway activity. Kibra contains two amino-terminal WW domains, an internal C2-like domain, and a carboxy-terminal glutamic acid-rich stretch. The C2 domain was first identified in PKC. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions.


:

Pssm-ID: 176062  Cd Length: 124  Bit Score: 202.08  E-value: 2.31e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156546890  700 AQVQIGLRYNAKSSSFMVIIAQLRNLHAFLIPHTSKVYFRVAVLPSSTDVSCLFRTKVHPPTESILFNDVFRVAISQTAL 779
Cdd:cd08680     1 AQVQIGLRYDSGDSSLVISVEQLRNLSALSIPENSKVYVRVALLPCSSSTSCLFRTKALEDQDKPVFNEVFRVPISSTKL 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 156546890  780 QQKTLRVDLCSVSKHRREECLAGTQISLADLPFSSEVFTLWYNL 823
Cdd:cd08680    81 YQKTLQVDVCSVGPDQQEECLGGAQISLADFESSEEMSTKWYNL 124
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 12-41 1.08e-10

WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds proline-rich peptide motifs in vitro.


:

Pssm-ID: 459800 [Multi-domain]  Cd Length: 30  Bit Score: 57.13  E-value: 1.08e-10
                           10        20        30
                   ....*....|....*....|....*....|
gi 156546890    12 LPRGWEEARDYDGKVFYIDHNTRRTSWIDP 41
Cdd:pfam00397    1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 59-88 7.11e-08

WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds proline-rich peptide motifs in vitro.


:

Pssm-ID: 459800 [Multi-domain]  Cd Length: 30  Bit Score: 49.43  E-value: 7.11e-08
                           10        20        30
                   ....*....|....*....|....*....|
gi 156546890    59 LPWGWEAGFDPQIGVYYIDHINKTTQIEDP 88
Cdd:pfam00397    1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 173-430 3.64e-05

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: 48.01  E-value: 3.64e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156546890  173 LRVKKLKRELSQMKQELLYKEqgfetLQQIDKKMSGGQSGYELSEAK--AILTELKSIRKAISSGEKEKQDLMQSLAKLQ 250
Cdd:COG1196   213 ERYRELKEELKELEAELLLLK-----LRELEAELEELEAELEELEAEleELEAELAELEAELEELRLELEELELELEEAQ 287

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156546890  251 ERFH-LDQNIGRSEPDLRcspvnsHLCLSRQ---------TLDAGSQTSISGDIGVRSRSNLAEKVRLSLQYEEAKRSMA 320
Cdd:COG1196   288 AEEYeLLAELARLEQDIA------RLEERRReleerleelEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELA 361

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156546890  321 NLKIELSKLDS------EAWpgaLDIEKEKLMLINEKEELLKELQFVTPQ-KRTQDELERLEAERQRLEEELLSVRgtpS 393
Cdd:COG1196   362 EAEEALLEAEAelaeaeEEL---EELAEELLEALRAAAELAAQLEELEEAeEALLERLERLEEELEELEEALAELE---E 435

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 156546890  394 RALAERLRLEERRKELLQKLEETTKLTTYLHSQLKSL 430
Cdd:COG1196   436 EEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEA 472
PRK10929 super family cl35973
putative mechanosensitive channel protein; Provisional
 1079-1161 1.59e-03

putative mechanosensitive channel protein; Provisional


The actual alignment was detected with superfamily member PRK10929:

Pssm-ID: 236798 [Multi-domain]  Cd Length: 1109  Bit Score: 42.73  E-value: 1.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156546890 1079 RQSRLNDELQALR----DLRQK-----LE--ELKAQGETDLPPGVLEDERFQRLLKQAEKQAEQS----KEEQKQglnAE 1143
Cdd:PRK10929  216 RSQQLDAYLQALRnqlnSQRQReaeraLEstELLAEQSGDLPKSIVAQFKINRELSQALNQQAQRmdliASQQRQ---AA 292

                          90
                  ....*....|....*...
gi 156546890 1144 KLMRQVSKDVCRLREQSQ 1161
Cdd:PRK10929  293 SQTLQVRQALNTLREQSQ 310
 
Name Accession Description Interval E-value
C2_Kibra cd08680
C2 domain found in Human protein Kibra; Kibra is thought to be a regulator of the Salvador ...
 700-823 2.31e-60

C2 domain found in Human protein Kibra; Kibra is thought to be a regulator of the Salvador (Sav)/Warts (Wts)/Hippo (Hpo) (SWH) signaling network, which limits tissue growth by inhibiting cell proliferation and promoting apoptosis. The core of the pathway consists of a MST and LATS family kinase cascade that ultimately phosphorylates and inactivates the YAP/Yorkie (Yki) transcription coactivator. The FERM domain proteins Merlin (Mer) and Expanded (Ex) are part of the upstream regulation controlling pathway mechanism. Kibra colocalizes and associates with Mer and Ex and is thought to transduce an extracellular signal via the SWH network. The apical scaffold machinery that contains Hpo, Wts, and Ex recruits Yki to the apical membrane facilitating its inhibitory phosphorlyation by Wts. Since Kibra associates with Ex and is apically located it is hypothesized that KIBRA is part of the scaffold, helps in the Hpo/Wts complex, and helps recruit Yki for inactivation that promotes SWH pathway activity. Kibra contains two amino-terminal WW domains, an internal C2-like domain, and a carboxy-terminal glutamic acid-rich stretch. The C2 domain was first identified in PKC. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions.


Pssm-ID: 176062  Cd Length: 124  Bit Score: 202.08  E-value: 2.31e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156546890  700 AQVQIGLRYNAKSSSFMVIIAQLRNLHAFLIPHTSKVYFRVAVLPSSTDVSCLFRTKVHPPTESILFNDVFRVAISQTAL 779
Cdd:cd08680     1 AQVQIGLRYDSGDSSLVISVEQLRNLSALSIPENSKVYVRVALLPCSSSTSCLFRTKALEDQDKPVFNEVFRVPISSTKL 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 156546890  780 QQKTLRVDLCSVSKHRREECLAGTQISLADLPFSSEVFTLWYNL 823
Cdd:cd08680    81 YQKTLQVDVCSVGPDQQEECLGGAQISLADFESSEEMSTKWYNL 124
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 12-41 1.08e-10

WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds proline-rich peptide motifs in vitro.


Pssm-ID: 459800 [Multi-domain]  Cd Length: 30  Bit Score: 57.13  E-value: 1.08e-10
                           10        20        30
                   ....*....|....*....|....*....|
gi 156546890    12 LPRGWEEARDYDGKVFYIDHNTRRTSWIDP 41
Cdd:pfam00397    1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
 11-43 9.27e-10

Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds proline-rich polypeptides.


Pssm-ID: 197736 [Multi-domain]  Cd Length: 33  Bit Score: 54.91  E-value: 9.27e-10
                            10        20        30
                    ....*....|....*....|....*....|...
gi 156546890     11 PLPRGWEEARDYDGKVFYIDHNTRRTSWIDPRD 43
Cdd:smart00456    1 PLPPGWEERKDPDGRPYYYNHETKETQWEKPRE 33
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
 13-43 2.68e-09

Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; functions as an interaction module in a diverse set of signalling proteins; binds specific proline-rich sequences but at low affinities compared to other peptide recognition proteins such as antibodies and receptors; WW domains have a single groove formed by a conserved Trp and Tyr which recognizes a pair of residues of the sequence X-Pro; variable loops and neighboring domains confer specificity in this domain; there are five distinct groups based on binding: 1) PPXY motifs 2) the PPLP motif; 3) PGM motifs; 4) PSP or PTP motifs; 5) PR motifs.


