Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199010   4 QAELENYKLQVELLQEKLQRSEDNRQQLEHKLDKILQKRTELDKSVRhKSRQKYQEFLEeqaKRNERNKKLVHMLERIDE 83
Cdd:COG1340     7 SSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVK-ELREEAQELRE---KRDELNEKVKELKEERDE 82

                          90       100
                  ....*....|....*....|....*
gi 1834199010  84 QTAAMSQRSERLKMMKLQYQMYFAK 108
Cdd:COG1340    83 LNEKLNELREELDELRKELAELNKA 107

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199010   4 QAELENYKLQVELLQEKLQRSEDNRQQLEHKLDKILQKRTELDKSVRhKSRQKYQEFLEeqaKRNERNKKLVHMLERIDE 83
Cdd:COG1340     7 SSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVK-ELREEAQELRE---KRDELNEKVKELKEERDE 82

                          90       100
                  ....*....|....*....|....*
gi 1834199010  84 QTAAMSQRSERLKMMKLQYQMYFAK 108
Cdd:COG1340    83 LNEKLNELREELDELRKELAELNKA 107

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]

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199010    4 QAELENYKLQVELLQEKLQRSEDNRQQLEHKLDKILQKRTELDKSVrHKSRQKYQEFLEE----QAKRNERNKKLVHMLE 79
Cdd:TIGR02168  294 ANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEEL-AELEEKLEELKEEleslEAELEELEAELEELES 372

                           90       100
                   ....*....|....*....|..
gi 1834199010   80 RIDEQTAAMSQRSERLKMMKLQ 101
Cdd:TIGR02168  373 RLEELEEQLETLRSKVAQLELQ 394

C-terminal prodomain of legumain; This family contains the C-terminal propeptide of legumain, a lysosomal endopeptidase with a specificity for hydrolysis of asparaginyl bonds. Legumain (also called vacuolar processing enzyme or VPE in plants, and asparaginyl endopeptidase or AEP in animals) is synthesized as a precursor with both N- and C-terminal propeptides. Prolegumain is directed to the lysosome or plant vacuole, where activation occurs at least partially by autolysis. The N-terminal catalytic domain is a cysteine protease from the C13 family. The C-terminal prodomain can be organized into an activation peptide (AP), spanning a helical region, and a C-terminal death domain-like fold, denoted as legumain stabilization and activity modulation (LSAM) domain. The C-terminal prodomain binds over the active site and inhibits the catalytic domain. During activation, the C-terminal prodomain is autocatalytically cleaved. This process is induced by pH changes. Human legumain has been shown to process the tetanus toxin generating the fragments found in class II antigen presentation. Legumain from plant seeds is thought to be responsible for the post-translational processing of seed proteins prior to storage. Legumain is highly expressed in some cancers such as colorectal cancer (CRC) and uveal melanoma (UM); it is associated with poor outcome in CRC and upregulation of legumain is associated with malignant behavior of UM. Thus, legumain may be used as a negative prognostic factor as well as a therapeutic target.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1834199010  14 VELLQEKLQRSEDN--RQQLEHKLDKILQKRTELDKSVRH------KSRQKYQEFLEEQAKRNERN--KKLVHMLER 80
Cdd:cd21115     4 LAILKRKLKKANDPeeKEELKKELEKLLQKREFIDETMKKivklvtGDEEEAERVLSTRRPLTDLDcyKEVVEHFRT 80

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199010   4 QAELENYKLQVELLQEKLQRSEDNRQQLEHKLDKILQKRTELDKSVRhKSRQKYQEFLEeqaKRNERNKKLVHMLERIDE 83
Cdd:COG1340     7 SSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVK-ELREEAQELRE---KRDELNEKVKELKEERDE 82

                          90       100
                  ....*....|....*....|....*
gi 1834199010  84 QTAAMSQRSERLKMMKLQYQMYFAK 108
Cdd:COG1340    83 LNEKLNELREELDELRKELAELNKA 107

Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, microtubule-binding protein consisting of two 1,600-amino acid-long coils, is essential for the full functioning of the mitotic checkpoint pathway. There are several leucine-rich repeats along the sequence of LEK1 that are considered to be zippers, though they do not appear to be binding DNA directly in this instance.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199010   6 ELENYKLQVELLQEKLQRSEDNRQQLEHKLDKILQKRTELDKSVrhksrQKYQEFLEEQAKRNERNKKLvhmLERIDEQT 85
Cdd:pfam10473  46 EAENSKAEVETLKAEIEEMAQNLRDLELDLVTLRSEKENLTKEL-----QKKQERVSELESLNSSLENL---LEEKEQEK 117

                          90
                  ....*....|....*....
gi 1834199010  86 AAMSQRSE-RLKMMKLQYQ 103
Cdd:pfam10473 118 VQMKEESKtAVEMLQTQLK 136

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199010   4 QAELENYKLQVELLQEKLQRSEDNRQQLEHKLDKILQKRTELDKSVRHKS---RQKYQEFLEEQAKRNERNKKLVHMLER 80
Cdd:COG4717   138 EAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSlatEEELQDLAEELEELQQRLAELEEELEE 217

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1834199010  81 IDEQTAAMSQRSERLKMMKLQYQMYfAKLVQNQTLRCI 118
Cdd:COG4717   218 AQEELEELEEELEQLENELEAAALE-ERLKEARLLLLI 254

HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199010   6 ELENyklQVELLQEKLQ----RSEDNrQQLEHKLDKILQKRTELdksvrHKSRQKYQEFLEEQAKRNERNkklvhMLERI 81
Cdd:pfam05622 336 ELQQ---QVEELQKALQeqgsKAEDS-SLLKQKLEEHLEKLHEA-----QSELQKKKEQIEELEPKQDSN-----LAQKI 401

                          90       100
                  ....*....|....*....|....*..
gi 1834199010  82 DEQTAAMSQRSERLKMMKLQYQMYFAK 108
Cdd:pfam05622 402 DELQEALRKKDEDMKAMEERYKKYVEK 428

YscO-like protein; This family of proteins is similar to the type III secretion protein YscO. The family includes Chlamydia trachomatis CT670 which is found in a type III secretion gene cluster. CT670 interacts with CT671, a putative YscP homolog and CT670 and CT671 may form a chaperone-effector pair.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199010  11 KLQVELLQEKLQRSEDNRQQ-LEHKLDKILQKRTELDK---SVRHKSRQKYQEFLEEQAKRNErnKKLVHMLERIDEQTA 86
Cdd:pfam16789  27 KRALEKEKEKLAELEAERDKvRKHKKAKMQQLRDEMDRgttSDKILQMKRYIKVVKERLKQEE--KKVQDQKEQVRTAAR 104

                          90
                  ....*....|.
gi 1834199010  87 AMSQRSERLKM 97
Cdd:pfam16789 105 NLEIAREELKK 115

Uncharacterized protein, contains DUF3084 domain [Function unknown];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199010   4 QAELENYKLQVELLQEKLQRSEDNRQQLEHKLDkilQKRTELDksvrhKSRQKYQEFLEEQAKRNERNKKLVHMLERIDE 83
Cdd:COG4372    51 REELEQAREELEQLEEELEQARSELEQLEEELE---ELNEQLQ-----AAQAELAQAQEELESLQEEAEELQEELEELQK 122

                          90
                  ....*....|...
gi 1834199010  84 QTAAMSQRSERLK 96
Cdd:COG4372   123 ERQDLEQQRKQLE 135

Uncharacterized protein, contains DUF3084 domain [Function unknown];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199010   4 QAELENYKLQVELLQEKLQRSEDNRQQLEHKLDKILQKRTELDKSVRHKSRQKyQEFLEEQAKRNERNKKLVHMLERIDE 83
Cdd:COG4372   100 QEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEEL-KELEEQLESLQEELAALEQELQALSE 178

