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Conserved domains on  [gi|124487287|ref|NP_001074602|]
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kinesin-like protein KIF16B isoform 2 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
KISc_KIF1A_KIF1B cd01365
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A ...
2-365 0e+00

Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A (Unc104) transports synaptic vesicles to the nerve terminal, KIF1B has been implicated in transport of mitochondria. Both proteins are expressed in neurons. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. In contrast to the majority of dimeric kinesins, most KIF1A/Unc104 kinesins are monomeric motors. A lysine-rich loop in KIF1A binds to the negatively charged C-terminus of tubulin and compensates for the lack of a second motor domain, allowing KIF1A to move processively.


:

Pssm-ID: 276816 [Multi-domain]  Cd Length: 361  Bit Score: 561.97  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287    2 ASVKVAVRVRPMNRREKDLEAKFIIQMEKSKTTITNLKIPEGGTGDSgRERTKTFTYDFSFYSADTKSPDYVSQEMVFKT 81
Cdd:cd01365     1 ANVKVAVRVRPFNSREKERNSKCIVQMSGKETTLKNPKQADKNNKAT-REVPKSFSFDYSYWSHDSEDPNYASQEQVYED 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287   82 LGTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGNSGDSGLIPRICEALFSRINETTRwDEASFRTEVSYLEIYNERVRDL 161
Cdd:cd01365    80 LGEELLQHAFEGYNVCLFAYGQTGSGKSYTMMGTQEQPGIIPRLCEDLFSRIADTTN-QNMSYSVEVSYMEIYNEKVRDL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  162 L-RRKSSKTFNLRVREHPKEGPYVEDLSKHLVQNYSDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQAKFDAE- 239
Cdd:cd01365   159 LnPKPKKNKGNLKVREHPVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVFTIVLTQKRHDAEt 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  240 -MPCETVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADLSQDAAnplvKKKQVFVPYRDSVLTWL 318
Cdd:cd01365   239 nLTTEKVSKISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKVISALADMSSGKS----KKKSSFIPYRDSVLTWL 314
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 124487287  319 LKDSLGGNSKTIMIATISPADVNYGETLSTLRYANRAKNIINKPTIN 365
Cdd:cd01365   315 LKENLGGNSKTAMIAAISPADINYEETLSTLRYADRAKKIVNRAVVN 361
PX_KIF16B_SNX23 cd06874
The phosphoinositide binding Phox Homology domain of KIF16B kinesin or Sorting Nexin 23; The ...
1179-1306 1.14e-77

The phosphoinositide binding Phox Homology domain of KIF16B kinesin or Sorting Nexin 23; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. KIF16B, also called sorting nexin 23 (SNX23), is a family-3 kinesin which harbors an N-terminal kinesin motor domain containing ATP and microtubule binding sites, a ForkHead Associated (FHA) domain, and a C-terminal PX domain. The PX domain of KIF16B binds to phosphatidylinositol-3-phosphate (PI3P) in early endosomes and plays a role in the transport of early endosomes to the plus end of microtubules. By regulating early endosome plus end motility, KIF16B modulates the balance between recycling and degradation of receptors. SNXs make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway.


:

Pssm-ID: 132784  Cd Length: 127  Bit Score: 251.92  E-value: 1.14e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287 1179 IKISIPRYVLCGQGKDEHFEFEVKISVLDETWTVFRRYSRFREMHKTLKLKYAELAALEFPPKKLFGNKDERVVAERRTH 1258
Cdd:cd06874     1 IKITIPRYVLRGQGKDEHFEFEVKITVLDETWTVFRRYSRFRELHKTMKLKYPEVAALEFPPKKLFGNKSERVAKERRRQ 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 124487287 1259 LEKYLREFFSVMLQSETSPLHiNKVGLTLSKHTICEFSPFFKKGVFDY 1306
Cdd:cd06874    81 LETYLRNFFSVCLKLPACPLY-PKVGRTLSKATLCDFSPFFRKGVFEN 127
FHA super family cl00062
forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small ...
446-562 1.42e-76

forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small phosphopeptide recognition modules mostly found in eubacteria and eukaryotes. It is about 95-120 residues long that fold into an 11-stranded beta-sandwich. FHA domains can mediate the recognition of phosphorylated and non-phosphorylated substrates, as well as protein oligomerization. They specifically recognize threonine phosphorylation (pThr) accompanying activation of protein serine/threonine kinases. FHA domains show diverse ligand specificity. They may recognize the pTXXD motif, the pTXXI/L motif, and TQ clusters (singly and multiply phosphorylated). In eukaryotes, FHA superfamily members include forkhead-type transcription factors, as well as other signaling proteins, such as many regulatory proteins, kinases, phosphatases, motor proteins called kinesins, and metabolic enzymes. Many of them localize to the nucleus, where they participate in establishing or maintaining cell cycle checkpoints, DNA repair, or transcriptional regulation. FHA domains play important roles in human diseases, particularly in relation to DNA damage responses and cancers. In bacteria, FHA domain-containing proteins may participate in injection of viral proteins into host cells, transmembrane transporters, and cell division. FHA domain-containing proteins rarely include more than one copy of the domain. The only exception in eukaryotes is the checkpoint kinase Rad53 from Saccharomyces cerevisiae, which harbors two FHA domains (FHA1 and FHA2) flanking a central kinase domain. The two FHA domains recognize different phosphorylated targets and function independently from one another. In contrast, Mycobacterium tuberculosis ABC transporter Rv1747 contains two FHA domains but only one of them is essential for protein function.


The actual alignment was detected with superfamily member cd22732:

Pssm-ID: 469597 [Multi-domain]  Cd Length: 117  Bit Score: 248.31  E-value: 1.42e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  446 GVVLDSELPHLIGIDDDLLSTGIILYHLKEGQTYVGREDASTEQDIVLHGLDLESEHCVFENAGGTVTLIPLRGSQCSVN 525
Cdd:cd22732     1 GVVLDSELPHLIGIDDDLLSTGIILYHLKEGRTYVGRDDATTEQDIVLHGLDLESEHCIFENLNGTVTLIPLNGAQCSVN 80
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 124487287  526 GVQIVDATQLNQGAVILLGRTNMFRFNHPKEAAKLRE 562
Cdd:cd22732    81 GVQITEATQLNQGAVILLGRTNMFRFNHPKEAAKLRE 117
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
599-1073 1.61e-16

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: 85.37  E-value: 1.61e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  599 ERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETRRKETEIVQRQIRKQEESLKRRSFHIENKLKDLLAEKER 678
Cdd:COG1196   290 EYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLE 369
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  679 FEEERLREQQGLEQQRRQEEESLFRIREELRKLQELNSHEQAEKvqifQELDRLHQEQNAQSAKLRLEKRRLEEEEKEQV 758
Cdd:COG1196   370 AEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALL----ERLERLEEELEELEEALAELEEEEEEEEEALE 445
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  759 QRVAHLEEQLRKRQDTAPLLcpgeaQRAQEEKRELESIREALLQAKEMRAGGDHTCRDELERAQQYFLEFKRRQLVKLAS 838
Cdd:COG1196   446 EAAEEEAELEEEEEALLELL-----AELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLR 520
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  839 LEKDLVQQ--------------------KDLLSKEVQEEKVALEHVKCDAGGDPSFLATDDGNILGGPPDLDKIKTAETR 898
Cdd:COG1196   521 GLAGAVAVligveaayeaaleaalaaalQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAA 600
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  899 LQSREHQLQDLLQNHLPALLEEKQRVLDALDS-GVLGLDTTLCQVEKEVGEKEEQIAQYQANASQLQQLRATFEFTANVA 977
Cdd:COG1196   601 VDLVASDLREADARYYVLGDTLLGRTLVAARLeAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAE 680
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  978 RQEEKVRRKEKEILESQEKQQREALEQAVAKLEQRRSALQRCSTLDLEIQEQRQKLGSLHTSEWSGWQASLETDGEALEM 1057
Cdd:COG1196   681 LEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPP 760
                         490
                  ....*....|....*.
gi 124487287 1058 DPARLEHEIHQLKQKI 1073
Cdd:COG1196   761 DLEELERELERLEREI 776
Kinesin_assoc super family cl24686
Kinesin-associated;
364-476 4.35e-11

Kinesin-associated;


The actual alignment was detected with superfamily member pfam16183:

Pssm-ID: 465047 [Multi-domain]  Cd Length: 177  Bit Score: 62.94  E-value: 4.35e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287   364 INEDANVKLIRELRAEIARLKTLL-AQG----------------NQIA-------------------------------- 394
Cdd:pfam16183    3 INEDPNNKLIRELKDEVARLRDLLyAQGlgdiidtiahptkkraNTPAanasaataamagaspspslsalssraasvssl 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287   395 ---LLDSPTALSMEEKLHQNEARVQELTKEWTNKWNETQNI-------LKEQTLALRKEG--IGVVLDSELPHLIGIDDD 462
Cdd:pfam16183   83 herIMFTPGSEEAIERLKETEKIIAELNETWEEKLRKTEAIrmerealLAEMGVAIREDGgtLGVFSPKKTPHLVNLNED 162
                          170
                   ....*....|....
gi 124487287   463 LLSTGIILYHLKEG 476
Cdd:pfam16183  163 PLMSECLLYYIKDG 176
 
Name Accession Description Interval E-value
KISc_KIF1A_KIF1B cd01365
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A ...
2-365 0e+00

Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A (Unc104) transports synaptic vesicles to the nerve terminal, KIF1B has been implicated in transport of mitochondria. Both proteins are expressed in neurons. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. In contrast to the majority of dimeric kinesins, most KIF1A/Unc104 kinesins are monomeric motors. A lysine-rich loop in KIF1A binds to the negatively charged C-terminus of tubulin and compensates for the lack of a second motor domain, allowing KIF1A to move processively.


Pssm-ID: 276816 [Multi-domain]  Cd Length: 361  Bit Score: 561.97  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287    2 ASVKVAVRVRPMNRREKDLEAKFIIQMEKSKTTITNLKIPEGGTGDSgRERTKTFTYDFSFYSADTKSPDYVSQEMVFKT 81
Cdd:cd01365     1 ANVKVAVRVRPFNSREKERNSKCIVQMSGKETTLKNPKQADKNNKAT-REVPKSFSFDYSYWSHDSEDPNYASQEQVYED 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287   82 LGTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGNSGDSGLIPRICEALFSRINETTRwDEASFRTEVSYLEIYNERVRDL 161
Cdd:cd01365    80 LGEELLQHAFEGYNVCLFAYGQTGSGKSYTMMGTQEQPGIIPRLCEDLFSRIADTTN-QNMSYSVEVSYMEIYNEKVRDL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  162 L-RRKSSKTFNLRVREHPKEGPYVEDLSKHLVQNYSDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQAKFDAE- 239
Cdd:cd01365   159 LnPKPKKNKGNLKVREHPVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVFTIVLTQKRHDAEt 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  240 -MPCETVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADLSQDAAnplvKKKQVFVPYRDSVLTWL 318
Cdd:cd01365   239 nLTTEKVSKISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKVISALADMSSGKS----KKKSSFIPYRDSVLTWL 314
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 124487287  319 LKDSLGGNSKTIMIATISPADVNYGETLSTLRYANRAKNIINKPTIN 365
Cdd:cd01365   315 LKENLGGNSKTAMIAAISPADINYEETLSTLRYADRAKKIVNRAVVN 361
KISc smart00129
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ...
3-365 1.70e-152

Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play important roles in intracellular transport of organelles and in cell division.


Pssm-ID: 214526 [Multi-domain]  Cd Length: 335  Bit Score: 462.43  E-value: 1.70e-152
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287      3 SVKVAVRVRPMNRREKDLEAKFIIQMEKSKTTITNLKIPEGgtgdsgRERTKTFTYDFSFysadtksPDYVSQEMVFKTL 82
Cdd:smart00129    1 NIRVVVRVRPLNKREKSRKSPSVVPFPDKVGKTLTVRSPKN------RQGEKKFTFDKVF-------DATASQEDVFEET 67
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287     83 GTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGNSGDSGLIPRICEALFSRINETTrwDEASFRTEVSYLEIYNERVRDLL 162
Cdd:smart00129   68 AAPLVDSVLEGYNATIFAYGQTGSGKTYTMIGTPDSPGIIPRALKDLFEKIDKRE--EGWQFSVKVSYLEIYNEKIRDLL 145
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287    163 RRKSSKtfnLRVREHPKEGPYVEDLSKHLVQNYSDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQAKFDAEMPC 242
Cdd:smart00129  146 NPSSKK---LEIREDEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKIKNSSSGS 222
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287    243 ETVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADLSqdaanplvkkKQVFVPYRDSVLTWLLKDS 322
Cdd:smart00129  223 GKASKLNLVDLAGSERAKKTGAEGDRLKEAGNINKSLSALGNVINALAQHS----------KSRHIPYRDSKLTRLLQDS 292
                           330       340       350       360
                    ....*....|....*....|....*....|....*....|...
gi 124487287    323 LGGNSKTIMIATISPADVNYGETLSTLRYANRAKNIINKPTIN 365
Cdd:smart00129  293 LGGNSKTLMIANVSPSSSNLEETLSTLRFASRAKEIKNKPIVN 335
Kinesin pfam00225
Kinesin motor domain;
9-358 2.55e-151

Kinesin motor domain;


Pssm-ID: 459720 [Multi-domain]  Cd Length: 326  Bit Score: 458.96  E-value: 2.55e-151
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287     9 RVRPMNRREKDLEAKFIIQMEKSKTTITNLKIpeggtgDSGRERTKTFTYDFSFYSADTkspdyvsQEMVFKTLGTDVVK 88
Cdd:pfam00225    1 RVRPLNEREKERGSSVIVSVESVDSETVESSH------LTNKNRTKTFTFDKVFDPEAT-------QEDVYEETAKPLVE 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287    89 SAFEGYNACVFAYGQTGSGKSYTMMGNSGDSGLIPRICEALFSRINETTrwDEASFRTEVSYLEIYNERVRDLLRRKSSK 168
Cdd:pfam00225   68 SVLEGYNVTIFAYGQTGSGKTYTMEGSDEQPGIIPRALEDLFDRIQKTK--ERSEFSVKVSYLEIYNEKIRDLLSPSNKN 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287   169 TFNLRVREHPKEGPYVEDLSKHLVQNYSDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQAKFDAEMPCE-TVSK 247
Cdd:pfam00225  146 KRKLRIREDPKKGVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNRSTGGEESvKTGK 225
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287   248 IHLVDLAGSERADATG-ATGVRLKEGGNINKSLVTLGNVISALADlsqdaanplvkKKQVFVPYRDSVLTWLLKDSLGGN 326
Cdd:pfam00225  226 LNLVDLAGSERASKTGaAGGQRLKEAANINKSLSALGNVISALAD-----------KKSKHIPYRDSKLTRLLQDSLGGN 294
                          330       340       350
                   ....*....|....*....|....*....|..
gi 124487287   327 SKTIMIATISPADVNYGETLSTLRYANRAKNI 358
Cdd:pfam00225  295 SKTLMIANISPSSSNYEETLSTLRFASRAKNI 326
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
27-507 2.61e-84

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 287.02  E-value: 2.61e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287   27 QMEKSKTTITNLKIPEGGTGDSGRER-----------TKTFTYDFSFYSADTkspdyvsQEMVFKTLGTDVVKSAFEGYN 95
Cdd:COG5059    18 EKSVSDIKSTIRIIPGELGERLINTSkkshvslekskEGTYAFDKVFGPSAT-------QEDVYEETIKPLIDSLLLGYN 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287   96 ACVFAYGQTGSGKSYTMMGNSGDSGLIPRICEALFSRINEttRWDEASFRTEVSYLEIYNERVRDLLrrkSSKTFNLRVR 175
Cdd:COG5059    91 CTVFAYGQTGSGKTYTMSGTEEEPGIIPLSLKELFSKLED--LSMTKDFAVSISYLEIYNEKIYDLL---SPNEESLNIR 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  176 EHPKEGPYVEDLSKHLVQNYSDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIkfTQAKFDAEMPCETVSKIHLVDLAG 255
Cdd:COG5059   166 EDSLLGVKVAGLTEKHVSSKEEILDLLRKGEKNRTTASTEINDESSRSHSIFQI--ELASKNKVSGTSETSKLSLVDLAG 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  256 SERADATGATGVRLKEGGNINKSLVTLGNVISALADlsqdaanplvKKKQVFVPYRDSVLTWLLKDSLGGNSKTIMIATI 335
Cdd:COG5059   244 SERAARTGNRGTRLKEGASINKSLLTLGNVINALGD----------KKKSGHIPYRESKLTRLLQDSLGGNCNTRVICTI 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  336 SPADVNYGETLSTLRYANRAKNIINKPTINEDANVKL--------IRELRAEIARLKTLLAQGNQIALLDSPTA--LSME 405
Cdd:COG5059   314 SPSSNSFEETINTLKFASRAKSIKNKIQVNSSSDSSReieeikfdLSEDRSEIEILVFREQSQLSQSSLSGIFAymQSLK 393
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  406 EKLHQNEARVQELTKEWTNKWNETQNILKEQTLALRKEG---------IGVVLDSELPHLIGIDDDLLSTGIILYHLKEG 476
Cdd:COG5059   394 KETETLKSRIDLIMKSIISGTFERKKLLKEEGWKYKSTLqflrieidrLLLLREEELSKKKTKIHKLNKLRHDLSSLLSS 473
                         490       500       510
                  ....*....|....*....|....*....|....*...
gi 124487287  477 QT-----YVGREDASTEQDIVLHGLDLES--EHCVFEN 507
Cdd:COG5059   474 IPeetsdRVESEKASKLRSSASTKLNLRSsrSHSKFRD 511
PX_KIF16B_SNX23 cd06874
The phosphoinositide binding Phox Homology domain of KIF16B kinesin or Sorting Nexin 23; The ...
1179-1306 1.14e-77

The phosphoinositide binding Phox Homology domain of KIF16B kinesin or Sorting Nexin 23; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. KIF16B, also called sorting nexin 23 (SNX23), is a family-3 kinesin which harbors an N-terminal kinesin motor domain containing ATP and microtubule binding sites, a ForkHead Associated (FHA) domain, and a C-terminal PX domain. The PX domain of KIF16B binds to phosphatidylinositol-3-phosphate (PI3P) in early endosomes and plays a role in the transport of early endosomes to the plus end of microtubules. By regulating early endosome plus end motility, KIF16B modulates the balance between recycling and degradation of receptors. SNXs make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway.


Pssm-ID: 132784  Cd Length: 127  Bit Score: 251.92  E-value: 1.14e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287 1179 IKISIPRYVLCGQGKDEHFEFEVKISVLDETWTVFRRYSRFREMHKTLKLKYAELAALEFPPKKLFGNKDERVVAERRTH 1258
Cdd:cd06874     1 IKITIPRYVLRGQGKDEHFEFEVKITVLDETWTVFRRYSRFRELHKTMKLKYPEVAALEFPPKKLFGNKSERVAKERRRQ 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 124487287 1259 LEKYLREFFSVMLQSETSPLHiNKVGLTLSKHTICEFSPFFKKGVFDY 1306
Cdd:cd06874    81 LETYLRNFFSVCLKLPACPLY-PKVGRTLSKATLCDFSPFFRKGVFEN 127
FHA_KIF16B cd22732
forkhead associated (FHA) domain found in kinesin-like protein KIF16B; KIF16B, also called ...
446-562 1.42e-76

forkhead associated (FHA) domain found in kinesin-like protein KIF16B; KIF16B, also called sorting nexin-23, is a plus end-directed microtubule-dependent motor protein involved in endosome transport and receptor recycling and degradation. It regulates the plus end motility of early endosomes and the balance between recycling and degradation of receptors such as EGF receptor (EGFR) and FGF receptor (FGFR). It regulates the Golgi to endosome transport of FGFR-containing vesicles during early development, a key process for developing basement membrane and epiblast and primitive endoderm lineages during early postimplantation development. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438784 [Multi-domain]  Cd Length: 117  Bit Score: 248.31  E-value: 1.42e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  446 GVVLDSELPHLIGIDDDLLSTGIILYHLKEGQTYVGREDASTEQDIVLHGLDLESEHCVFENAGGTVTLIPLRGSQCSVN 525
Cdd:cd22732     1 GVVLDSELPHLIGIDDDLLSTGIILYHLKEGRTYVGRDDATTEQDIVLHGLDLESEHCIFENLNGTVTLIPLNGAQCSVN 80
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 124487287  526 GVQIVDATQLNQGAVILLGRTNMFRFNHPKEAAKLRE 562
Cdd:cd22732    81 GVQITEATQLNQGAVILLGRTNMFRFNHPKEAAKLRE 117
PLN03188 PLN03188
kinesin-12 family protein; Provisional
4-392 2.54e-75

kinesin-12 family protein; Provisional


Pssm-ID: 215621 [Multi-domain]  Cd Length: 1320  Bit Score: 274.89  E-value: 2.54e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287    4 VKVAVRVRPMNrreKDLEAKFIIQ-MEKSKTTITNlkipeggtgdsgrertKTFTYDfsfYSADTKSpdyvSQEMVFKTL 82
Cdd:PLN03188  100 VKVIVRMKPLN---KGEEGEMIVQkMSNDSLTING----------------QTFTFD---SIADPES----TQEDIFQLV 153
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287   83 GTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGN---------SGDS-GLIPRICEALFSRINE-----TTRwdEASFRTE 147
Cdd:PLN03188  154 GAPLVENCLAGFNSSVFAYGQTGSGKTYTMWGPanglleehlSGDQqGLTPRVFERLFARINEeqikhADR--QLKYQCR 231
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  148 VSYLEIYNERVRDLLRrKSSKtfNLRVREHPKEGPYVEDLSKHLVQNYSDVEELMDAGNINRTTAATGMNDVSSRSHAIF 227
Cdd:PLN03188  232 CSFLEIYNEQITDLLD-PSQK--NLQIREDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVF 308
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  228 T-IKFTQAKFDAE-MPCETVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADLSQDAanplvkkKQ 305
Cdd:PLN03188  309 TcVVESRCKSVADgLSSFKTSRINLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILAEISQTG-------KQ 381
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  306 VFVPYRDSVLTWLLKDSLGGNSKTIMIATISPADVNYGETLSTLRYANRAKNIINKPTINE----DANV--KLIRELRAE 379
Cdd:PLN03188  382 RHIPYRDSRLTFLLQESLGGNAKLAMVCAISPSQSCKSETFSTLRFAQRAKAIKNKAVVNEvmqdDVNFlrEVIRQLRDE 461
                         410
                  ....*....|...
gi 124487287  380 IARLKtllAQGNQ 392
Cdd:PLN03188  462 LQRVK---ANGNN 471
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
599-1073 1.61e-16

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 85.37  E-value: 1.61e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  599 ERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETRRKETEIVQRQIRKQEESLKRRSFHIENKLKDLLAEKER 678
Cdd:COG1196   290 EYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLE 369
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  679 FEEERLREQQGLEQQRRQEEESLFRIREELRKLQELNSHEQAEKvqifQELDRLHQEQNAQSAKLRLEKRRLEEEEKEQV 758
Cdd:COG1196   370 AEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALL----ERLERLEEELEELEEALAELEEEEEEEEEALE 445
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  759 QRVAHLEEQLRKRQDTAPLLcpgeaQRAQEEKRELESIREALLQAKEMRAGGDHTCRDELERAQQYFLEFKRRQLVKLAS 838
Cdd:COG1196   446 EAAEEEAELEEEEEALLELL-----AELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLR 520
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  839 LEKDLVQQ--------------------KDLLSKEVQEEKVALEHVKCDAGGDPSFLATDDGNILGGPPDLDKIKTAETR 898
Cdd:COG1196   521 GLAGAVAVligveaayeaaleaalaaalQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAA 600
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  899 LQSREHQLQDLLQNHLPALLEEKQRVLDALDS-GVLGLDTTLCQVEKEVGEKEEQIAQYQANASQLQQLRATFEFTANVA 977
Cdd:COG1196   601 VDLVASDLREADARYYVLGDTLLGRTLVAARLeAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAE 680
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  978 RQEEKVRRKEKEILESQEKQQREALEQAVAKLEQRRSALQRCSTLDLEIQEQRQKLGSLHTSEWSGWQASLETDGEALEM 1057
Cdd:COG1196   681 LEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPP 760
                         490
                  ....*....|....*.
gi 124487287 1058 DPARLEHEIHQLKQKI 1073
Cdd:COG1196   761 DLEELERELERLEREI 776
PX smart00312
PhoX homologous domain, present in p47phox and p40phox; Eukaryotic domain of unknown function ...
1192-1265 4.31e-12

PhoX homologous domain, present in p47phox and p40phox; Eukaryotic domain of unknown function present in phox proteins, PLD isoforms, a PI3K isoform.


Pssm-ID: 214610  Cd Length: 105  Bit Score: 63.90  E-value: 4.31e-12
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124487287   1192 GKDEHFEFEVKISVLD--ETWTVFRRYSRFREMHKTLKLKYAELAALEFPPKKLFG---NKDERVVAERRTHLEKYLRE 1265
Cdd:smart00312    8 GDGKHYYYVIEIETKTglEEWTVSRRYSDFLELHSKLKKHFPRSILPPLPGKKLFGrlnNFSEEFIEKRRRGLEKYLQS 86
PX pfam00787
PX domain; PX domains bind to phosphoinositides.
1207-1265 1.36e-11

PX domain; PX domains bind to phosphoinositides.