Pssm-ID: 238122 [Multi-domain]  Cd Length: 31  Bit Score: 53.30  E-value: 2.68e-09
                          10        20        30
                  ....*....|....*....|....*....|.
gi 156546890   13 PRGWEEARDYDGKVFYIDHNTRRTSWIDPRD 43
Cdd:cd00201     1 PPGWEERWDPDGRVYYYNHNTKETQWEDPRE 31
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 59-88 7.11e-08

WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds proline-rich peptide motifs in vitro.


Pssm-ID: 459800 [Multi-domain]  Cd Length: 30  Bit Score: 49.43  E-value: 7.11e-08
                           10        20        30
                   ....*....|....*....|....*....|
gi 156546890    59 LPWGWEAGFDPQIGVYYIDHINKTTQIEDP 88
Cdd:pfam00397    1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
 62-89 1.51e-05

Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; functions as an interaction module in a diverse set of signalling proteins; binds specific proline-rich sequences but at low affinities compared to other peptide recognition proteins such as antibodies and receptors; WW domains have a single groove formed by a conserved Trp and Tyr which recognizes a pair of residues of the sequence X-Pro; variable loops and neighboring domains confer specificity in this domain; there are five distinct groups based on binding: 1) PPXY motifs 2) the PPLP motif; 3) PGM motifs; 4) PSP or PTP motifs; 5) PR motifs.


Pssm-ID: 238122 [Multi-domain]  Cd Length: 31  Bit Score: 42.90  E-value: 1.51e-05
                          10        20
                  ....*....|....*....|....*...
gi 156546890   62 GWEAGFDPQIGVYYIDHINKTTQIEDPR 89
Cdd:cd00201     3 GWEERWDPDGRVYYYNHNTKETQWEDPR 30
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
 59-89 1.58e-05

Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds proline-rich polypeptides.


Pssm-ID: 197736 [Multi-domain]  Cd Length: 33  Bit Score: 42.59  E-value: 1.58e-05
                            10        20        30
                    ....*....|....*....|....*....|.
gi 156546890     59 LPWGWEAGFDPQIGVYYIDHINKTTQIEDPR 89
Cdd:smart00456    2 LPPGWEERKDPDGRPYYYNHETKETQWEKPR 32
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 173-430 3.64e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.01  E-value: 3.64e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156546890  173 LRVKKLKRELSQMKQELLYKEqgfetLQQIDKKMSGGQSGYELSEAK--AILTELKSIRKAISSGEKEKQDLMQSLAKLQ 250
Cdd:COG1196   213 ERYRELKEELKELEAELLLLK-----LRELEAELEELEAELEELEAEleELEAELAELEAELEELRLELEELELELEEAQ 287

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156546890  251 ERFH-LDQNIGRSEPDLRcspvnsHLCLSRQ---------TLDAGSQTSISGDIGVRSRSNLAEKVRLSLQYEEAKRSMA 320
Cdd:COG1196   288 AEEYeLLAELARLEQDIA------RLEERRReleerleelEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELA 361

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156546890  321 NLKIELSKLDS------EAWpgaLDIEKEKLMLINEKEELLKELQFVTPQ-KRTQDELERLEAERQRLEEELLSVRgtpS 393
Cdd:COG1196   362 EAEEALLEAEAelaeaeEEL---EELAEELLEALRAAAELAAQLEELEEAeEALLERLERLEEELEELEEALAELE---E 435

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 156546890  394 RALAERLRLEERRKELLQKLEETTKLTTYLHSQLKSL 430
Cdd:COG1196   436 EEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEA 472
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
164-430 3.87e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 48.14  E-value: 3.87e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156546890  164 LKAEISTTRLRVKKLKRELSQMKQ-ELLYKEQG---FETLQQIDKKMSG-GQSGYELSEAKAILTELKSIRKAISSGEKE 238
Cdd:PRK03918  167 LGEVIKEIKRRIERLEKFIKRTENiEELIKEKEkelEEVLREINEISSElPELREELEKLEKEVKELEELKEEIEELEKE 246

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156546890  239 KQDLMQSLAKLQERF-HLDQNIGRSEPDLRCspvnshlcLSRQtldAGSQTSISGDIgvrsrsnlAEKVRLSLQYEEAKR 317
Cdd:PRK03918  247 LESLEGSKRKLEEKIrELEERIEELKKEIEE--------LEEK---VKELKELKEKA--------EEYIKLSEFYEEYLD 307

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156546890  318 SMANLKIELSKLDSEA------WPGALDIEKEKLMLINEKEELLKELQFVTPQKRTQDELERLEAERQRLEEELLSVrgT 391
Cdd:PRK03918  308 ELREIEKRLSRLEEEIngieerIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGL--T 385

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 156546890  392 PSRALAERLRLEERRKELLQKLEETTKLTTYLHSQLKSL 430
Cdd:PRK03918  386 PEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKEL 424
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 115-415 3.98e-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: 44.66  E-value: 3.98e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156546890   115 KELYHVKEQRLALALDEYVRLNDAYKEKSSSHTSLFSGSSSSTKYDPdiLKAEISTTRL-----RVKKLKRELSQMKQEL 189
Cdd:TIGR02168  171 KERRKETERKLERTRENLDRLEDILNELERQLKSLERQAEKAERYKE--LKAELRELELallvlRLEELREELEELQEEL 248

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156546890   190 LYKEQGFETLQqidkkmsggqsgyelSEAKAILTELKSIRKAISSGEKEKQDL---MQSLAKLQERfhLDQNIGRSEPDL 266
Cdd:TIGR02168  249 KEAEEELEELT---------------AELQELEEKLEELRLEVSELEEEIEELqkeLYALANEISR--LEQQKQILRERL 311

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156546890   267 RcSPVNSHLCLSRQTLDAGSQTSISGDIGVRSRSNLAE----KVRLSLQYEEAKRSMANLKIELSKLDSEawpgaLDIEK 342
Cdd:TIGR02168  312 A-NLERQLEELEAQLEELESKLDELAEELAELEEKLEElkeeLESLEAELEELEAELEELESRLEELEEQ-----LETLR 385

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 156546890   343 EKLMLINEKEELL-KELQfvtpqkRTQDELERLEAERQRLEEELLSVRGTPSRALAERL--RLEERRKELLQKLEE 415
Cdd:TIGR02168  386 SKVAQLELQIASLnNEIE------RLEARLERLEDRRERLQQEIEELLKKLEEAELKELqaELEELEEELEELQEE 455
PRK10929 PRK10929
putative mechanosensitive channel protein; Provisional
 1079-1161 1.59e-03

putative mechanosensitive channel protein; Provisional


Pssm-ID: 236798 [Multi-domain]  Cd Length: 1109  Bit Score: 42.73  E-value: 1.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156546890 1079 RQSRLNDELQALR----DLRQK-----LE--ELKAQGETDLPPGVLEDERFQRLLKQAEKQAEQS----KEEQKQglnAE 1143
Cdd:PRK10929  216 RSQQLDAYLQALRnqlnSQRQReaeraLEstELLAEQSGDLPKSIVAQFKINRELSQALNQQAQRmdliASQQRQ---AA 292

                          90
                  ....*....|....*...
gi 156546890 1144 KLMRQVSKDVCRLREQSQ 1161
Cdd:PRK10929  293 SQTLQVRQALNTLREQSQ 310
Phage_Nu1 pfam07471
Phage DNA packaging protein Nu1; Terminase, the DNA packaging enzyme of bacteriophage lambda, ...
 1093-1168 1.91e-03

Phage DNA packaging protein Nu1; Terminase, the DNA packaging enzyme of bacteriophage lambda, is a heteromultimer composed of subunits Nu1 and A. The smaller Nu1 terminase subunit has a low-affinity ATPase stimulated by non-specific DNA.