                  ...
gi 1834199010  84 QTA 86
Cdd:COG4372   179 AEA 181

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199010   4 QAELENYKLQVELLQEKLQRsEDnRQQLEHKLDKILQKRTELDKSVRHKSRQKYQEFLEEQakrnERNKKLVHMLERIDE 83
Cdd:pfam13868  93 YEEKLQEREQMDEIVERIQE-ED-QAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEER----EEDERILEYLKEKAE 166

                          90       100       110
                  ....*....|....*....|....*....|
gi 1834199010  84 QTAAMSQRSERLKMMKlqyQMYFAKLVQNQ 113
Cdd:pfam13868 167 REEEREAEREEIEEEK---EREIARLRAQQ 193

C-terminal prodomain of legumain; This family contains the C-terminal propeptide of legumain, a lysosomal endopeptidase with a specificity for hydrolysis of asparaginyl bonds. Legumain (also called vacuolar processing enzyme or VPE in plants, and asparaginyl endopeptidase or AEP in animals) is synthesized as a precursor with both N- and C-terminal propeptides. Prolegumain is directed to the lysosome or plant vacuole, where activation occurs at least partially by autolysis. The N-terminal catalytic domain is a cysteine protease from the C13 family. The C-terminal prodomain can be organized into an activation peptide (AP), spanning a helical region, and a C-terminal death domain-like fold, denoted as legumain stabilization and activity modulation (LSAM) domain. The C-terminal prodomain binds over the active site and inhibits the catalytic domain. During activation, the C-terminal prodomain is autocatalytically cleaved. This process is induced by pH changes. Human legumain has been shown to process the tetanus toxin generating the fragments found in class II antigen presentation. Legumain from plant seeds is thought to be responsible for the post-translational processing of seed proteins prior to storage. Legumain is highly expressed in some cancers such as colorectal cancer (CRC) and uveal melanoma (UM); it is associated with poor outcome in CRC and upregulation of legumain is associated with malignant behavior of UM. Thus, legumain may be used as a negative prognostic factor as well as a therapeutic target.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1834199010  14 VELLQEKLQRSEDN--RQQLEHKLDKILQKRTELDKSVRH------KSRQKYQEFLEEQAKRNERN--KKLVHMLER 80
Cdd:cd21115     4 LAILKRKLKKANDPeeKEELKKELEKLLQKREFIDETMKKivklvtGDEEEAERVLSTRRPLTDLDcyKEVVEHFRT 80

Inter-Src homology 2 (iSH2) helical domain of Class IA Phosphoinositide 3-kinase Regulatory subunits; PI3Ks catalyze the transfer of the gamma-phosphoryl group from ATP to the 3-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) or its derivatives. They 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 classified according to their substrate specificity, regulation, and domain structure. Class IA PI3Ks are heterodimers of a p110 catalytic (C) subunit and a p85-related regulatory (R) subunit. The R subunit down-regulates PI3K basal activity, stabilizes the C subunit, and plays a role in the activation downstream of tyrosine kinases. All R subunits contain two SH2 domains that flank an intervening helical domain (iSH2), which binds to the N-terminal adaptor-binding domain (ABD) of the catalytic subunit. In vertebrates, there are three genes (PIK3R1, PIK3R2, and PIK3R3) that encode for different Class IA PI3K R subunits.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1834199010   7 LENYklqvELLQEKLQRSEDNRQQLEHKLDKILQKRTELD------KSVRH---KSRQKYQEFLEEQAKRNERNKKLVH 76
Cdd:cd12923    78 MENN----ELLKSRLKELEESKEQLEEDLRKQVAYNRELEremnslKPELMqlrKQKDQYLRWLKRKGVSQEEINQLLK 152

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]

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199010    4 QAELENYKLQVELLQEKLQRSEDNRQQLEHKLDKILQKRTELDKSVRHKsRQKYQEFLEEQAKRNERNKKLVHMLERIDE 83
Cdd:TIGR02168  238 REELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEEL-QKELYALANEISRLEQQKQILRERLANLER 316

                           90       100
                   ....*....|....*....|....*.
gi 1834199010   84 QTAAMSQRSERLKMMKLQYQMYFAKL 109
Cdd:TIGR02168  317 QLEELEAQLEELESKLDELAEELAEL 342