Pssm-ID: 459940  Cd Length: 84  Bit Score: 61.49  E-value: 1.36e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 124487287  1207 DETWTVFRRYSRFREMHKTLKLKYAELAALEFPPKKLFGNKDERVVAERRTHLEKYLRE 1265
Cdd:pfam00787    6 LEEWSVRRRYSDFVELHKKLLRKFPSVIIPPLPPKRWLGRYNEEFIEKRRKGLEQYLQR 64
Kinesin_assoc pfam16183
Kinesin-associated;
364-476 4.35e-11

Kinesin-associated;


Pssm-ID: 465047 [Multi-domain]  Cd Length: 177  Bit Score: 62.94  E-value: 4.35e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287   364 INEDANVKLIRELRAEIARLKTLL-AQG----------------NQIA-------------------------------- 394
Cdd:pfam16183    3 INEDPNNKLIRELKDEVARLRDLLyAQGlgdiidtiahptkkraNTPAanasaataamagaspspslsalssraasvssl 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287   395 ---LLDSPTALSMEEKLHQNEARVQELTKEWTNKWNETQNI-------LKEQTLALRKEG--IGVVLDSELPHLIGIDDD 462
Cdd:pfam16183   83 herIMFTPGSEEAIERLKETEKIIAELNETWEEKLRKTEAIrmerealLAEMGVAIREDGgtLGVFSPKKTPHLVNLNED 162
                          170
                   ....*....|....
gi 124487287   463 LLSTGIILYHLKEG 476
Cdd:pfam16183  163 PLMSECLLYYIKDG 176
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
597-1075 6.06e-09

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 60.75  E-value: 6.06e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287   597 EFERQQREELEKLESKRKLIEEMEEKQKSDK-------------AELERMQQEVETRRKETEIVQRQIRKQEESLKRRSF 663
Cdd:TIGR00618  233 EALQQTQQSHAYLTQKREAQEEQLKKQQLLKqlrarieelraqeAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRI 312
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287   664 HIENKLKDLLAEKERFEEERLREQQGLEQQRRQEEESLFRIREELRKLQELNSHEQAEKVQIFQELDRLHQEQNAQSAKL 743
Cdd:TIGR00618  313 HTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLT 392
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287   744 RLEKRRLEEEEKEQV----------------QRVAHLEEQLRKRQDTAPLLCPGEAQRAQEEKRELESIREALLQAKEMr 807
Cdd:TIGR00618  393 QKLQSLCKELDILQReqatidtrtsafrdlqGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKER- 471
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287   808 aggdhtcRDELERAQQYFLEFKRRQLVKLASLEKdLVQQKDLLSKEVQEEKVALEHVKCDAGGDPSFLATDDGNILGGP- 886
Cdd:TIGR00618  472 -------EQQLQTKEQIHLQETRKKAVVLARLLE-LQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETs 543
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287   887 -PDLDKIKTAET-RLQSREHQLQDLLQN-------------HLPALLEEKQRVLDALDSGVLGLDTTLCQVEKEVGEKEE 951
Cdd:TIGR00618  544 eEDVYHQLTSERkQRASLKEQMQEIQQSfsiltqcdnrskeDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQP 623
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287   952 QIAQYQANASQ------LQQLRATFEFTA-NVARQEEKVRRKEKEILESQEKQQREALEQAV-AKLEQRRSALQRCSTLD 1023
Cdd:TIGR00618  624 EQDLQDVRLHLqqcsqeLALKLTALHALQlTLTQERVREHALSIRVLPKELLASRQLALQKMqSEKEQLTYWKEMLAQCQ 703
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 124487287  1024 LEIQEQRQKLGSL--HTSEWSGWQASLETDGEALEMDPARLEHEI-HQLKQKICE 1075
Cdd:TIGR00618  704 TLLRELETHIEEYdrEFNEIENASSSLGSDLAAREDALNQSLKELmHQARTVLKA 758
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
592-862 6.89e-09

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: 60.14  E-value: 6.89e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287   592 YNPGLEFERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETRRKETEivqrQIRKQEESLKRRSFHIENKlkd 671
Cdd:pfam17380  260 YNGQTMTENEFLNQLLHIVQHQKAVSERQQQEKFEKMEQERLRQEKEEKAREVE----RRRKLEEAEKARQAEMDRQ--- 332
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287   672 llaekerfeEERLREQQGLEQQRRQEEEslfRIREELRK--LQELNSHEQAEKVQIFQELDRLHQEQNAQSaklrlekrr 749
Cdd:pfam17380  333 ---------AAIYAEQERMAMERERELE---RIRQEERKreLERIRQEEIAMEISRMRELERLQMERQQKN--------- 391
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287   750 LEEEEKEQVQRVAHLEEQLRKRQDTAPLLCPGEAQRAQEEKRELESIREALLQAKEMraggDHTCRDELERAQQyfLEFK 829
Cdd:pfam17380  392 ERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREM----ERVRLEEQERQQQ--VERL 465
                          250       260       270
                   ....*....|....*....|....*....|...
gi 124487287   830 RRQlvklaslEKDLVQQKDLLSKEVQEEKVALE 862
Cdd:pfam17380  466 RQQ-------EEERKRKKLELEKEKRDRKRAEE 491
FHA COG1716
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];
471-551 3.16e-07

Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];


Pssm-ID: 441322 [Multi-domain]  Cd Length: 96  Bit Score: 49.57  E-value: 3.16e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  471 YHLKEGQTYVGRedaSTEQDIVLHGLDLESEHCVFENAGGTVTLIPLrGSQ--CSVNGVQIVDATQLNQGAVILLGRTnM 548
Cdd:COG1716    16 FPLDGGPLTIGR---APDNDIVLDDPTVSRRHARIRRDGGGWVLEDL-GSTngTFVNGQRVTEPAPLRDGDVIRLGKT-E 90

                  ...
gi 124487287  549 FRF 551
Cdd:COG1716    91 LRF 93
PTZ00121 PTZ00121
MAEBL; Provisional
597-797 1.45e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 53.22  E-value: 1.45e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  597 EFERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVEtrrkETEIVQRQIRKQEESLKRRSFHIENKlkdllaek 676
Cdd:PTZ00121 1616 EEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEE----ENKIKAAEEAKKAEEDKKKAEEAKKA-------- 1683
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  677 erfeeerlreqqglEQQRRQEEESLFRIREELRKLQELNSHE-----QAEKVQIFQELDRLHQEQNAQSAKLRLEKRRLE 751
Cdd:PTZ00121 1684 --------------EEDEKKAAEALKKEAEEAKKAEELKKKEaeekkKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEA 1749
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 124487287  752 EEEKEQVQRVAHLEEQLRKRQDTAPLLCPG---EAQRAQEEKRELESIR 797
Cdd:PTZ00121 1750 KKDEEEKKKIAHLKKEEEKKAEEIRKEKEAvieEELDEEDEKRRMEVDK 1798
Yop-YscD_cpl pfam16697
Inner membrane component of T3SS, cytoplasmic domain; Yop-YscD-cpl is the cytoplasmic domain ...
471-555 1.78e-04

Inner membrane component of T3SS, cytoplasmic domain; Yop-YscD-cpl is the cytoplasmic domain of Yop proteins like YscD from Proteobacteria. YscD forms part of the inner membrane component of the bacterial type III secretion injectosome apparatus.


Pssm-ID: 465238 [Multi-domain]  Cd Length: 94  Bit Score: 41.86  E-value: 1.78e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287   471 YHLKEGQTYVGREDastEQDIVLHGLDLESEHCVFENAGGTVTLIPLR-GSQCSVNGVQIVDAT-QLNQGAVILLGRTnM 548
Cdd:pfam16697   12 FPLEGGRYRIGSDP---DCDIVLSDKEVSRVHLKLEVDDEGWRLDDLGsGNGTLVNGQRVTELGiALRPGDRIELGQT-E 87

                   ....*..
gi 124487287   549 FRFNHPK 555
Cdd:pfam16697   88 FCLVPAD 94
COG5391 COG5391
Phox homology (PX) domain protein [Intracellular trafficking and secretion / General function ...
1211-1267 6.85e-03

Phox homology (PX) domain protein [Intracellular trafficking and secretion / General function prediction only];


Pssm-ID: 227680 [Multi-domain]  Cd Length: 524  Bit Score: 40.55  E-value: 6.85e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124487287 1211 TVFRRYSRFREMHKTLKLKYAELAALEFPPKKLFGNK-----DERVVAERRTHLEKYLREFF 1267
Cdd:COG5391   174 VVRRRYSDFESLHSILIKLLPLCAIPPLPSKKSNSEYygdrfSDEFIEERRQSLQNFLRRVS 235
 
Name Accession Description Interval E-value
KISc_KIF1A_KIF1B cd01365
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A ...
2-365 0e+00

Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A (Unc104) transports synaptic vesicles to the nerve terminal, KIF1B has been implicated in transport of mitochondria. Both proteins are expressed in neurons. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. In contrast to the majority of dimeric kinesins, most KIF1A/Unc104 kinesins are monomeric motors. A lysine-rich loop in KIF1A binds to the negatively charged C-terminus of tubulin and compensates for the lack of a second motor domain, allowing KIF1A to move processively.


Pssm-ID: 276816 [Multi-domain]  Cd Length: 361  Bit Score: 561.97  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287    2 ASVKVAVRVRPMNRREKDLEAKFIIQMEKSKTTITNLKIPEGGTGDSgRERTKTFTYDFSFYSADTKSPDYVSQEMVFKT 81
Cdd:cd01365     1 ANVKVAVRVRPFNSREKERNSKCIVQMSGKETTLKNPKQADKNNKAT-REVPKSFSFDYSYWSHDSEDPNYASQEQVYED 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287   82 LGTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGNSGDSGLIPRICEALFSRINETTRwDEASFRTEVSYLEIYNERVRDL 161
Cdd:cd01365    80 LGEELLQHAFEGYNVCLFAYGQTGSGKSYTMMGTQEQPGIIPRLCEDLFSRIADTTN-QNMSYSVEVSYMEIYNEKVRDL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  162 L-RRKSSKTFNLRVREHPKEGPYVEDLSKHLVQNYSDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQAKFDAE- 239
Cdd:cd01365   159 LnPKPKKNKGNLKVREHPVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVFTIVLTQKRHDAEt 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  240 -MPCETVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADLSQDAAnplvKKKQVFVPYRDSVLTWL 318
Cdd:cd01365   239 nLTTEKVSKISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKVISALADMSSGKS----KKKSSFIPYRDSVLTWL 314
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 124487287  319 LKDSLGGNSKTIMIATISPADVNYGETLSTLRYANRAKNIINKPTIN 365
Cdd:cd01365   315 LKENLGGNSKTAMIAAISPADINYEETLSTLRYADRAKKIVNRAVVN 361
KISc smart00129
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ...
3-365 1.70e-152

Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play important roles in intracellular transport of organelles and in cell division.


Pssm-ID: 214526 [Multi-domain]  Cd Length: 335  Bit Score: 462.43  E-value: 1.70e-152
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287      3 SVKVAVRVRPMNRREKDLEAKFIIQMEKSKTTITNLKIPEGgtgdsgRERTKTFTYDFSFysadtksPDYVSQEMVFKTL 82
Cdd:smart00129    1 NIRVVVRVRPLNKREKSRKSPSVVPFPDKVGKTLTVRSPKN------RQGEKKFTFDKVF-------DATASQEDVFEET 67
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287     83 GTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGNSGDSGLIPRICEALFSRINETTrwDEASFRTEVSYLEIYNERVRDLL 162
Cdd:smart00129   68 AAPLVDSVLEGYNATIFAYGQTGSGKTYTMIGTPDSPGIIPRALKDLFEKIDKRE--EGWQFSVKVSYLEIYNEKIRDLL 145
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287    163 RRKSSKtfnLRVREHPKEGPYVEDLSKHLVQNYSDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQAKFDAEMPC 242
Cdd:smart00129  146 NPSSKK---LEIREDEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKIKNSSSGS 222
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287    243 ETVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADLSqdaanplvkkKQVFVPYRDSVLTWLLKDS 322
Cdd:smart00129  223 GKASKLNLVDLAGSERAKKTGAEGDRLKEAGNINKSLSALGNVINALAQHS----------KSRHIPYRDSKLTRLLQDS 292
                           330       340       350       360
                    ....*....|....*....|....*....|....*....|...
gi 124487287    323 LGGNSKTIMIATISPADVNYGETLSTLRYANRAKNIINKPTIN 365
Cdd:smart00129  293 LGGNSKTLMIANVSPSSSNLEETLSTLRFASRAKEIKNKPIVN 335
Kinesin pfam00225
Kinesin motor domain;
9-358 2.55e-151

Kinesin motor domain;


Pssm-ID: 459720 [Multi-domain]  Cd Length: 326  Bit Score: 458.96  E-value: 2.55e-151
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287     9 RVRPMNRREKDLEAKFIIQMEKSKTTITNLKIpeggtgDSGRERTKTFTYDFSFYSADTkspdyvsQEMVFKTLGTDVVK 88
Cdd:pfam00225    1 RVRPLNEREKERGSSVIVSVESVDSETVESSH------LTNKNRTKTFTFDKVFDPEAT-------QEDVYEETAKPLVE 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287    89 SAFEGYNACVFAYGQTGSGKSYTMMGNSGDSGLIPRICEALFSRINETTrwDEASFRTEVSYLEIYNERVRDLLRRKSSK 168
Cdd:pfam00225   68 SVLEGYNVTIFAYGQTGSGKTYTMEGSDEQPGIIPRALEDLFDRIQKTK--ERSEFSVKVSYLEIYNEKIRDLLSPSNKN 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287   169 TFNLRVREHPKEGPYVEDLSKHLVQNYSDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQAKFDAEMPCE-TVSK 247
Cdd:pfam00225  146 KRKLRIREDPKKGVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNRSTGGEESvKTGK 225
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287   248 IHLVDLAGSERADATG-ATGVRLKEGGNINKSLVTLGNVISALADlsqdaanplvkKKQVFVPYRDSVLTWLLKDSLGGN 326
Cdd:pfam00225  226 LNLVDLAGSERASKTGaAGGQRLKEAANINKSLSALGNVISALAD-----------KKSKHIPYRDSKLTRLLQDSLGGN 294
                          330       340       350
                   ....*....|....*....|....*....|..
gi 124487287   327 SKTIMIATISPADVNYGETLSTLRYANRAKNI 358
Cdd:pfam00225  295 SKTLMIANISPSSSNYEETLSTLRFASRAKNI 326
KISc cd00106
Kinesin motor domain; Kinesin motor domain. This catalytic (head) domain has ATPase activity ...
3-356 7.39e-143

Kinesin motor domain; Kinesin motor domain. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type), in some its is found in the middle (M-type), or C-terminal (C-type). N-type and M-type kinesins are (+) end-directed motors, while C-type kinesins are (-) end-directed motors, i.e. they transport cargo towards the (-) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276812 [Multi-domain]  Cd Length: 326  Bit Score: 436.69  E-value: 7.39e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287    3 SVKVAVRVRPMNRREKDLEAKFIIQMEKSKTTITNLKIPEGGTgdsgrertKTFTYDFSFYSADTkspdyvsQEMVFKTL 82
Cdd:cd00106     1 NVRVAVRVRPLNGREARSAKSVISVDGGKSVVLDPPKNRVAPP--------KTFAFDAVFDSTST-------QEEVYEGT 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287   83 GTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGNSGDS-GLIPRICEALFSRINETtRWDEASFRTEVSYLEIYNERVRDL 161
Cdd:cd00106    66 AKPLVDSALEGYNGTIFAYGQTGSGKTYTMLGPDPEQrGIIPRALEDIFERIDKR-KETKSSFSVSASYLEIYNEKIYDL 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  162 LRRKSSKtfNLRVREHPKEGPYVEDLSKHLVQNYSDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQAKFDAEMP 241
Cdd:cd00106   145 LSPVPKK--PLSLREDPKRGVYVKGLTEVEVGSLEDALELLDAGNKNRTTASTNMNEHSSRSHAVFTIHVKQRNREKSGE 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  242 CETVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADlsqdaanplvkKKQVFVPYRDSVLTWLLKD 321
Cdd:cd00106   223 SVTSSKLNLVDLAGSERAKKTGAEGDRLKEGGNINKSLSALGKVISALAD-----------GQNKHIPYRDSKLTRLLQD 291
                         330       340       350
                  ....*....|....*....|....*....|....*
gi 124487287  322 SLGGNSKTIMIATISPADVNYGETLSTLRYANRAK 356
Cdd:cd00106   292 SLGGNSKTIMIACISPSSENFEETLSTLRFASRAK 326
KISc_KIF3 cd01371
Kinesin motor domain, kinesins II or KIF3_like proteins; Kinesin motor domain, kinesins II or ...
3-358 4.45e-119

Kinesin motor domain, kinesins II or KIF3_like proteins; Kinesin motor domain, kinesins II or KIF3_like proteins. Subgroup of kinesins, which form heterotrimers composed of 2 kinesins and one non-motor accessory subunit. Kinesins II play important roles in ciliary transport, and have been implicated in neuronal transport, melanosome transport, the secretory pathway, and mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In this group the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276822 [Multi-domain]  Cd Length: 334  Bit Score: 374.10  E-value: 4.45e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287    3 SVKVAVRVRPMNRREKDLEAKFIIQMEKSKTTITnLKIPEGGTGdsgrERTKTFTYDfSFYSADTKspdyvsQEMVFKTL 82
Cdd:cd01371     2 NVKVVVRCRPLNGKEKAAGALQIVDVDEKRGQVS-VRNPKATAN----EPPKTFTFD-AVFDPNSK------QLDVYDET 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287   83 GTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGNSGDS---GLIPRICEALFSRINETTrwDEASFRTEVSYLEIYNERVR 159
Cdd:cd01371    70 ARPLVDSVLEGYNGTIFAYGQTGTGKTYTMEGKREDPelrGIIPNSFAHIFGHIARSQ--NNQQFLVRVSYLEIYNEEIR 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  160 DLLRRKSSKtfNLRVREHPKEGPYVEDLSKHLVQNYSDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQAKF--D 237
Cdd:cd01371   148 DLLGKDQTK--RLELKERPDTGVYVKDLSMFVVKNADEMEHVMNLGNKNRSVGATNMNEDSSRSHAIFTITIECSEKgeD 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  238 AEMPCeTVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADlsqdaanplvkKKQVFVPYRDSVLTW 317
Cdd:cd01371   226 GENHI-RVGKLNLVDLAGSERQSKTGATGERLKEATKINLSLSALGNVISALVD-----------GKSTHIPYRDSKLTR 293
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 124487287  318 LLKDSLGGNSKTIMIATISPADVNYGETLSTLRYANRAKNI 358
Cdd:cd01371   294 LLQDSLGGNSKTVMCANIGPADYNYDETLSTLRYANRAKNI 334
KISc_KIF4 cd01372
Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members ...
3-358 1.56e-115

Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members of this group seem to perform a variety of functions, and have been implicated in neuronal organelle transport and chromosome segregation during mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276823 [Multi-domain]  Cd Length: 341  Bit Score: 364.73  E-value: 1.56e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287    3 SVKVAVRVRPMNRREKDLEAKFIIQMEKSKTTITnlkipeggtgdsgRERTKTFTYDFSFysaDTKSPdyvsQEMVFKTL 82
Cdd:cd01372     2 SVRVAVRVRPLLPKEIIEGCRICVSFVPGEPQVT-------------VGTDKSFTFDYVF---DPSTE----QEEVYNTC 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287   83 GTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGNSGDS------GLIPRICEALFSRINETTrwDEASFRTEVSYLEIYNE 156
Cdd:cd01372    62 VAPLVDGLFEGYNATVLAYGQTGSGKTYTMGTAYTAEedeeqvGIIPRAIQHIFKKIEKKK--DTFEFQLKVSFLEIYNE 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  157 RVRDLLRRKSSKTFNLRVREHPKEGPYVEDLSKHLVQNYSDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQAKF 236
Cdd:cd01372   140 EIRDLLDPETDKKPTISIREDSKGGITIVGLTEVTVLSAEDMMSCLEQGSLSRTTASTAMNSQSSRSHAIFTITLEQTKK 219
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  237 DAEMPC--------ETVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADLSQDAAnplvkkkqvFV 308
Cdd:cd01372   220 NGPIAPmsaddknsTFTSKFHFVDLAGSERLKRTGATGDRLKEGISINSGLLALGNVISALGDESKKGA---------HV 290
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 124487287  309 PYRDSVLTWLLKDSLGGNSKTIMIATISPADVNYGETLSTLRYANRAKNI 358
Cdd:cd01372   291 PYRDSKLTRLLQDSLGGNSHTLMIACVSPADSNFEETLNTLKYANRARNI 340
KISc_KIP3_like cd01370
Kinesin motor domain, KIP3-like subgroup; Kinesin motor domain, KIP3-like subgroup. The yeast ...
3-358 1.53e-104

Kinesin motor domain, KIP3-like subgroup; Kinesin motor domain, KIP3-like subgroup. The yeast kinesin KIP3 plays a role in positioning the mitotic spindle. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276821 [Multi-domain]  Cd Length: 345  Bit Score: 335.08  E-value: 1.53e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287    3 SVKVAVRVRPMNRREKDLEAKFIIQ-MEKS------KTTITNLKIPEGGTGDSGRERTKTFTYDFsfysaDTKSPDYVSQ 75
Cdd:cd01370     1 SLTVAVRVRPFSEKEKNEGFRRIVKvMDNHmlvfdpKDEEDGFFHGGSNNRDRRKRRNKELKYVF-----DRVFDETSTQ 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287   76 EMVFKTLGTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGNSGDSGLIPRICEALFSRINETTrwDEASFRTEVSYLEIYN 155
Cdd:cd01370    76 EEVYEETTKPLVDGVLNGYNATVFAYGATGAGKTHTMLGTPQEPGLMVLTMKELFKRIESLK--DEKEFEVSMSYLEIYN 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  156 ERVRDLLRrKSSKTfnLRVREHPKEGPYVEDLSKHLVQNYSDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQAK 235
Cdd:cd01370   154 ETIRDLLN-PSSGP--LELREDAQNGIVVAGLTEHSPKSAEEILELLMKGNRNRTQEPTDANATSSRSHAVLQITVRQQD 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  236 FDAEMPCET-VSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADLsqdaanplvKKKQVFVPYRDSV 314
Cdd:cd01370   231 KTASINQQVrQGKLSLIDLAGSERASATNNRGQRLKEGANINRSLLALGNCINALADP---------GKKNKHIPYRDSK 301
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 124487287  315 LTWLLKDSLGGNSKTIMIATISPADVNYGETLSTLRYANRAKNI 358
Cdd:cd01370   302 LTRLLKDSLGGNCRTVMIANISPSSSSYEETHNTLKYANRAKNI 345
KISc_KLP2_like cd01373
Kinesin motor domain, KIF15-like subgroup; Kinesin motor domain, KIF15-like subgroup. Members ...
4-367 1.74e-103

Kinesin motor domain, KIF15-like subgroup; Kinesin motor domain, KIF15-like subgroup. Members of this subgroup seem to play a role in mitosis and meiosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276824 [Multi-domain]  Cd Length: 347  Bit Score: 332.17  E-value: 1.74e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287    4 VKVAVRVRPMNRREKDLEAKFIIQMEkSKTTITNLKIPEggtgdsgrertKTFTYDfSFYSADTkspdyvSQEMVFKTLG 83
Cdd:cd01373     3 VKVFVRIRPPAEREGDGEYGQCLKKL-SSDTLVLHSKPP-----------KTFTFD-HVADSNT------NQESVFQSVG 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287   84 TDVVKSAFEGYNACVFAYGQTGSGKSYTMMGNS--------GDSGLIPRICEALFSRIN--ETTRWDEASFRTEVSYLEI 153
Cdd:cd01373    64 KPIVESCLSGYNGTIFAYGQTGSGKTYTMWGPSesdnesphGLRGVIPRIFEYLFSLIQreKEKAGEGKSFLCKCSFLEI 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  154 YNERVRDLLRRKSSktfNLRVREHPKEGPYVEDLSKHLVQNYSDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQ 233
Cdd:cd01373   144 YNEQIYDLLDPASR---NLKLREDIKKGVYVENLVEEYVTSAEDVYQVLSKGWSNRKVAATSMNRESSRSHAVFTCTIES 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  234 AKFDAEMPCETVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADLSQDaanplvkkKQVFVPYRDS 313
Cdd:cd01373   221 WEKKACFVNIRTSRLNLVDLAGSERQKDTHAEGVRLKEAGNINKSLSCLGHVINALVDVAHG--------KQRHVCYRDS 292
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 124487287  314 VLTWLLKDSLGGNSKTIMIATISPADVNYGETLSTLRYANRAKNIINKPTINED 367
Cdd:cd01373   293 KLTFLLRDSLGGNAKTAIIANVHPSSKCFGETLSTLRFAQRAKLIKNKAVVNED 346
KISc_CENP_E cd01374
Kinesin motor domain, CENP-E/KIP2-like subgroup; Kinesin motor domain, CENP-E/KIP2-like ...
3-358 8.67e-102

Kinesin motor domain, CENP-E/KIP2-like subgroup; Kinesin motor domain, CENP-E/KIP2-like subgroup, involved in chromosome movement and/or spindle elongation during mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276825 [Multi-domain]  Cd Length: 321  Bit Score: 326.60  E-value: 8.67e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287    3 SVKVAVRVRPMNRREKDLEAKFIiqMEKSKTTITNLKIPEGgtgdsgrertkTFTYDFSFysaDTKSPDYVsqemVFKTL 82
Cdd:cd01374     1 KITVTVRVRPLNSREIGINEQVA--WEIDNDTIYLVEPPST-----------SFTFDHVF---GGDSTNRE----VYELI 60
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287   83 GTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGNSGDSGLIPRICEALFSRINETTRWDeasFRTEVSYLEIYNERVRDLL 162
Cdd:cd01374    61 AKPVVKSALEGYNGTIFAYGQTSSGKTFTMSGDEDEPGIIPLAIRDIFSKIQDTPDRE---FLLRVSYLEIYNEKINDLL 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  163 rrkSSKTFNLRVREHPKEGPYVEDLSKHLVQNYSDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIK-FTQAKFDAEMP 241
Cdd:cd01374   138 ---SPTSQNLKIRDDVEKGVYVAGLTEEIVSSPEHALSLIARGEKNRHVGETDMNERSSRSHTIFRITiESSERGELEEG 214
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  242 CETVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADlsqdaanplvKKKQVFVPYRDSVLTWLLKD 321
Cdd:cd01374   215 TVRVSTLNLIDLAGSERAAQTGAAGVRRKEGSHINKSLLTLGTVISKLSE----------GKVGGHIPYRDSKLTRILQP 284
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 124487287  322 SLGGNSKTIMIATISPADVNYGETLSTLRYANRAKNI 358
Cdd:cd01374   285 SLGGNSRTAIICTITPAESHVEETLNTLKFASRAKKI 321
KISc_KHC_KIF5 cd01369
Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, ...
1-358 9.02e-100

Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup. Members of this group have been associated with organelle transport. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276820 [Multi-domain]  Cd Length: 325  Bit Score: 321.20  E-value: 9.02e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287    1 MASVKVAVRVRPMNRREKDLEAKFIIqmekskttitnlKIPEGGTGD-SGRERTKTFTYDFSFYsADTkspdyvSQEMVF 79
Cdd:cd01369     1 ECNIKVVCRFRPLNELEVLQGSKSIV------------KFDPEDTVViATSETGKTFSFDRVFD-PNT------TQEDVY 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287   80 KTLGTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGNSGDS---GLIPRICEALFSRINETTrwDEASFRTEVSYLEIYNE 156
Cdd:cd01369    62 NFAAKPIVDDVLNGYNGTIFAYGQTSSGKTYTMEGKLGDPesmGIIPRIVQDIFETIYSMD--ENLEFHVKVSYFEIYME 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  157 RVRDLLrrKSSKTfNLRVREHPKEGPYVEDLSKHLVQNYSDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQAkf 236
Cdd:cd01369   140 KIRDLL--DVSKT-NLSVHEDKNRGPYVKGATERFVSSPEEVLDVIDEGKSNRHVAVTNMNEESSRSHSIFLINVKQE-- 214
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  237 DAEMPCETVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADlsqdaanplvkKKQVFVPYRDSVLT 316
Cdd:cd01369   215 NVETEKKKSGKLYLVDLAGSEKVSKTGAEGAVLDEAKKINKSLSALGNVINALTD-----------GKKTHIPYRDSKLT 283
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 124487287  317 WLLKDSLGGNSKTIMIATISPADVNYGETLSTLRYANRAKNI 358
Cdd:cd01369   284 RILQDSLGGNSRTTLIICCSPSSYNESETLSTLRFGQRAKTI 325
KISc_C_terminal cd01366
Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, ...
9-360 1.08e-99

Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins. Ncd is a spindle motor protein necessary for chromosome segregation in meiosis. KIFC2/KIFC3-like kinesins have been implicated in motility of the Golgi apparatus as well as dentritic and axonal transport in neurons. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In this subgroup the motor domain is found at the C-terminus (C-type). C-type kinesins are (-) end-directed motors, i.e. they transport cargo towards the (-) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276817 [Multi-domain]  Cd Length: 329  Bit Score: 321.08  E-value: 1.08e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287    9 RVRPMNRREKDLEAKFI-IQMEKSKTTITNlkipeggtgdSGRERTKTFTYDFSFysadtkSPDyVSQEMVFKTLGTdVV 87
Cdd:cd01366     9 RVRPLLPSEENEDTSHItFPDEDGQTIELT----------SIGAKQKEFSFDKVF------DPE-ASQEDVFEEVSP-LV 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287   88 KSAFEGYNACVFAYGQTGSGKSYTMMGNSGDSGLIPRICEALFSRINE--TTRWdeaSFRTEVSYLEIYNERVRDLLRRK 165
Cdd:cd01366    71 QSALDGYNVCIFAYGQTGSGKTYTMEGPPESPGIIPRALQELFNTIKElkEKGW---SYTIKASMLEIYNETIRDLLAPG 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  166 SSKTFNLRVREHPKEGP-YVEDLSKHLVQNYSDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKF------TQAKfda 238
Cdd:cd01366   148 NAPQKKLEIRHDSEKGDtTVTNLTEVKVSSPEEVRQLLKKASKNRSTASTAMNEHSSRSHSVFILHIsgrnlqTGEI--- 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  239 empceTVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALAdlsqdaanplvkKKQVFVPYRDSVLTWL 318
Cdd:cd01366   225 -----SVGKLNLVDLAGSERLNKSGATGDRLKETQAINKSLSALGDVISALR------------QKQSHIPYRNSKLTYL 287
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 124487287  319 LKDSLGGNSKTIMIATISPADVNYGETLSTLRYANRAKNIIN 360
Cdd:cd01366   288 LQDSLGGNSKTLMFVNISPAESNLNETLNSLRFASKVNSCEL 329
KISc_BimC_Eg5 cd01364
Kinesin motor domain, BimC/Eg5 spindle pole proteins; Kinesin motor domain, BimC/Eg5 spindle ...
1-367 8.65e-89