Pssm-ID: 369382 [Multi-domain]  Cd Length: 164  Bit Score: 40.41  E-value: 1.91e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 156546890  1093 LRQKLEELKAQGETDLPPGVLEDERFQRLLKQAEKQAEQSKEEQKQGLNAEKLMRQVSKDVCRLREQSQKVPRQVQ 1168
Cdd:pfam07471   62 LRREVEELRAAGEADLDPGTIEYERRRLTAAQADAQELKNADAKKQVAETEQVTKTLARVAAEIAAILRTIPLLLQ 137
HMMR_N pfam15905
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ...
 137-417 6.17e-03

Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.


Pssm-ID: 464932 [Multi-domain]  Cd Length: 329  Bit Score: 40.18  E-value: 6.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156546890   137 DAYKEKSSSHTSLFSGSSSSTKYDPDILKAEISTTRLRVKKLKRELSQMKqeLLYKEQGfetlqQIDKKMSGGQSGYELS 216
Cdd:pfam15905   34 AAESQPNLNNSKDASTPATARKVKSLELKKKSQKNLKESKDQKELEKEIR--ALVQERG-----EQDKRLQALEEELEKV 106

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156546890   217 EAK--AILTELKSIRKAISSGEKEKQDLMQSLAKLQERFHLDQNigrsepDLRCSPVNSHLCLSRQTLDAGSQTSISGDI 294
Cdd:pfam15905  107 EAKlnAAVREKTSLSASVASLEKQLLELTRVNELLKAKFSEDGT------QKKMSSLSMELMKLRNKLEAKMKEVMAKQE 180

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156546890   295 GVRSRSNLAEKvrlslQYEEAKRSMANLKIELSkldseawpgalDIEKEKlmlINEKEELLKELQFVTPQKRTQDELERL 374
Cdd:pfam15905  181 GMEGKLQVTQK-----NLEHSKGKVAQLEEKLV-----------STEKEK---IEEKSETEKLLEYITELSCVSEQVEKY 241

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 156546890   375 EAERQRLEE-------ELLSVRGTPSRALAERLRLEERRKELLQKLEETT 417
Cdd:pfam15905  242 KLDIAQLEEllkekndEIESLKQSLEEKEQELSKQIKDLNEKCKLLESEK 291
 
Name Accession Description Interval E-value
C2_Kibra cd08680
C2 domain found in Human protein Kibra; Kibra is thought to be a regulator of the Salvador ...
 700-823 2.31e-60

C2 domain found in Human protein Kibra; Kibra is thought to be a regulator of the Salvador (Sav)/Warts (Wts)/Hippo (Hpo) (SWH) signaling network, which limits tissue growth by inhibiting cell proliferation and promoting apoptosis. The core of the pathway consists of a MST and LATS family kinase cascade that ultimately phosphorylates and inactivates the YAP/Yorkie (Yki) transcription coactivator. The FERM domain proteins Merlin (Mer) and Expanded (Ex) are part of the upstream regulation controlling pathway mechanism. Kibra colocalizes and associates with Mer and Ex and is thought to transduce an extracellular signal via the SWH network. The apical scaffold machinery that contains Hpo, Wts, and Ex recruits Yki to the apical membrane facilitating its inhibitory phosphorlyation by Wts. Since Kibra associates with Ex and is apically located it is hypothesized that KIBRA is part of the scaffold, helps in the Hpo/Wts complex, and helps recruit Yki for inactivation that promotes SWH pathway activity. Kibra contains two amino-terminal WW domains, an internal C2-like domain, and a carboxy-terminal glutamic acid-rich stretch. The C2 domain was first identified in PKC. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions.


Pssm-ID: 176062  Cd Length: 124  Bit Score: 202.08  E-value: 2.31e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156546890  700 AQVQIGLRYNAKSSSFMVIIAQLRNLHAFLIPHTSKVYFRVAVLPSSTDVSCLFRTKVHPPTESILFNDVFRVAISQTAL 779
Cdd:cd08680     1 AQVQIGLRYDSGDSSLVISVEQLRNLSALSIPENSKVYVRVALLPCSSSTSCLFRTKALEDQDKPVFNEVFRVPISSTKL 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 156546890  780 QQKTLRVDLCSVSKHRREECLAGTQISLADLPFSSEVFTLWYNL 823
Cdd:cd08680    81 YQKTLQVDVCSVGPDQQEECLGGAQISLADFESSEEMSTKWYNL 124
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 12-41 1.08e-10

WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds proline-rich peptide motifs in vitro.


Pssm-ID: 459800 [Multi-domain]  Cd Length: 30  Bit Score: 57.13  E-value: 1.08e-10
                           10        20        30
                   ....*....|....*....|....*....|
gi 156546890    12 LPRGWEEARDYDGKVFYIDHNTRRTSWIDP 41
Cdd:pfam00397    1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
 11-43 9.27e-10

Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds proline-rich polypeptides.


Pssm-ID: 197736 [Multi-domain]  Cd Length: 33  Bit Score: 54.91  E-value: 9.27e-10
                            10        20        30
                    ....*....|....*....|....*....|...
gi 156546890     11 PLPRGWEEARDYDGKVFYIDHNTRRTSWIDPRD 43
Cdd:smart00456    1 PLPPGWEERKDPDGRPYYYNHETKETQWEKPRE 33
C2C_KIAA1228 cd04030
C2 domain third repeat present in uncharacterized human KIAA1228-like proteins; KIAA proteins ...
 698-823 1.25e-09

C2 domain third repeat present in uncharacterized human KIAA1228-like proteins; KIAA proteins are uncharacterized human proteins. They were compiled by the Kazusa mammalian cDNA project which identified more than 2000 human genes. They are identified by 4 digit codes that precede the KIAA designation. Many KIAA genes are still functionally uncharacterized including KIAA1228. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the third C2 repeat, C2C, and has a type-II topology.