Kinesin motor domain, BimC/Eg5 spindle pole proteins; Kinesin motor domain, BimC/Eg5 spindle pole proteins, participate in spindle assembly and chromosome segregation during cell division. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type), N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276815 [Multi-domain]  Cd Length: 353  Bit Score: 291.92  E-value: 8.65e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287    1 MASVKVAVRVRPMNRREKDLEAKFIIQMEKSKTTITnlkIPEGGTGDSGRerTKTFTYDFSFYSAdtkspdyVSQEMVFK 80
Cdd:cd01364     1 GKNIQVVVRCRPFNLRERKASSHSVVEVDPVRKEVS---VRTGGLADKSS--TKTYTFDMVFGPE-------AKQIDVYR 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287   81 TLGTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGN-----------SGDSGLIPRICEALFSRINETtrwdEASFRTEVS 149
Cdd:cd01364    69 SVVCPILDEVLMGYNCTIFAYGQTGTGKTYTMEGDrspneeytwelDPLAGIIPRTLHQLFEKLEDN----GTEYSVKVS 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  150 YLEIYNERVRDLLRRKSSKTFNLRVREHP--KEGPYVEDLSKHLVQNYSDVEELMDAGNINRTTAATGMNDVSSRSHAIF 227
Cdd:cd01364   145 YLEIYNEELFDLLSPSSDVSERLRMFDDPrnKRGVIIKGLEEITVHNKDEVYQILEKGAAKRKTAATLMNAQSSRSHSVF 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  228 TIkfTQAKFDAEMPCETV---SKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADlsqdaanplvkkK 304
Cdd:cd01364   225 SI--TIHIKETTIDGEELvkiGKLNLVDLAGSENIGRSGAVDKRAREAGNINQSLLTLGRVITALVE------------R 290
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 124487287  305 QVFVPYRDSVLTWLLKDSLGGNSKTIMIATISPADVNYGETLSTLRYANRAKNIINKPTINED 367
Cdd:cd01364   291 APHVPYRESKLTRLLQDSLGGRTKTSIIATISPASVNLEETLSTLEYAHRAKNIKNKPEVNQK 353
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
27-507 2.61e-84

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 287.02  E-value: 2.61e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287   27 QMEKSKTTITNLKIPEGGTGDSGRER-----------TKTFTYDFSFYSADTkspdyvsQEMVFKTLGTDVVKSAFEGYN 95
Cdd:COG5059    18 EKSVSDIKSTIRIIPGELGERLINTSkkshvslekskEGTYAFDKVFGPSAT-------QEDVYEETIKPLIDSLLLGYN 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287   96 ACVFAYGQTGSGKSYTMMGNSGDSGLIPRICEALFSRINEttRWDEASFRTEVSYLEIYNERVRDLLrrkSSKTFNLRVR 175
Cdd:COG5059    91 CTVFAYGQTGSGKTYTMSGTEEEPGIIPLSLKELFSKLED--LSMTKDFAVSISYLEIYNEKIYDLL---SPNEESLNIR 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  176 EHPKEGPYVEDLSKHLVQNYSDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIkfTQAKFDAEMPCETVSKIHLVDLAG 255
Cdd:COG5059   166 EDSLLGVKVAGLTEKHVSSKEEILDLLRKGEKNRTTASTEINDESSRSHSIFQI--ELASKNKVSGTSETSKLSLVDLAG 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  256 SERADATGATGVRLKEGGNINKSLVTLGNVISALADlsqdaanplvKKKQVFVPYRDSVLTWLLKDSLGGNSKTIMIATI 335
Cdd:COG5059   244 SERAARTGNRGTRLKEGASINKSLLTLGNVINALGD----------KKKSGHIPYRESKLTRLLQDSLGGNCNTRVICTI 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  336 SPADVNYGETLSTLRYANRAKNIINKPTINEDANVKL--------IRELRAEIARLKTLLAQGNQIALLDSPTA--LSME 405
Cdd:COG5059   314 SPSSNSFEETINTLKFASRAKSIKNKIQVNSSSDSSReieeikfdLSEDRSEIEILVFREQSQLSQSSLSGIFAymQSLK 393
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  406 EKLHQNEARVQELTKEWTNKWNETQNILKEQTLALRKEG---------IGVVLDSELPHLIGIDDDLLSTGIILYHLKEG 476
Cdd:COG5059   394 KETETLKSRIDLIMKSIISGTFERKKLLKEEGWKYKSTLqflrieidrLLLLREEELSKKKTKIHKLNKLRHDLSSLLSS 473
                         490       500       510
                  ....*....|....*....|....*....|....*...
gi 124487287  477 QT-----YVGREDASTEQDIVLHGLDLES--EHCVFEN 507
Cdd:COG5059   474 IPeetsdRVESEKASKLRSSASTKLNLRSsrSHSKFRD 511
PX_KIF16B_SNX23 cd06874
The phosphoinositide binding Phox Homology domain of KIF16B kinesin or Sorting Nexin 23; The ...
1179-1306 1.14e-77

The phosphoinositide binding Phox Homology domain of KIF16B kinesin or Sorting Nexin 23; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. KIF16B, also called sorting nexin 23 (SNX23), is a family-3 kinesin which harbors an N-terminal kinesin motor domain containing ATP and microtubule binding sites, a ForkHead Associated (FHA) domain, and a C-terminal PX domain. The PX domain of KIF16B binds to phosphatidylinositol-3-phosphate (PI3P) in early endosomes and plays a role in the transport of early endosomes to the plus end of microtubules. By regulating early endosome plus end motility, KIF16B modulates the balance between recycling and degradation of receptors. SNXs make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway.


Pssm-ID: 132784  Cd Length: 127  Bit Score: 251.92  E-value: 1.14e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287 1179 IKISIPRYVLCGQGKDEHFEFEVKISVLDETWTVFRRYSRFREMHKTLKLKYAELAALEFPPKKLFGNKDERVVAERRTH 1258
Cdd:cd06874     1 IKITIPRYVLRGQGKDEHFEFEVKITVLDETWTVFRRYSRFRELHKTMKLKYPEVAALEFPPKKLFGNKSERVAKERRRQ 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 124487287 1259 LEKYLREFFSVMLQSETSPLHiNKVGLTLSKHTICEFSPFFKKGVFDY 1306
Cdd:cd06874    81 LETYLRNFFSVCLKLPACPLY-PKVGRTLSKATLCDFSPFFRKGVFEN 127
FHA_KIF16B cd22732
forkhead associated (FHA) domain found in kinesin-like protein KIF16B; KIF16B, also called ...
446-562 1.42e-76

forkhead associated (FHA) domain found in kinesin-like protein KIF16B; KIF16B, also called sorting nexin-23, is a plus end-directed microtubule-dependent motor protein involved in endosome transport and receptor recycling and degradation. It regulates the plus end motility of early endosomes and the balance between recycling and degradation of receptors such as EGF receptor (EGFR) and FGF receptor (FGFR). It regulates the Golgi to endosome transport of FGFR-containing vesicles during early development, a key process for developing basement membrane and epiblast and primitive endoderm lineages during early postimplantation development. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438784 [Multi-domain]  Cd Length: 117  Bit Score: 248.31  E-value: 1.42e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  446 GVVLDSELPHLIGIDDDLLSTGIILYHLKEGQTYVGREDASTEQDIVLHGLDLESEHCVFENAGGTVTLIPLRGSQCSVN 525
Cdd:cd22732     1 GVVLDSELPHLIGIDDDLLSTGIILYHLKEGRTYVGRDDATTEQDIVLHGLDLESEHCIFENLNGTVTLIPLNGAQCSVN 80
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 124487287  526 GVQIVDATQLNQGAVILLGRTNMFRFNHPKEAAKLRE 562
Cdd:cd22732    81 GVQITEATQLNQGAVILLGRTNMFRFNHPKEAAKLRE 117
PLN03188 PLN03188
kinesin-12 family protein; Provisional
4-392 2.54e-75

kinesin-12 family protein; Provisional


Pssm-ID: 215621 [Multi-domain]  Cd Length: 1320  Bit Score: 274.89  E-value: 2.54e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287    4 VKVAVRVRPMNrreKDLEAKFIIQ-MEKSKTTITNlkipeggtgdsgrertKTFTYDfsfYSADTKSpdyvSQEMVFKTL 82
Cdd:PLN03188  100 VKVIVRMKPLN---KGEEGEMIVQkMSNDSLTING----------------QTFTFD---SIADPES----TQEDIFQLV 153
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287   83 GTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGN---------SGDS-GLIPRICEALFSRINE-----TTRwdEASFRTE 147
Cdd:PLN03188  154 GAPLVENCLAGFNSSVFAYGQTGSGKTYTMWGPanglleehlSGDQqGLTPRVFERLFARINEeqikhADR--QLKYQCR 231
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  148 VSYLEIYNERVRDLLRrKSSKtfNLRVREHPKEGPYVEDLSKHLVQNYSDVEELMDAGNINRTTAATGMNDVSSRSHAIF 227
Cdd:PLN03188  232 CSFLEIYNEQITDLLD-PSQK--NLQIREDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVF 308
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  228 T-IKFTQAKFDAE-MPCETVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADLSQDAanplvkkKQ 305
Cdd:PLN03188  309 TcVVESRCKSVADgLSSFKTSRINLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILAEISQTG-------KQ 381
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  306 VFVPYRDSVLTWLLKDSLGGNSKTIMIATISPADVNYGETLSTLRYANRAKNIINKPTINE----DANV--KLIRELRAE 379
Cdd:PLN03188  382 RHIPYRDSRLTFLLQESLGGNAKLAMVCAISPSQSCKSETFSTLRFAQRAKAIKNKAVVNEvmqdDVNFlrEVIRQLRDE 461
                         410
                  ....*....|...
gi 124487287  380 IARLKtllAQGNQ 392
Cdd:PLN03188  462 LQRVK---ANGNN 471
KISc_KIF23_like cd01368
Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members ...
4-356 1.31e-73

Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members of this group may play a role in mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276819 [Multi-domain]  Cd Length: 345  Bit Score: 248.85  E-value: 1.31e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287    4 VKVAVRVRPMNRREKDLEAKFIIQMEKSkTTITnLKIPEGGTGDSGRERTKTFTYDFSFYSadTKSPDYvSQEMVFKTLG 83
Cdd:cd01368     3 VKVYLRVRPLSKDELESEDEGCIEVINS-TTVV-LHPPKGSAANKSERNGGQKETKFSFSK--VFGPNT-TQKEFFQGTA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287   84 TDVVKSAFEGYNACVFAYGQTGSGKSYTMMGNSGDSGLIPRICEALFSRINETTRWdeasfrteVSYLEIYNERVRDLLR 163
Cdd:cd01368    78 LPLVQDLLHGKNGLLFTYGVTNSGKTYTMQGSPGDGGILPRSLDVIFNSIGGYSVF--------VSYIEIYNEYIYDLLE 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  164 RKSSKTF----NLRVREHPKEGPYVEDLSKHLVQNYSDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQAKFDAE 239
Cdd:cd01368   150 PSPSSPTkkrqSLRLREDHNGNMYVAGLTEIEVKSTEEARKVLKRGQKNRSVAGTKLNRESSRSHSVFTIKLVQAPGDSD 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  240 MPCE------TVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALadlsqdaANPLVKKKQVFVPYRDS 313
Cdd:cd01368   230 GDVDqdkdqiTVSQLSLVDLAGSERTSRTQNTGERLKEAGNINTSLMTLGTCIEVL-------RENQLQGTNKMVPFRDS 302
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 124487287  314 VLTWLLKDSLGGNSKTIMIATISPADVNYGETLSTLRYANRAK 356
Cdd:cd01368   303 KLTHLFQNYFDGEGKASMIVNVNPCASDYDETLHVMKFSAIAQ 345
KISc_KIF9_like cd01375
Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play ...
3-356 3.06e-72

Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play a role in cell shape remodeling. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276826 [Multi-domain]  Cd Length: 334  Bit Score: 244.80  E-value: 3.06e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287    3 SVKVAVRVRPMNRrekdlEAKFIIQMEKSKTTITNLKIPEGGTGDSGRERTK-TFTYDFSFYSAdtkspdyvSQEMVFKT 81
Cdd:cd01375     1 KVQAFVRVRPTDD-----FAHEMIKYGEDGKSISIHLKKDLRRGVVNNQQEDwSFKFDGVLHNA--------SQELVYET 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287   82 LGTDVVKSAFEGYNACVFAYGQTGSGKSYTMMG---NSGDSGLIPRICEALFSRINEttRWDEAsFRTEVSYLEIYNERV 158
Cdd:cd01375    68 VAKDVVSSALAGYNGTIFAYGQTGAGKTFTMTGgteNYKHRGIIPRALQQVFRMIEE--RPTKA-YTVHVSYLEIYNEQL 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  159 RDLL--RRKSSKTFN-LRVREHPKEGPYVEDLSKHLVQNYSDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQAK 235
Cdd:cd01375   145 YDLLstLPYVGPSVTpMTILEDSPQNIFIKGLSLHLTSQEEEALSLLFLGETNRIIASHTMNKNSSRSHCIFTIHLEAHS 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  236 FDAEMPCETVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADlsqdaanplvkKKQVFVPYRDSVL 315
Cdd:cd01375   225 RTLSSEKYITSKLNLVDLAGSERLSKTGVEGQVLKEATYINKSLSFLEQAIIALSD-----------KDRTHVPFRQSKL 293
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 124487287  316 TWLLKDSLGGNSKTIMIATISPADVNYGETLSTLRYANRAK 356
Cdd:cd01375   294 THVLRDSLGGNCNTVMVANIYGEAAQLEETLSTLRFASRVK 334
KISc_KID_like cd01376
Kinesin motor domain, KIF22/Kid-like subgroup; Kinesin motor domain, KIF22/Kid-like subgroup. ...
4-356 4.86e-69

Kinesin motor domain, KIF22/Kid-like subgroup; Kinesin motor domain, KIF22/Kid-like subgroup. Members of this group might play a role in regulating chromosomal movement along microtubules in mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276827 [Multi-domain]  Cd Length: 319  Bit Score: 235.09  E-value: 4.86e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287    4 VKVAVRVRPMNRREKDLEAKFIIQMEKSKTTItnLKIPeggtgdsgRERTKTFTYDF-SFYSADTkspdyvSQEMVFKTL 82
Cdd:cd01376     2 VRVAVRVRPFVDGTAGASDPSCVSGIDSCSVE--LADP--------RNHGETLKYQFdAFYGEES------TQEDIYARE 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287   83 GTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGNSGDSGLIPRICEALFsRINETTRWdeaSFRTEVSYLEIYNERVRDLL 162
Cdd:cd01376    66 VQPIVPHLLEGQNATVFAYGSTGAGKTFTMLGSPEQPGLMPLTVMDLL-QMTRKEAW---ALSFTMSYLEIYQEKILDLL 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  163 RRKSSktfNLRVREHPKEGPYVEDLSKHLVQNYSDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQAKFDAEMPC 242
Cdd:cd01376   142 EPASK---ELVIREDKDGNILIPGLSSKPIKSMAEFEEAFLPASKNRTVAATRLNDNSSRSHAVLLIKVDQRERLAPFRQ 218
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  243 ETvSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALadlsqdaanplvKKKQVFVPYRDSVLTWLLKDS 322
Cdd:cd01376   219 RT-GKLNLIDLAGSEDNRRTGNEGIRLKESGAINSSLFVLSKVVNAL------------NKNLPRIPYRDSKLTRLLQDS 285
                         330       340       350
                  ....*....|....*....|....*....|....
gi 124487287  323 LGGNSKTIMIATISPADVNYGETLSTLRYANRAK 356
Cdd:cd01376   286 LGGGSRCIMVANIAPERTFYQDTLSTLNFAARSR 319
KISc_KIF2_like cd01367
Kinesin motor domain, KIF2-like group; Kinesin motor domain, KIF2-like group. KIF2 is a ...
4-356 5.79e-68

Kinesin motor domain, KIF2-like group; Kinesin motor domain, KIF2-like group. KIF2 is a protein expressed in neurons, which has been associated with axonal transport and neuron development; alternative splice forms have been implicated in lysosomal translocation. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In this subgroup the motor domain is found in the middle (M-type) of the protein chain. M-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second (KIF2 may be slower). To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276818 [Multi-domain]  Cd Length: 328  Bit Score: 232.19  E-value: 5.79e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287    4 VKVAVRVRPMNRREKDLEAKFIIQMEKSKTTITNLkipeggtgdsgrERTK----------TFTYDFSFYSAdtkspdyV 73
Cdd:cd01367     2 IKVCVRKRPLNKKEVAKKEIDVVSVPSKLTLIVHE------------PKLKvdltkyienhTFRFDYVFDES-------S 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287   74 SQEMVFKTLGTDVVKSAFEGYNACVFAYGQTGSGKSYTMMG----NSGDSGLIPRICEALFSRINETTRWDEasFRTEVS 149
Cdd:cd01367    63 SNETVYRSTVKPLVPHIFEGGKATCFAYGQTGSGKTYTMGGdfsgQEESKGIYALAARDVFRLLNKLPYKDN--LGVTVS 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  150 YLEIYNERVRDLLRRKSSktfnLRVREHPKEGPYVEDLSKHLVQNYSDVEELMDAGNINRTTAATGMNDVSSRSHAIFTI 229
Cdd:cd01367   141 FFEIYGGKVFDLLNRKKR----VRLREDGKGEVQVVGLTEKPVTSAEELLELIESGSSLRTTGQTSANSQSSRSHAILQI 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  230 KFTQAKFDAempceTVSKIHLVDLAGSER-ADATGATGVRLKEGGNINKSLVTLGNVISALAdlsqdaanplvkKKQVFV 308
Cdd:cd01367   217 ILRDRGTNK-----LHGKLSFVDLAGSERgADTSSADRQTRMEGAEINKSLLALKECIRALG------------QNKAHI 279
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 124487287  309 PYRDSVLTWLLKDSL-GGNSKTIMIATISPADVNYGETLSTLRYANRAK 356
Cdd:cd01367   280 PFRGSKLTQVLKDSFiGENSKTCMIATISPGASSCEHTLNTLRYADRVK 328
FHA_KIF16 cd22708
forkhead associated (FHA) domain found in the kinesin-like protein KIF16 family; The KIF16 ...
446-554 1.38e-65

forkhead associated (FHA) domain found in the kinesin-like protein KIF16 family; The KIF16 family includes StARD9/KIF16A and KIF16B. StARD9, also called START domain-containing protein 9, or kinesin-like protein KIF16A, is a microtubule-dependent motor protein required for spindle pole assembly during mitosis. It is required to stabilize the pericentriolar material (PCM). KIF16B, also called sorting nexin-23, is a plus end-directed microtubule-dependent motor protein involved in endosome transport and receptor recycling and degradation. It regulates the plus end motility of early endosomes and the balance between recycling and degradation of receptors such as EGF receptor (EGFR) and FGF receptor (FGFR). It regulates the Golgi to endosome transport of FGFR-containing vesicles during early development, a key process for developing basement membrane and epiblast and primitive endoderm lineages during early postimplantation development. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438760 [Multi-domain]  Cd Length: 109  Bit Score: 216.75  E-value: 1.38e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  446 GVVLDSELPHLIGIDDDLLSTGIILYHLKEGQTYVGREDASTEQDIVLHGLDLESEHCVFENAGGTVTLIPLRGSQCSVN 525
Cdd:cd22708     1 GVVLDSELPHLIGIDDDLLSTGVVLYHLKEGKTRIGREDAPQEQDIVLDGEDIEAEHCIIENVGGVVTLHPLPGALCAVN 80
                          90       100
                  ....*....|....*....|....*....
gi 124487287  526 GVQIVDATQLNQGAVILLGRTNMFRFNHP 554
Cdd:cd22708    81 GQVITQPTRLTQGDVILLGKTNMFRFNHP 109
FHA_KIF16A_STARD9 cd22731
forkhead associated (FHA) domain found in StAR-related lipid transfer protein 9 (StARD9); ...
446-564 2.49e-49

forkhead associated (FHA) domain found in StAR-related lipid transfer protein 9 (StARD9); StARD9, also called START domain-containing protein 9, or kinesin-like protein KIF16A, is a microtubule-dependent motor protein required for spindle pole assembly during mitosis. It is required to stabilize the pericentriolar material (PCM). The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438783 [Multi-domain]  Cd Length: 119  Bit Score: 170.73  E-value: 2.49e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  446 GVVLDSELPHLIGIDDDLLSTGIILYHLKEGQTYVGREDASTEQDIVLHGLDLESEHCVFENAGGTVTLIPLRGSQCSVN 525
Cdd:cd22731     1 GVTIDSNLPHLIAMDDDILSTGVVLYHLREGTTKIGRSDSEQEQDIVLQGPWIERDHCMIHNECGVVTLRPAQGAQCTVN 80
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 124487287  526 GVQIVDATQLNQGAVILLGRTNMFRFNHPKEAAKLREKR 564
Cdd:cd22731    81 GREVTESCRLSQGAVIVLGKTHKFRFNHPAEAAILRQRR 119
FHA_PHLB1 cd22713
forkhead associated (FHA) domain found in pleckstrin homology-like domain family B member 1 ...
438-561 1.03e-33

forkhead associated (FHA) domain found in pleckstrin homology-like domain family B member 1 (PHLDB1) and similar proteins; PHLDB1, also called protein LL5-alpha (LL5A), acts as an insulin-responsive protein that enhances Akt activation. PHLDB1 contains a pleckstrin homology domain, which binds phosphatidylinositol PI(3,4)P(2), PI(3,5)P(2), and PI(3,4,5)P(3), as well as a Forkhead-associated (FHA) domain and coiled coil regions. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438765  Cd Length: 120  Bit Score: 125.90  E-value: 1.03e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  438 LALRKEGIGVVLDSELPHLIGIDDDLLSTGIILYHLKEGQTYVGREDASTeqdIVLHGLDLESEHCVFENAGGTVTLIPL 517
Cdd:cd22713     1 LELTETGKALKVQTEKPHLVSLGSGRLSTAVTLLPLPEGKTTIGTAASDI---ISLQGPGVEPEHCYIENINGTVTLYPC 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 124487287  518 rGSQCSVNGVQIVDATQLNQGAVILLGRTNMFRFNHPKEAAKLR 561
Cdd:cd22713    78 -GNLCSVDGLPITEPTRLTQGCMICLGRSNYFRFNHPAEAKRMK 120
FHA_KIF1 cd22705
forkhead associated (FHA) domain found in the kinesin-like protein KIF1 family; The KIF1 ...
453-553 2.10e-31

forkhead associated (FHA) domain found in the kinesin-like protein KIF1 family; The KIF1 family includes KIF1A, KIF1B, and KIF1C. KIF1A, also called axonal transporter of synaptic vesicles (ATSV), microtubule-based motor KIF1A, Unc-104- and KIF1A-related protein, or Unc-104, is an axonal transporter of synaptic vesicles, which is mutated in hereditary sensory and autonomic neuropathy type 2. It is also required for neuronal dense core vesicle (DCV) transport to dendritic spines and axons. The calcium-dependent interaction with CALM1 increases vesicle motility, and interaction with the scaffolding proteins PPFIA2 and TANC2 recruits DCVs to synaptic sites. KIF1B, also called Klp, is a motor for anterograde transport of mitochondria. It has a microtubule plus end-directed motility. Isoform 1 mediates the transport of synaptic vesicles in neuronal cells, while isoform 2 is required for induction of neuronal apoptosis. KIF1C is a new kinesin-like protein involved in vesicle transport from the Golgi apparatus to the endoplasmic reticulum. It has a microtubule plus end-directed motility. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438757 [Multi-domain]  Cd Length: 101  Bit Score: 118.88  E-value: 2.10e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  453 LPHLIGIDDDLLSTGIILYHLKEGQTYVGREDASTEQDIVLHGLDLESEHCVFENAGGTVTLIPLRGSQCSVNGVQIVDA 532
Cdd:cd22705     1 TPHLVNLNEDPLMSECLLYYIKPGITRVGRADADVPQDIQLSGTHILEEHCTFENEDGVVTLEPCEGALTYVNGKRVTEP 80
                          90       100
                  ....*....|....*....|.
gi 124487287  533 TQLNQGAVILLGRTNMFRFNH 553
Cdd:cd22705    81 TRLKTGSRVILGKNHVFRFNH 101
PX_RUN cd07277
The phosphoinositide binding Phox Homology domain of uncharacterized proteins containing PX ...
1179-1300 3.85e-31

The phosphoinositide binding Phox Homology domain of uncharacterized proteins containing PX and RUN domains; The PX domain is a phosphoinositide (PI) binding module involved in targeting proteins to PI-enriched membranes. Members in this subfamily are uncharacterized proteins containing an N-terminal RUN domain and a C-terminal PX domain. PX domain harboring proteins have been implicated in highly diverse functions such as cell signaling, vesicular trafficking, protein sorting, lipid modification, cell polarity and division, activation of T and B cells, and cell survival. In addition to protein-lipid interaction, the PX domain may also be involved in protein-protein interaction. The RUN domain is found in GTPases in the Rap and Rab families and may play a role in Ras-like signaling pathways.