Pssm-ID: 175996 [Multi-domain]  Cd Length: 127  Bit Score: 57.28  E-value: 1.25e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156546890  698 ETAQVQIGLRYNAKSSSFMVIIAQLRNLHAFLIPHTSKVYFRVAVLPSSTdVSCLFRTKVHPPTESILFNDVFRVAISQT 777
Cdd:cd04030     1 PLGRIQLTIRYSSQRQKLIVTVHKCRNLPPCDSSDIPDPYVRLYLLPDKS-KSTRRKTSVKKDNLNPVFDETFEFPVSLE 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 156546890  778 ALQQKTLRVDLC-SVSKHRREECLAGT-QISLADLPFsSEVFTLWYNL 823
Cdd:cd04030    80 ELKRRTLDVAVKnSKSFLSREKKLLGQvLIDLSDLDL-SKGFTQWYDL 126
C2A_Synaptotagmin-8 cd08387
C2A domain first repeat present in Synaptotagmin 8; Synaptotagmin is a membrane-trafficking ...
 699-820 1.31e-09

C2A domain first repeat present in Synaptotagmin 8; Synaptotagmin is a membrane-trafficking protein characterized by a N-terminal transmembrane region, a linker, and 2 C-terminal C2 domains. Previously all synaptotagmins were thought to be calcium sensors in the regulation of neurotransmitter release and hormone secretion, but it has been shown that not all of them bind calcium. Of the 17 identified synaptotagmins only 8 bind calcium (1-3, 5-7, 9, 10). The function of the two C2 domains that bind calcium are: regulating the fusion step of synaptic vesicle exocytosis (C2A) and binding to phosphatidyl-inositol-3,4,5-triphosphate (PIP3) in the absence of calcium ions and to phosphatidylinositol bisphosphate (PIP2) in their presence (C2B). C2B also regulates also the recycling step of synaptic vesicles. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the first C2 repeat, C2A, and has a type-I topology.


Pssm-ID: 176033 [Multi-domain]  Cd Length: 124  Bit Score: 57.03  E-value: 1.31e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156546890  699 TAQVQIGLRYNAKSSSFMVIIAQLRNLHAFLIPHTSKVYFRVAVLPsstDVSCLFRTKVHPPTESILFNDVFRVAISQTA 778
Cdd:cd08387     2 RGELHFSLEYDKDMGILNVKLIQARNLQPRDFSGTADPYCKVRLLP---DRSNTKQSKIHKKTLNPEFDESFVFEVPPQE 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 156546890  779 LQQKTLRVDLCSVSKHRREECLAGTQISLADLPFSSEVfTLW 820
Cdd:cd08387    79 LPKRTLEVLLYDFDQFSRDECIGVVELPLAEVDLSEKL-DLW 119
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
 13-43 2.68e-09

Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; functions as an interaction module in a diverse set of signalling proteins; binds specific proline-rich sequences but at low affinities compared to other peptide recognition proteins such as antibodies and receptors; WW domains have a single groove formed by a conserved Trp and Tyr which recognizes a pair of residues of the sequence X-Pro; variable loops and neighboring domains confer specificity in this domain; there are five distinct groups based on binding: 1) PPXY motifs 2) the PPLP motif; 3) PGM motifs; 4) PSP or PTP motifs; 5) PR motifs.


Pssm-ID: 238122 [Multi-domain]  Cd Length: 31  Bit Score: 53.30  E-value: 2.68e-09
                          10        20        30
                  ....*....|....*....|....*....|.
gi 156546890   13 PRGWEEARDYDGKVFYIDHNTRRTSWIDPRD 43
Cdd:cd00201     1 PPGWEERWDPDGRVYYYNHNTKETQWEDPRE 31
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 59-88 7.11e-08

WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds proline-rich peptide motifs in vitro.


Pssm-ID: 459800 [Multi-domain]  Cd Length: 30  Bit Score: 49.43  E-value: 7.11e-08
                           10        20        30
                   ....*....|....*....|....*....|
gi 156546890    59 LPWGWEAGFDPQIGVYYIDHINKTTQIEDP 88
Cdd:pfam00397    1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
C2A_SLP cd08521
C2 domain first repeat present in Synaptotagmin-like proteins; All Slp members basically share ...
 701-823 1.89e-06

C2 domain first repeat present in Synaptotagmin-like proteins; All Slp members basically share an N-terminal Slp homology domain (SHD) and C-terminal tandem C2 domains (named the C2A domain and the C2B domain) with the SHD and C2 domains being separated by a linker sequence of various length. Slp1/JFC1 and Slp2/exophilin 4 promote granule docking to the plasma membrane. Additionally, their C2A domains are both Ca2+ independent, unlike the case in Slp3 and Slp4/granuphilin in which their C2A domains are Ca2+ dependent. It is thought that SHD (except for the Slp4-SHD) functions as a specific Rab27A/B-binding domain. In addition to Slps, rabphilin, Noc2, and Munc13-4 also function as Rab27-binding proteins. It has been demonstrated that Slp3 and Slp4/granuphilin promote dense-core vesicle exocytosis. Slp5 mRNA has been shown to be restricted to human placenta and liver suggesting a role in Rab27A-dependent membrane trafficking in specific tissues. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the first C2 repeat, C2A, and has a type-I topology.


Pssm-ID: 176056 [Multi-domain]  Cd Length: 123  Bit Score: 48.02  E-value: 1.89e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156546890  701 QVQIGLRYNAKSSSFMVIIAQLRNLhAFLIP--HTSKVYFRVAVLPSSTDVSCLfRTKVHPPTESILFNDVFRVAISQTA 778
Cdd:cd08521     2 EIEFSLSYNYKTGSLEVHIKECRNL-AYADEkkKRSNPYVKVYLLPDKSKQSKR-KTSVKKNTTNPVFNETLKYHISKSQ 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 156546890  779 LQQKTLRVdlcSVSKHR---REECLAGTQISLADLPFSSEVFtLWYNL 823
Cdd:cd08521    80 LETRTLQL---SVWHHDrfgRNTFLGEVEIPLDSWDLDSQQS-EWYPL 123
C2 cd00030
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ...
 715-823 5.86e-06

C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions.


Pssm-ID: 175973 [Multi-domain]  Cd Length: 102  Bit Score: 46.29  E-value: 5.86e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156546890  715 FMVIIAQLRNLHAFLIPHTSKVYFRVAVLPSSTdvsclFRTKVHPPTESILFNDVFRVAISQTalQQKTLRVDLCSVSKH 794
Cdd:cd00030     1 LRVTVIEARNLPAKDLNGKSDPYVKVSLGGKQK-----FKTKVVKNTLNPVWNETFEFPVLDP--ESDTLTVEVWDKDRF 73

                          90       100
                  ....*....|....*....|....*....
gi 156546890  795 RREECLAGTQISLADLPFSSEVFTLWYNL 823
Cdd:cd00030    74 SKDDFLGEVEIPLSELLDSGKEGELWLPL 102
C2A_Synaptotagmin-1-5-6-9-10 cd08385
C2A domain first repeat present in Synaptotagmins 1, 5, 6, 9, and 10; Synaptotagmin is a ...
 702-794 8.11e-06