Pssm-ID: 132810  Cd Length: 118  Bit Score: 118.60  E-value: 3.85e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287 1179 IKISIPRYVLCGQGKDEHFEFEVKISVLDETWTVFRRYSRFREMHKTLKLKYAELAALEFPPKKLFGNKDERVVAERRTH 1258
Cdd:cd07277     1 INVWIPSVFLRGKGSDAHHVYQVYIRIRDDEWNVYRRYSEFYELHKKLKKKFPVVRSFDFPPKKAIGNKDAKFVEERRKR 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 124487287 1259 LEKYLREFFSVMLQsETSPLHINKvgltlSKHTICEFSPFFK 1300
Cdd:cd07277    81 LQVYLRRVVNTLIQ-TSPELTACP-----SKETLIKLLPFFG 116
FHA_KIF14 cd22707
forkhead associated (FHA) domain found in kinesin-like protein KIF14 and similar proteins; ...
450-554 6.48e-27

forkhead associated (FHA) domain found in kinesin-like protein KIF14 and similar proteins; KIF14 is a microtubule motor protein that binds to microtubules with high affinity through each tubulin heterodimer and has an ATPase activity. It plays a role in many processes like cell division, cytokinesis and in cell proliferation and apoptosis. KIF14 is a potential oncogene and is involved in the metastasis of various cancers. Mutations of KIF14 cause primary microcephaly by impairing cytokinesis. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438759 [Multi-domain]  Cd Length: 108  Bit Score: 106.20  E-value: 6.48e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  450 DSELPHLIGIDDDLLSTGIILYHLKEGQTYVGREDASTEQDIVLHGLDLESEHCVFENAGGTVTLIPLRGSQCSVNGVQI 529
Cdd:cd22707     4 DNKLPNLVNLNEDPQLSEMLLYMLKEGQTRVGRSKASSSHDIQLSGALIADDHCTIENNGGKVTIIPVGDAETYVNGELI 83
                          90       100
                  ....*....|....*....|....*
gi 124487287  530 VDATQLNQGAVILLGRTNMFRFNHP 554
Cdd:cd22707    84 SEPTVLHHGDRVILGGDHYFRFNHP 108
FHA_KIF1B cd22727
forkhead associated (FHA) domain found in kinesin-like protein KIF1B; KIF1B, also called Klp, ...
454-556 4.67e-26

forkhead associated (FHA) domain found in kinesin-like protein KIF1B; KIF1B, also called Klp, is a motor for anterograde transport of mitochondria. It has a microtubule plus end-directed motility. Isoform 1 mediates the transport of synaptic vesicles in neuronal cells, while isoform 2 is required for induction of neuronal apoptosis. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438779 [Multi-domain]  Cd Length: 110  Bit Score: 103.96  E-value: 4.67e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  454 PHLIGIDDDLLSTGIILYHLKEGQTYVGREDASTEQDIVLHGLDLESEHCVF-----ENAGGTVTLIPLRGSQCSVNGVQ 528
Cdd:cd22727     3 PHLVNLNEDPLMSECLLYYIKDGITRVGQADAERRQDIVLSGAHIKEEHCIFrsernNNGEVIVTLEPCERSETYVNGKR 82
                          90       100
                  ....*....|....*....|....*...
gi 124487287  529 IVDATQLNQGAVILLGRTNMFRFNHPKE 556
Cdd:cd22727    83 VVQPVQLRSGNRIIMGKNHVFRFNHPEQ 110
FHA_KIF1A cd22726
forkhead associated (FHA) domain found in kinesin-like protein KIF1A; KIF1A, also called ...
454-562 5.56e-26

forkhead associated (FHA) domain found in kinesin-like protein KIF1A; KIF1A, also called axonal transporter of synaptic vesicles (ATSV), microtubule-based motor KIF1A, Unc-104- and KIF1A-related protein, or Unc-104, is an axonal transporter of synaptic vesicles, which is mutated in hereditary sensory and autonomic neuropathy type 2. It is also required for neuronal dense core vesicle (DCV) transport to dendritic spines and axons. The calcium-dependent interaction with CALM1 increases vesicle motility, and interaction with the scaffolding proteins PPFIA2 and TANC2 recruits DCVs to synaptic sites. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438778 [Multi-domain]  Cd Length: 115  Bit Score: 103.85  E-value: 5.56e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  454 PHLIGIDDDLLSTGIILYHLKEGQTYVGREDASTEQDIVLHGLDLESEHCVFENAGGT-----VTLIPLRGSQCSVNGVQ 528
Cdd:cd22726     2 PHLVNLNEDPLMSECLLYYIKDGITRVGREDAERRQDIVLSGHFIKEEHCIFRSDTRSggeavVTLEPCEGADTYVNGKK 81
                          90       100       110
                  ....*....|....*....|....*....|....
gi 124487287  529 IVDATQLNQGAVILLGRTNMFRFNHPKEAAKLRE 562
Cdd:cd22726    82 VTEPSILRSGNRIIMGKSHVFRFNHPEQARQERE 115
FHA_KIF28P cd22709
forkhead associated (FHA) domain found in kinesin-like protein KIF28P and similar proteins; ...
454-554 8.51e-25

forkhead associated (FHA) domain found in kinesin-like protein KIF28P and similar proteins; KIF28P, also called kinesin-like protein 6 (KLP6), is a microtubule-dependent motor protein required for mitochondrion morphology and transport of mitochondria in neuronal cells. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438761 [Multi-domain]  Cd Length: 102  Bit Score: 99.98  E-value: 8.51e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  454 PHLIGIDDDLLSTGIILYHLKEGQTYVGREDASTEQDIVLHGLDLESEHCVFENAGGTVTLIPLR-GSQCSVNGVQIVDA 532
Cdd:cd22709     1 PHLLNLNEDPQLSGVIVHFLQEGETTIGRADAEPEPDIVLSGLSIQKQHAVITNTDGKVTIEPVSpGAKVIVNGVPVTGE 80
                          90       100
                  ....*....|....*....|..
gi 124487287  533 TQLNQGAVILLGRTNMFRFNHP 554
Cdd:cd22709    81 TELHHLDRVILGSNHLYVFVGP 102
Motor_domain cd01363
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ...
6-288 1.99e-24

Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the P-loop NTPase family and provide the driving force in myosin and kinesin mediated processes. Some of the names do not match with what is given in the sequence list. This is because they are based on the current nomenclature by Kollmar/Sebe-Pedros.


Pssm-ID: 276814 [Multi-domain]  Cd Length: 170  Bit Score: 101.27  E-value: 1.99e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287    6 VAVRVRPMNRREkdleakfIIQMEKSKTTitnlkipeggtgDSGRERtktftydfsfysadtkspdYVSQEMVFKTLGtD 85
Cdd:cd01363     1 VLVRVNPFKELP-------IYRDSKIIVF------------YRGFRR-------------------SESQPHVFAIAD-P 41
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287   86 VVKSAFEGYN-ACVFAYGQTGSGKSYTMMgnsgdsGLIPRICEALFSRIN--ETTRWDEASFRTevsyleiynervrdll 162
Cdd:cd01363    42 AYQSMLDGYNnQSIFAYGESGAGKTETMK------GVIPYLASVAFNGINkgETEGWVYLTEIT---------------- 99
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  163 rrkssktfnlrvrehpkegpyvedlskhlVQNYSDVEELMDAGNINRtTAATGMNDVSSRSHAIFTIkftqakfdaempc 242
Cdd:cd01363   100 -----------------------------VTLEDQILQANPILEAFG-NAKTTRNENSSRFGKFIEI------------- 136
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 124487287  243 etvskihLVDLAGSERadatgatgvrlkeggnINKSLVTLGNVISA 288
Cdd:cd01363   137 -------LLDIAGFEI----------------INESLNTLMNVLRA 159
PX_domain cd06093
The Phox Homology domain, a phosphoinositide binding module; The PX domain is a ...
1180-1268 2.56e-20

The Phox Homology domain, a phosphoinositide binding module; The PX domain is a phosphoinositide (PI) binding module involved in targeting proteins to membranes. Proteins containing PX domains interact with PIs and have been implicated in highly diverse functions such as cell signaling, vesicular trafficking, protein sorting, lipid modification, cell polarity and division, activation of T and B cells, and cell survival. Many members of this superfamily bind phosphatidylinositol-3-phosphate (PI3P) but in some cases, other PIs such as PI4P or PI(3,4)P2, among others, are the preferred substrates. In addition to protein-lipid interaction, the PX domain may also be involved in protein-protein interaction, as in the cases of p40phox, p47phox, and some sorting nexins (SNXs). The PX domain is conserved from yeast to humans and is found in more than 100 proteins. The majority of PX domain-containing proteins are SNXs, which play important roles in endosomal sorting.


Pssm-ID: 132768 [Multi-domain]  Cd Length: 106  Bit Score: 87.41  E-value: 2.56e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287 1180 KISIPRYVLCGQGKDEHFEFEVKISVLD-ETWTVFRRYSRFREMHKTLKLKYAELAALEFPPKKLFGNKDERVVAERRTH 1258
Cdd:cd06093     1 SVSIPDYEKVKDGGKKYVVYIIEVTTQGgEEWTVYRRYSDFEELHEKLKKKFPGVILPPLPPKKLFGNLDPEFIEERRKQ 80
                          90
                  ....*....|
gi 124487287 1259 LEKYLREFFS 1268
Cdd:cd06093    81 LEQYLQSLLN 90
FHA_KIF13 cd22706
forkhead associated (FHA) domain found in the kinesin-like protein KIF13 family; The KIF13 ...
471-554 1.37e-19

forkhead associated (FHA) domain found in the kinesin-like protein KIF13 family; The KIF13 family includes KIF13A and KIF13B. KIF13A, also called kinesin-like protein RBKIN, is a plus end-directed microtubule-dependent motor protein involved in intracellular transport and in regulating various processes such as mannose-6-phosphate receptor (M6PR) transport to the plasma membrane, endosomal sorting during melanosome biogenesis, and cytokinesis. It mediates the transport of M6PR-containing vesicles from trans-Golgi network to the plasma membrane via direct interaction with the AP-1 complex. During melanosome maturation, KIF13A is required for delivering melanogenic enzymes from recycling endosomes to nascent melanosomes by creating peripheral recycling endosomal subdomains in melanocytes. It is also required for the abscission step in cytokinesis: it mediates translocation of ZFYVE26, and possibly TTC19, to the midbody during cytokinesis. KIF13B, also called kinesin-like protein GAKIN, is a novel kinesin-like protein that associates with the human homolog of the Drosophila discs large tumor suppressor in T lymphocytes. It is involved in reorganization of the cortical cytoskeleton. It regulates axon formation by promoting the formation of extra axons. KIF13B may be functionally important for the intracellular trafficking of membrane-associated guanylate kinase homologs (MAGUKs) and associated protein complexes. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438758 [Multi-domain]  Cd Length: 101  Bit Score: 85.04  E-value: 1.37e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  471 YHLKEgQTYVGREDASTEQDIVLHGLDLESEHCVFENAGGTVTLIPLRGSQCSVNGVQIVDATQLNQGAVILLGRTNMFR 550
Cdd:cd22706    19 YYLKE-HTLIGRSDAPTQQDIQLSGLGIQPEHCIITIENEDVYLTPLEGARTCVNGSIVTEKTQLRHGDRILWGNNHFFR 97

                  ....
gi 124487287  551 FNHP 554
Cdd:cd22706    98 LNCP 101
FHA_KIF1C cd22728
forkhead associated (FHA) domain found in kinesin-like protein KIF1C; KIF1C is a new ...
454-553 4.10e-19

forkhead associated (FHA) domain found in kinesin-like protein KIF1C; KIF1C is a new kinesin-like protein involved in vesicle transport from the Golgi apparatus to the endoplasmic reticulum. It has a microtubule plus end-directed motility. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438780 [Multi-domain]  Cd Length: 102  Bit Score: 83.77  E-value: 4.10e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  454 PHLIGIDDDLLSTGIILYHLKEGQTYVGREDAsteqDIVLHGLDLESEHCVF-----ENAGGTVTLIPLRGSQCSVNGVQ 528
Cdd:cd22728     2 PHLVNLNEDPLMSECLLYHIKDGVTRVGQVDV----DIKLSGQFIREQHCLFrsipnPSGEVVVTLEPCEGAETYVNGKQ 77
                          90       100
                  ....*....|....*....|....*
gi 124487287  529 IVDATQLNQGAVILLGRTNMFRFNH 553
Cdd:cd22728    78 VTEPLVLKSGNRIVMGKNHVFRFNH 102
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
599-1073 1.61e-16

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 85.37  E-value: 1.61e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  599 ERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETRRKETEIVQRQIRKQEESLKRRSFHIENKLKDLLAEKER 678
Cdd:COG1196   290 EYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLE 369
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  679 FEEERLREQQGLEQQRRQEEESLFRIREELRKLQELNSHEQAEKvqifQELDRLHQEQNAQSAKLRLEKRRLEEEEKEQV 758
Cdd:COG1196   370 AEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALL----ERLERLEEELEELEEALAELEEEEEEEEEALE 445
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  759 QRVAHLEEQLRKRQDTAPLLcpgeaQRAQEEKRELESIREALLQAKEMRAGGDHTCRDELERAQQYFLEFKRRQLVKLAS 838
Cdd:COG1196   446 EAAEEEAELEEEEEALLELL-----AELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLR 520
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  839 LEKDLVQQ--------------------KDLLSKEVQEEKVALEHVKCDAGGDPSFLATDDGNILGGPPDLDKIKTAETR 898
Cdd:COG1196   521 GLAGAVAVligveaayeaaleaalaaalQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAA 600
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  899 LQSREHQLQDLLQNHLPALLEEKQRVLDALDS-GVLGLDTTLCQVEKEVGEKEEQIAQYQANASQLQQLRATFEFTANVA 977
Cdd:COG1196   601 VDLVASDLREADARYYVLGDTLLGRTLVAARLeAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAE 680
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  978 RQEEKVRRKEKEILESQEKQQREALEQAVAKLEQRRSALQRCSTLDLEIQEQRQKLGSLHTSEWSGWQASLETDGEALEM 1057
Cdd:COG1196   681 LEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPP 760
                         490
                  ....*....|....*.
gi 124487287 1058 DPARLEHEIHQLKQKI 1073
Cdd:COG1196   761 DLEELERELERLEREI 776
Microtub_bd pfam16796
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding ...
3-162 9.15e-16

Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding site.


Pssm-ID: 465274 [Multi-domain]  Cd Length: 144  Bit Score: 75.72  E-value: 9.15e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287     3 SVKVAVRVRPMNRREkdleakfiIQMEKSKTTITNLKIpeggtgdsgRERTKTFTYDFSFYSADTkspdyvsQEMVFKTL 82
Cdd:pfam16796   21 NIRVFARVRPELLSE--------AQIDYPDETSSDGKI---------GSKNKSFSFDRVFPPESE-------QEDVFQEI 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287    83 GTdVVKSAFEGYNACVFAYGQTGSGksytmmgnsGDSGLIPRICEALFSRINETTRwdEASFRTEVSYLEIYNERVRDLL 162
Cdd:pfam16796   77 SQ-LVQSCLDGYNVCIFAYGQTGSG---------SNDGMIPRAREQIFRFISSLKK--GWKYTIELQFVEIYNESSQDLL 144
FHA_AFDN cd22711
forkhead associated (FHA) domain found in afadin and similar proteins; Afadin, also called ...
453-554 1.97e-15

forkhead associated (FHA) domain found in afadin and similar proteins; Afadin, also called ALL1-fused gene from chromosome 6 protein, protein AF-6, Afadin adherens junction formation factor, or MLLT4, is a nectin- and actin-filament-binding protein that connects nectin to the actin cytoskeleton. It is essential for the organization of adherens junctions. It may play a key role in the organization of epithelial structures of the embryonic ectoderm. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438763 [Multi-domain]  Cd Length: 106  Bit Score: 73.51  E-value: 1.97e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  453 LPHLI-----GIDDDLLstgiILYHLKEGQTYVG--REDASTEQDIVLHGLDLESEHCVFENAGGTVTLIPLRG-SQCSV 524
Cdd:cd22711     1 LPYLLelspdGSDRDKP----RRHRLQPNVTEVGseRSPANSGQFIQLFGPDILPRHCVITHMEGVVTVTPASQdAETYV 76
                          90       100       110
                  ....*....|....*....|....*....|
gi 124487287  525 NGVQIVDATQLNQGAVILLGRTNMFRFNHP 554
Cdd:cd22711    77 NGQRIYETTMLQHGMVVQFGRSHTFRFCDP 106
PX_IRAS cd06875
The phosphoinositide binding Phox Homology domain of the Imidazoline Receptor ...
1176-1265 9.02e-14

The phosphoinositide binding Phox Homology domain of the Imidazoline Receptor Antisera-Selected; The PX domain is a phosphoinositide binding (PI) module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. Imidazoline Receptor Antisera-Selected (IRAS), also called nischarin, contains an N-terminal PX domain, leucine rich repeats, and a predicted coiled coil domain. The PX domain of IRAS binds to phosphatidylinositol-3-phosphate in membranes. Together with the coiled coil domain, it is essential for the localization of IRAS to endosomes. IRAS has been shown to interact with integrin and inhibit cell migration. Its interaction with alpha5 integrin causes a redistribution of the receptor from the cell surface to endosomal structures, suggesting that IRAS may function as a sorting nexin (SNX) which regulates the endosomal trafficking of integrin. SNXs make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway.


Pssm-ID: 132785  Cd Length: 116  Bit Score: 68.85  E-value: 9.02e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287 1176 KDPIKISIPRYVLcgqgKDEHFEFEVKISVLDETWTVFRRYSRFREMHKTLKLKYAELAALeFPPKKLFGNKDERVVAER 1255
Cdd:cd06875     1 EPETKIRIPSAET----VEGYTVYIIEVKVGSVEWTVKHRYSDFAELHDKLVAEHKVDKDL-LPPKKLIGNKSPSFVEKR 75
                          90
                  ....*....|
gi 124487287 1256 RTHLEKYLRE 1265
Cdd:cd06875    76 RKELEIYLQT 85
FHA_KIF13A cd22729
forkhead associated (FHA) domain found in kinesin-like protein KIF13A; KIF13A, also called ...
456-564 6.36e-13

forkhead associated (FHA) domain found in kinesin-like protein KIF13A; KIF13A, also called kinesin-like protein RBKIN, is a plus end-directed microtubule-dependent motor protein involved in intracellular transport and in regulating various processes such as mannose-6-phosphate receptor (M6PR) transport to the plasma membrane, endosomal sorting during melanosome biogenesis, and cytokinesis. It mediates the transport of M6PR-containing vesicles from trans-Golgi network to the plasma membrane via direct interaction with the AP-1 complex. During melanosome maturation, KIF13A is required for delivering melanogenic enzymes from recycling endosomes to nascent melanosomes by creating peripheral recycling endosomal subdomains in melanocytes. It is also required for the abscission step in cytokinesis: it mediates translocation of ZFYVE26, and possibly TTC19, to the midbody during cytokinesis. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438781 [Multi-domain]  Cd Length: 109  Bit Score: 66.45  E-value: 6.36e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  456 LIGIDDDLLSTGIILYHLKeGQTYVGredASTEQDIVLHGLDLESEHCVFE-NAGGTVTLIPLRGSQCSVNGVQIVDATQ 534
Cdd:cd22729     4 LVNLNADPALNELLVYYLK-DHTRVG---ADTSQDIQLFGIGIQPEHCVIDiAADGDVTLTPKENARTCVNGTLVCSVTQ 79
                          90       100       110
                  ....*....|....*....|....*....|
gi 124487287  535 LNQGAVILLGRTNMFRFNHPKEAAKLREKR 564
Cdd:cd22729    80 LWHGDRILWGNNHFFRINLPKRKRRDWLKE 109
PX_SNX13 cd06873
The phosphoinositide binding Phox Homology domain of Sorting Nexin 13; The PX domain is a ...
1207-1265 8.32e-13

The phosphoinositide binding Phox Homology domain of Sorting Nexin 13; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. SNX13, also called RGS-PX1, contains an N-terminal PXA domain, a regulator of G protein signaling (RGS) domain, a PX domain, and a C-terminal domain that is conserved in some SNXs. It specifically binds to the stimulatory subunit of the heterotrimeric G protein G(alpha)s, serving as its GTPase activating protein, through the RGS domain. It preferentially binds phosphatidylinositol-3-phosphate (PI3P) through the PX domain and is localized in early endosomes. SNX13 is involved in endosomal sorting of EGFR into multivesicular bodies (MVB) for delivery to the lysosome.


Pssm-ID: 132783  Cd Length: 120  Bit Score: 66.14  E-value: 8.32e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 124487287 1207 DETWTVFRRYSRFREMHKTLKLKYAELAALEFPPKKLFGNKDERVVAERRTHLEKYLRE 1265
Cdd:cd06873    38 EESWHVYRRYSDFHDLHMRLKEKFPNLSKLSFPGKKTFNNLDRAFLEKRRKMLNQYLQS 96
FHA_KIF13B cd22730
forkhead associated (FHA) domain found in kinesin-like protein KIF13B; KIF13B, also called ...
456-554 1.74e-12

forkhead associated (FHA) domain found in kinesin-like protein KIF13B; KIF13B, also called kinesin-like protein GAKIN, is a novel kinesin-like protein that associates with the human homolog of the Drosophila discs large tumor suppressor in T lymphocytes. It is involved in reorganization of the cortical cytoskeleton. It regulates axon formation by promoting the formation of extra axons. KIF13B may be functionally important for the intracellular trafficking of membrane-associated guanylate kinase homologs (MAGUKs) and associated protein complexes. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438782 [Multi-domain]  Cd Length: 99  Bit Score: 64.93  E-value: 1.74e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  456 LIGIDDDLLSTGIILYHLKEgQTYVGREDAsteQDIVLHGLDLESEHCVFE-NAGGTVTLIPLRGSQCSVNGVQIVDATQ 534
Cdd:cd22730     4 LVNLNADPALNELLVYYLKE-HTLIGSADS---QDIQLCGMGILPEHCIIDiTPEGQVMLTPQKNTRTFVNGSAVTSPIQ 79
                          90       100
                  ....*....|....*....|
gi 124487287  535 LNQGAVILLGRTNMFRFNHP 554
Cdd:cd22730    80 LHHGDRILWGNNHFFRINLP 99
PX smart00312
PhoX homologous domain, present in p47phox and p40phox; Eukaryotic domain of unknown function ...
1192-1265 4.31e-12

PhoX homologous domain, present in p47phox and p40phox; Eukaryotic domain of unknown function present in phox proteins, PLD isoforms, a PI3K isoform.


Pssm-ID: 214610  Cd Length: 105  Bit Score: 63.90  E-value: 4.31e-12
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124487287   1192 GKDEHFEFEVKISVLD--ETWTVFRRYSRFREMHKTLKLKYAELAALEFPPKKLFG---NKDERVVAERRTHLEKYLRE 1265
Cdd:smart00312    8 GDGKHYYYVIEIETKTglEEWTVSRRYSDFLELHSKLKKHFPRSILPPLPGKKLFGrlnNFSEEFIEKRRRGLEKYLQS 86
PX_MONaKA cd06871
The phosphoinositide binding Phox Homology domain of Modulator of Na,K-ATPase; The PX domain ...
1191-1263 4.75e-12

The phosphoinositide binding Phox Homology domain of Modulator of Na,K-ATPase; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. MONaKA (Modulator of Na,K-ATPase) binds the plasma membrane ion transporter, Na,K-ATPase, and modulates its enzymatic and ion pump activities. It modulates brain Na,K-ATPase and may be involved in regulating electrical excitability and synaptic transmission. MONaKA contains an N-terminal PX domain and a C-terminal catalytic kinase domain. The PX domain interacts with PIs and plays a role in targeting proteins to PI-enriched membranes.


Pssm-ID: 132781  Cd Length: 120  Bit Score: 64.30  E-value: 4.75e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124487287 1191 QGKDEHFEFEVKI---SVLDETWTVFRRYSRFREMHKTLKLKYAELAaleFPPKKLFGNKDERVVAERRTHLEKYL 1263
Cdd:cd06871    16 QNIQSHTEYIIRVqrgPSPENSWQVIRRYNDFDLLNASLQISGISLP---LPPKKLIGNMDREFIAERQQGLQNYL 88
PX pfam00787
PX domain; PX domains bind to phosphoinositides.
1207-1265 1.36e-11

PX domain; PX domains bind to phosphoinositides.


Pssm-ID: 459940  Cd Length: 84  Bit Score: 61.49  E-value: 1.36e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 124487287  1207 DETWTVFRRYSRFREMHKTLKLKYAELAALEFPPKKLFGNKDERVVAERRTHLEKYLRE 1265
Cdd:pfam00787    6 LEEWSVRRRYSDFVELHKKLLRKFPSVIIPPLPPKRWLGRYNEEFIEKRRKGLEQYLQR 64
Kinesin_assoc pfam16183
Kinesin-associated;
364-476 4.35e-11

Kinesin-associated;


Pssm-ID: 465047 [Multi-domain]  Cd Length: 177  Bit Score: 62.94  E-value: 4.35e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287   364 INEDANVKLIRELRAEIARLKTLL-AQG----------------NQIA-------------------------------- 394
Cdd:pfam16183    3 INEDPNNKLIRELKDEVARLRDLLyAQGlgdiidtiahptkkraNTPAanasaataamagaspspslsalssraasvssl 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287   395 ---LLDSPTALSMEEKLHQNEARVQELTKEWTNKWNETQNI-------LKEQTLALRKEG--IGVVLDSELPHLIGIDDD 462
Cdd:pfam16183   83 herIMFTPGSEEAIERLKETEKIIAELNETWEEKLRKTEAIrmerealLAEMGVAIREDGgtLGVFSPKKTPHLVNLNED 162
                          170
                   ....*....|....
gi 124487287   463 LLSTGIILYHLKEG 476
Cdd:pfam16183  163 PLMSECLLYYIKDG 176
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
610-1056 4.52e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 64.19  E-value: 4.52e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  610 ESKRKLIEE----MEEKQKSDKAE--LERMQQEVEtrrkETEIVQRQIRKQEESLKR-----RSFH-IENKLKDLLAEKE 677
Cdd:COG1196   155 EERRAIIEEaagiSKYKERKEEAErkLEATEENLE----RLEDILGELERQLEPLERqaekaERYReLKEELKELEAELL 230
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  678 RFEEERLREQQGLEQQRRQEEESlfRIREELRKLQELNSHEQAEKVQIfQELDRLHQEQNAQSAKLRLEKRRLEEEEKEQ 757
Cdd:COG1196   231 LLKLRELEAELEELEAELEELEA--ELEELEAELAELEAELEELRLEL-EELELELEEAQAEEYELLAELARLEQDIARL 307
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  758 VQRVAHLEEQLRKRQDTAPLLcpgeAQRAQEEKRELESIREALLQAKEmraggdhtcrdELERAQQYFLEFKRRQLVKLA 837
Cdd:COG1196   308 EERRRELEERLEELEEELAEL----EEELEELEEELEELEEELEEAEE-----------ELEEAEAELAEAEEALLEAEA 372
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  838 SLEKDLVQQKDLLSKEVQEEKVALEhvkcdaggdpsflatddgnilggppDLDKIKTAETRLQSREHQLQDLLQNHLpAL 917
Cdd:COG1196   373 ELAEAEEELEELAEELLEALRAAAE-------------------------LAAQLEELEEAEEALLERLERLEEELE-EL 426
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  918 LEEKQRVLDALDsgvlgldttlcQVEKEVGEKEEQIAQYQANASQLQQLRATFEFTANVARQEEKVRRKEKEILESQEKQ 997
Cdd:COG1196   427 EEALAELEEEEE-----------EEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLL 495
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 124487287  998 QREALEQAVAKLEQRRSALQRcstldleiqeQRQKLGSLHTSEWSGWQASLETDGEALE 1056
Cdd:COG1196   496 LLEAEADYEGFLEGVKAALLL----------AGLRGLAGAVAVLIGVEAAYEAALEAAL 544
FHA cd00060
forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small ...
455-551 4.70e-10

forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small phosphopeptide recognition modules mostly found in eubacteria and eukaryotes. It is about 95-120 residues long that fold into an 11-stranded beta-sandwich. FHA domains can mediate the recognition of phosphorylated and non-phosphorylated substrates, as well as protein oligomerization. They specifically recognize threonine phosphorylation (pThr) accompanying activation of protein serine/threonine kinases. FHA domains show diverse ligand specificity. They may recognize the pTXXD motif, the pTXXI/L motif, and TQ clusters (singly and multiply phosphorylated). In eukaryotes, FHA superfamily members include forkhead-type transcription factors, as well as other signaling proteins, such as many regulatory proteins, kinases, phosphatases, motor proteins called kinesins, and metabolic enzymes. Many of them localize to the nucleus, where they participate in establishing or maintaining cell cycle checkpoints, DNA repair, or transcriptional regulation. FHA domains play important roles in human diseases, particularly in relation to DNA damage responses and cancers. In bacteria, FHA domain-containing proteins may participate in injection of viral proteins into host cells, transmembrane transporters, and cell division. FHA domain-containing proteins rarely include more than one copy of the domain. The only exception in eukaryotes is the checkpoint kinase Rad53 from Saccharomyces cerevisiae, which harbors two FHA domains (FHA1 and FHA2) flanking a central kinase domain. The two FHA domains recognize different phosphorylated targets and function independently from one another. In contrast, Mycobacterium tuberculosis ABC transporter Rv1747 contains two FHA domains but only one of them is essential for protein function.


Pssm-ID: 438714 [Multi-domain]  Cd Length: 92  Bit Score: 57.67  E-value: 4.70e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  455 HLIGIDDDllsTGIILYHLKEGQTYVGRedaSTEQDIVLHGLDLESEHCVFENAGGTVTLIPLrGSQC--SVNGVQIVDA 532
Cdd:cd00060     1 RLIVLDGD---GGGREFPLTKGVVTIGR---SPDCDIVLDDPSVSRRHARIEVDGGGVYLEDL-GSTNgtFVNGKRITPP 73
                          90
                  ....*....|....*....
gi 124487287  533 TQLNQGAVILLGRTNmFRF 551
Cdd:cd00060    74 VPLQDGDVIRLGDTT-FRF 91
PX_MDM1p cd06876
The phosphoinositide binding Phox Homology domain of yeast MDM1p; The PX domain is a ...
1209-1269 1.37e-09

The phosphoinositide binding Phox Homology domain of yeast MDM1p; The PX domain is a phosphoinositide binding (PI) module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. Yeast MDM1p is a filament-like protein localized in punctate structures distributed throughout the cytoplasm. It plays an important role in nuclear and mitochondrial transmission to daughter buds. Members of this subfamily show similar domain architectures as some sorting nexins (SNXs). Some members are similar to SNX19 in that they contain an N-terminal PXA domain, a central PX domain, and a C-terminal domain that is conserved in some SNXs. Others are similar to SNX13 and SNX14, which also harbor these three domains as well as a regulator of G protein signaling (RGS) domain in between the PXA and PX domains. SNXs make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway.


Pssm-ID: 132786  Cd Length: 133  Bit Score: 57.70  E-value: 1.37e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 124487287 1209 TWTVFRRYSRFREMHKTLKLKYAELAALEFPPKKLFGNKDER--VVAERRTHLEKYLREFFSV 1269
Cdd:cd06876    56 GWVVARRYSEFLELHKYLKKRYPGVLKLDFPQKRKISLKYSKtlLVEERRKALEKYLQELLKI 118
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
597-1075 6.06e-09

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 60.75  E-value: 6.06e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287   597 EFERQQREELEKLESKRKLIEEMEEKQKSDK-------------AELERMQQEVETRRKETEIVQRQIRKQEESLKRRSF 663
Cdd:TIGR00618  233 EALQQTQQSHAYLTQKREAQEEQLKKQQLLKqlrarieelraqeAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRI 312
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287   664 HIENKLKDLLAEKERFEEERLREQQGLEQQRRQEEESLFRIREELRKLQELNSHEQAEKVQIFQELDRLHQEQNAQSAKL 743
Cdd:TIGR00618  313 HTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLT 392
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287   744 RLEKRRLEEEEKEQV----------------QRVAHLEEQLRKRQDTAPLLCPGEAQRAQEEKRELESIREALLQAKEMr 807
Cdd:TIGR00618  393 QKLQSLCKELDILQReqatidtrtsafrdlqGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKER- 471
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287   808 aggdhtcRDELERAQQYFLEFKRRQLVKLASLEKdLVQQKDLLSKEVQEEKVALEHVKCDAGGDPSFLATDDGNILGGP- 886
Cdd:TIGR00618  472 -------EQQLQTKEQIHLQETRKKAVVLARLLE-LQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETs 543
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287   887 -PDLDKIKTAET-RLQSREHQLQDLLQN-------------HLPALLEEKQRVLDALDSGVLGLDTTLCQVEKEVGEKEE 951
Cdd:TIGR00618  544 eEDVYHQLTSERkQRASLKEQMQEIQQSfsiltqcdnrskeDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQP 623
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287   952 QIAQYQANASQ------LQQLRATFEFTA-NVARQEEKVRRKEKEILESQEKQQREALEQAV-AKLEQRRSALQRCSTLD 1023
Cdd:TIGR00618  624 EQDLQDVRLHLqqcsqeLALKLTALHALQlTLTQERVREHALSIRVLPKELLASRQLALQKMqSEKEQLTYWKEMLAQCQ 703
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 124487287  1024 LEIQEQRQKLGSL--HTSEWSGWQASLETDGEALEMDPARLEHEI-HQLKQKICE 1075
Cdd:TIGR00618  704 TLLRELETHIEEYdrEFNEIENASSSLGSDLAAREDALNQSLKELmHQARTVLKA 758
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
600-1073 6.27e-09

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 60.17  E-value: 6.27e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  600 RQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETRRKETEIVQRQIRKQEESLKRRSfhIENKLKDLLAEKERF 679
Cdd:COG4717    74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEA--LEAELAELPERLEEL 151
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  680 EEERLREQQgLEQQRRQEEESLFRIREELRKLQELNSHEQAEKVQIF-QELDRLHQEQNAQSAKLRLEKrrleeeekeqv 758
Cdd:COG4717   152 EERLEELRE-LEEELEELEAELAELQEELEELLEQLSLATEEELQDLaEELEELQQRLAELEEELEEAQ----------- 219
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  759 QRVAHLEEQLRKRQDTAPLLCPGEAQRAQEEKRELESIREAL------LQAKEMRAGGDHTCRDELERAQQYFLEFKRRQ 832
Cdd:COG4717   220 EELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALlglggsLLSLILTIAGVLFLVLGLLALLFLLLAREKAS 299
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  833 LVKLASLEKDLVQQKDLLSKEVQEEkvalehvkCDAGGDPSFLATDDgnILGGPPDLDKIKTAETRLQSREHQLQdllqn 912
Cdd:COG4717   300 LGKEAEELQALPALEELEEEELEEL--------LAALGLPPDLSPEE--LLELLDRIEELQELLREAEELEEELQ----- 364
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  913 hLPALLEEKQRVLDALDSGvlgldttlcqvekevgekeeQIAQYQANASQLQQLRatfEFTANVARQEEKVRRKEKEILE 992
Cdd:COG4717   365 -LEELEQEIAALLAEAGVE--------------------DEEELRAALEQAEEYQ---ELKEELEELEEQLEELLGELEE 420
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  993 SQEKQQREALEQAVAKLEQRRSALQRcstldlEIQEQRQKLGSLHTSewsgwQASLETDGEAlemdpARLEHEIHQLKQK 1072
Cdd:COG4717   421 LLEALDEEELEEELEELEEELEELEE------ELEELREELAELEAE-----LEQLEEDGEL-----AELLQELEELKAE 484

                  .
gi 124487287 1073 I 1073
Cdd:COG4717   485 L 485
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
592-862 6.89e-09

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: 60.14  E-value: 6.89e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287   592 YNPGLEFERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETRRKETEivqrQIRKQEESLKRRSFHIENKlkd 671
Cdd:pfam17380  260 YNGQTMTENEFLNQLLHIVQHQKAVSERQQQEKFEKMEQERLRQEKEEKAREVE----RRRKLEEAEKARQAEMDRQ--- 332
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287   672 llaekerfeEERLREQQGLEQQRRQEEEslfRIREELRK--LQELNSHEQAEKVQIFQELDRLHQEQNAQSaklrlekrr 749
Cdd:pfam17380  333 ---------AAIYAEQERMAMERERELE---RIRQEERKreLERIRQEEIAMEISRMRELERLQMERQQKN--------- 391
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287   750 LEEEEKEQVQRVAHLEEQLRKRQDTAPLLCPGEAQRAQEEKRELESIREALLQAKEMraggDHTCRDELERAQQyfLEFK 829
Cdd:pfam17380  392 ERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREM----ERVRLEEQERQQQ--VERL 465
                          250       260       270
                   ....*....|....*....|....*....|...
gi 124487287   830 RRQlvklaslEKDLVQQKDLLSKEVQEEKVALE 862
Cdd:pfam17380  466 RQQ-------EEERKRKKLELEKEKRDRKRAEE 491
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
601-823 9.87e-09

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: 60.07  E-value: 9.87e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287   601 QQREELEKLESKRKLIE----EMEEKQKSDKAELERMQQEVETRRKETEIVQRQIRKQEESLKRRSFHIENkLKDLLAEK 676
Cdd:TIGR02168  674 ERRREIEELEEKIEELEekiaELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQ-LEERIAQL 752
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287   677 ERFEEERLREQQGLEQQRRQEEESLFRIREELRKLQELNSHEQAEKVQIFQELDRL---HQEQNAQSAKLRLEKRRLEEE 753
Cdd:TIGR02168  753 SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELraeLTLLNEEAANLRERLESLERR 832
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287   754 EKEQVQRVAHLEEQLRKRQDTAPLLcPGEAQRAQEEKRELESIREALLQAKEMRAGGDHTCRDELERAQQ 823
Cdd:TIGR02168  833 IAATERRLEDLEEQIEELSEDIESL-AAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSE 901
PX_SNARE cd06897
The phosphoinositide binding Phox Homology domain of SNARE proteins from fungi; The PX domain ...
1180-1265 1.11e-08

The phosphoinositide binding Phox Homology domain of SNARE proteins from fungi; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. This subfamily is composed of fungal proteins similar to Saccharomyces cerevisiae Vam7p. They contain an N-terminal PX domain and a C-terminal SNARE domain. The SNARE (Soluble NSF attachment protein receptor) family of proteins are integral membrane proteins that serve as key factors for vesicular trafficking. Vam7p is anchored at the vacuolar membrane through the specific interaction of its PX domain with phosphatidylinositol-3-phosphate (PI3P) present in bilayers. It plays an essential role in vacuole fusion. The PX domain is involved in targeting of proteins to PI-enriched membranes, and may also be involved in protein-protein interaction.


Pssm-ID: 132807  Cd Length: 108  Bit Score: 54.20  E-value: 1.11e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287 1180 KISIPRYVLCGQGkdeHFEFEVKISVLDETWTVFRRYSRFREMHKTL-KLKYAELAAlEFPPKKLF--GNKDERVVAERR 1256
Cdd:cd06897     2 EISIPTTSVSPKP---YTVYNIQVRLPLRSYTVSRRYSEFVALHKQLeSEVGIEPPY-PLPPKSWFlsTSSNPKLVEERR 77

                  ....*....
gi 124487287 1257 THLEKYLRE 1265
Cdd:cd06897    78 VGLEAFLRA 86
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
600-865 4.12e-08

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: 57.83  E-value: 4.12e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287   600 RQQREELEKLESKRKLIEEME-------EKQKSDKAELERMQQEvetRRKETEIVQRQIRKQE-ESLKRRSFHIE-NKLK 670
Cdd:pfam17380  302 RQEKEEKAREVERRRKLEEAEkarqaemDRQAAIYAEQERMAME---RERELERIRQEERKRElERIRQEEIAMEiSRMR 378
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287   671 DLlaekerfeeerlreqQGLEQQRRQEEEslfRIREELRKLQELNSHEQAEKVQIFQELDRLHQEQNAQSAKLRLEKRRL 750
Cdd:pfam17380  379 EL---------------ERLQMERQQKNE---RVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRL 440
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287   751 EEEEKEQVQRVaHLEEQlrKRQDTAPLLCPGEAQRaQEEKRELESIREALLQAKEMRAggdHTCRDELERAQQYFLEFKR 830
Cdd:pfam17380  441 EEERAREMERV-RLEEQ--ERQQQVERLRQQEEER-KRKKLELEKEKRDRKRAEEQRR---KILEKELEERKQAMIEEER 513
                          250       260       270
                   ....*....|....*....|....*....|....*
gi 124487287   831 RQLVklasLEKDLVQQKDLLSKEVQEEKVALEHVK 865
Cdd:pfam17380  514 KRKL----LEKEMEERQKAIYEEERRREAEEERRK 544
FHA_RADIL-like cd22712
forkhead associated (FHA) domain found in the Ras-associating and dilute domain-containing ...
451-554 4.59e-08

forkhead associated (FHA) domain found in the Ras-associating and dilute domain-containing protein (Radil)-like family; The Radil-like family includes Radil and Ras-interacting protein 1 (Rain). Radil acts as an important small GTPase Rap1 effector required for cell spreading and migration. It regulates neutrophil adhesion and motility by linking Rap1 to beta2-integrin activation. Rain, also called Rasip1, is an endothelial-specific Ras-interacting protein required for the proper formation of vascular structures that develop via both vasculogenesis and angiogenesis. It acts as a critical and vascular-specific regulator of GTPase signaling, cell architecture, and adhesion, which is essential for endothelial cell morphogenesis and blood vessel tubulogenesis. Rain interacts with Ras in a GTP-dependent manner and may serve as an effector for endomembrane-associated Ras. Both Radil and Rain contain an FHA domain. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438764 [Multi-domain]  Cd Length: 120  Bit Score: 52.69  E-value: 4.59e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  451 SELPHLIGI-----DDDLLstgiiLYHLKEGQTYVGREDASTEQ-DIVLHGLDLESEHCV-----------FENAGGT-- 511
Cdd:cd22712     1 SDYPYLLTLrgfspKQDLL-----VYPLLEQVILVGSRTEGARKvDISLRAPDILPQHCWirrkpeplsddEDSDKESad 75
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 124487287  512 --VTLIPLRGSQCSVNGVQIVDATQLNQGAVILLGRTNMFRFNHP 554
Cdd:cd22712    76 yrVVLSPLRGAHVTVNGVPVLSETELHPGDLLGIGEHYLFLFKDP 120
PX_CISK cd06870
The phosphoinositide binding Phox Homology Domain of Cytokine-Independent Survival Kinase; The ...
1193-1268 5.09e-08

The phosphoinositide binding Phox Homology Domain of Cytokine-Independent Survival Kinase; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Cytokine-independent survival kinase (CISK), also called Serum- and Glucocorticoid-induced Kinase 3 (SGK3), plays a role in cell growth and survival. It is expressed in most tissues and is most abundant in the embryo and adult heart and spleen. It was originally discovered in a screen for antiapoptotic genes. It phosphorylates and inhibits the proapoptotic proteins, Bad and FKHRL1. CISK/SGK3 also regulates many transporters, ion channels, and receptors. It plays a critical role in hair follicle morphogenesis and hair cycling. N-terminal to a catalytic kinase domain, CISK contains a PX domain which binds highly phosphorylated PIs, directs membrane localization, and regulates the enzyme's activity.


Pssm-ID: 132780  Cd Length: 109  Bit Score: 52.41  E-value: 5.09e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 124487287 1193 KDEHFE-FEVKISVLDETWTVFRRYSRFREMHKTLKLKYAELaALEFPPKKLFGNK-DERVVAERRTHLEKYLREFFS 1268
Cdd:cd06870    16 KKKRFTvYKVVVSVGRSSWFVFRRYAEFDKLYESLKKQFPAS-NLKIPGKRLFGNNfDPDFIKQRRAGLDEFIQRLVS 92
PX_SNX20_21_like cd07279
The phosphoinositide binding Phox Homology domain of Sorting Nexins 20 and 21; The PX domain ...
1214-1269 6.26e-08

The phosphoinositide binding Phox Homology domain of Sorting Nexins 20 and 21; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. This subfamily consists of SNX20, SNX21, and similar proteins. SNX20 interacts with P-Selectin glycoprotein ligand-1 (PSGL-1), a surface-expressed mucin that acts as a ligand for the selectin family of adhesion proteins. It may function in the sorting and cycling of PSGL-1 into endosomes. SNX21, also called SNX-L, is distinctly and highly-expressed in fetal liver and may be involved in protein sorting and degradation during embryonic liver development.


Pssm-ID: 132812  Cd Length: 112  Bit Score: 52.33  E-value: 6.26e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 124487287 1214 RRYSRFREMHKTLKLKY-AELAALEFPPKKLFGNKDERVVAERRTHLEKYLREFFSV 1269
Cdd:cd07279    40 RRYSDFLKLYKALRKQHpQLMAKVSFPRKVLMGNFSSELIAERSRAFEQFLGHILSI 96
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
597-872 1.00e-07

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: 56.60  E-value: 1.00e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287   597 EFERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETRRKETEIVQRQIRKQEESLKRRSFHIENKLKDLLAEK 676
Cdd:TIGR02168  257 ELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELA 336
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287   677 ERFEEERLREQQGLEQQRRQEEEslfrIREELRKLQELNSHEQAEKVQIFQ---ELDRLHQEQNAQSAKLRLEKRRLEEE 753
Cdd:TIGR02168  337 EELAELEEKLEELKEELESLEAE----LEELEAELEELESRLEELEEQLETlrsKVAQLELQIASLNNEIERLEARLERL 412
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287   754 EKEQVQRVAHLEEQLRKRQDTAPLLCPGEAQRAQEEKRELESIREALLQAKEmraggdhTCRDELERAQQYFLEFkRRQL 833
Cdd:TIGR02168  413 EDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALE-------ELREELEEAEQALDAA-EREL 484
                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 124487287   834 VKLASLEKDLVQQKDLLSKEVQEEKVALEHVKCDAGGDP 872
Cdd:TIGR02168  485 AQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILG 523
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
599-1012 2.13e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 55.71  E-value: 2.13e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  599 ERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETRRKETEIVQRQIRKQEESLKRRSFHIENKLKDLLAEKER 678
Cdd:COG1196   325 LAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEE 404
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  679 FEEERLREQQGLEQQRRQEEESLFRIREELRKLQELNSHEQAEKVQIFQ------ELDRLHQEQNAQSAKLRLEKRRLEE 752
Cdd:COG1196   405 LEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAEleeeeeALLELLAELLEEAALLEAALAELLE 484
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  753 EEKEQVQRVAHLEEQLRKRQ------------DTAPLLCPGEAQRAQEEKRELESIREALLqakemrAGGDHTCRDELER 820
Cdd:COG1196   485 ELAEAAARLLLLLEAEADYEgflegvkaalllAGLRGLAGAVAVLIGVEAAYEAALEAALA------AALQNIVVEDDEV 558
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  821 AQQYFLEFKRRQLVKLASLEKDLVQQKDLLSKEVQEEKV--ALEHVKCDAGGDPSFLATDDGNILGGPPDLDKIKTAETR 898
Cdd:COG1196   559 AAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIgaAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRR 638
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  899 LQSREHQLQDL--------------------LQNHLPALLEEKQRVLDALDSGVLGLDTTLCQVEKEVGEKEEQIAQYQA 958
Cdd:COG1196   639 AVTLAGRLREVtlegeggsaggsltggsrreLLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLE 718
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  959 NASQLQQLRATFEFT--------------------------ANVARQEEKVRRKEKEI-------------LESQE---- 995
Cdd:COG1196   719 EELEEEALEEQLEAEreelleelleeeelleeealeelpepPDLEELERELERLEREIealgpvnllaieeYEELEeryd 798
                         490
                  ....*....|....*....
gi 124487287  996 --KQQREALEQAVAKLEQR 1012
Cdd:COG1196   799 flSEQREDLEEARETLEEA 817
FHA COG1716
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];
471-551 3.16e-07

Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];


Pssm-ID: 441322 [Multi-domain]  Cd Length: 96  Bit Score: 49.57  E-value: 3.16e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  471 YHLKEGQTYVGRedaSTEQDIVLHGLDLESEHCVFENAGGTVTLIPLrGSQ--CSVNGVQIVDATQLNQGAVILLGRTnM 548
Cdd:COG1716    16 FPLDGGPLTIGR---APDNDIVLDDPTVSRRHARIRRDGGGWVLEDL-GSTngTFVNGQRVTEPAPLRDGDVIRLGKT-E 90

                  ...
gi 124487287  549 FRF 551
Cdd:COG1716    91 LRF 93
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
612-1018 3.19e-07

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: 55.07  E-value: 3.19e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287   612 KRKLIEEM------EEKQKSDKAELErmqqEVETRRKETEIVQRQIRKQEESLKRRSFHIEnKLKDLLAEKERFEEERLR 685
Cdd:TIGR02169  155 RRKIIDEIagvaefDRKKEKALEELE----EVEENIERLDLIIDEKRQQLERLRREREKAE-RYQALLKEKREYEGYELL 229
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287   686 EQ-QGLEQQRRQEEESLFRIREELRKLQELNSHEQAEKVQIFQELDRLHQEQNAQSaklrlekrrleEEEKEQVQ-RVAH 763
Cdd:TIGR02169  230 KEkEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLG-----------EEEQLRVKeKIGE 298
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287   764 LEEQLRKRQDTAPLlCPGEAQRAQEEKRELESIREALLQAKEmraggdhtcrdELERAqqyfLEFKRRQLVKLASLEKDL 843
Cdd:TIGR02169  299 LEAEIASLERSIAE-KERELEDAEERLAKLEAEIDKLLAEIE-----------ELERE----IEEERKRRDKLTEEYAEL 362
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287   844 VQQKDLLSKEVQEEKVALEHVKcdaggdpsflatddgnilggppdlDKIKTAETRLQSREHQLQDLLQNhLPALLEEKQR 923
Cdd:TIGR02169  363 KEELEDLRAELEEVDKEFAETR------------------------DELKDYREKLEKLKREINELKRE-LDRLQEELQR 417
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287   924 vldaldsgvlgldttlcqvekevgeKEEQIAQYQANASQLQQLRATFEFTANVARQE-EKVRRKEKEILE--SQEKQQRE 1000
Cdd:TIGR02169  418 -------------------------LSEELADLNAAIAGIEAKINELEEEKEDKALEiKKQEWKLEQLAAdlSKYEQELY 472
                          410
                   ....*....|....*...
gi 124487287  1001 ALEQAVAKLEQRRSALQR 1018
Cdd:TIGR02169  473 DLKEEYDRVEKELSKLQR 490
PX_SNX22 cd06880
The phosphoinositide binding Phox Homology domain of Sorting Nexin 22; The PX domain is a ...
1179-1263 5.56e-07

The phosphoinositide binding Phox Homology domain of Sorting Nexin 22; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. SNX22 may be involved in recruiting other proteins to the membrane via protein-protein and protein-ligand interaction. The biological function of SNX22 is not yet known.


Pssm-ID: 132790  Cd Length: 110  Bit Score: 49.20  E-value: 5.56e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287 1179 IKISIP--RYVLCGQGKdEHFEFEVKISVLDETWTVFRRYSRFREMHKTLKLKYaelAALEFPPKKLfGNKDERVVAERR 1256
Cdd:cd06880     1 IEVSIPsyRLEVDESEK-PYTVFTIEVLVNGRRHTVEKRYSEFHALHKKLKKSI---KTPDFPPKRV-RNWNPKVLEQRR 75

                  ....*..
gi 124487287 1257 THLEKYL 1263
Cdd:cd06880    76 QGLEAYL 82
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
596-1073 6.18e-07

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: 54.29  E-value: 6.18e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287   596 LEFERQQREEL--------EKLESKRKLIEEMEEKQKSDKAELERMQQEVETRRKETEIVQR---QIRKQEESLKRRSFH 664
Cdd:TIGR02168  325 LEELESKLDELaeelaeleEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSkvaQLELQIASLNNEIER 404
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287   665 IENKLKDLLAEKERFEEERLREQQGLEQQRRQE-EESLFRIREELRKLQELNSHEQAEKVQIFQELDRLHQEQNAQSAKL 743
Cdd:TIGR02168  405 LEARLERLEDRRERLQQEIEELLKKLEEAELKElQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAEREL 484
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287   744 RLEKrrleeeekeqvQRVAHLEEQLRKRQDtapllcPGEAQRAQEEKR-----------ELESIREALLQAKEMRAGG-- 810
Cdd:TIGR02168  485 AQLQ-----------ARLDSLERLQENLEG------FSEGVKALLKNQsglsgilgvlsELISVDEGYEAAIEAALGGrl 547
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287   811 DHTCRDELERAQQYFLEFKRRQLVKLASLEKDLVQQKDLLSKEVQEEK-------VALEHVKCDAGGDPSF--------- 874
Cdd:TIGR02168  548 QAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKniegflgVAKDLVKFDPKLRKALsyllggvlv 627
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287   875 --------------------------LATDDGNILGGPPDLD--------KIKTAETRLQSREHQLQDLLQNhlpalLEE 920
Cdd:TIGR02168  628 vddldnalelakklrpgyrivtldgdLVRPGGVITGGSAKTNssilerrrEIEELEEKIEELEEKIAELEKA-----LAE 702
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287   921 KQRVLDALDSGVLGLDTTLCQVEKEVGEKEEQIAQYQANASQLQQLRATFEFTANVARQEEKVRRKEKEILESQEKQQRE 1000
Cdd:TIGR02168  703 LRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEA 782
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 124487287  1001 ALEQAVAKLEQrrsALQRCSTLDLEIQEQRQKLGSLHTSewsgwQASLETDGEALEMDPARLEHEIHQLKQKI 1073
Cdd:TIGR02168  783 EIEELEAQIEQ---LKEELKALREALDELRAELTLLNEE-----AANLRERLESLERRIAATERRLEDLEEQI 847
PX_SNX15_like cd06881
The phosphoinositide binding Phox Homology domain of Sorting Nexin 15-like proteins; The PX ...
1211-1263 7.73e-07

The phosphoinositide binding Phox Homology domain of Sorting Nexin 15-like proteins; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. Members of this subfamily have similarity to sorting nexin 15 (SNX15), which contains an N-terminal PX domain and a C-terminal Microtubule Interacting and Trafficking (MIT) domain. SNXs make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNX15 plays a role in protein trafficking processes in the endocytic pathway and the trans-Golgi network. The PX domain of SNX15 interacts with the PDGF receptor and is responsible for the membrane association of the protein. Other members of this subfamily contain an additional C-terminal kinase domain, similar to human RPK118, which binds sphingosine kinase and the antioxidant peroxiredoxin-3 (PRDX3). RPK118 may be involved in the transport of proteins such as PRDX3 from the cytoplasm to its site of function in the mitochondria.