C2A domain first repeat present in Synaptotagmins 1, 5, 6, 9, and 10; Synaptotagmin is a membrane-trafficking protein characterized by a N-terminal transmembrane region, a linker, and 2 C-terminal C2 domains. Synaptotagmin 1, a member of class 1 synaptotagmins, is located in the brain and endocranium and localized to the synaptic vesicles and secretory granules. It functions as a Ca2+ sensor for fast exocytosis as do synaptotagmins 5, 6, and 10. It is distinguished from the other synaptotagmins by having an N-glycosylated N-terminus. Synaptotagmins 5, 6, and 10, members of class 3 synaptotagmins, are located primarily in the brain and localized to the active zone and plasma membrane. They is distinguished from the other synaptotagmins by having disulfide bonds at its N-terminus. Synaptotagmin 6 also regulates the acrosome reaction, a unique Ca2+-regulated exocytosis, in sperm. Synaptotagmin 9, a class 5 synaptotagmins, is located in the brain and localized to the synaptic vesicles. It is thought to be a Ca2+-sensor for dense-core vesicle exocytosis. Previously all synaptotagmins were thought to be calcium sensors in the regulation of neurotransmitter release and hormone secretion, but it has been shown that not all of them bind calcium. Of the 17 identified synaptotagmins only 8 bind calcium (1-3, 5-7, 9, 10). The function of the two C2 domains that bind calcium are: regulating the fusion step of synaptic vesicle exocytosis (C2A) and binding to phosphatidyl-inositol-3,4,5-triphosphate (PIP3) in the absence of calcium ions and to phosphatidylinositol bisphosphate (PIP2) in their presence (C2B). C2B also regulates also the recycling step of synaptic vesicles. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the first C2 repeat, C2A, and has a type-I topology.


Pssm-ID: 176031 [Multi-domain]  Cd Length: 124  Bit Score: 46.49  E-value: 8.11e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156546890  702 VQIGLRYNAKSSSFMVIIAQLRNLHAFLIPHTSKVYFRVAVLPsstDVSCLFRTKVHPPTESILFNDVFRVAISQTALQQ 781
Cdd:cd08385     5 LQFSLDYDFQSNQLTVGIIQAADLPAMDMGGTSDPYVKVYLLP---DKKKKFETKVHRKTLNPVFNETFTFKVPYSELGN 81

                          90
                  ....*....|....*.
gi 156546890  782 KTLRV---DLCSVSKH 794
Cdd:cd08385    82 KTLVFsvyDFDRFSKH 97
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
 62-89 1.51e-05

Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; functions as an interaction module in a diverse set of signalling proteins; binds specific proline-rich sequences but at low affinities compared to other peptide recognition proteins such as antibodies and receptors; WW domains have a single groove formed by a conserved Trp and Tyr which recognizes a pair of residues of the sequence X-Pro; variable loops and neighboring domains confer specificity in this domain; there are five distinct groups based on binding: 1) PPXY motifs 2) the PPLP motif; 3) PGM motifs; 4) PSP or PTP motifs; 5) PR motifs.


Pssm-ID: 238122 [Multi-domain]  Cd Length: 31  Bit Score: 42.90  E-value: 1.51e-05
                          10        20
                  ....*....|....*....|....*...
gi 156546890   62 GWEAGFDPQIGVYYIDHINKTTQIEDPR 89
Cdd:cd00201     3 GWEERWDPDGRVYYYNHNTKETQWEDPR 30
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
 59-89 1.58e-05

Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds proline-rich polypeptides.


Pssm-ID: 197736 [Multi-domain]  Cd Length: 33  Bit Score: 42.59  E-value: 1.58e-05
                            10        20        30
                    ....*....|....*....|....*....|.
gi 156546890     59 LPWGWEAGFDPQIGVYYIDHINKTTQIEDPR 89
Cdd:smart00456    2 LPPGWEERKDPDGRPYYYNHETKETQWEKPR 32
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 173-430 3.64e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.01  E-value: 3.64e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156546890  173 LRVKKLKRELSQMKQELLYKEqgfetLQQIDKKMSGGQSGYELSEAK--AILTELKSIRKAISSGEKEKQDLMQSLAKLQ 250
Cdd:COG1196   213 ERYRELKEELKELEAELLLLK-----LRELEAELEELEAELEELEAEleELEAELAELEAELEELRLELEELELELEEAQ 287

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156546890  251 ERFH-LDQNIGRSEPDLRcspvnsHLCLSRQ---------TLDAGSQTSISGDIGVRSRSNLAEKVRLSLQYEEAKRSMA 320
Cdd:COG1196   288 AEEYeLLAELARLEQDIA------RLEERRReleerleelEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELA 361

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156546890  321 NLKIELSKLDS------EAWpgaLDIEKEKLMLINEKEELLKELQFVTPQ-KRTQDELERLEAERQRLEEELLSVRgtpS 393
Cdd:COG1196   362 EAEEALLEAEAelaeaeEEL---EELAEELLEALRAAAELAAQLEELEEAeEALLERLERLEEELEELEEALAELE---E 435

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 156546890  394 RALAERLRLEERRKELLQKLEETTKLTTYLHSQLKSL 430
Cdd:COG1196   436 EEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEA 472
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
164-430 3.87e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 48.14  E-value: 3.87e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156546890  164 LKAEISTTRLRVKKLKRELSQMKQ-ELLYKEQG---FETLQQIDKKMSG-GQSGYELSEAKAILTELKSIRKAISSGEKE 238
Cdd:PRK03918  167 LGEVIKEIKRRIERLEKFIKRTENiEELIKEKEkelEEVLREINEISSElPELREELEKLEKEVKELEELKEEIEELEKE 246

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156546890  239 KQDLMQSLAKLQERF-HLDQNIGRSEPDLRCspvnshlcLSRQtldAGSQTSISGDIgvrsrsnlAEKVRLSLQYEEAKR 317
Cdd:PRK03918  247 LESLEGSKRKLEEKIrELEERIEELKKEIEE--------LEEK---VKELKELKEKA--------EEYIKLSEFYEEYLD 307

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156546890  318 SMANLKIELSKLDSEA------WPGALDIEKEKLMLINEKEELLKELQFVTPQKRTQDELERLEAERQRLEEELLSVrgT 391
Cdd:PRK03918  308 ELREIEKRLSRLEEEIngieerIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGL--T 385

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 156546890  392 PSRALAERLRLEERRKELLQKLEETTKLTTYLHSQLKSL 430
Cdd:PRK03918  386 PEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKEL 424
C2B_Synaptotagmin cd00276
C2 domain second repeat present in Synaptotagmin; Synaptotagmin is a membrane-trafficking ...
 700-800 4.93e-05

C2 domain second repeat present in Synaptotagmin; Synaptotagmin is a membrane-trafficking protein characterized by a N-terminal transmembrane region, a linker, and 2 C-terminal C2 domains. There are several classes of Synaptotagmins. Previously all synaptotagmins were thought to be calcium sensors in the regulation of neurotransmitter release and hormone secretion, but it has been shown that not all of them bind calcium. Of the 17 identified synaptotagmins only 8 bind calcium (1-3, 5-7, 9, 10). The function of the two C2 domains that bind calcium are: regulating the fusion step of synaptic vesicle exocytosis (C2A) and binding to phosphatidyl-inositol-3,4,5-triphosphate (PIP3) in the absence of calcium ions and to phosphatidylinositol bisphosphate (PIP2) in their presence (C2B). C2B also regulates also the recycling step of synaptic vesicles. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the second C2 repeat, C2B, and has a type-I topology.