Pssm-ID: 132791  Cd Length: 117  Bit Score: 49.24  E-value: 7.73e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 124487287 1211 TVFRRYSRFREMHKTLKLKYAELAALE----FPPKKLFGNKDERVVAERRTHLEKYL 1263
Cdd:cd06881    39 VVWKRYSDFKKLHRELSRLHKQLYLSGsfppFPKGKYFGRFDAAVIEERRQAILELL 95
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
580-823 1.06e-06

Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 53.03  E-value: 1.06e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287   580 SKSCENLSAVMLYNPGLEFERQQREELEKLESKRKLIEEMEEKQKSDKAELERMqqEVETRRKETEivqRQIRKQEESLK 659
Cdd:pfam15709  295 GRSSPTQTFVVTGNMESEEERSEEDPSKALLEKREQEKASRDRLRAERAEMRRL--EVERKRREQE---EQRRLQQEQLE 369
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287   660 RRsfhiENKLKDLLAEKERFEEERLREQQGLEQQRRQEEESLFRIREELRKLQELNSHEQAEKVQIFQELDRLHQEQNAQ 739
Cdd:pfam15709  370 RA----EKMREELELEQQRRFEEIRLRKQRLEEERQRQEEEERKQRLQLQAAQERARQQQEEFRRKLQELQRKKQQEEAE 445
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287   740 SAKLRLekrrleeeekeqvQRVAHLEEQLRKRQDTapLLCPGEAQRAQEEKRELESIREALLQAKEMRAGGDHTCRDELE 819
Cdd:pfam15709  446 RAEAEK-------------QRQKELEMQLAEEQKR--LMEMAEEERLEYQRQKQEAEEKARLEAEERRQKEEEAARLALE 510

                   ....
gi 124487287   820 RAQQ 823
Cdd:pfam15709  511 EAMK 514
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
596-808 1.44e-06

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: 52.82  E-value: 1.44e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287   596 LEFERQQREEL--EKLESKRKLIEEMEEKQKSDKAELERMQQeveTRRKETEIVQRQIRKQEESLKRRSFHIEnklkdll 673
Cdd:pfam17380  383 LQMERQQKNERvrQELEAARKVKILEEERQRKIQQQKVEMEQ---IRAEQEEARQREVRRLEEERAREMERVR------- 452
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287   674 aekerfeEERLREQQGLEQQRRQEEEslfrireelRKLQELNSHEQAEKVQIFQELDRL----HQEQNAQSAKLRLEKRR 749
Cdd:pfam17380  453 -------LEEQERQQQVERLRQQEEE---------RKRKKLELEKEKRDRKRAEEQRRKilekELEERKQAMIEEERKRK 516
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 124487287   750 LEEEEKEQVQRVAHLEEQLRKRQdtapllcpgEAQRAQEEKRELESIREALLQAKEMRA 808
Cdd:pfam17380  517 LLEKEMEERQKAIYEEERRREAE---------EERRKQQEMEERRRIQEQMRKATEERS 566
PTZ00121 PTZ00121
MAEBL; Provisional
597-797 1.45e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 53.22  E-value: 1.45e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  597 EFERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVEtrrkETEIVQRQIRKQEESLKRRSFHIENKlkdllaek 676
Cdd:PTZ00121 1616 EEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEE----ENKIKAAEEAKKAEEDKKKAEEAKKA-------- 1683
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  677 erfeeerlreqqglEQQRRQEEESLFRIREELRKLQELNSHE-----QAEKVQIFQELDRLHQEQNAQSAKLRLEKRRLE 751
Cdd:PTZ00121 1684 --------------EEDEKKAAEALKKEAEEAKKAEELKKKEaeekkKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEA 1749
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 124487287  752 EEEKEQVQRVAHLEEQLRKRQDTAPLLCPG---EAQRAQEEKRELESIR 797
Cdd:PTZ00121 1750 KKDEEEKKKIAHLKKEEEKKAEEIRKEKEAvieEELDEEDEKRRMEVDK 1798
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
759-1073 1.49e-06

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: 52.75  E-value: 1.49e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287   759 QRVAHLEEQLRKRQDTAPLLcPGEAQRAQEEKRELESIREALLQAKEMRAGGDHTCRDELERA---QQYFLEFKRRQLVK 835
Cdd:TIGR02168  677 REIEELEEKIEELEEKIAEL-EKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLeaeVEQLEERIAQLSKE 755
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287   836 LASLEKDLVQQKDLLSKEVQEEKVALEHvkcdaggdpsfLATDDGNILGGPPDLDKIKTAETRLQSREHQLQDLLQNHLP 915
Cdd:TIGR02168  756 LTELEAEIEELEERLEEAEEELAEAEAE-----------IEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRE 824
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287   916 ALLEEKQRVLDAldsgvlgldttlcqvEKEVGEKEEQIAQYQANASQLQQLRATFEFTANVARQEEKVRRKEKEILESQE 995
Cdd:TIGR02168  825 RLESLERRIAAT---------------ERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEAL 889
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287   996 KQQREALEQAVAKL---EQRRSALQR--------CSTLDLEIQEQRQKLGSLHTSEWSGWQASLETDGE---ALEMDPAR 1061
Cdd:TIGR02168  890 ALLRSELEELSEELrelESKRSELRReleelrekLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEAlenKIEDDEEE 969
                          330
                   ....*....|..
gi 124487287  1062 LEHEIHQLKQKI 1073
Cdd:TIGR02168  970 ARRRLKRLENKI 981
PTZ00121 PTZ00121
MAEBL; Provisional
556-1032 2.18e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 52.45  E-value: 2.18e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  556 EAAKLREKRKSGLLSSFSLSMTDLSKSCENLSAVMLYNPGLEFERQQREELEKLESKRKLIEEM----EEKQKSD----K 627
Cdd:PTZ00121 1360 EAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAkkkaEEKKKADeakkK 1439
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  628 AELERMQQEVETRRKETEIVQRQIRKQEEslKRRSFHIENKLKDLLAEKERFEEERLREQQGLEQQRRQEEEslfRIREE 707
Cdd:PTZ00121 1440 AEEAKKADEAKKKAEEAKKAEEAKKKAEE--AKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAK---KKADE 1514
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  708 LRKLQELNSHEQAEKVQIFQELDRLHQEQNAQSAKLRLEKRRLEeeekeQVQRVAHLEEQLRKRQDTAPLLCPGEAQRAQ 787
Cdd:PTZ00121 1515 AKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELK-----KAEEKKKAEEAKKAEEDKNMALRKAEEAKKA 1589
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  788 EEKReLESIREALLQAKEMRAggdhtcrDELERAQQyflEFKRRQLVKLASLEKDLVQQkdlLSKEVQEEKVALEHVKCD 867
Cdd:PTZ00121 1590 EEAR-IEEVMKLYEEEKKMKA-------EEAKKAEE---AKIKAEELKKAEEEKKKVEQ---LKKKEAEEKKKAEELKKA 1655
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  868 AggdpsflatddgnilggppDLDKIKTAETRLQSREHQLQdllQNHLPALLEEKQRVLDALdsgvlgldttlcQVEKEVG 947
Cdd:PTZ00121 1656 E-------------------EENKIKAAEEAKKAEEDKKK---AEEAKKAEEDEKKAAEAL------------KKEAEEA 1701
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  948 EKEEQIAQYQAN-ASQLQQLRATFEFTANVARQEEKVRRKEKEILESQEKQQREALEQAVAKLEQRRSALQRCSTLDLEI 1026
Cdd:PTZ00121 1702 KKAEELKKKEAEeKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVI 1781

                  ....*.
gi 124487287 1027 QEQRQK 1032
Cdd:PTZ00121 1782 EEELDE 1787
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
604-1072 2.20e-06

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 52.28  E-value: 2.20e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287   604 EELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETRRKETEIVQRQIRKQEESLKRRSFHIENKLKDL------LAEKE 677
Cdd:TIGR00618  170 MNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTqqshayLTQKR 249
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287   678 RFEEERLREQQGLEQQRRQEEE--SLFRIREELRKLQELNSH------EQAEKVQIFQELDRLHQEQNAQSAK------- 742
Cdd:TIGR00618  250 EAQEEQLKKQQLLKQLRARIEElrAQEAVLEETQERINRARKaaplaaHIKAVTQIEQQAQRIHTELQSKMRSrakllmk 329
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287   743 -LRLEKRRLEEEEKEQVQRVAHLEEQLRKRQDTAPLLCPGEAQRAQEEK---RELESIREALLQAKEMRAGGDHTCRDel 818
Cdd:TIGR00618  330 rAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTqhiHTLQQQKTTLTQKLQSLCKELDILQR-- 407
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287   819 ERAQQYFLEFKRRQL-VKLASLEKDLV-QQKDLLSKEVQEEKVALEHVKCDAGGDPSFLATDDGNILGGppDLDKIKTAE 896
Cdd:TIGR00618  408 EQATIDTRTSAFRDLqGQLAHAKKQQElQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQ--TKEQIHLQE 485
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287   897 TRLQSREHQLQDLLQNhLPALLEEKQRVLDA--LDSGVLGLDTTLCQVEKEVGEKEEQI-----AQYQANASQLQQLRAT 969
Cdd:TIGR00618  486 TRKKAVVLARLLELQE-EPCPLCGSCIHPNParQDIDNPGPLTRRMQRGEQTYAQLETSeedvyHQLTSERKQRASLKEQ 564
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287   970 FEFTANVARQEEKVRRKEKEILE--SQEKQQREALEQAVAKLEQRRSALQRCSTLDLEIQEQRQKLgSLHTSEWSGWQAS 1047
Cdd:TIGR00618  565 MQEIQQSFSILTQCDNRSKEDIPnlQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDV-RLHLQQCSQELAL 643
                          490       500
                   ....*....|....*....|....*
gi 124487287  1048 LETDGEALEMDPARLEHEIHQLKQK 1072
Cdd:TIGR00618  644 KLTALHALQLTLTQERVREHALSIR 668
PX_SNX20 cd07300
The phosphoinositide binding Phox Homology domain of Sorting Nexin 20; The PX domain is a ...
1214-1269 2.58e-06

The phosphoinositide binding Phox Homology domain of Sorting Nexin 20; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. Some SNXs are localized in early endosome structures such as clathrin-coated pits, while others are located in late structures of the endocytic pathway. SNX20 interacts with P-Selectin glycoprotein ligand-1 (PSGL-1), a surface-expressed mucin that acts as a ligand for the selectin family of adhesion proteins. The PX domain of SNX20 binds PIs and targets the SNX20/PSGL-1 complex to endosomes. SNX20 may function in the sorting and cycling of PSGL-1 into endosomes.


Pssm-ID: 132833  Cd Length: 114  Bit Score: 47.50  E-value: 2.58e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 124487287 1214 RRYSRFREMHKTLKLKYAE-LAALEFPPKKLFGNKDERVVAERRTHLEKYLREFFSV 1269
Cdd:cd07300    40 RRYSDFLKLHQELLSDFSEeLEDVVFPKKKLTGNFSEEIIAERRVALRDYLTLLYSL 96
PX_SNX25 cd06878
The phosphoinositide binding Phox Homology domain of Sorting Nexin 25; The PX domain is a ...
1210-1263 4.10e-06

The phosphoinositide binding Phox Homology domain of Sorting Nexin 25; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. The function of SNX25 is not yet known. It has been found in exosomes from human malignant pleural effusions. SNX25 shows the same domain architecture as SNX13 and SNX14, containing an N-terminal PXA domain, a regulator of G protein signaling (RGS) domain, a PX domain, and a C-terminal domain that is conserved in some SNXs.


Pssm-ID: 132788  Cd Length: 127  Bit Score: 47.37  E-value: 4.10e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 124487287 1210 WTVFRRYSRFREMHKTLKLKYAELAALEFP--PKKLFGNKDERVVAERRTHLEKYL 1263
Cdd:cd06878    50 WVVTRKLSEFHDLHRKLKECSSWLKKVELPslSKKWFKSIDKKFLDKSKNQLQKYL 105
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
602-865 5.33e-06

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: 51.22  E-value: 5.33e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287   602 QREELEKLESKRKLIEEMeekqksdKAELERMQQEVETRRKETEIVQRQIRKQEESLKRRSFHIEnKLKDLLAEKERFEE 681
Cdd:TIGR02169  669 SRSEPAELQRLRERLEGL-------KRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIE-QLEQEEEKLKERLE 740
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287   682 ERLREQQGLEQQRRQEEESLFRIREELRKLQE--------LNSHEQAEKVQIFQELDRLHQEQNAQsaklrlekrrleee 753
Cdd:TIGR02169  741 ELEEDLSSLEQEIENVKSELKELEARIEELEEdlhkleeaLNDLEARLSHSRIPEIQAELSKLEEE-------------- 806
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287   754 EKEQVQRVAHLEEQLRKRQDtapllcpgEAQRAQEEKRELESIREALLQAKEMRaggdhtcRDELErAQQYFLEFKRRQL 833
Cdd:TIGR02169  807 VSRIEARLREIEQKLNRLTL--------EKEYLEKEIQELQEQRIDLKEQIKSI-------EKEIE-NLNGKKEELEEEL 870
                          250       260       270
                   ....*....|....*....|....*....|..
gi 124487287   834 VKLASLEKDLVQQKDLLSKEVQEEKVALEHVK 865
Cdd:TIGR02169  871 EELEAALRDLESRLGDLKKERDELEAQLRELE 902
PTZ00121 PTZ00121
MAEBL; Provisional
599-853 5.51e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 51.30  E-value: 5.51e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  599 ERQQREELEKLESKRKLIE--EMEEKQKSD---KAELERMQQE---VETRRKETEIVQRQIRKQEESLKrrsfhIENKLK 670
Cdd:PTZ00121 1520 EAKKADEAKKAEEAKKADEakKAEEKKKADelkKAEELKKAEEkkkAEEAKKAEEDKNMALRKAEEAKK-----AEEARI 1594
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  671 DLLAEKERFEEERLREQQGLEQQRRQEEESLFRIREELRKLQELNSHE-----QAEKVQIFQELDRLHQEQNAQSAKLRL 745
Cdd:PTZ00121 1595 EEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEaeekkKAEELKKAEEENKIKAAEEAKKAEEDK 1674
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  746 ---EKRRLEEEEKEQVQRVAHLEEQLRKRQDTAPLLCPGEAQRAQEEKRELE----SIREALLQAKEMRAGGDHTCRDEL 818
Cdd:PTZ00121 1675 kkaEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEenkiKAEEAKKEAEEDKKKAEEAKKDEE 1754
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 124487287  819 ERAQQYFLEFKRRQLVKLASLEKDLVQQKDLLSKE 853
Cdd:PTZ00121 1755 EKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEED 1789
PTZ00121 PTZ00121
MAEBL; Provisional
599-1011 5.84e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 51.30  E-value: 5.84e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  599 ERQQREELEKLESKRKL--IEEMEEKQKSDKAELERMQQEVETRRKETEivqrQIRKQEESLKRRSfhiENKLK-DLLAE 675
Cdd:PTZ00121 1340 EAKKAAEAAKAEAEAAAdeAEAAEEKAEAAEKKKEEAKKKADAAKKKAE----EKKKADEAKKKAE---EDKKKaDELKK 1412
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  676 KERFEEERLREQQGLEQQRRQEEesLFRIREELRKLQELNshEQAEKVQIFQELDRLHQE-QNAQSAKLRLEKRRLEEEE 754
Cdd:PTZ00121 1413 AAAAKKKADEAKKKAEEKKKADE--AKKKAEEAKKADEAK--KKAEEAKKAEEAKKKAEEaKKADEAKKKAEEAKKADEA 1488
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  755 KEQVQRVAHLEEQLRKRQDTAPllcPGEAQRAQEEKRELESIREA--LLQAKEMRAGGDHTCRDELERAQqyflEFKRRQ 832
Cdd:PTZ00121 1489 KKKAEEAKKKADEAKKAAEAKK---KADEAKKAEEAKKADEAKKAeeAKKADEAKKAEEKKKADELKKAE----ELKKAE 1561
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  833 LVKLASLEKDLVQQKDLLSKEVQE----EKVALEHVKCDAGGDPSFLATDdgnilGGPPDLDKIKTAETRLQSREHQLQD 908
Cdd:PTZ00121 1562 EKKKAEEAKKAEEDKNMALRKAEEakkaEEARIEEVMKLYEEEKKMKAEE-----AKKAEEAKIKAEELKKAEEEKKKVE 1636
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  909 LLQNHLpallEEKQRVLDALDSGVLGLDTTLCQVEKEVGEKEEQIAQYQANASQLQQLRATFEFTANVARQEEKVRRKEK 988
Cdd:PTZ00121 1637 QLKKKE----AEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEA 1712
                         410       420
                  ....*....|....*....|...
gi 124487287  989 EILESQEkQQREALEQAVAKLEQ 1011
Cdd:PTZ00121 1713 EEKKKAE-ELKKAEEENKIKAEE 1734
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
596-792 6.45e-06

Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 50.34  E-value: 6.45e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287   596 LEFERQQREEleklESKRKLIEEMEEKQKSDKAELERMQQevetRRKEtEIVQRQIRKQEESLKRRSFHIENKLKDLLAE 675
Cdd:pfam15709  348 LEVERKRREQ----EEQRRLQQEQLERAEKMREELELEQQ----RRFE-EIRLRKQRLEEERQRQEEEERKQRLQLQAAQ 418
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287   676 KERFEEERLREQQGLEQQRRQEEESLFRIREELRKLQELNSH--EQAEKVQIFQELDRLHQEQNAQSAKLrlekrrleee 753
Cdd:pfam15709  419 ERARQQQEEFRRKLQELQRKKQQEEAERAEAEKQRQKELEMQlaEEQKRLMEMAEEERLEYQRQKQEAEE---------- 488
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 124487287   754 ekeqvQRVAHLEEQLRKRQDTAPLLCPGEAQRAQEEKRE 792
Cdd:pfam15709  489 -----KARLEAEERRQKEEEAARLALEEAMKQAQEQARQ 522
PX_SNX19_like_plant cd06872
The phosphoinositide binding Phox Homology domain of uncharacterized SNX19-like plant proteins; ...
1207-1264 6.69e-06

The phosphoinositide binding Phox Homology domain of uncharacterized SNX19-like plant proteins; The PX domain is a phosphoinositide (PI) binding module involved in targeting proteins to PI-enriched membranes. Members in this subfamily are uncharacterized plant proteins containing an N-terminal PXA domain, a central PX domain, and a C-terminal domain that is conserved in some sorting nexins (SNXs). This is the same domain architecture found in SNX19. SNX13 and SNX14 also contain these three domains but also contain a regulator of G protein signaling (RGS) domain in between the PXA and PX domains. SNXs make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. In addition to protein-lipid interaction, the PX domain may also be involved in protein-protein interaction.


Pssm-ID: 132782  Cd Length: 107  Bit Score: 46.36  E-value: 6.69e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 124487287 1207 DETWTVFRRYSRFREMHKtlKLKYAELAALEFPPKKLFGNK-DERVVAERRTHLEKYLR 1264
Cdd:cd06872    30 NETWVVKRRFRNFETLHR--RLKEVPKYNLELPPKRFLSSSlDGAFIEERCKLLDKYLK 86
PX_PI3K_C2 cd06883
The phosphoinositide binding Phox Homology Domain of Class II Phosphoinositide 3-Kinases; The ...
1207-1269 6.86e-06

The phosphoinositide binding Phox Homology Domain of Class II Phosphoinositide 3-Kinases; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. The Phosphoinositide 3-Kinase (PI3K) family of enzymes catalyzes the phosphorylation of the 3-hydroxyl group of the inositol ring of phosphatidylinositol. PI3Ks play an important role in a variety of fundamental cellular processes, including cell motility, the Ras pathway, vesicle trafficking and secretion, immune cell activation and apoptosis. They are also involved in the regulation of clathrin-mediated membrane trafficking as well as ATP-dependent priming of neurosecretory granule exocytosis. PI3Ks are divided into three main classes (I, II, and III) based on their substrate specificity, regulation, and domain structure. Class II PI3Ks preferentially use PI as a substrate to produce PI3P, but can also phosphorylate PI4P to produce PI(3,4)P2. They function as monomers and do not associate with any regulatory subunits. Class II enzymes contain an N-terminal Ras binding domain, a lipid binding C2 domain, a PI3K homology domain of unknown function, an ATP-binding cataytic domain, a PX domain, and a second C2 domain at the C-terminus. Class II PI3Ks include three vertebrate isoforms (alpha, beta, and gamma), the Drosophila PI3K_68D, and similar proteins.


Pssm-ID: 132793  Cd Length: 109  Bit Score: 46.20  E-value: 6.86e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124487287 1207 DETWTVFRRYSRFREMHKTLKLKYAELAALEFPPKKLFGNKDERVVAERR-THLEKYLREFFSV 1269
Cdd:cd06883    29 TEPSFVFRTFEEFQELHNKLSLLFPSLKLPSFPARVVLGRSHIKQVAERRkIELNSYLKSLFNA 92
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
608-996 1.01e-05

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: 50.06  E-value: 1.01e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287   608 KLESKRKLIEEME--EKQKSDKAELERMQQEVETRRKETEIVQRQIRKQEESLKRRS-----FH-IENKLKDL-LAEKER 678
Cdd:TIGR02168  153 KPEERRAIFEEAAgiSKYKERRKETERKLERTRENLDRLEDILNELERQLKSLERQAekaerYKeLKAELRELeLALLVL 232
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287   679 FEEERLREQQGLEQQRRQEEESLFRIREELRKLQELNSHEQAEKVQIFQELDRLHQEQNAQSAKLRLEKRRLEeeekEQV 758
Cdd:TIGR02168  233 RLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQ----ILR 308
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287   759 QRVAHLEEQLRKRQDTAPLLcpgeAQRAQEEKRELESIREALLQAKEMRAGgdhtCRDELERAQQYFLEFKRR------Q 832
Cdd:TIGR02168  309 ERLANLERQLEELEAQLEEL----ESKLDELAEELAELEEKLEELKEELES----LEAELEELEAELEELESRleeleeQ 380
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287   833 LVKLASLEKDLVQQKDLLSKEVQEEKVALEHvkcdaggdpsflatddgnilggppdldkiktAETRLQSREHQLQDLLQN 912
Cdd:TIGR02168  381 LETLRSKVAQLELQIASLNNEIERLEARLER-------------------------------LEDRRERLQQEIEELLKK 429
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287   913 HLPALLEEKQRVLDALDSGVLGLDTTLCQVEKEVGEKEEQIAQ----YQANASQLQQLRATFEFTANVARQEEKVRRKEK 988
Cdd:TIGR02168  430 LEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEaeqaLDAAERELAQLQARLDSLERLQENLEGFSEGVK 509

                   ....*...
gi 124487287   989 EILESQEK 996
Cdd:TIGR02168  510 ALLKNQSG 517
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
603-858 1.06e-05

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: 50.06  E-value: 1.06e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287   603 REELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETRRKETEIVQRQIRKQE----------ESLKRRSFHIENKLKDL 672
Cdd:TIGR02168  235 EELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQkelyalaneiSRLEQQKQILRERLANL 314
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287   673 LAEKERFEEERLREQQGLEQQR------RQEEESLFRIREELRKLQELNSHEQAEKVQIFQELDRLHQEQNAQSAKLRLE 746
Cdd:TIGR02168  315 ERQLEELEAQLEELESKLDELAeelaelEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQ 394
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287   747 KRRLEEEEKEQVQRVAHLEEQL-RKRQDTAPLLCPGEAQRAQEEKRELESIREALLQAKEMRAggdhTCRDELERAQQYf 825
Cdd:TIGR02168  395 IASLNNEIERLEARLERLEDRReRLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELE----RLEEALEELREE- 469
                          250       260       270
                   ....*....|....*....|....*....|...
gi 124487287   826 LEFKRRQLVKLASLEKDLVQQKDLLsKEVQEEK 858
Cdd:TIGR02168  470 LEEAEQALDAAERELAQLQARLDSL-ERLQENL 501
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
597-1018 1.50e-05

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: 49.68  E-value: 1.50e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287   597 EFERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETRRKETEIvqrqirkQEESLKRRSFHIENKLKDLlaek 676
Cdd:TIGR02169  167 EFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQAL-------LKEKREYEGYELLKEKEAL---- 235
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287   677 erfeeerlreqqglEQQRRQEEESLFRIREELRKLQELNSHEQAEKVQIFQELDRLHQEQNAQSaklrlekrrleEEEKE 756
Cdd:TIGR02169  236 --------------ERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLG-----------EEEQL 290
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287   757 QVQ-RVAHLEEQLRKRQDTAPlLCPGEAQRAQEEKRELESIREALLQAKEmraggdhtcrdELERAqqyfLEFKRRQLVK 835
Cdd:TIGR02169  291 RVKeKIGELEAEIASLERSIA-EKERELEDAEERLAKLEAEIDKLLAEIE-----------ELERE----IEEERKRRDK 354
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287   836 LASLEKDLVQQKDLLSKEVQEEKVALEHVKcdaggdpsflatddgnilggppdlDKIKTAETRLQSREHQLQDLLQNhLP 915
Cdd:TIGR02169  355 LTEEYAELKEELEDLRAELEEVDKEFAETR------------------------DELKDYREKLEKLKREINELKRE-LD 409
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287   916 ALLEEKQRV----------LDALDSGVLGLDTTLcqvekevGEKEEQIAQYQANASQLQQLRATFEftANVARQEEKVRR 985
Cdd:TIGR02169  410 RLQEELQRLseeladlnaaIAGIEAKINELEEEK-------EDKALEIKKQEWKLEQLAADLSKYE--QELYDLKEEYDR 480
                          410       420       430
                   ....*....|....*....|....*....|...
gi 124487287   986 KEKEILESQEKqqrealeqaVAKLEQRRSALQR 1018
Cdd:TIGR02169  481 VEKELSKLQRE---------LAEAEAQARASEE 504
PTZ00121 PTZ00121
MAEBL; Provisional
555-805 1.54e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 49.75  E-value: 1.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  555 KEAAKLREKRKSGLLSSFSLSMTDLSKSCENLSAVMLYNPGLEFERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQ 634
Cdd:PTZ00121 1561 EEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKK 1640
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  635 QEVETRRKeteivQRQIRKQEESLKRRsfhienklKDLLAEKERFEEERLREQQGLEQQRRQEEESLFRIREELRKLQEL 714
Cdd:PTZ00121 1641 KEAEEKKK-----AEELKKAEEENKIK--------AAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEEL 1707
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  715 NSHEqAEKVQIFQELDRLHQEQNAQSaklrlekRRLEEEEKEQVQRVahleEQLRKRQdtapllcpGEAQRAQEEKRELE 794
Cdd:PTZ00121 1708 KKKE-AEEKKKAEELKKAEEENKIKA-------EEAKKEAEEDKKKA----EEAKKDE--------EEKKKIAHLKKEEE 1767
                         250
                  ....*....|.
gi 124487287  795 SIREALLQAKE 805
Cdd:PTZ00121 1768 KKAEEIRKEKE 1778
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
599-1073 2.82e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 48.76  E-value: 2.82e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  599 ERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETRRKETeiVQRQIRKQEESLKRRsfhiENKLKDLLAEKER 678
Cdd:COG4913   297 LEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQ--LEREIERLERELEER----ERRRARLEALLAA 370
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  679 FEEERLREQQGLEQQRRQEEESLFRIREELRKLQELNSHEQAEKVQIFQELDRLHQEQNAQSAKLRLEKRRleeeekeQV 758
Cdd:COG4913   371 LGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPAR-------LL 443
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  759 QRVAHLEEQLRKRQDTAPLLC------PGEAQ--------------------------------------------RAQE 788
Cdd:COG4913   444 ALRDALAEALGLDEAELPFVGelievrPEEERwrgaiervlggfaltllvppehyaaalrwvnrlhlrgrlvyervRTGL 523
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  789 EKRELESIREALLQAK--------------EMRAGGDHTC---RDELER--------------------------AQQYF 825
Cdd:COG4913   524 PDPERPRLDPDSLAGKldfkphpfrawleaELGRRFDYVCvdsPEELRRhpraitragqvkgngtrhekddrrriRSRYV 603
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  826 LEFKRRQlvKLASLEKDLVQQKDLLSkEVQEEKVALEhvkcDAGGDPSFLATDDGNILGGPPDLDKIKTAETRLQSREHQ 905
Cdd:COG4913   604 LGFDNRA--KLAALEAELAELEEELA-EAEERLEALE----AELDALQERREALQRLAEYSWDEIDVASAEREIAELEAE 676
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  906 LQDLLQNhlPALLEEKQRVLDALDSGVLGLDTTLCQVEKEVGEKEEQIAQYQANASQLQQLRATFEFTANVARQEEKVRR 985
Cdd:COG4913   677 LERLDAS--SDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEER 754
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  986 KEKEILESQEKQQREALEQAVAKLEQRRSALQRcstldlEIQEQRQKLGSLHTSEWSGWQASLETDGEALEMdPARLEHE 1065
Cdd:COG4913   755 FAAALGDAVERELRENLEERIDALRARLNRAEE------ELERAMRAFNREWPAETADLDADLESLPEYLAL-LDRLEED 827

                  ....*....
gi 124487287 1066 -IHQLKQKI 1073
Cdd:COG4913   828 gLPEYEERF 836
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
600-1017 3.51e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 48.23  E-value: 3.51e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  600 RQQREELEKLESKRKLIEEMEEKQKSDKAELERMQqEVETRRKETEIVQRQIRKQEESLKRRSFHIENKLKDLLAEKERF 679
Cdd:COG4717   115 REELEKLEKLLQLLPLYQELEALEAELAELPERLE-ELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEE 193
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  680 EEERLREQQGLEQQRRQEEESLFRIREELRKL-QELNSHE-QAEKVQIFQELDRLHQEQNAQSAKLRLEKRRLEEEEKEQ 757
Cdd:COG4717   194 LQDLAEELEELQQRLAELEEELEEAQEELEELeEELEQLEnELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLIL 273
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  758 --------VQRVAHLEEQLRKRQDTApllcPGEAQRAQEEKRELESIREALLQAKEMRAGGDHTCRDELERAQQYFLEFK 829
Cdd:COG4717   274 tiagvlflVLGLLALLFLLLAREKAS----LGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEEL 349
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  830 RRQLVKLASLEKDLVQQkdllskEVQEEKVALEHvKCDAGGDPSFLAtddgnilggppdLDKIKTAETRLQSREHQLQDL 909
Cdd:COG4717   350 QELLREAEELEEELQLE------ELEQEIAALLA-EAGVEDEEELRA------------ALEQAEEYQELKEELEELEEQ 410
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  910 LQNHLPALLEEkqrvLDALDSGVLgldttlcqvekevgekEEQIAQYQANASQLQQLRAtfEFTANVARQEEKVRRKEKE 989
Cdd:COG4717   411 LEELLGELEEL----LEALDEEEL----------------EEELEELEEELEELEEELE--ELREELAELEAELEQLEED 468
                         410       420
                  ....*....|....*....|....*...
gi 124487287  990 ILESQEKQQREALEQAVAKLEQRRSALQ 1017
Cdd:COG4717   469 GELAELLQELEELKAELRELAEEWAALK 496
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
586-858 3.96e-05

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: 47.45  E-value: 3.96e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  586 LSAVMLYNPGLEFERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETRRKETEIVQRQIRKQEESLKRrsfhI 665
Cdd:COG4942     6 LLALLLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAA----L 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  666 ENKLKDLlaekerfeeerlreQQGLEQQRRQEEESLFRIREELRKLQELNSHEQAEKVqifqeldrLHQEQNAQSAKLRL 745
Cdd:COG4942    82 EAELAEL--------------EKEIAELRAELEAQKEELAELLRALYRLGRQPPLALL--------LSPEDFLDAVRRLQ 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  746 EKRRLEEEEKEQVQRVAHLEEQLRKRQDTApllcPGEAQRAQEEKRELESIREALLQAKEMRaggdhtcRDELERAQQYF 825
Cdd:COG4942   140 YLKYLAPARREQAEELRADLAELAALRAEL----EAERAELEALLAELEEERAALEALKAER-------QKLLARLEKEL 208
                         250       260       270
                  ....*....|....*....|....*....|...
gi 124487287  826 LEfKRRQLVKLASLEKDLVQQKDLLSKEVQEEK 858
Cdd:COG4942   209 AE-LAAELAELQQEAEELEALIARLEAEAAAAA 240
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
595-1036 3.98e-05

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 48.11  E-value: 3.98e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  595 GLEFERQQ-REELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETRRKETEIVQRQIRKQE----------ESLKRRSF 663
Cdd:PRK02224  210 GLESELAElDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETErereelaeevRDLRERLE 289
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  664 HIENKLKDLLAEKERFEEERLREQQGLEQQRRQEEESLFRIREELRKLQELNshEQAEKVQifqeldrlhqeqnaqsakl 743
Cdd:PRK02224  290 ELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHN--EEAESLR------------------- 348
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  744 rlekrrleeeekeqvQRVAHLEEQLRKRQDTAPLLcPGEAQRAQEEKRELESIREAL---LQAKEMRAGGDHTCRDELER 820
Cdd:PRK02224  349 ---------------EDADDLEERAEELREEAAEL-ESELEEAREAVEDRREEIEELeeeIEELRERFGDAPVDLGNAED 412
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  821 AQQYFLEFKRRQLVKLASLEKDLVQQKDllskEVQEEKVALEHVKCDAGGDPsflatddgniLGGPPDLDKIKTAETRLQ 900
Cdd:PRK02224  413 FLEELREERDELREREAELEATLRTARE----RVEEAEALLEAGKCPECGQP----------VEGSPHVETIEEDRERVE 478
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  901 SREHQLQDLLQNHlpALLEEKqrvLDALDSGVlgldttlcqvekevgEKEEQIAQYQANASQLQQLRATFEFTANVARQE 980
Cdd:PRK02224  479 ELEAELEDLEEEV--EEVEER---LERAEDLV---------------EAEDRIERLEERREDLEELIAERRETIEEKRER 538
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 124487287  981 EKVRRKEKEILESQEKQQREA-----------------LEQAVAKLEQRRSALQRCSTLDLEIQEQRQKLGSL 1036
Cdd:PRK02224  539 AEELRERAAELEAEAEEKREAaaeaeeeaeeareevaeLNSKLAELKERIESLERIRTLLAAIADAEDEIERL 611
PX_SNX27 cd06886
The phosphoinositide binding Phox Homology domain of Sorting Nexin 27; The PX domain is a ...
1176-1269 5.08e-05

The phosphoinositide binding Phox Homology domain of Sorting Nexin 27; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. SNX27 contains an N-terminal PDZ domain followed by a PX domain and a Ras-Associated (RA) domain. It binds G protein-gated potassium (Kir3) channels, which play a role in neuronal excitability control, through its PDZ domain. SNX27 downregulates Kir3 channels by promoting their movement in the endosome, reducing surface expression and increasing degradation. SNX27 also associates with 5-hydroxytryptamine type 4 receptor (5-HT4R), cytohesin associated scaffolding protein (CASP), and diacylglycerol kinase zeta, and may play a role in their intracellular trafficking and endocytic recycling. The SNX27 PX domain preferentially binds to phosphatidylinositol-3-phosphate (PI3P) and is important for targeting to the early endosome.