Pssm-ID: 175975 [Multi-domain]  Cd Length: 134  Bit Score: 44.50  E-value: 4.93e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156546890  700 AQVQIGLRYNAKSSSFMVIIAQLRNLHAFLIPHTSKVYFRVAVLPSSTDVSClFRTKVHPPTESILFNDVFRVAISQTAL 779
Cdd:cd00276     1 GELLLSLSYLPTAERLTVVVLKARNLPPSDGKGLSDPYVKVSLLQGGKKLKK-KKTSVKKGTLNPVFNEAFSFDVPAEQL 79

                          90       100
                  ....*....|....*....|.
gi 156546890  780 QQKTLRVDLCSVSKHRREECL 800
Cdd:cd00276    80 EEVSLVITVVDKDSVGRNEVI 100
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 176-453 2.16e-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: 45.14  E-value: 2.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156546890  176 KKLKRELSQMKQELLYKEQGFETLQQidkkmsggqsgyelsEAKAILTELKSIRKAISSGEKEKQDLMQSLAKLQERFH- 254
Cdd:COG4942    23 AEAEAELEQLQQEIAELEKELAALKK---------------EEKALLKQLAALERRIAALARRIRALEQELAALEAELAe 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156546890  255 LDQNIGRSEPDLrcspvnshlclsrqtldAGSQTSISGDIGVRSRSNLAEKVRLSLQYEEAKRSMANLKI--ELSKLDSE 332
Cdd:COG4942    88 LEKEIAELRAEL-----------------EAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYlkYLAPARRE 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156546890  333 AwpgALDIEKEKLMLINEKEELLKElqfvtpQKRTQDELERLEAERQRLEEELLSVRgtpsRALAerlRLEERRKELLQK 412
Cdd:COG4942   151 Q---AEELRADLAELAALRAELEAE------RAELEALLAELEEERAALEALKAERQ----KLLA---RLEKELAELAAE 214

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 156546890  413 LEETTKLTTYLHSQLKSLSASTLSMSSGSSLGSLASSRGSL 453
Cdd:COG4942   215 LAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGKL 255
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 164-385 2.80e-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: 2.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156546890  164 LKAEISTTRLRVKKLKRELSQMKQEllykeqgfetLQQIDKKMSGGQsgyelSEAKAILTELKSIRKAISSGEKEKQDLM 243
Cdd:COG4942    32 LQQEIAELEKELAALKKEEKALLKQ----------LAALERRIAALA-----RRIRALEQELAALEAELAELEKEIAELR 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156546890  244 QSLAKLQERF-----HLDQNIGRSEPDLRCSPVNShlclsrqtLDAGSQTSISGDIgVRSRSNLAEKVRLSLQY-EEAKR 317
Cdd:COG4942    97 AELEAQKEELaellrALYRLGRQPPLALLLSPEDF--------LDAVRRLQYLKYL-APARREQAEELRADLAElAALRA 167

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 156546890  318 SMANLKIELSKLDSEawpgaLDIEKEKL-MLINEKEELLKELQfvTPQKRTQDELERLEAERQRLEEEL 385
Cdd:COG4942   168 ELEAERAELEALLAE-----LEEERAALeALKAERQKLLARLE--KELAELAAELAELQQEAEELEALI 229
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 115-415 3.98e-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: 44.66  E-value: 3.98e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156546890   115 KELYHVKEQRLALALDEYVRLNDAYKEKSSSHTSLFSGSSSSTKYDPdiLKAEISTTRL-----RVKKLKRELSQMKQEL 189
Cdd:TIGR02168  171 KERRKETERKLERTRENLDRLEDILNELERQLKSLERQAEKAERYKE--LKAELRELELallvlRLEELREELEELQEEL 248

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156546890   190 LYKEQGFETLQqidkkmsggqsgyelSEAKAILTELKSIRKAISSGEKEKQDL---MQSLAKLQERfhLDQNIGRSEPDL 266
Cdd:TIGR02168  249 KEAEEELEELT---------------AELQELEEKLEELRLEVSELEEEIEELqkeLYALANEISR--LEQQKQILRERL 311

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156546890   267 RcSPVNSHLCLSRQTLDAGSQTSISGDIGVRSRSNLAE----KVRLSLQYEEAKRSMANLKIELSKLDSEawpgaLDIEK 342
Cdd:TIGR02168  312 A-NLERQLEELEAQLEELESKLDELAEELAELEEKLEElkeeLESLEAELEELEAELEELESRLEELEEQ-----LETLR 385

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 156546890   343 EKLMLINEKEELL-KELQfvtpqkRTQDELERLEAERQRLEEELLSVRGTPSRALAERL--RLEERRKELLQKLEE 415
Cdd:TIGR02168  386 SKVAQLELQIASLnNEIE------RLEARLERLEDRRERLQQEIEELLKKLEEAELKELqaELEELEEELEELQEE 455
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 162-432 4.95e-04

chromosome segregation protein SMC, primarily archaeal 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. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 44.67  E-value: 4.95e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156546890   162 DILKAEISTTRLRVKKLKRELSQMK--QELLYKEQGFEtlqqidkkmsggqsGYEL-SEAKAILTELKSIRKAISSGEKE 238
Cdd:TIGR02169  187 ERLDLIIDEKRQQLERLRREREKAEryQALLKEKREYE--------------GYELlKEKEALERQKEAIERQLASLEEE 252

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156546890   239 KQDLMQSLAKLQERFHlDQNIGRSEPDLRCSPVNSHLCLSRQTLDAGSQTSISgdigvRSRSNLAEKVRlslQYEEAKRS 318
Cdd:TIGR02169  253 LEKLTEEISELEKRLE-EIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIA-----SLERSIAEKER---ELEDAEER 323

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156546890   319 MANLKIELSKLDSEAWPGALDIEKEKLMLINEKEELlKELQfvtpqkrtqdelERLEAERQRLEEELLSVRGTPSRALAE 398
Cdd:TIGR02169  324 LAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEY-AELK------------EELEDLRAELEEVDKEFAETRDELKDY 390

                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 156546890   399 RLRLE---ERRKELLQKLEETTKLTTYLHSQLKSLSA 432
Cdd:TIGR02169  391 REKLEklkREINELKRELDRLQEELQRLSEELADLNA 427
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 165-418 7.83e-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: 43.89  E-value: 7.83e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156546890   165 KAEISTTRLRVKKLKRELSQMKQELLYKEQGFETLQQidkkmsggqsgyelsEAKAILTELKSIRKAISSGEKEKQDLMQ 244
Cdd:TIGR02168  676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEE---------------ELEQLRKELEELSRQISALRKDLARLEA 740

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156546890   245 SLAKLQERFHlDQNIGRSEPDLRCSPVNSHLCLSRQTLDAGSQTSISGDIGVRSRSNLAEKVRLSL-----QYEEAKRSM 319
Cdd:TIGR02168  741 EVEQLEERIA-QLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALdelraELTLLNEEA 819

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156546890   320 ANLKIELSKLDSEawpgALDIEKEKLMLINEKEELLKELQFVTPQKRT--------QDELERLEAERQRLEEELLSVRGT 391
Cdd:TIGR02168  820 ANLRERLESLERR----IAATERRLEDLEEQIEELSEDIESLAAEIEEleelieelESELEALLNERASLEEALALLRSE 895

                          250       260
                   ....*....|....*....|....*..
gi 156546890   392 PSRALAERLRLEERRKELLQKLEETTK 418
Cdd:TIGR02168  896 LEELSEELRELESKRSELRRELEELRE 922
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 224-417 9.74e-04

chromosome segregation protein SMC, primarily archaeal 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. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 43.52  E-value: 9.74e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156546890   224 ELKSIRKAISSGEKEKQDLMQSLAKL-QERFHLDQNIGRSEpdlrcspvnshlclsRQTLDAGSQTSISGDIGVRSRSNL 302
Cdd:TIGR02169  675 ELQRLRERLEGLKRELSSLQSELRRIeNRLDELSQELSDAS---------------RKIGEIEKEIEQLEQEEEKLKERL 739

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156546890   303 AEKVRlslQYEEAKRSMANLKIELSKLDSEAWPGALDIEKEKLMLINEKEELLKElqfvtPQKRTQDELERLEAERQRLE 382
Cdd:TIGR02169  740 EELEE---DLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHS-----RIPEIQAELSKLEEEVSRIE 811

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 156546890   383 EELLSVRGTPSRALAERLRLEERRKELLQKLEETT 417
Cdd:TIGR02169  812 ARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLK 846
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 164-415 1.49e-03

chromosome segregation protein SMC, primarily archaeal 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. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 42.75  E-value: 1.49e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156546890   164 LKAEISTTRLRVKKLKRELSQMKQELLYKEQGFETLQQI-------------DKKMSGGQSGYELSEAKAILTELKSIRK 230
Cdd:TIGR02169  672 EPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQElsdasrkigeiekEIEQLEQEEEKLKERLEELEEDLSSLEQ 751

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156546890   231 AISSGEKEKQDLMQSLAKLQERFH-LDQNIGRSEPDLRCSPVNShlclSRQTLDagSQTSISGDIGVRSRSNLAEKVRLS 309
Cdd:TIGR02169  752 EIENVKSELKELEARIEELEEDLHkLEEALNDLEARLSHSRIPE----IQAELS--KLEEEVSRIEARLREIEQKLNRLT 825

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156546890   310 LQYEEAKRSMANLKIELSKLDSEawpgALDIEKEKLMLINEKEELLKELQFVTPQKRT-QDELERLEAERQRLEEELLSV 388
Cdd:TIGR02169  826 LEKEYLEKEIQELQEQRIDLKEQ----IKSIEKEIENLNGKKEELEEELEELEAALRDlESRLGDLKKERDELEAQLREL 901

                          250       260
                   ....*....|....*....|....*..
gi 156546890   389 RGTPSRALAERLRLEERRKELLQKLEE 415
Cdd:TIGR02169  902 ERKIEELEAQIEKKRKRLSELKAKLEA 928
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
78-432 1.58e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.83  E-value: 1.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156546890   78 HINKTTQIEDPRKQWRGEQEKMlKDYLSVAQDALRTQKELYHVKEQRLAL-----ALDEYVRLNDAYKEKsssHTSLFSG 152
Cdd:COG4717    66 PELNLKELKELEEELKEAEEKE-EEYAELQEELEELEEELEELEAELEELreeleKLEKLLQLLPLYQEL---EALEAEL 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156546890  153 SSSSTKYDpdilkaEISTTRLRVKKLKRELSQMKQELLYKEQGFETLQQIDKKMSGGQSGYELSEAKAILTELKSIRKAI 232
Cdd:COG4717   142 AELPERLE------ELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEEL 215

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156546890  233 SSGEKEKQDLMQSLAKLQ---ERFHLDQNIGRSEPDLRCSPV------NSHLCLSRQTLDAGSQTSISGDIGVRSRSNLA 303
Cdd:COG4717   216 EEAQEELEELEEELEQLEnelEAAALEERLKEARLLLLIAAAllallgLGGSLLSLILTIAGVLFLVLGLLALLFLLLAR 295

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156546890  304 EKVRLSLQYEEAKRSMAnlKIELSKLDSEAWPGALDIEKE-KLMLINEKEELLKELQFVTPQKRTQDELERLEAERQRLE 382
Cdd:COG4717   296 EKASLGKEAEELQALPA--LEELEEEELEELLAALGLPPDlSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIA 373

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 156546890  383 EELLSVRGTPSRALAERLRLEERRKELLQKLEEttkLTTYLHSQLKSLSA 432
Cdd:COG4717   374 ALLAEAGVEDEEELRAALEQAEEYQELKEELEE---LEEQLEELLGELEE 420
PRK10929 PRK10929
putative mechanosensitive channel protein; Provisional
 1079-1161 1.59e-03

putative mechanosensitive channel protein; Provisional


Pssm-ID: 236798 [Multi-domain]  Cd Length: 1109  Bit Score: 42.73  E-value: 1.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156546890 1079 RQSRLNDELQALR----DLRQK-----LE--ELKAQGETDLPPGVLEDERFQRLLKQAEKQAEQS----KEEQKQglnAE 1143
Cdd:PRK10929  216 RSQQLDAYLQALRnqlnSQRQReaeraLEstELLAEQSGDLPKSIVAQFKINRELSQALNQQAQRmdliASQQRQ---AA 292

                          90
                  ....*....|....*...
gi 156546890 1144 KLMRQVSKDVCRLREQSQ 1161
Cdd:PRK10929  293 SQTLQVRQALNTLREQSQ 310
Phage_Nu1 pfam07471
Phage DNA packaging protein Nu1; Terminase, the DNA packaging enzyme of bacteriophage lambda, ...
 1093-1168 1.91e-03

Phage DNA packaging protein Nu1; Terminase, the DNA packaging enzyme of bacteriophage lambda, is a heteromultimer composed of subunits Nu1 and A. The smaller Nu1 terminase subunit has a low-affinity ATPase stimulated by non-specific DNA.


Pssm-ID: 369382 [Multi-domain]  Cd Length: 164  Bit Score: 40.41  E-value: 1.91e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 156546890  1093 LRQKLEELKAQGETDLPPGVLEDERFQRLLKQAEKQAEQSKEEQKQGLNAEKLMRQVSKDVCRLREQSQKVPRQVQ 1168
Cdd:pfam07471   62 LRREVEELRAAGEADLDPGTIEYERRRLTAAQADAQELKNADAKKQVAETEQVTKTLARVAAEIAAILRTIPLLLQ 137
COG4026 COG4026
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General ...
 338-420 3.90e-03

Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General function prediction only];


Pssm-ID: 443204 [Multi-domain]  Cd Length: 287  Bit Score: 40.87  E-value: 3.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156546890  338 LDIEKEKLMLINEKEELLKELQfvtpqkRTQDELERLEAERQRLEEELLSVRGTPSRALAERLRLEERRKELLQK-LEET 416
Cdd:COG4026   138 LELKEKIDEIAKEKEKLTKENE------ELESELEELREEYKKLREENSILEEEFDNIKSEYSDLKSRFEELLKKrLLEV 211