Pssm-ID: 132796  Cd Length: 106  Bit Score: 43.55  E-value: 5.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287 1176 KDPIKISIPRYvlcgqgkdEHFEFEvkisvlDETWTVF-----------RRYSRFREMHKTLKLKYAELAALEFPPKKLF 1244
Cdd:cd06886     1 KRSVPISIPDY--------KHVEQN------GEKFVVYniymagrqlcsRRYREFANLHQNLKKEFPDFQFPKLPGKWPF 66
                          90       100
                  ....*....|....*....|....*
gi 124487287 1245 GNKDERVVAERRThLEKYLREFFSV 1269
Cdd:cd06886    67 SLSEQQLDARRRG-LEQYLEKVCSI 90
PRK12704 PRK12704
phosphodiesterase; Provisional
602-729 5.69e-05

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 47.47  E-value: 5.69e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  602 QREELEKLESKRKLIEEMEEKQKSDKAELERmqqEVETRRKETEIVQRQIRKQEESLKRRSFHIENKLKDLLAekerFEE 681
Cdd:PRK12704   45 EEAKKEAEAIKKEALLEAKEEIHKLRNEFEK---ELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEK----KEK 117
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 124487287  682 ERLREQQGLEQQRRQEEEslfRIREELRKLQELN--SHEQAeKVQIFQEL 729
Cdd:PRK12704  118 ELEQKQQELEKKEEELEE---LIEEQLQELERISglTAEEA-KEILLEKV 163
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
599-1036 6.68e-05

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 47.66  E-value: 6.68e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287   599 ERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETR---------------RKETEIVQRQIRKQEES--LKRR 661
Cdd:TIGR00618  430 KKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEReqqlqtkeqihlqetRKKAVVLARLLELQEEPcpLCGS 509
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287   662 SFHIENKLKDLLaekerFEEERLREQQGLEQQRRQEEESLFRIREELRKLQELNSHEQAEKVQIFQELDRLHQEQNAQSA 741
Cdd:TIGR00618  510 CIHPNPARQDID-----NPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKE 584
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287   742 KLRLEKRRleeeekeqVQRVAHLEEQLRKRQDTAPLLCPGEAQRAQEEKRELESIREALLQAKEMRAGGDHTCRDELERA 821
Cdd:TIGR00618  585 DIPNLQNI--------TVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLT 656
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287   822 QQYflefKRRQLVKLASLEKDLVQQKDLLSKEVQEEKVALEHVKCDAGGDPSFLATDDGNILGGPPDLDKIKTAETRLQS 901
Cdd:TIGR00618  657 QER----VREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGS 732
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287   902 REHQLQDLLQNHLPALLEEKQRVLDAL-------DSGVLGLDTTLCQVEKEVGEKEEQIAQYQANASQLQQLRAtfefta 974
Cdd:TIGR00618  733 DLAAREDALNQSLKELMHQARTVLKARteahfnnNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEA------ 806
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124487287   975 nvaRQEEKVRRKEKEILESQEKQQREaLEQAVAKLEQRRSALQRCSTLDLEIQEQRQKLGSL 1036
Cdd:TIGR00618  807 ---EIGQEIPSDEDILNLQCETLVQE-EEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQL 864
FHA_Ki67 cd22673
forkhead associated (FHA) domain found in proliferation marker protein Ki-67 and similar ...
473-551 7.23e-05

forkhead associated (FHA) domain found in proliferation marker protein Ki-67 and similar proteins; Ki-67, also called antigen identified by monoclonal antibody Ki-67, antigen KI-67, or antigen Ki67, acts as a biological surfactant to disperse mitotic chromosomes. It is required to maintain individual mitotic chromosomes dispersed in the cytoplasm following nuclear envelope disassembly. Ki-67 binds DNA with a preference for supercoiled DNA and AT-rich DNA. It may also play a role in chromatin organization. Ki-67 contains an FHA domain at its N-terminus. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438725 [Multi-domain]  Cd Length: 95  Bit Score: 42.97  E-value: 7.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  473 LKEGQTYVGRedaSTEQDIVLHGLDLESEHCVFE-NAGGTVTLIPLrgSQCS---VNGVQIVDATQLNQGAVILLGrTNM 548
Cdd:cd22673    18 LTKKSCTFGR---DLSCDIRIQLPGVSREHCRIEvDENGKAYLENL--STTNptlVNGKAIEKSAELKDGDVITIG-GRS 91

                  ...
gi 124487287  549 FRF 551
Cdd:cd22673    92 FRF 94
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
782-1036 1.22e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.45  E-value: 1.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  782 EAQRAQEEKRELESIREALLQAKEmraggdhtCRDELERAQQYFLEFkRRQLVKLASLEkdlvQQKDLLSKEVQEEKVAL 861
Cdd:COG4913   226 AADALVEHFDDLERAHEALEDARE--------QIELLEPIRELAERY-AAARERLAELE----YLRAALRLWFAQRRLEL 292
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  862 EHVKCDAGGDpsflatddgnilggppDLDKIKTAETRLQSREHQLQDLLQNHLPALLEEKQRVLDALDSGVLGLDTTLcq 941
Cdd:COG4913   293 LEAELEELRA----------------ELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLEREL-- 354
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  942 vekevgekeeqiAQYQANASQLQQLRATFEFTANVARQE-EKVRRKEKEILEsQEKQQREALEQAVAKLEQRRSALQRcs 1020
Cdd:COG4913   355 ------------EERERRRARLEALLAALGLPLPASAEEfAALRAEAAALLE-ALEEELEALEEALAEAEAALRDLRR-- 419
                         250
                  ....*....|....*.
gi 124487287 1021 tldlEIQEQRQKLGSL 1036
Cdd:COG4913   420 ----ELRELEAEIASL 431
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
603-1136 1.23e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.45  E-value: 1.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  603 REELEKLESKRKLIEEMEE------KQKSDKAELERMQQ--EVETRRKETEIVQRQIRKQEESLKRrsfhienkLKDLLA 674
Cdd:COG4913   241 HEALEDAREQIELLEPIRElaeryaAARERLAELEYLRAalRLWFAQRRLELLEAELEELRAELAR--------LEAELE 312
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  675 EKERFEEERLREQQGLEQQRRQEE-ESLFRIREELRKLQElnshEQAEKVQIFQELDRLHQEQNAQSAKLRLEKRRLEEE 753
Cdd:COG4913   313 RLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLER----ELEERERRRARLEALLAALGLPLPASAEEFAALRAE 388
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  754 EKEQVQRVAHLEEQLRKRQDTApllcPGEAQRAQEEKRELESIREALLQAKEMRAGGDHTCRDELERAqqyfLEFKRRQ- 832
Cdd:COG4913   389 AAALLEALEEELEALEEALAEA----EAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEA----LGLDEAEl 460
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  833 -----LVKLASLEKD----------------LVQQKDLlsKEVQE--------EKVALEHVKcDAGGDPSFLATDDGNIL 883
Cdd:COG4913   461 pfvgeLIEVRPEEERwrgaiervlggfaltlLVPPEHY--AAALRwvnrlhlrGRLVYERVR-TGLPDPERPRLDPDSLA 537
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  884 GgppdldKIKTAETRLQSRehqLQDLLQNHLPALLEEKQRVLDALDSGVlgldTTLCQVEKEVGEKEEQIAQYQANASQL 963
Cdd:COG4913   538 G------KLDFKPHPFRAW---LEAELGRRFDYVCVDSPEELRRHPRAI----TRAGQVKGNGTRHEKDDRRRIRSRYVL 604
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  964 QqlratFEFTANVARQEEKVRRKEKEILESQEkqQREALEQAVAKLEQRRSALQRCS----------TLDLEIQEQRQKL 1033
Cdd:COG4913   605 G-----FDNRAKLAALEAELAELEEELAEAEE--RLEALEAELDALQERREALQRLAeyswdeidvaSAEREIAELEAEL 677
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287 1034 GSLHTSewSGWQASLETDGEALEMDPARLEHEIHQLKQKIcevDGVQRPHHGILEGQAVLSSL---PPSGGNSHLAPLMD 1110
Cdd:COG4913   678 ERLDAS--SDDLAALEEQLEELEAELEELEEELDELKGEI---GRLEKELEQAEEELDELQDRleaAEDLARLELRALLE 752
                         570       580
                  ....*....|....*....|....*..
gi 124487287 1111 ARISAYIEEEVQRRLHD-LHRAIGDAN 1136
Cdd:COG4913   753 ERFAAALGDAVERELREnLEERIDALR 779
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
550-720 1.37e-04

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 46.27  E-value: 1.37e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287   550 RFNHPKEAA---KLREKRKSGLLSSFSLSMTDLSKSCENLSAVMLY----NPGLEFERQQREELEKLESKRKLiEEMEEK 622
Cdd:pfam17380  393 RVRQELEAArkvKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRrleeERAREMERVRLEEQERQQQVERL-RQQEEE 471
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287   623 QKSDKAELERMQQEvetrRKETEIVQRQIRKQE-ESLKRRSFHIENKLKDLLAEKERFEEERLREQQ--GLEQQRR--QE 697
Cdd:pfam17380  472 RKRKKLELEKEKRD----RKRAEEQRRKILEKElEERKQAMIEEERKRKLLEKEMEERQKAIYEEERrrEAEEERRkqQE 547
                          170       180
                   ....*....|....*....|...
gi 124487287   698 EESLFRIREELRKLQELNSHEQA 720
Cdd:pfam17380  548 MEERRRIQEQMRKATEERSRLEA 570
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
555-1037 1.37e-04

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 46.50  E-value: 1.37e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287   555 KEAAKLREKRKSGLLSSFSLSMTDLSKSCENLSAVM--LYNPGLEFERQQREEL----EKLESKRKLIEEMEEKQK---- 624
Cdd:pfam02463  207 KKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLqeLLRDEQEEIESSKQEIekeeEKLAQVLKENKEEEKEKKlqee 286
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287   625 ----------SDKAELERMQQEVETRRKETEIVQRQIRKQEESLKRRSFHIENKLKDLLAEKERFEEERLREQQgLEQQR 694
Cdd:pfam02463  287 elkllakeeeELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEE-LEKLQ 365
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287   695 RQEEESLFRIREELRKLQELNSHEQAEKVQifQELDRLHQEQNAQSAKLRLEKRRLEEEEKEQVQRVAHLEEQLRKRQDT 774
Cdd:pfam02463  366 EKLEQLEEELLAKKKLESERLSSAAKLKEE--ELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQ 443
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287   775 APLLCPGEA---QRAQEEKRELESIREALLQAKEMRAGGDHTCRDELERAQQYFLEFKRRQLVK-LASLEKDLVQQKDLL 850
Cdd:pfam02463  444 GKLTEEKEElekQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSgLKVLLALIKDGVGGR 523
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287   851 SKEVQEEKVALEHVKCDAGGDPSFLATDDGNILGGPPDLDKIKTAETR-----LQSREHQLQDLLQNHLPALLEEKQRVL 925
Cdd:pfam02463  524 IISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTelplgARKLRLLIPKLKLPLKSIAVLEIDPIL 603
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287   926 DALDSGVLGLDTTLCQVEKEVGEKEEQIAQYQ-------ANASQLQQLRATFEFTANVARQEEKVRRKEKEILESQEKQQ 998
Cdd:pfam02463  604 NLAQLDKATLEADEDDKRAKVVEGILKDTELTklkesakAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQE 683
                          490       500       510
                   ....*....|....*....|....*....|....*....
gi 124487287   999 REalEQAVAKLEQRRSALQRCSTLDLEIQEQRQKLGSLH 1037
Cdd:pfam02463  684 KA--ESELAKEEILRRQLEIKKKEQREKEELKKLKLEAE 720
PX_SNX8_Mvp1p_like cd06866
The phosphoinositide binding Phox Homology domain of Sorting Nexin 8 and yeast Mvp1p; The PX ...
1196-1264 1.52e-04

The phosphoinositide binding Phox Homology domain of Sorting Nexin 8 and yeast Mvp1p; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. Some SNXs are localized in early endosome structures such as clathrin-coated pits, while others are located in late structures of the endocytic pathway. SNX8 and the yeast counterpart Mvp1p are involved in sorting and delivery of late-Golgi proteins, such as carboxypeptidase Y, to vacuoles.


Pssm-ID: 132776  Cd Length: 105  Bit Score: 42.22  E-value: 1.52e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124487287 1196 HFEFEVKiSVLDETwTVFRRYSRFREMHKTLKLKYAELAALEFPPKKLFGNKDERVVAERRTHLEKYLR 1264
Cdd:cd06866    18 HVEYEVS-SKRFKS-TVYRRYSDFVWLHEYLLKRYPYRMVPALPPKRIGGSADREFLEARRRGLSRFLN 84
PTZ00121 PTZ00121
MAEBL; Provisional
599-1072 1.58e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 46.29  E-value: 1.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  599 ERQQREELEKLESKRKLIEEM-----------EEKQKSD--KAELERMQQEVETRRKETEIVQRQIRKQE---ESLKRRS 662
Cdd:PTZ00121 1294 EAKKAEEKKKADEAKKKAEEAkkadeakkkaeEAKKKADaaKKKAEEAKKAAEAAKAEAEAAADEAEAAEekaEAAEKKK 1373
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  663 FHIENKLKDLLAEKERFEEERLREQQGLEQQRRQEE-----------ESLFRIREELRKLQELNshEQAEKVQIFQELDR 731
Cdd:PTZ00121 1374 EEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADElkkaaaakkkaDEAKKKAEEKKKADEAK--KKAEEAKKADEAKK 1451
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  732 LHQEQNAQSAKLRLEKRRLEEEEKEQVQRVAHLEEQLRKRQDTAPLLCPgEAQRAQEEKRELESIREA--LLQAKEMRAG 809
Cdd:PTZ00121 1452 KAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKAD-EAKKAAEAKKKADEAKKAeeAKKADEAKKA 1530
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  810 GDHTCRDELERAQqyflEFKRRQLVKLASLEKDLVQQKDLLSKEVQEEKVALEHVKCDAGGDPSflATDDGNILGGPPDL 889
Cdd:PTZ00121 1531 EEAKKADEAKKAE----EKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAE--EARIEEVMKLYEEE 1604
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  890 DKIKTAETRLQSREHQLQDLLQNHlpalLEEKQRVldaldsgvlgldttlcQVEKEVGEKEEQIAQYQANASQLQQLRAt 969
Cdd:PTZ00121 1605 KKMKAEEAKKAEEAKIKAEELKKA----EEEKKKV----------------EQLKKKEAEEKKKAEELKKAEEENKIKA- 1663
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  970 feftANVARQEEKVRRKEKEiLESQEKQQREALEQAVAKLEQRRSALQRCSTLDLEIQEQRQKLGSLHTSEWSGWQASLE 1049
Cdd:PTZ00121 1664 ----AEEAKKAEEDKKKAEE-AKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKE 1738
                         490       500
                  ....*....|....*....|....*..
gi 124487287 1050 TDGEALEMDPARLEHE----IHQLKQK 1072
Cdd:PTZ00121 1739 AEEDKKKAEEAKKDEEekkkIAHLKKE 1765
RNase_Y_N pfam12072
RNase Y N-terminal region;
612-725 1.72e-04

RNase Y N-terminal region;


Pssm-ID: 463456 [Multi-domain]  Cd Length: 201  Bit Score: 44.11  E-value: 1.72e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287   612 KRKLIEEMEEKQKSdKAELERmqqEVETRRKETEIVQRQIRKQEESLKRRSFHIENKLKDLLAekerFEEERLREQQGLE 691
Cdd:pfam12072   52 KEALLEAKEEIHKL-RAEAER---ELKERRNELQRQERRLLQKEETLDRKDESLEKKEESLEK----KEKELEAQQQQLE 123
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 124487287   692 QQRRQEEEslfRIREELRKLQELN--SHEQAEKVQI 725
Cdd:pfam12072  124 EKEEELEE---LIEEQRQELERISglTSEEAKEILL 156
Yop-YscD_cpl pfam16697
Inner membrane component of T3SS, cytoplasmic domain; Yop-YscD-cpl is the cytoplasmic domain ...
471-555 1.78e-04

Inner membrane component of T3SS, cytoplasmic domain; Yop-YscD-cpl is the cytoplasmic domain of Yop proteins like YscD from Proteobacteria. YscD forms part of the inner membrane component of the bacterial type III secretion injectosome apparatus.


Pssm-ID: 465238 [Multi-domain]  Cd Length: 94  Bit Score: 41.86  E-value: 1.78e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287   471 YHLKEGQTYVGREDastEQDIVLHGLDLESEHCVFENAGGTVTLIPLR-GSQCSVNGVQIVDAT-QLNQGAVILLGRTnM 548
Cdd:pfam16697   12 FPLEGGRYRIGSDP---DCDIVLSDKEVSRVHLKLEVDDEGWRLDDLGsGNGTLVNGQRVTELGiALRPGDRIELGQT-E 87

                   ....*..
gi 124487287   549 FRFNHPK 555
Cdd:pfam16697   88 FCLVPAD 94
PX_SNX17_31 cd06885
The phosphoinositide binding Phox Homology domain of Sorting Nexins 17 and 31; The PX domain ...
1215-1263 1.89e-04

The phosphoinositide binding Phox Homology domain of Sorting Nexins 17 and 31; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Members of this subfamily include sorting nexin 17 (SNX17), SNX31, and similar proteins. They contain an N-terminal PX domain followed by a truncated FERM (4.1, ezrin, radixin, and moesin) domain and a unique C-terminal region. SNXs make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. SNX17 is known to regulate the trafficking and processing of a number of proteins. It binds some members of the low-density lipoprotein receptor (LDLR) family such as LDLR, VLDLR, ApoER2, and others, regulating their endocytosis. It also binds P-selectin and may regulate its lysosomal degradation. SNX17 is highly expressed in neurons. It binds amyloid precursor protein (APP) and may be involved in its intracellular trafficking and processing to amyloid beta peptide, which plays a central role in the pathogenesis of Alzheimer's disease. The biological function of SNX31 is unknown.


Pssm-ID: 132795  Cd Length: 104  Bit Score: 41.93  E-value: 1.89e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 124487287 1215 RYSRFREMHKTLKLKYAELAALEFPPKKLFGNKDERVVaERRTHLEKYL 1263
Cdd:cd06885    34 RYSQLHGLNEQLKKEFGNRKLPPFPPKKLLPLTPAQLE-ERRLQLEKYL 81
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
599-805 1.95e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 45.28  E-value: 1.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  599 ERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETRRKETEIVQRQIRKQEESLKRRSFHIEnKLKDLLAEKER 678
Cdd:COG4372    30 SEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELA-QAQEELESLQE 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  679 FEEERLREQQGLEQQRRQEEESLFRIREELRKLQELNSHEQAEKVQIFQELDRLHQE----QNAQSAKLRLEKRRLEEEE 754
Cdd:COG4372   109 EAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEElaalEQELQALSEAEAEQALDEL 188
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 124487287  755 KEQVQRVAHLEEQLRKRQDTAPLLCPGEAQRAQEEKRELESIREALLQAKE 805
Cdd:COG4372   189 LKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALL 239
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
601-862 1.99e-04

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 46.12  E-value: 1.99e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287   601 QQREELEKLESKRKLIEEMEEKQKSDKAELERmqqEVETRRKETEIVQRQIRKQEESLKRRSFHIENKLKDLLAEKERFE 680
Cdd:pfam02463  192 LEELKLQELKLKEQAKKALEYYQLKEKLELEE---EYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLA 268
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287   681 EERLREQQGLEQQRRQEEESLFRIREELRKLQELNSHEQA-----EKVQIFQELDRLHQEQNAQSAKLRLEKRRLEEEEK 755
Cdd:pfam02463  269 QVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRkvddeEKLKESEKEKKKAEKELKKEKEEIEELEKELKELE 348
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287   756 EQVQRVAHLEEQLRKRQDTAPLLCPGEAQRAQEEKRELESIREALLQAKEMRAGGDHTCRDELERAQQYFLEFKRRQLVK 835
Cdd:pfam02463  349 IKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEE 428
                          250       260
                   ....*....|....*....|....*..
gi 124487287   836 lasLEKDLVQQKDLLSKEVQEEKVALE 862
Cdd:pfam02463  429 ---LEILEEEEESIELKQGKLTEEKEE 452
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
775-1036 2.14e-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: 2.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  775 APLLCPGEAQRAQEEKRELESIREALLQAKEmraggdhtcrdELERAQQyflefKRRQLVK-LASLEKDLVQQKDLLsKE 853
Cdd:COG4942    11 LALAAAAQADAAAEAEAELEQLQQEIAELEK-----------ELAALKK-----EEKALLKqLAALERRIAALARRI-RA 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  854 VQEEKVALEHvkcdaggdpsflatddgnilggppDLDKIKTAETRLQSREHQLQDLLQNHLPALLEEKQRVLDAL---DS 930
Cdd:COG4942    74 LEQELAALEA------------------------ELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALllsPE 129
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  931 GVLGLDTTLCQVEKEVGEKEEQIAQYQANASQLQQLRATFEFTANVARQEEKVRRKEKEILESQEKQQREALEQAVAKLE 1010
Cdd:COG4942   130 DFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELA 209
                         250       260
                  ....*....|....*....|....*.
gi 124487287 1011 QRRSALQrcstldlEIQEQRQKLGSL 1036
Cdd:COG4942   210 ELAAELA-------ELQQEAEELEAL 228
PX_p40phox cd06882
The phosphoinositide binding Phox Homology domain of the p40phox subunit of NADPH oxidase; The ...
1191-1268 2.83e-04

The phosphoinositide binding Phox Homology domain of the p40phox subunit of NADPH oxidase; The PX domain is a phosphoinositide binding module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. p40phox contains an N-terminal PX domain, a central SH3 domain that binds p47phox, and a C-terminal PB1 domain that interacts with p67phox. It is a cytosolic subunit of the phagocytic NADPH oxidase complex (also called Nox2 or gp91phox) which plays a crucial role in the cellular response to bacterial infection. NADPH oxidase catalyzes the transfer of electrons from NADPH to oxygen during phagocytosis forming superoxide and reactive oxygen species. p40phox positively regulates NADPH oxidase in both phosphatidylinositol-3-phosphate (PI3P)-dependent and PI3P-independent manner. The PX domain is a phospholipid-binding module involved in the membrane targeting of proteins. The p40phox PX domain binds to PI3P, an abundant lipid in phagosomal membranes, playing an important role in the localization of NADPH oxidase. The PX domain of p40phox is also involved in protein-protein interaction.


Pssm-ID: 132792  Cd Length: 123  Bit Score: 42.04  E-value: 2.83e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287 1191 QGKDEHFEF--EVKISVlDETWTVFRRYSRFREMHKTLKLKY---AELAAL-----EFPPKKLFGNKDErvVAERRT-HL 1259
Cdd:cd06882    15 RGFTNYYVFviEVKTKG-GSKYLIYRRYRQFFALQSKLEERFgpeAGSSAYdctlpTLPGKIYVGRKAE--IAERRIpLL 91

                  ....*....
gi 124487287 1260 EKYLREFFS 1268
Cdd:cd06882    92 NRYMKELLS 100
PX_SNX16 cd07276
The phosphoinositide binding Phox Homology domain of Sorting Nexin 16; The PX domain is a ...
1194-1267 3.39e-04

The phosphoinositide binding Phox Homology domain of Sorting Nexin 16; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. SNX16 contains a central PX domain followed by a coiled-coil region. SNX16 is localized in early and recycling endosomes through the binding of its PX domain to phosphatidylinositol-3-phosphate (PI3P). It plays a role in epidermal growth factor (EGF) signaling by regulating EGF receptor membrane trafficking.


Pssm-ID: 132809  Cd Length: 110  Bit Score: 41.63  E-value: 3.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287 1194 DEHFEFEV-KISVL---DETWTVFRRYSRFREMHKTLKLKYAELaALEFPPKKLFGNK------DERV----------VA 1253
Cdd:cd07276    15 EERARFTVyKIRVEnkvGDSWFVFRRYTDFVRLNDKLKQMFPGF-RLSLPPKRWFKDNfdpdflEERQlglqafvnniMA 93
                          90
                  ....*....|....
gi 124487287 1254 ERRTHLEKYLREFF 1267
Cdd:cd07276    94 HKDIAKCKLVREFF 107
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
595-923 3.89e-04

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 44.96  E-value: 3.89e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287   595 GLEFERQQREELEKLESK-----RKLIEEMEEK------QKSDKAELERMQQEVETRRKETEIVQRQIRKQEESLKRRSF 663
Cdd:pfam02463  164 GSRLKRKKKEALKKLIEEtenlaELIIDLEELKlqelklKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQ 243
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287   664 HIENKLKDLLAEKERFEEERLREQQGLEQQRRQEEESLFRIREELRKLQELNSHEQAEKVQIFQELDRLHQEQNAQSAKL 743
Cdd:pfam02463  244 ELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEK 323
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287   744 RLEKRRLEEEEKEQVQRVAHLEEQLRKRQdtaPLLCPGEAQRAQEEKRELESIREALLQAKEMRAGGDHTCRDELERAQQ 823
Cdd:pfam02463  324 KKAEKELKKEKEEIEELEKELKELEIKRE---AEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELK 400
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287   824 YFLEFKRRQLVKLASLEKDLVQ-QKDLLSKEVQEEKVALEHVKCDAGGDPSFLATDDGNILGGPPDLDKIKTAETRLQSR 902
Cdd:pfam02463  401 SEEEKEAQLLLELARQLEDLLKeEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLV 480
                          330       340
                   ....*....|....*....|.
gi 124487287   903 EHQLQDLLQNHLPALLEEKQR 923
Cdd:pfam02463  481 KLQEQLELLLSRQKLEERSQK 501
FHA_RADIL cd22733
forkhead associated (FHA) domain found in Ras-associating and dilute domain-containing protein ...
452-554 5.13e-04

forkhead associated (FHA) domain found in Ras-associating and dilute domain-containing protein (Radil); Radil acts as an important small GTPase Rap1 effector required for cell spreading and migration. It regulates neutrophil adhesion and motility through linking Rap1 to beta2-integrin activation. It contains an FHA domain. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438785  Cd Length: 113  Bit Score: 40.94  E-value: 5.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  452 ELPHLIGIDDDLLSTGIILYHLKEGQTYVGREDASTEQDIVLHGLDLESEHCVFE-------NAGGTVTLIPLRGSQCSV 524
Cdd:cd22733     4 QSPHLLLLQGYNQQHDCLVYLLNREQHTVGQETPSSKPNISLSAPDILPLHCTIRrvrlpkhRSEEKLVLEPIPGAHVSV 83
                          90       100       110
                  ....*....|....*....|....*....|
gi 124487287  525 NGVQIVDATQLNQGAVILLGRTNMFRFNHP 554
Cdd:cd22733    84 NFSEVERTTLLRHGDLLSFGAYYLFLFKDP 113
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
665-1073 5.55e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 44.37  E-value: 5.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  665 IENKLKDLLAEKERFEEERLREQQGLEQQRRQEEESLFRIREELRKLQELNSHE---QAEKVQIFQELDRLHQEQNAQSA 741
Cdd:COG4717    51 LEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELeelEAELEELREELEKLEKLLQLLPL 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  742 KLRLEKRRLEEEE--------KEQVQRVAHLEEQLRKRQDTA-----------PLLCPGEAQRAQEEKRELESIREALLQ 802
Cdd:COG4717   131 YQELEALEAELAElperleelEERLEELRELEEELEELEAELaelqeeleellEQLSLATEEELQDLAEELEELQQRLAE 210
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  803 AKEMRAggdhTCRDELERAQQyflefkrrqlvKLASLEKDLVQQKDLLSKEVQEEKVALEHVKCDAGGDPSFLATDDGNI 882
Cdd:COG4717   211 LEEELE----EAQEELEELEE-----------ELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTI 275
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  883 LG------GPPDLDKIKTAETRLQSREHQLQDLLQNHLPALleEKQRVLDALDSgvLGLDTTLcqVEKEVGEKEEQIAQY 956
Cdd:COG4717   276 AGvlflvlGLLALLFLLLAREKASLGKEAEELQALPALEEL--EEEELEELLAA--LGLPPDL--SPEELLELLDRIEEL 349
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  957 QANASQLQQLRAtfeftanvARQEEKVRRKEKEILESQEKQQREALEQAVAKLEQRRSALQRCSTLDLEIQEQrqkLGSL 1036
Cdd:COG4717   350 QELLREAEELEE--------ELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEEL---LGEL 418
                         410       420       430
                  ....*....|....*....|....*....|....*..
gi 124487287 1037 HTSEWSGWQASLETDGEALEMDPARLEHEIHQLKQKI 1073
Cdd:COG4717   419 EELLEALDEEELEEELEELEEELEELEEELEELREEL 455
FHA pfam00498
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.
478-543 9.45e-04

FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.


Pssm-ID: 459831 [Multi-domain]  Cd Length: 66  Bit Score: 38.71  E-value: 9.45e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124487287   478 TYVGRedaSTEQDIVLHGLDLESEHCVFE-NAGGTVTLIPLRGSQ-CSVNGVQI-VDATQLNQGAVILL 543
Cdd:pfam00498    1 VTIGR---SPDCDIVLDDPSVSRRHAEIRyDGGGRFYLEDLGSTNgTFVNGQRLgPEPVRLKDGDVIRL 66
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
603-1136 1.23e-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: 43.52  E-value: 1.23e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287   603 REELEKLESKrklIEEMEEKQKSDKAELERMQQEVETRRKETEIVQRQIRKQEESLKRRSF---HIENKLKDLLAEKERF 679
Cdd:TIGR02169  363 KEELEDLRAE---LEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEelaDLNAAIAGIEAKINEL 439
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287   680 EEERLREQQGLEQQRRQ----------EEESLFRIREELRKLQELNSHEQAEKVQIFQELDRLHQEQNAQSAKLRLEKRR 749
Cdd:TIGR02169  440 EEEKEDKALEIKKQEWKleqlaadlskYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKAS 519
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287   750 LE-------EEEKEQVQRVAHLEEQLRKRQDTAPLLCPGEAQRAQEEKRELESIREALLQAKEMRAGGDH---------- 812
Cdd:TIGR02169  520 IQgvhgtvaQLGSVGERYATAIEVAAGNRLNNVVVEDDAVAKEAIELLKRRKAGRATFLPLNKMRDERRDlsilsedgvi 599
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287   813 -------TCRDELERAQQYF---------LEFKRRQL--VKLASLEKDLVQQ-------------KDLLSKEVQEEKVAL 861
Cdd:TIGR02169  600 gfavdlvEFDPKYEPAFKYVfgdtlvvedIEAARRLMgkYRMVTLEGELFEKsgamtggsraprgGILFSRSEPAELQRL 679
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287   862 EHVKCDAGGDPSFLATDDGNILGGPPDL-DKIKTAETRLQSREHQLQDLLQNH--LPALLEEKQRVLDALDSGVLGLDTT 938
Cdd:TIGR02169  680 RERLEGLKRELSSLQSELRRIENRLDELsQELSDASRKIGEIEKEIEQLEQEEekLKERLEELEEDLSSLEQEIENVKSE 759
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287   939 LCQVEKEVGEKEEQIAQYQA---------NASQLQQLRATFEFT-ANVARQEEKVRRKEKEIleSQEKQQREALEQAVAK 1008
Cdd:TIGR02169  760 LKELEARIEELEEDLHKLEEalndlearlSHSRIPEIQAELSKLeEEVSRIEARLREIEQKL--NRLTLEKEYLEKEIQE 837
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  1009 LEQRRSALQ-RCSTLDLEIQEQRQKLGSLHT--SEWSGWQASLETDGEALEMDPARLEHEIHQLKQKICEVDG-VQRPHH 1084
Cdd:TIGR02169  838 LQEQRIDLKeQIKSIEKEIENLNGKKEELEEelEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAqIEKKRK 917
                          570       580       590       600       610       620
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124487287  1085 GILEGQAVLSSL---------PPSGGNSHLAPLMDARISAYIEEEVQRRLhdlhRAIGDAN 1136
Cdd:TIGR02169  918 RLSELKAKLEALeeelseiedPKGEDEEIPEEELSLEDVQAELQRVEEEI----RALEPVN 974
PX_RPK118_like cd07287
The phosphoinositide binding Phox Homology domain of RPK118-like proteins; The PX domain is a ...
1211-1267 1.73e-03

The phosphoinositide binding Phox Homology domain of RPK118-like proteins; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. Members of this subfamily bear similarity to human RPK118, which contains an N-terminal PX domain, a Microtubule Interacting and Trafficking (MIT) domain, and a kinase domain. RPK118 binds sphingosine kinase, a key enzyme in the synthesis of sphingosine 1-phosphate (SPP), a lipid messenger involved in many cellular events. RPK118 may be involved in transmitting SPP-mediated signaling. It also binds the antioxidant peroxiredoxin-3 (PRDX3) and may be involved in the transport of PRDX3 from the cytoplasm to its site of function in the mitochondria. Members of this subfamily also show similarity to sorting nexin 15 (SNX15), which contains PX and MIT domains but does not contain a kinase domain. SNXs make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNX15 plays a role in protein trafficking processes in the endocytic pathway and the trans-Golgi network. The PX domain of SNX15 interacts with the PDGF receptor and is responsible for the membrane association of the protein.


Pssm-ID: 132820  Cd Length: 118  Bit Score: 39.56  E-value: 1.73e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124487287 1211 TVFRRYSRFREMHKTLKLKYAELAALE--FPP---KKLFGNKDERVVAERRTHLE---------------KYLREFF 1267
Cdd:cd07287    39 VVWKRYSDFKKLHKDLWQIHKNLCRQSelFPPfakAKVFGRFDESVIEERRQCAEdllqfsanipalynsSQLEDFF 115
PX_SNX15 cd07288
The phosphoinositide binding Phox Homology domain of Sorting Nexin 15; The PX domain is a ...
1212-1264 1.96e-03

The phosphoinositide binding Phox Homology domain of Sorting Nexin 15; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. SNX15 contains an N-terminal PX domain and a C-terminal Microtubule Interacting and Trafficking (MIT) domain. It plays a role in protein trafficking processes in the endocytic pathway and the trans-Golgi network. The PX domain of SNX15 interacts with the PDGF receptor and is responsible for the membrane association of the protein.


Pssm-ID: 132821  Cd Length: 118  Bit Score: 39.57  E-value: 1.96e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 124487287 1212 VFRRYSRFREMHKTLKLKYAEL--AALEFPP---KKLFGNKDERVVAERRTHLEKYLR 1264
Cdd:cd07288    40 VWKRYSDLKKLHGELAYTHRNLfrRQEEFPPfprAQVFGRFEAAVIEERRNAAEAMLL 97
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
597-926 2.40e-03

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


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 42.19  E-value: 2.40e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287   597 EFERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETRRKETEIVQRQIRKQEE---SLKRRSFHIENKLKDLl 673
Cdd:pfam07888   77 ELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEdikTLTQRVLERETELERM- 155
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287   674 aekerfeeerLREQQGLEQQRRQEEESLFRIREELRKLQELNSHEQAEkvqiFQELDRLHQEQNAQSAKLRLEKRRLEEE 753
Cdd:pfam07888  156 ----------KERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKE----FQELRNSLAQRDTQVLQLQDTITTLTQK 221
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287   754 EKEQVQRVAHLE---EQLRKRQDtapLLCPGEaQRAQEEKRELES-----------IREALLQAKEMR---AGGDHTCRD 816
Cdd:pfam07888  222 LTTAHRKEAENEallEELRSLQE---RLNASE-RKVEGLGEELSSmaaqrdrtqaeLHQARLQAAQLTlqlADASLALRE 297
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287   817 ELERAQQyflefKRRQLVKLASLEKDLVQQ--KDLLSKE--VQEEKVALEHVKCDaggdpsflatddgniLGGPPDLDKI 892
Cdd:pfam07888  298 GRARWAQ-----ERETLQQSAEADKDRIEKlsAELQRLEerLQEERMEREKLEVE---------------LGREKDCNRV 357
                          330       340       350
                   ....*....|....*....|....*....|....*
gi 124487287   893 KTAETRLQSREHQL-QDLLQNHLPALLEEKQRVLD 926
Cdd:pfam07888  358 QLSESRRELQELKAsLRVAQKEKEQLQAEKQELLE 392
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
599-787 2.79e-03

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 41.74  E-value: 2.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  599 ERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETRRKETEIVQRQIRKQEESLKRRSFHIENK---------- 668
Cdd:COG3883    29 QAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSggsvsyldvl 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  669 -----LKDLLAEKERFEEERLREQQGLEQQRRQeeeslfriREELRKLQELNSHEQAEKVQIFQELDRLHQEQNAQSAKL 743
Cdd:COG3883   109 lgsesFSDFLDRLSALSKIADADADLLEELKAD--------KAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQ 180
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 124487287  744 RLEKRRLEEEEKEQVQRVAHLEEQLRKRQDTAPLLCPGEAQRAQ 787
Cdd:COG3883   181 EALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAA 224
PRK11637 PRK11637
AmiB activator; Provisional
957-1040 3.60e-03

AmiB activator; Provisional


Pssm-ID: 236942 [Multi-domain]  Cd Length: 428  Bit Score: 41.22  E-value: 3.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  957 QANASQLQQLRAtfEFTANVARQEEKvRRKEKEILESQEKQQrealeqavAKLEQRRSALQRC-STLDLEIQEQRQKLGS 1035
Cdd:PRK11637  169 QETIAELKQTRE--ELAAQKAELEEK-QSQQKTLLYEQQAQQ--------QKLEQARNERKKTlTGLESSLQKDQQQLSE 237

                  ....*
gi 124487287 1036 LHTSE 1040
Cdd:PRK11637  238 LRANE 242
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
600-805 3.77e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 41.58  E-value: 3.77e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287   600 RQQREELEKLESKR-----------KLIEEMEEKQKSDKAELERMQQEVETRRKETEIVQRQIRKQEESLKRRSFHIENK 668
Cdd:TIGR02168  820 ANLRERLESLERRIaaterrledleEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEEL 899
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287   669 LKDLlaekerfeeerlreqQGLEQQRRQEEESLFRIREELRKLQElnsHEQAEKVQIFQELDRLHQEQNAQSAKLRLEKR 748
Cdd:TIGR02168  900 SEEL---------------RELESKRSELRRELEELREKLAQLEL---RLEGLEVRIDNLQERLSEEYSLTLEEAEALEN 961
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 124487287   749 RLEEEEKEQVQRVAHLEEQLrKRQDTAPLLCPGEAQRAQEEKRELESIREALLQAKE 805
Cdd:TIGR02168  962 KIEDDEEEARRRLKRLENKI-KELGPVNLAAIEEYEELKERYDFLTAQKEDLTEAKE 1017
PRK12704 PRK12704
phosphodiesterase; Provisional
601-674 3.78e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 41.30  E-value: 3.78e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 124487287  601 QQREELEK-LESKRKLIEEMEEKQKSDKAELERMQQEVETRRKETEIVQRQIRKQEESLKRRSFHIENKLKDLLA 674
Cdd:PRK12704   68 KLRNEFEKeLRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQ 142
Mitofilin pfam09731
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ...
600-699 3.88e-03

Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.


Pssm-ID: 430783 [Multi-domain]  Cd Length: 618  Bit Score: 41.67  E-value: 3.88e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287   600 RQQREELEKLEskRKLIEEMEEKQKSDKAELERMQQevetrRKETEIVQRQIRKQEESLKRRSFHIENKLKDLLAekerf 679
Cdd:pfam09731  319 EKQKEELDKLA--EELSARLEEVRAADEAQLRLEFE-----REREEIRESYEEKLRTELERQAEAHEEHLKDVLV----- 386
                           90       100
                   ....*....|....*....|
gi 124487287   680 eeerlreQQGLEQQRRQEEE 699
Cdd:pfam09731  387 -------EQEIELQREFLQD 399
PX_SNX19 cd06893
The phosphoinositide binding Phox Homology domain of Sorting Nexin 19; The PX domain is a ...
1209-1279 3.91e-03

The phosphoinositide binding Phox Homology domain of Sorting Nexin 19; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. SNX19 contains an N-terminal PXA domain, a central PX domain, and a C-terminal domain that is conserved in some SNXs. These domains are also found in SNX13 and SNX14, which also contain a regulator of G protein signaling (RGS) domain in between the PXA and PX domains. SNX19 interacts with IA-2, a major autoantigen found in type-1 diabetes. It inhibits the conversion of phosphatidylinositol-4,5-bisphosphate [PI(4,5)P2] to PI(3,4,5)P3, which leads in the decrease of protein phosphorylation in the Akt signaling pathway, resulting in apoptosis. SNX19 may also be implicated in coronary heart disease and thyroid oncocytic tumors.


Pssm-ID: 132803 [Multi-domain]  Cd Length: 132  Bit Score: 39.06  E-value: 3.91e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124487287 1209 TWTVFRRYSRFREMHKTL--KLKYAELAALEFPPKKL----FGNKDERVVAERRTHLEKYLREFFSVMLQSETSPLH 1279
Cdd:cd06893    50 THTVNRRFREFLTLQTRLeeNPKFRKIMNVKGPPKRLfdlpFGNMDKDKIEARRGLLETFLRQLCSIPEISNSEEVQ 126
PX_SNX14 cd06877
The phosphoinositide binding Phox Homology domain of Sorting Nexin 14; The PX domain is a ...
1180-1264 4.02e-03

The phosphoinositide binding Phox Homology domain of Sorting Nexin 14; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. SNX14 may be involved in recruiting other proteins to the membrane via protein-protein and protein-ligand interaction. It is expressed in the embryonic nervous system of mice, and is co-expressed in the motoneurons and the anterior pituary with Islet-1. SNX14 shows a similar domain architecture as SNX13, containing an N-terminal PXA domain, a regulator of G protein signaling (RGS) domain, a PX domain, and a C-terminal domain that is conserved in some SNXs.


Pssm-ID: 132787  Cd Length: 119  Bit Score: 38.51  E-value: 4.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287 1180 KISIPRY--VLCGQGKDEHFEFEVKI--------SVLDETWTVFRRYSRFRemhkTLKLKYAE----LAALEFPPKKLFG 1245
Cdd:cd06877     4 RVSIPYVemRRDPSNGERIYVFCIEVerndrrakGHEPQHWSVLRRYNEFY----VLESKLTEfhgeFPDAPLPSRRIFG 79
                          90
                  ....*....|....*....
gi 124487287 1246 NKDERVVAERRTHLEKYLR 1264
Cdd:cd06877    80 PKSYEFLESKREIFEEFLQ 98
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
603-862 4.36e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.59  E-value: 4.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  603 REELEKLESKRKLIEEMEEKQKS---DKAELERMQQEVETRRKETEIVQRQIRKQEESLKRRSFHIEN--KLKDLLAEKE 677
Cdd:PRK03918  227 EKEVKELEELKEEIEELEKELESlegSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEyiKLSEFYEEYL 306
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  678 RFEEERLREQQGLEQQRRQEEESLFRIREELRKLQELnsheQAEKVQIFQELDRL---HQEQNAQSAKLRLEKRRLEEEE 754
Cdd:PRK03918  307 DELREIEKRLSRLEEEINGIEERIKELEEKEERLEEL----KKKLKELEKRLEELeerHELYEEAKAKKEELERLKKRLT 382
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  755 KEQVQRVAHLEEQLRKRQDTAPLlcpgEAQRAQEEKRELESIREALLQAKEMRAGGDH---TCRDELEraQQYFLEFKRR 831
Cdd:PRK03918  383 GLTPEKLEKELEELEKAKEEIEE----EISKITARIGELKKEIKELKKAIEELKKAKGkcpVCGRELT--EEHRKELLEE 456
                         250       260       270
                  ....*....|....*....|....*....|.
gi 124487287  832 QLVKLASLEKDLVQQKDLLSKeVQEEKVALE 862
Cdd:PRK03918  457 YTAELKRIEKELKEIEEKERK-LRKELRELE 486
PX_UP1_plant cd06879
The phosphoinositide binding Phox Homology domain of uncharacterized plant proteins; The PX ...
1194-1278 4.66e-03

The phosphoinositide binding Phox Homology domain of uncharacterized plant proteins; The PX domain is a phosphoinositide (PI) binding module involved in targeting proteins to PI-enriched membranes. Members in this subfamily are uncharacterized fungal proteins containing a PX domain. PX domain harboring proteins have been implicated in highly diverse functions such as cell signaling, vesicular trafficking, protein sorting, lipid modification, cell polarity and division, activation of T and B cells, and cell survival. In addition to protein-lipid interaction, the PX domain may also be involved in protein-protein interaction.


Pssm-ID: 132789  Cd Length: 138  Bit Score: 38.85  E-value: 4.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287 1194 DEHFEFEVKISVLDETWT---VFRRYSRFREMHKTLKLKYAELAALEFPPKKLFGNKDERVVAERRTHLEKYLREFFSVM 1270
Cdd:cd06879    44 DKFYRVQVGVQSPEGITTmrgVLRRFNDFLKLHTDLKKLFPKKKLPAAPPKGLLRMKNRALLEERRHSLEEWMGKLLSDI 123

                  ....*...
gi 124487287 1271 LQSETSPL 1278
Cdd:cd06879   124 DLSRSVPV 131
PX_SNX1_2_like cd06859
The phosphoinositide binding Phox Homology domain of Sorting Nexins 1 and 2; The PX domain is ...
1211-1264 4.82e-03

The phosphoinositide binding Phox Homology domain of Sorting Nexins 1 and 2; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. This subfamily consists of SNX1, SNX2, and similar proteins. They harbor a Bin/Amphiphysin/Rvs (BAR) domain, which detects membrane curvature, C-terminal to the PX domain. Both domains have been shown to determine the specific membrane-targeting of SNX1. SNX1 and SNX2 are components of the retromer complex, a membrane coat multimeric complex required for endosomal retrieval of lysosomal hydrolase receptors to the Golgi. The retromer consists of a cargo-recognition subcomplex and a subcomplex formed by a dimer of sorting nexins (SNX1 and/or SNX2), which ensures effcient cargo sorting by facilitating proper membrane localization of the cargo-recognition subcomplex.


Pssm-ID: 132769 [Multi-domain]  Cd Length: 114  Bit Score: 38.33  E-value: 4.82e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 124487287 1211 TVFRRYSRFREMHKTLKLKYAELAALEFPPKKLFGNKDERV--VAERRTHLEKYLR 1264
Cdd:cd06859    38 SVLRRYSDFLWLYERLVEKYPGRIVPPPPEKQAVGRFKVKFefIEKRRAALERFLR 93
Caldesmon pfam02029
Caldesmon;
594-803 5.65e-03

Caldesmon;


Pssm-ID: 460421 [Multi-domain]  Cd Length: 495  Bit Score: 41.01  E-value: 5.65e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287   594 PGLEFERQQREELEKLESKR-KLIEEMEEKQK---------SDKAELERMQQEVETR---RKETEIVQRQIRKQEESLKR 660
Cdd:pfam02029   56 GGLDEEEAFLDRTAKREERRqKRLQEALERQKefdptiadeKESVAERKENNEEEENsswEKEEKRDSRLGRYKEEETEI 135
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287   661 RSFHI-ENKLKDllaekerfeEERLREQQGLEQQRRQEEESLFR----IREELRKLQELNSHEQAEKVQIFQELDRLHQE 735
Cdd:pfam02029  136 REKEYqENKWST---------EVRQAEEEGEEEEDKSEEAEEVPtenfAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPE 206
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124487287   736 QNAQSAKLRLEKRRLEEEEkeqvqRVAHLEEQLRKRQDTAPLLCPGEA------QRAQEEKRELESIREALLQA 803
Cdd:pfam02029  207 VKSQNGEEEVTKLKVTTKR-----RQGGLSQSQEREEEAEVFLEAEQKleelrrRRQEKESEEFEKLRQKQQEA 275
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
600-700 5.76e-03

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 40.58  E-value: 5.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  600 RQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETRRKETEIVQRQIRKQEESLKRRSFHIENKLKDLLAEKERF 679
Cdd:COG3883   129 DADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAA 208
                          90       100
                  ....*....|....*....|.
gi 124487287  680 EEERLREQQGLEQQRRQEEES 700
Cdd:COG3883   209 EAAAAAAAAAAAAAAAAAAAA 229
COG5391 COG5391
Phox homology (PX) domain protein [Intracellular trafficking and secretion / General function ...
1211-1267 6.85e-03

Phox homology (PX) domain protein [Intracellular trafficking and secretion / General function prediction only];


Pssm-ID: 227680 [Multi-domain]  Cd Length: 524  Bit Score: 40.55  E-value: 6.85e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124487287 1211 TVFRRYSRFREMHKTLKLKYAELAALEFPPKKLFGNK-----DERVVAERRTHLEKYLREFF 1267
Cdd:COG5391   174 VVRRRYSDFESLHSILIKLLPLCAIPPLPSKKSNSEYygdrfSDEFIEERRQSLQNFLRRVS 235
mukB PRK04863
chromosome partition protein MukB;
603-850 6.86e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 41.10  E-value: 6.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  603 REELEKLESKRK----------LIEEMEEKQKSDKAELERMQQEVETRRKETEIVQRQIRKQEESLKRRS-FHIENKLKD 671
Cdd:PRK04863  900 REQLDEAEEAKRfvqqhgnalaQLEPIVSVLQSDPEQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQRRAhFSYEDAAEM 979
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  672 LlaekerfeEERLREQQGLEQQRRQEEESLFRIREELRKLQElnshEQAEKVQIFQELDRLHQEQNaqsaklrlekrrle 751
Cdd:PRK04863  980 L--------AKNSDLNEKLRQRLEQAEQERTRAREQLRQAQA----QLAQYNQVLASLKSSYDAKR-------------- 1033
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  752 eeekeqvQRVAHLEEQLrkrQDTAPLLCPGEAQRAQEEKRELesirEALLQAKEMRaggdhtcRDELERaQQYFLEFKRR 831
Cdd:PRK04863 1034 -------QMLQELKQEL---QDLGVPADSGAEERARARRDEL----HARLSANRSR-------RNQLEK-QLTFCEAEMD 1091
                         250       260
                  ....*....|....*....|
gi 124487287  832 QLVK-LASLEKDLVQQKDLL 850
Cdd:PRK04863 1092 NLTKkLRKLERDYHEMREQV 1111
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
578-865 7.25e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.82  E-value: 7.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  578 DLSKSCENLSAVMLYnpgLEFERqqrEELEKLESKRkliEEMEEKQKSDKAELERMQQEVetrrKETEIVQRQIRKQEES 657
Cdd:PRK03918  159 DYENAYKNLGEVIKE---IKRRI---ERLEKFIKRT---ENIEELIKEKEKELEEVLREI----NEISSELPELREELEK 225
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  658 LKRRSFHIEnKLKDLLAEKERFEEERLREQQGLEQQRRQEEESLFRIREELRKLQEL--NSHEQAEKVQIFQELDRLHQE 735
Cdd:PRK03918  226 LEKEVKELE-ELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKvkELKELKEKAEEYIKLSEFYEE 304
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487287  736 QNAQSAKLRLEKRRLEEEEKEQVQRVAHLEEQLRKRQDTAPLL--CPGEAQRAQEEKRELESIREALLQAKEMRAggDHT 813
Cdd:PRK03918  305 YLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLkeLEKRLEELEERHELYEEAKAKKEELERLKK--RLT 382
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 124487287  814 CRdELERAQQYFLEFKRRQLvKLASLEKDLVQQKDLLSKEVQEEKVALEHVK 865
Cdd:PRK03918  383 GL-TPEKLEKELEELEKAKE-EIEEEISKITARIGELKKEIKELKKAIEELK 432
 
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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