                  ....
gi 156546890  417 TKLT 420
Cdd:COG4026   212 FSLE 215
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 95-419 4.21e-03

chromosome segregation protein SMC, primarily archaeal 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. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 41.59  E-value: 4.21e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156546890    95 EQEKMLKDYLSVAQDALRTQKELYHVKEQRLALALDEYVRLN------DAYKEKSSSHTSLFSGSSSSTKYDPDILKAEI 168
Cdd:TIGR02169  681 ERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEkeieqlEQEEEKLKERLEELEEDLSSLEQEIENVKSEL 760

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156546890   169 STTRLRVKKLKRELSQMKQEL--LYKEQGFETLQQIDKKMSggqsgyelseakAILTELKSIRKAISSGEKEKQDLMQSL 246
Cdd:TIGR02169  761 KELEARIEELEEDLHKLEEALndLEARLSHSRIPEIQAELS------------KLEEEVSRIEARLREIEQKLNRLTLEK 828

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156546890   247 AKLQERFHLDQNIgRSEPDLRCSPVNSHLCLSRqtLDAGSQTSISGDIGVRSRSNLAEKVRLSLQYEEAKRSMANLKIEL 326
Cdd:TIGR02169  829 EYLEKEIQELQEQ-RIDLKEQIKSIEKEIENLN--GKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKI 905

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156546890   327 SKLDSEawpgaLDIEKEKLMLINEK-EELLKELQFVTPQKRTQDE-------LERLEAERQRLEEELLSVRGTPSRALAE 398
Cdd:TIGR02169  906 EELEAQ-----IEKKRKRLSELKAKlEALEEELSEIEDPKGEDEEipeeelsLEDVQAELQRVEEEIRALEPVNMLAIQE 980

                          330       340       350
                   ....*....|....*....|....*....|....*
gi 156546890   399 --------------RLRLEERRKELLQKLEETTKL 419
Cdd:TIGR02169  981 yeevlkrldelkekRAKLEEERKAILERIEEYEKK 1015
HMMR_N pfam15905
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ...
 137-417 6.17e-03

Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.


Pssm-ID: 464932 [Multi-domain]  Cd Length: 329  Bit Score: 40.18  E-value: 6.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156546890   137 DAYKEKSSSHTSLFSGSSSSTKYDPDILKAEISTTRLRVKKLKRELSQMKqeLLYKEQGfetlqQIDKKMSGGQSGYELS 216
Cdd:pfam15905   34 AAESQPNLNNSKDASTPATARKVKSLELKKKSQKNLKESKDQKELEKEIR--ALVQERG-----EQDKRLQALEEELEKV 106

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156546890   217 EAK--AILTELKSIRKAISSGEKEKQDLMQSLAKLQERFHLDQNigrsepDLRCSPVNSHLCLSRQTLDAGSQTSISGDI 294
Cdd:pfam15905  107 EAKlnAAVREKTSLSASVASLEKQLLELTRVNELLKAKFSEDGT------QKKMSSLSMELMKLRNKLEAKMKEVMAKQE 180

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156546890   295 GVRSRSNLAEKvrlslQYEEAKRSMANLKIELSkldseawpgalDIEKEKlmlINEKEELLKELQFVTPQKRTQDELERL 374
Cdd:pfam15905  181 GMEGKLQVTQK-----NLEHSKGKVAQLEEKLV-----------STEKEK---IEEKSETEKLLEYITELSCVSEQVEKY 241

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 156546890   375 EAERQRLEE-------ELLSVRGTPSRALAERLRLEERRKELLQKLEETT 417
Cdd:pfam15905  242 KLDIAQLEEllkekndEIESLKQSLEEKEQELSKQIKDLNEKCKLLESEK 291
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 172-418 6.46e-03

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: 40.88  E-value: 6.46e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156546890   172 RLRVKKLKRELSQMKQELLYKEqgFETLQQIDKKMSGGQSGYElseakAILTELKSIRKaISSGEKEKQDLMQSLAKLQE 251
Cdd:pfam17380  352 RIRQEERKRELERIRQEEIAME--ISRMRELERLQMERQQKNE-----RVRQELEAARK-VKILEEERQRKIQQQKVEME 423

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156546890   252 RFHLDQNIGRSEPDLRCSPVNSHLCLSRQTLDAGSQTSISgdigvRSRSNLAEKVRLSLQYEEAKRSMANLKIELSKLDS 331
Cdd:pfam17380  424 QIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVE-----RLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILE 498

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156546890   332 EAWPgaldiEKEKLMLINEKEELLKELQFVTPQKRTQDELERLEAERQRLE----EELLSVRGTPSRALAERLRLE--ER 405
Cdd:pfam17380  499 KELE-----ERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKqqemEERRRIQEQMRKATEERSRLEamER 573

                          250
                   ....*....|...
gi 156546890   406 RKELLQKLEETTK 418
Cdd:pfam17380  574 EREMMRQIVESEK 586
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
84-432 7.47e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.52  E-value: 7.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156546890   84 QIEDPRKQWRGEQEKM--LKDYLSVAQDALRTQKELYHVKEQ--RLALALDEYVRLNDAYKEKSSSHTSLFSGSSSSTKY 159
Cdd:COG4717   106 ELEAELEELREELEKLekLLQLLPLYQELEALEAELAELPERleELEERLEELRELEEELEELEAELAELQEELEELLEQ 185

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156546890  160 DPDILKAEISTTRLRVKKLKRELSQMKQELLYKEQGFETLQQ----IDKKMSGGQSGYELSEAK------AILTELKSIR 229
Cdd:COG4717   186 LSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEeleqLENELEAAALEERLKEARlllliaAALLALLGLG 265

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156546890  230 KAISSGEKEKQDLMQSLAKLQerFHLDQNIGRSEPDLRCSPVNSHLCLSRQTLDAGSQTSISGDIGVRSRSNLAEKVRLS 309
Cdd:COG4717   266 GSLLSLILTIAGVLFLVLGLL--ALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELL 343

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156546890  310 LQYEEAKRSMAnlkiELSKLDSEawpgaLDIEKeklmLINEKEELLKELQFVTPQKRTQ-----DELERLEAERQRLEEE 384
Cdd:COG4717   344 DRIEELQELLR----EAEELEEE-----LQLEE----LEQEIAALLAEAGVEDEEELRAaleqaEEYQELKEELEELEEQ 410

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 156546890  385 LLSVRGTPSRALA--ERLRLEERRKELLQKLEETTKLTTYLHSQLKSLSA 432
Cdd:COG4717   411 LEELLGELEELLEalDEEELEEELEELEEELEELEEELEELREELAELEA 460
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 307-432 8.65e-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: 40.43  E-value: 8.65e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156546890   307 RLSLQYEEAKRSMANLKIELSKLDSEAwpgaLDIEKEKLMLINEKEELLKELqfvtpqKRTQDELERLEAERQRLEEELl 386
Cdd:TIGR02168  681 ELEEKIEELEEKIAELEKALAELRKEL----EELEEELEQLRKELEELSRQI------SALRKDLARLEAEVEQLEERI- 749

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 156546890   387 svrgtpSRALAERLRLEERRKELLQKLEETTKLTTYLHSQLKSLSA 432
Cdd:TIGR02168  750 ------AQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEA 789
 
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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